identifier	name	definition	synonyms	alts	parents	species
10	Vanin family		VNN		so:0005855	
100	Ubiquitin like modifier activating enzymes	Ubiquitin-activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction, which (among other things) can target a protein for degradation via a proteasome. This covalent attachment of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic organisms.	UBA		so:0005855	
1000	Cytochrome P450 family 1		CYP1		hgnc.genegroup:862	
1001	Cytochrome P450 family 2		CYP2		hgnc.genegroup:862	
1002	Cytochrome P450 family 3		CYP3		hgnc.genegroup:862	
1003	Cytochrome P450 family 4		CYP4		hgnc.genegroup:862	
1004	Cytochrome P450 family 5		CYP5		hgnc.genegroup:862	
1005	Cytochrome P450 family 7		CYP7		hgnc.genegroup:862	
1006	Cytochrome P450 family 8		CYP8		hgnc.genegroup:862	
1007	Cytochrome P450 family 11		CYP11		hgnc.genegroup:862	
1008	Cytochrome P450 family 17		CYP17		hgnc.genegroup:862	
1009	Cytochrome P450 family 19		CYP19		hgnc.genegroup:862	
1010	Cytochrome P450 family 20		CYP20		hgnc.genegroup:862	
1011	Cytochrome P450 family 21		CYP21		hgnc.genegroup:862	
1012	Cytochrome P450 family 24		CYP24		hgnc.genegroup:862	
1013	Cytochrome P450 family 26		CYP26		hgnc.genegroup:862	
1014	Cytochrome P450 family 27		CYP27		hgnc.genegroup:862	
1015	Cytochrome P450 family 39		CYP39		hgnc.genegroup:862	
1016	Cytochrome P450 family 46		CYP46		hgnc.genegroup:862	
1017	Cytochrome P450 family 51		CYP51		hgnc.genegroup:862	
1019	Death effector domain containing				so:0005855	
102	Ubiquitin conjugating enzymes E2	Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome.The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein.	UBE2		so:0005855	
1021	Death associated protein kinases		DAPK		so:0005855	
1022	Autophagy related		ATG		so:0005855	
1023	CCR4-NOT transcription complex		CNOT		so:0005855	
1024	DNA glycosylases	DNA glycosylases are a family of enzymes involved in base excision repair, classified under EC number EC 3.2.2. Base excision repair is the mechanism by which damaged bases in DNA are removed and replaced. DNA glycosylases catalyze the first step of this process. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. This is accomplished by flipping the damaged base out of the double helix followed by cleavage of the N- glycosidic bond.  Glycosylases were first discovered in bacteria, and have since been found in all kingdoms of life. In addition to their role in base excision repair DNA glycosylase enzymes have been implicated in the repression of gene silencing in A. thaliana, N. tabacum and other plants by active demethylation. 5-methylcytosine residues are excised and replaced with unmethylated cytosines allowing access to the chromatin structure of the enzymes and proteins necessary for transcription and subsequent translation.  			so:0005855	
1025	Methyl-CpG binding domain containing		MBD		so:0005855	
1026	MutS homologs	Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element ( Klenow fragment ) of the DNA polymerase complex. The post-replicative Mismatch Repair System (MMRS) of Escherichia coli involves MutS (Mutator S), MutL and MutH proteins, and acts to correct point mutations or small insertion/deletion loops produced during DNA replication.  MutS and MutL are involved in preventing recombination between partially homologous DNA sequences. The assembly of MMRS is initiated by MutS, which recognizes and binds to mispaired nucleotides and allows further action of MutL and MutH to eliminate a portion of newly synthesized DNA strand containing the mispaired base.  MutS can also collaborate with methyltransferases in the repair of O(6)-methylguanine damage, which would otherwise pair with thymine during replication to create an O(6)mG:T mismatch.  MutS exists as a dimer, where the two monomers have different conformations and form a heterodimer at the structural level.  Only one monomer recognises the mismatch specifically and has ADP bound. Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure,  and is composed of: N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease. Connector domain, which is similar in structure to Holliday junction resolvase ruvC. Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA. Clamp domain, which is inserted between the two subdomains of the core domain at the top of the lever helices; the clamp domain has a beta-sheet structure. ATPase domain (connected to the core domain), which has a classical Walker A motif. HTH (helix-turn-helix) domain, which is involved in dimer contacts.  Homologues of MutS have been found in many species including eukaryotes (MSH 1, 2, 3, 4, 5, and 6 proteins), archaea and bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E. coli MutS, there is significant diversity of function among the MutS family members. This diversity is even seen within species, where many species encode multiple MutS homologues with distinct functions.  Inter-species homologues may have arisen through frequent ancient horizontal gene transfer of MutS (and MutL) from bacteria to archaea and eukaryotes via endosymbiotic ancestors of mitochondria and chloroplasts.  .	MSH		so:0005855	
1027	MutL homologs		MLH		so:0005855	
1028	Cytosolic iron-sulfur assembly components				hgnc.genegroup:1854	
1029	Paf1/RNA polymerase II complex 				so:0005855	
1031	Golgi associated, gamma adaptin ear containing, ARF binding proteins		GGA		so:0005855	
1032	Cullins	Cullins are a family of hydrophobic proteins providing a scaffold for ubiquitin ligases (E3). All eukaryotes appear to have cullins. They combine with RING proteins to form Cullin-RING ubiquitin ligases (CRLs) that are highly diverse and play a role in myriad cellular processes.  The human genome contains eight cullin genes  CUL1, part of SCF complex CUL2, part of ECS complex ( Elongin C - CUL2 - SOCS-box ) CUL3, part of CUL3-BTB complex CUL4A CUL4B CUL5 CUL7 CUL9, also known as PARC  There is also a more distant member called ANAPC2 (or APC2), part of the Anaphase-promoting complex. CUL1, 2, 3, 4A, 4B, 5 and 7 each form part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms.  The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as CUL9, also known as p53 cytoplasmic anchor PARC, and the ANAPC2 subunit of the anaphase-promoting complex/cyclosome; both CUL9 and ANAPC2 have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins.    With the exception of ANAPC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognises and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Nedd8CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae (Baker's yeast), and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue. 	CUL		so:0005855	
1033	SCY1 like pseudokinases	SCYL (SCY1) is a family of pseudokinases found in almost all eukaryotes, involved in trafficking of secretory proteins, nuclear tRNA export, and chromosome biology. 	SCYL		so:0005855	
1034	SMC5-6 protein complex				so:0005855	
1035	Glycerol-3-phosphate acyltransferases		GPAT		so:0005855	
1036	Membrane bound O-acyltransferase family	The MBOAT (membrane bound O-acyl transferase) family of membrane proteins is a family of various acyltransferase enzymes. All family members contain multiple transmembrane domains and most carry two conserved residues which might be active-site residues, a conserved histidine (His) embedded in a hydrophobic stretch of residues and an asparagine (Asn) or histidine within a more hydrophilic region some 30-50 residues upstream.  MBOAT enzymes catalyze the transfer of an acyl group from acyl-coenzyme to one of several different substrates. The family is found from bacteria to eukaryotes, and the active region lies outside the membrane.  The family may be grouped into four categories, according to function:	MBOAT		so:0005855	
1038	Biogenesis of lysosomal organelles complex 2 		BLOC2S		so:0005855	
1039	Biogenesis of lysosomal organelles complex 3 		BLOC3S		so:0005855	
104	Aminopeptidases	Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein (N-terminus) or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Aminopeptidases are used in essential cellular functions. Many, but not all, of these peptidases are zinc metalloenzymes.			so:0005855	
1040	Ragulator complex 		LAMTOR		so:0005855	
1041	CTD family phosphatases				hgnc.genegroup:814|hgnc.genegroup:702	
1042	5'-nucleotidases	5'-nucleotidase ( EC 3.1.3.5 ) is an enzyme which catalyzes the phosphorylytic cleavage of 5'nucleotides.  Although originally found in snake venom,  the activity of 5'nucleotidase has been described for bacteria and plant cells, and is widely distributed in vertebrate tissue.  In mammalian cells the enzyme is predominantly located in the plasma membrane and its primary role is in the conversion of extracellular nucleotides (e.g. 5'-AMP), which are generally impermeable, to the corresponding nucleoside (e.g. adenosine) which can readily enter most cells.  Consequently, the enzyme plays a key role in the metabolism of nucleotides. The enzyme has a wide substrate specificity for nucleotides and has been shown to hydrolyze 5'nucleotides rapidly, ribose-5-phosphate slowly, and other phosphate esters extremely slowly (if at all).  	NT5		hgnc.genegroup:1076	
1043	Lipins		LPIN		hgnc.genegroup:1045|hgnc.genegroup:1066	
1044	EYA transcriptional coactivator and phosphatases		EYA		hgnc.genegroup:702	
1045	HAD Asp-based non-protein phosphatases				hgnc.genegroup:1083	
1046	Cellular communication network factors				so:0005855	
1048	BLOC-1 related complex subunits		BORCS		so:0005855	
1049	RecQ like helicases	RecQ helicase is a family of helicase enzymes initially found in Escherichia coli  that has been shown to be important in genome maintenance.    They function through catalyzing the reaction ATP + H 2 O → ADP + P and thus driving the unwinding of paired DNA and translocating in the 3' to 5' direction. These enzymes can also drive the reaction NTP + H 2 O → NDP + P to drive the unwinding of either DNA or RNA.	RECQL		hgnc.genegroup:1167	
105	Yip1 domain containing		YIPF		hgnc.genegroup:1144	
1050	Topoisomerases	Topoisomerases are enzymes that regulate the overwinding or underwinding of DNA. The winding problem of DNA arises due to the intertwined nature of its double-helical structure. During DNA replication and transcription, DNA becomes overwound ahead of a replication fork. If left unabated, this tension would eventually stop the ability of the enzymes involved in these processes to continue down the DNA strand. In order to prevent and correct these types of topological problems caused by the double helix, topoisomerases bind to either single-stranded or double-stranded DNA and cut the phosphate backbone of the DNA. This intermediate break allows the DNA to be untangled or unwound, and, at the end of these processes, the DNA backbone is resealed again. Since the overall chemical composition and connectivity of the DNA do not change, the tangled and untangled DNAs are chemical isomers, differing only in their global topology, thus their name. Topoisomerases are isomerase enzymes that act on the topology of DNA.  Bacterial topoisomerase and human topoisomerase proceed via the same mechanism for replication and transcription.	TOP		so:0005855	
1051	Nucleoporins	The nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC).  The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nuclear pores in turn allow the transport of water-soluble molecules across the nuclear envelope. Nucleoporins, a family of around 30 proteins, are the main components of the nuclear pore complex in eukaryotic cells. Nucleoporin 62 is the most abundant member of this family.  Nucleoporins are able to transport molecules across the nuclear envelope at a very high rate. A single NPC is able to transport 60,000 protein molecules across the nuclear envelope every minute. 	NUP		so:0005855	
1052	IgLON cell adhesion molecules		IGLON		hgnc.genegroup:1410	
1053	14-3-3 phospho-serine/phospho-threonine binding proteins	14-3-3 proteins are a family of conserved regulatory molecules that are expressed in all eukaryotic cells. 14-3-3 proteins have the ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors. More than 200 signaling proteins have been reported as 14-3-3 ligands. The name 14-3-3 refers to the particular elution and migration pattern of these proteins on DEAE -cellulose chromatography and starch-gel electrophoresis. The 14-3-3 proteins eluted in the 14th fraction of bovine brain homogenate and were found on positions 3.3 of subsequent electrophoresis by Moore and Perez (1967). Elevated amounts of 14-3-3 proteins are found in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. 	YWHA		so:0005855	
1054	Ribosomal proteins	A ribosomal protein is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. A large part of the knowledge about these organic molecules has come from the study of E. coli ribosomes. Most ribosomal proteins have been isolated and specific antibodies have been produced. These, together with electronic microscopy and the use of certain reactives, have allowed for the determination of the topography of the proteins in the ribosome. E.coli, other bacteria and Archaea have a 30S small subunit and a 50S large subunit, whereas humans and yeasts have a 40S small subunit and a 60S large subunit.  Equivalent subunits are frequently numbered differently between bacteria, Archaea, yeasts and humans. 			so:0005855	
1055	Exocyst complex	The exocyst is an octameric protein complex involved in vesicle trafficking, specifically the tethering and spatial targeting of post- Golgi vesicles to the plasma membrane prior to vesicle fusion. It is implicated in a number of cell processes, including exocytosis and also cell migration and growth.	EXOC		so:0005855	
1056	TNF receptor associated factors	TNF receptor associated factors also known as TRAFs are a family of proteins primarily involved in the regulation of inflammation, antiviral responses and apoptosis.  Currently, seven TRAF proteins have been characterized in mammals : TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, TRAF6 and TRAF7. Except for TRAF7, these proteins share a relatively conserved secondary structure, including a namesake C-terminal TRAF domain that mediates interactions with other signaling components such as the transmembrane TNF receptors and CD40.	TRAF		so:0005855	
1057	BCL2 family	Apoptosis regulator Bcl-2 is a family of evolutionarily related proteins. These proteins govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro- apoptotic ( Bax, BAD, Bak and Bok among others) or anti-apoptotic (including Bcl-2 proper, Bcl-xL, and Bcl-w, among an assortment of others). There are a total of 25 genes in the Bcl-2 family known to date.	BCL2		so:0005855	
1058	ATAC complex		ATAC		so:0005855	
1059	SAGA complex				so:0005855	
106	Y-box binding proteins		YBX		so:0005855	
1060	Cohesin complex	Cohesin is a protein complex that regulates the separation of sister chromatids during cell division, either mitosis or meiosis.			so:0005855	
1061	Mediator complex	Mediator is a multiprotein complex that functions as a transcriptional coactivator in all eukaryotes. It was discovered by Roger D. Kornberg, winner of the 2006 Nobel Prize in Chemistry. It is also referred to in scientific literature as the vitamin D receptor interacting protein ( DRIP ) coactivator complex and the thyroid hormone receptor-associated proteins ( TRAP ). The mediator complex is required for the successful transcription of nearly all class II gene promoters in yeast.  It works in the same manner in mammals. The human Mediator complex has 31+ subunits and is 1.2 MDa in size. Its large surface area provides great potential for protein–protein interaction, even though its sequences do not contain many predicted functional domains. Mediator has been shown to associate with general transcription factors, as well as RNA polymerase II, and is essential for activator-dependent transcription. It has also been demonstrated that the Mediator complex is involved in activator-independent transcription, implying that it may provide a fundamental control of the formation of the initiation complex.  Mediator functions as a coactivator and binds to the C-terminal domain of RNA polymerase II holoenzyme, acting as a bridge between this enzyme and transcription factors.  	MED		so:0005855	
1062	GOLD domain containing				so:0005855	
1063	SEC14 family		SEC14		hgnc.genegroup:1062	
1064	Transmembrane p24 trafficking proteins		TMED		hgnc.genegroup:1062	
1065	Insulin like growth factor binding proteins		IGFBP		so:0005855	
1066	Lipid phosphatases				hgnc.genegroup:1076	
1067	Phospholipid phosphatases		PLPP		hgnc.genegroup:1126|hgnc.genegroup:1066	
1070	Sphingosine-1-phosphate phosphatases		SGPP		hgnc.genegroup:1066	
1071	Acid phosphatases	Acid phosphatase ( EC 3.1.3.2, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid phosphohydrolase, acid phosphomonoester hydrolase, uteroferrin, acid nucleoside diphosphate phosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum) ) is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. 	ACP		hgnc.genegroup:1076	
1072	Alkaline phosphatases	Alkaline phosphatase ( ALP, ALKP, ALPase, Alk Phos ) ( EC 3.1.3.1 ) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment.	ALP		hgnc.genegroup:1076	
1073	Sugar phosphatases				hgnc.genegroup:1076	
1074	Glucose 6-phosphatases, catalytic	Glucose 6-phosphatase ( EC 3.1.3.9, G6Pase) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins.  This catalysis completes the final step in gluconeogenesis and glycogenolysis and therefore plays a key role in the homeostatic regulation of blood glucose levels.  G6Pase is a complex of multiple component proteins, including transporters for G6P, glucose, and phosphate. The main phosphatase function is performed by the G6Pase catalytic subunit.	G6PC		hgnc.genegroup:1073	
1075	Fructose-1,6-bisphosphatases	Fructose bisphosphatase ( EC 3.1.3.11 ) is an enzyme that converts fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis and the Calvin cycle which are both anabolic pathways. Fructose bisphosphatase catalyses the reverse of the reaction which is catalysed by phosphofructokinase in glycolysis.	FBP		hgnc.genegroup:1073	
1076	Phosphatases				so:0005855	
1077	6-phosphofructo-2-kinases/fructose-2,6-biphosphatases		PFKFB		hgnc.genegroup:1073	
1078	Phosphoglycerate mutases	Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor -dependent (dPGM) or cofactor-independent (iPGM).  The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria.	PGAM		so:0005855	
1079	Phosphoinositide phosphatases				hgnc.genegroup:1066	
1082	Bisphosphoglycerate phosphatases	In enzymology, a bisphosphoglycerate phosphatase ( EC 3.1.3.13 ) is an enzyme that catalyzes the chemical reaction  2,3-bisphospho-D-glycerate + H 2 O 3-phospho-D-glycerate + phosphate  Thus, the two substrates of this enzyme are 2,3-bisphospho-D-glycerate and H 2 O, whereas its two products are 3-phospho-D-glycerate and phosphate. 			hgnc.genegroup:1073	
1083	HAD Asp-based phosphatases	The HAD phosphatase family are named after the bacterial enzyme haloacid dehydrogenase and employ an Asp-based catalytic mechanism. The family includes both protein and non-protein phosphatases.			hgnc.genegroup:1076	
1084	Golgins				so:0005855	
1085	MCM family	Mini chromosome maintenance complex (or minichromosome maintenance protein complex, or mini-chromosome maintenance (MCM) 2-7 helicase complex ) has a role in both the initiation and the elongation phases of eukaryotic DNA replication, specifically the formation and elongation of the replication fork. MCM is a component of the pre-replication complex, which is a component of the licensing factor. MCM is a hexamer of six related polypeptides (MCM2 through MCM7) that form a ring structure.  	MCM		hgnc.genegroup:1167	
1086	MADS box family	The MADS box is a conserved sequence motif found in genes which comprise the MADS-box gene family.  The MADS box encodes the DNA-binding MADS domain. The MADS domain binds to DNA sequences of high similarity to the motif CC 6 GG termed the CArG-box.  MADS-domain proteins are generally transcription factors.   The length of the MADS-box reported by various researchers varies somewhat, but typical lengths are in the range of 168 to 180 base pairs, i.e. the encoded MADS domain has a length of 56 to 60 amino acids.     There is evidence that the MADS domain evolved from a sequence stretch of a type II topoisomerase in a common ancestor of all extant eukaryotes. 			so:0005855	
1087	LEM domain containing		LEMD		so:0005855	
1089	Spindlin family		SPIN		so:0005855	
1090	Atypical chemokine receptors		ACKR		hgnc.genegroup:189	
1091	C-C motif chemokine receptors		CCR		hgnc.genegroup:189	
1092	X-C motif chemokine receptors		XCR		hgnc.genegroup:189	
1093	C-X-3-C motif chemokine receptors		CX3CR		hgnc.genegroup:189	
1094	C-X-C motif chemokine receptors		CXCR		hgnc.genegroup:189	
1095	EPH receptors	Ephrin receptors (Ephs) are a group of receptors that are activated in response to binding ephrin. Ephs form the largest known subfamily of receptor tyrosine kinases (RTKs). Both Ephs and their corresponding ephrin ligands are membrane-bound proteins that require direct cell-cell interactions for Eph receptor activation. Ephephrin signaling has recently been identified to play a critical role in the maintenance of several processes during adulthood including long-term potentiation,  angiogenesis,  and stem cell differentiation and cancer. 	EPH		hgnc.genegroup:321|hgnc.genegroup:555	
1096	Erb-b2 receptor tyrosine kinases	The ErbB family of proteins contains four receptor tyrosine kinases, structurally related to the epidermal growth factor receptor (EGFR), its first discovered member. In humans, the family includes Her1 (EGFR, ErbB1 ), Her2 (Neu, ErbB2), Her3 (ErbB3), and Her4 (ErbB4). The gene symbol, ErbB, is derived from the name of a viral oncogene to which these receptors are homologous: erythroblastic leukemia viral oncogene. Insufficient ErbB signaling in humans is associated with the development of neurodegenerative diseases, such as multiple sclerosis and Alzheimer's Disease,  while excessive ErbB signaling is associated with the development of a wide variety of types of solid tumor.	ERBB		hgnc.genegroup:321	
1097	Myosin heavy chains, class I	Myosin-I isoforms are the single-headed, membrane-associated members of the myosin superfamily found in most eukaryotic cells. They play essential roles in membrane dynamics, cytoskeletal structure, mechanical signal-transduction and endosome processing.	MYO1		hgnc.genegroup:656	
1098	Myosin heavy chains, class II	Myosin-II isoforms are the major contractile proteins in muscle and also play several crucial roles in non-muscle contractility. Myosin-II molecules contain two motor domains and assemble into bipolar filaments.	MYH		hgnc.genegroup:656	
1099	Myosin heavy chains, class III	Class III myosins (MYO3) are novel in that they contain an amino-terminal kinase domain connected to the canonical myosin motor domain.	MYO3		hgnc.genegroup:656	
1100	Myosin heavy chains, class V	Myosin-V transports vesicles along actin filament tracks over long distances as a single, two-headed molecule.	MYO5		hgnc.genegroup:656	
1101	Myosin heavy chains, class VI	Due to a unique addition to the lever arm-positioning region (converter), class VI myosins move in the opposite direction (toward the minus-end of actin filaments) compared to other characterized myosin classes.	MYO6		hgnc.genegroup:656	
1102	Myosin heavy chains, class VII	The class VII myosins are characterized by the presence of two FERM domains in their C-terminal tail region	MYO7		hgnc.genegroup:656	
1103	Myosin heavy chains, class IX	Class IX myosins are single-headed actin motors that have a conserved RhoGAP domain and an insertion in loop2 of the myosin head domain.	MYO9		hgnc.genegroup:656	
1104	Myosin heavy chains, class X	Myosin-X is the founding member of a class of unconventional myosins characterized by a tail domain containing multiple pleckstrin homology domains.	MYO10		hgnc.genegroup:656	
1105	Myosin heavy chains, class XV		MYO15		hgnc.genegroup:656	
1106	Myosin heavy chains, class XVI		MYO16		hgnc.genegroup:656	
1107	Myosin heavy chains, class XVIII		MYO18		hgnc.genegroup:656	
1108	Myosin heavy chains, class XIX		MYO19		hgnc.genegroup:656	
1109	Keratins	Keratin is a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human skin. It is the key structural component of hair and nails, and it provides the necessary strength and toughness for masticatory organs, such as the tongue and the hard palate. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized tissues found in reptiles, birds, amphibians, and mammals. The only other biological matter known to approximate the toughness of keratinized tissue is chitin.   	KRT		hgnc.genegroup:607	
1110	Schlafen family		SLFN		so:0005855	
1111	ESCRT complexes	The endosomal sorting complexes required for transport ( ESCRT ) machinery is made up of cytosolic protein complexes, known as ESCRT-0, ESCRT-I, ESCRT-II, and ESCRT-III. Together with a number of accessory proteins, these ESCRT complexes enable a unique mode of membrane remodeling that results in membranes bending/budding away from the cytoplasm.   These ESCRT components have been isolated and studied in a number of organisms including yeast and humans.  The ESCRT machinery plays a vital role in a number of cellular processes including multivesicular body (MVB) biogenesis, cellular abscission, and viral budding. Multivesicular body (MVB) biogenesis is a process in which ubiquitin tagged proteins enter organelles called endosomes via the formation of vesicles. This process is essential for cells to destroy misfolded and damaged proteins.  Without ESCRT machinery, these proteins can build up and lead to neurodegenerative disease. For example, abnormalities in ESCRT-III components can lead to neurological disorders such as hereditary spastic paraplegia (HSP).  Cellular abscission, the process by which the membrane connecting two daughter cells is cleaved, is also mediated by ESCRT machinery. Without the ESCRT complexes, daughter cells could not separate and abnormal cells containing twice the amount of DNA would be generated. These cells would inevitably be destroyed through a process known as apoptosis. Lastly, viral budding, or the process by which specific types of viruses exit cells, may not occur in the absence of ESCRT machinery. This would inevitably prevent viruses from spreading from cell to cell.			so:0005855	
1112	Actinins		ACTN		hgnc.genegroup:863	
1113	Spectrins	Spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells. The protein is named spectrin since it was first isolated as a major protein component of human red blood cells which had been treated with mild detergents; the detergents lysed the cells and the hemoglobin and other cytoplasmic components were washed out. In the light microscope the basic shape of the red blood cell could still be seen as the spectrin containing submembranous cytoskeleton preserved the shape of the cell in outline. This became known as a red blood cell 'ghost', and so the major protein of the ghost was named spectrin. Spectrin forms pentagonal or hexagonal arrangements, forming a scaffolding and playing an important role in maintenance of plasma membrane integrity and cytoskeletal structure.  The hexagonal arrangements are formed by tetramers of spectrin subunits associating with short actin filaments at either end of the tetramer. These short actin filaments act as junctional complexes allowing the formation of the hexagonal mesh. In certain types of brain injury such as diffuse axonal injury, spectrin is irreversibly cleaved by the proteolytic enzyme calpain, destroying the cytoskeleton.  Spectrin cleavage causes the membrane to form blebs and ultimately to be degraded, usually leading to the death of the cell.  Spectrin subunits may also be cleaved by caspase family enzymes, and calpain and caspase produce different spectrin breakdown products which can be detected by western blotting with appropriate antibodies. Calpain cleavage may indicate activation of necrosis, while caspase cleavage may indicate apoptosis. 	SPT		so:0005855	
1114	Flotillins	Flotillins are ubiquitous and highly conserved proteins. They were initially discovered as being associated with specific caveolin-independent cholesterol- and glycosphingolipid-enriched membrane microdomains and as being expressed during axon regeneration. Flotillins have a role in a large number of physiopathological processes, mainly through their function in membrane receptor clustering and in the regulation of clathrin-independent endocytosis.	FLOT		so:0005855	
1115	ESCRT-0				hgnc.genegroup:1111	
1116	ESCRT-I				hgnc.genegroup:1111	
1117	ESCRT-II				hgnc.genegroup:1111	
1118	ESCRT-III				hgnc.genegroup:1111	
1119	ESCRT-III associated factors				hgnc.genegroup:1118	
1120	ESCRT-IV				hgnc.genegroup:1111	
1121	Eukaryotic translation initiation factor 3		EIF3		so:0005855	
1122	BBSome	The BBSome is a component of the basal body and is involved in formation of the primary cilium.  The BBSome is a complex of seven Bardet-Biedl syndrome (BBS) proteins: BBS1, BBS2, BBS4, BBS5, BBS7, TTC8 (aka BBS8) and BBS9. In addition the BBSome contains the BBIP10 protein. 			hgnc.genegroup:615	
1124	SNAREs	SNARE proteins (an acronym derived from ' SNAP (Soluble NSF Attachment Protein) REceptor') are a large protein superfamily.  The primary role of SNARE proteins is to mediate vesicle fusion, that is, the fusion of vesicles with their target membrane bound compartments (such as a lysosome). The best studied SNAREs are those that mediate docking of synaptic vesicles with the presynaptic membrane in neurons. 			so:0005855	
1125	Xeroderma pigmentosum complementation groups	Xeroderma pigmentosum, or XP, is an autosomal recessive genetic disorder of DNA repair in which the ability to repair damage caused by ultraviolet (UV) light is deficient.  :574 In extreme cases, all exposure to sunlight must be forbidden, no matter how small; as such, individuals with the disease are often colloquially referred to as children of the night.  Multiple basal cell carcinomas (basaliomas) and other skin malignancies frequently occur at a young age in those with XP; metastatic malignant melanoma and squamous cell carcinoma  are the two most common causes of death in XP victims. This disease involves both sexes and all races, with an incidence of 1:250,000 in the United States.  XP is roughly six times more common in Japanese people  than in other groups. Normally, damage to DNA in epidermal cells occurs during exposure to UV light. The absorption of the high-energy light leads to the formation of pyrimidine dimers, namely cyclobutane-pyrimidine dimers and pyrimidine-6-4-pyrimidone photoproducts. In a healthy, normal human being, the damage is first excised by endonucleases. DNA polymerase then repairs the missing sequence, and ligase 'seals' the transaction. This process is known as nucleotide excision repair.	XP		hgnc.genegroup:1269	
1126	Phospholipid phosphatase superfamily				so:0005855	
1127	Phospholipid phosphatase related		PLPPR		hgnc.genegroup:1126	
1130	Yippee like family		YPEL		so:0005855	
1131	Gemins		GEMIN		hgnc.genegroup:1500	
1132	N-acetyltransferases		NAT		so:0005855	
1133	Arylamine N-acetyltransferases	In enzymology, an arylamine N-acetyltransferase ( EC 2.3.1.5 ) is an enzyme that catalyzes the chemical reaction  acetyl-CoA + an arylamine CoA + an N-acetylarylamine  Thus, the two substrates of this enzyme are acetyl-CoA and arylamine, whereas its two products are CoA and N-acetylarylamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:arylamine N-acetyltransferase. Other names in common use include arylamine acetylase, beta-naphthylamine N-acetyltransferase, 4-aminobiphenyl N-acetyltransferase, acetyl CoA-arylamine N-acetyltransferase, 2-naphthylamine N-acetyltransferase, arylamine acetyltransferase, indoleamine N-acetyltransferase, N-acetyltransferase, p-aminosalicylate N-acetyltransferase, serotonin acetyltransferase, and serotonin N-acetyltransferase.			hgnc.genegroup:1132	
1134	GCN5 related N-acetyltransferases				hgnc.genegroup:1132	
1135	Transmembrane channel like family		TMC		so:0005855	
1136	MAGE family		MAGE		so:0005855	
1138	Stathmins	Stathmin 1/oncoprotein 18, also known as STMN1, is a highly conserved 17 kDa protein. Its function as an important regulatory protein of microtubule dynamics has been well-characterized.  Eukaryotic microtubules are one of three major components of the cell's cytoskeleton. They are highly dynamic structures that continuously alternate between assembly and disassembly. Stathmin performs an important function in regulating rapid microtubule remodeling of the cytoskeleton in response to the cell's needs. Microtubules are cylindrical polymers of α,β-tubulin. Their assembly is in part determined by the concentration of free tubulin in the cytoplasm.  At low concentrations of free tubulin, the growth rate at the microtubule ends is slowed and results in an increased rate of depolymerization (disassembly).  	STMN		so:0005855	
1139	BAG cochaperones		BAG		so:0005855	
1140	Tropomodulins	Tropomodulin is a protein which binds and caps the minus end of actin (the 'pointed' end), regulating the length of actin filaments in muscle and non-muscle cells. The protein functions by physically blocking the spontaneous dissociation of ADP -bound actin monomers from the minus end of the actin fibre. This, along with plus end capping proteins, such as capZ stabilise the structure of the actin filament. End capping is particularly important when long-lived actin filaments are necessary, for example: in myofibrils. Inhibition of tropomodulin capping activity leads to dramatic increase in thin filament length from its pointed end. 	TMOD		so:0005855	
1141	Pentraxins		PTX		so:0005855	
1142	Long pentraxins				hgnc.genegroup:1141	
1143	Short pentraxins				hgnc.genegroup:1141	
1144	YIP superfamily				so:0005855	
1145	AF4/FMR2 family		AFF		so:0005855	
1146	GRAM domain containing		GRAM		so:0005855	
1147	PWWP domain containing		PWWP		so:0005855	
1149	NADH:ubiquinone oxidoreductase core subunits		NDUF, MT-ND		hgnc.genegroup:640	
1150	NADH:ubiquinone oxidoreductase supernumerary subunits		NDUF		hgnc.genegroup:640	
1151	Phosphatidylinositol transfer proteins		PITPN		so:0005855	
1153	Regulatory factor X family		RFX		so:0005855	
1156	MAPK activated protein kinases		MAPKAPK		hgnc.genegroup:652	
1157	RAF family	This family includes the RAF kinases and the KSR scaffold proteins. All of the genes are related by homology but the KSR genes are 'pseudokinases' and have no kinase function.			so:0005855	
1158	Volume regulated anion channel subunits		LRRC8		hgnc.genegroup:294|hgnc.genegroup:278	
1159	Integrin beta subunits		ITGB		hgnc.genegroup:597	
1160	Integrin alpha subunits		ITGA		hgnc.genegroup:597	
1161	Taste 1 receptors	The TAS1R1+TAS1R3 heterodimer receptor functions as the savory receptor, responding to L-amino acid binding, especially L-glutamate. The umami taste is most frequently associated with the food additive monosodium glutamate (MSG) and can be enhanced through the binding of inosine monophosphate (IMP) and guanosine monophosphate (GMP) molecules.  The TAS1R2+TAS1R3 heterodimer receptor functions as the sweet receptor by binding to a wide variety of sugars and sugar substitutes. TAS1R2+3 expressing cells are found in circumvallate papillae and foliate papillae near the back of the tongue and palate taste receptor cells in the roof of the mouth.	TAS1R		hgnc.genegroup:289	
1162	Taste 2 receptors	The TAS2R proteins function as bitter taste receptors. There are 43 human TAS2R genes, each of which (excluding the five pseudogenes) lacks introns and codes for a GPCR protein. These proteins, as opposed to TAS1R proteins, have short extracellular domains and are located in circumvallate papillae, palate, foliate papillae, and epiglottis taste buds, with reduced expression in fungiform papillae.	TAS2R		hgnc.genegroup:289	
1163	LIMS zinc finger family		LIMS		hgnc.genegroup:1218	
1164	CDC42 effector proteins		CDC42EP		so:0005855	
1165	CCAAT/enhancer binding proteins 		CEBP		so:0005855	
1166	Helicases	Helicases are a class of enzymes vital to all living organisms. Their main function is to unpackage an organism's genes. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands (i.e., DNA, RNA, or RNA-DNA hybrid) using energy derived from ATP hydrolysis. There are many helicases resulting from the great variety of processes in which strand separation must be catalyzed. Approximately 1% of eukaryotic genes code for helicases.  The human genome codes for 95 non-redundant helicases: 64 RNA helicases and 31 DNA helicases.  Many cellular processes, such as DNA replication, transcription, translation, recombination, DNA repair, and ribosome biogenesis involve the separation of nucleic acid strands that necessitates the use of helicases.			so:0005855	
1167	DNA helicases				hgnc.genegroup:1166	
1168	RNA helicases				hgnc.genegroup:1166	
1169	UPF1 like RNA helicases				hgnc.genegroup:1168	
1171	SCF complex	Skp, Cullin, F-box containing complex (or SCF complex ) is a multi-protein E3 ubiquitin ligase complex catalyzing the ubiquitination of proteins destined for proteasomal degradation. It has important roles in the ubiquitination of proteins involved in the cell cycle and also marks various other cellular proteins for destruction.  Core Components SCF contains three core subunits, and a number of less critical components:  F-box protein ( e.g. Cdc4 ) – Contributes to the specificity of SCF by aggregating to target proteins independently of the complex and then binding to the Skp1 component, thus allowing the protein to be brought into proximity with the functional E2 protein. The F-box is also essential in regulating SCF activity during the course of the cell-cycle. SCF levels are thought to remain constant throughout the cell-cycle. Instead, F-box affinity for protein substrates is regulated through cdk/cyclin mediated phosphorylation of target proteins.  Skp1 – Skp1 is a bridging protein and forms part of the horseshoe-shaped complex in tandem with cullin (cul1). Skp1 is essential in the recognition and binding of the F-box.  Cullin ( CUL1 ) – CUL1 forms the major structural scaffold of the SCF complex and links the skp1 domain with the Rbx1 domain.  RBX1 – Rbx1 contains a small zinc-binding domain called the RING Finger, to which the E2-ubiquitin conjugate binds, allowing the transferral of the ubiquitin to a lysine residue on the target protein.  SCF and Cell Cycle Regulation Progression through the cell cycle in eukaryotes is regulated through synthesisdephosphorylation of cell-cycle-regulating proteins. Two ubiquitin ligases are crucial in the cell cycle. The anaphase-promoting complex or cyclosome ( APC/C ) controls the metaphase – anaphase transition when bound to its substrate-specific activating subunit Cdc20 :  this complex ubiquitinylates the separase -inhibiting protein securin, paving the way for separase to break cohesin and thus separate the sister chromatids at the centromere. APC/C with another activating subunit, Cdh1, is active in G1 phase and controls levels of the mitosis-regulating B-type cyclins. SCF controls the transitions between G1/S and G2/M phases. Two F-box-protein-bound SCF complexes (SCF- Skp2 and SCF- β-TrCP ), are most well studied among over 70 F-box proteins identified in humans. SCF-Skp2 mainly ubiquitinates and degrades cyclin-dependent kinase inhibitors (CKIs) such as p27 and p21 as well as the G1-/S-specific cyclin E, in vivo and in vitro.  Therefore, SCF-Skp2 promotes cell-cycle progression and cell growth.  On the other hand, SCF-βTrCP promotes proteolysis of Emi1, an APC/C-Cdh1 inhibitor, and Wee1, a Cdk1 inhibitor, in early mitosis via phosphorylation at their degron (the amino acid motif DSGXXS, where X can be any amino acid) by kinases such as Polo-like kinase 1 (Plk1) and Cdk1–cyclin B. SCF-βTrCP and APC/C control each other to regulate timely progression through the cell cycle.  Lists of substrates of SCF-Skp2 and -βTrCP are still growing. SCF and Plant Hormone Signaling In plants, the plant hormone auxin stimulates binding of SCF-TIR1 to the AUX/IAA repressor and then the degradation of the repressor, resulting in the activation of auxin-responsive genes. The TIR1 F-box protein acts as an auxin receptor and directly links reception of auxin to degradation of the Aux/IAA proteins. TIR1 (Transport Inhibitor Response 1) belongs to AFBs (Auxin Signaling F-box proteins).  In plants, the plant hormone Jasmonate allows binding between SCF-COI1 to the JAZ transcription factor. Degradation of the JAZ transcription factor allows for the transcription of the jasmonate responsive genes. 			so:0005855	
1172	Lysozymes		LY		hgnc.genegroup:1650	
1173	Lysozymes, g-type		LYG		hgnc.genegroup:1172	
1174	Lysozymes, c-type	Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes ( EC 3.2.1.17 ) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene.  	LYZ		hgnc.genegroup:1172	
1175	Growth hormone family				hgnc.genegroup:542	
1178	Diacylglycerol kinases	Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.  In bacteria, DGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains.  The best conserved region is a stretch of 12 residues which are located in a cytoplasmic loop between the second and third transmembrane domains. Some Gram-positive bacteria also encode a soluble diacylglycerol kinase capable of reintroducing DAG into the phospholipid biosynthesis pathway. DAG accumulates in Gram-positive bacteria as a result of the transfer of glycerol-1-phosphate moieties from phosphatidylglycerol to lipotechoic acid. 	DGK		so:0005855	
1179	Sushi domain containing	Sushi domain is an evolutionary conserved protein domain. Sushi domains, also known as Complement control protein (CCP) modules, or short consensus repeats (SCR), exist in a wide variety of complement and adhesion proteins. The structure is known for this domain; it is based on a beta-sandwich arrangement - one face made up of three beta-strands hydrogen-bonded to form a triple-stranded region at its centre, and the other face formed from two separate beta-strands. 			so:0005855	
1180	Myosin phosphatase targeting family		MYPT		so:0005855	
1181	Activating leukocyte immunoglobulin like receptors	Activating LILRs (LILRAs) have short cytoplasmic domains lacking signaling motifs but transmit activating signals by linking to immunoreceptor tyrosine-based activation motifs of the FcR gamma-chain.	LILRA		hgnc.genegroup:630	
1182	Inhibitory leukocyte immunoglobulin like receptors	Inhibitory LILRs (LILRBs) contain cytoplasmic tails with immunoreceptor tyrosine-based inhibitory motifs that provide negative signals.	LILRB		hgnc.genegroup:630	
1183	TEA domain transcription factors		TEAD		so:0005855	
1184	Prickle planar cell polarity proteins		PRICKLE		so:0005855	
1185	Type I classical cadherins	Classical cadherins have an ectodomain comprising at least five consecutive cadherin repeats, a single transmembrane domain and a cytoplasmic domain containing two conserved motifs for binding to catenins. Type I classical cadherins are characterised by the presence of an HAV motif in the first extracellular repeat. 	CDH		hgnc.genegroup:18	
1186	Type II classical cadherins	Classical cadherins have an ectodomain comprising at least five consecutive cadherin repeats, a single transmembrane domain and a cytoplasmic domain containing two conserved motifs for binding to catenins. Type II classical cadherins differ from type I classical cadherins because they lack an HAV motif in the first extracellular repeat. 	CDH		hgnc.genegroup:18	
1187	7D cadherins	The striking common features of [7D-cadherins] are the seven extracellular cadherin repeats and the partial lack of the Ca2+-binding motifs at the interface between cadherin repeats 2 and 3.			hgnc.genegroup:18	
1188	Desmosomal cadherins	The desmosomal cadherins, desmogleins (Dsgs) and desmocollins (Dscs), are transmembrane molecules that mediate adhesion through their extracellular domains and serve as a scaffold for assembly of the desmosomal plaque through their cytoplasmic domains.	DSC, DSG		hgnc.genegroup:18	
1189	CELSR cadherins		CELSR		hgnc.genegroup:18	
1191	Mannosidases	Mannosidase is an enzyme which hydrolyzes mannose.  			hgnc.genegroup:1650	
1192	Mannosidases type alpha				hgnc.genegroup:1191	
1193	Mannosidases alpha class 1	Class 1 alpha-mannosidases recognize and cleave only alpha-1,2–linked mannose residues from the Man9GlcNAc2 high-mannose precursor.	MAN1		hgnc.genegroup:1192	
1194	Mannosidases alpha class 2	Glycoside hydrolases of family 38 are Class II α-mannosidases. They range in breadth of specificity from the Golgi α-mannosidase (2A1), which has a dual specificity for α-1,6 and α-1,3-linked mannoses, to the lysosomal mannosidases, which have either broad (2B1 cleaves α1,2, α1,3 and α1,6 linkages) or narrow specificities (2B2 is specific for α-1,6). There have been GH38 mannosidases identified in a number of different localizations, classed into subfamilies with different substrate specificities and biochemical properties, and, presumably, different physiological roles. The Golgi enzyme is identified as 2A1 (Class 2, A for Golgi, enzyme 1). Lysosomal GH38 mannosidases are indicated by 'B' (2B1, 2B2) and those likely existing in the cytoplasm by 'C'.	MAN2		hgnc.genegroup:1192	
1195	Mannosidases endo-alpha		MANEA		hgnc.genegroup:1192	
1196	Mannosidases type beta	Beta-mannosidase ( EC 3.2.1.25, mannanase, mannase, beta-D-mannosidase, beta-mannoside mannohydrolase, exo-beta-D-mannanase, lysosomal beta A mannosidase ) is an enzyme with system name beta-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene.	MANBA		hgnc.genegroup:1191	
1197	PR/SET domain family	Prdm genes encode transcription factors with a subtype of SET domain known as the PRDF1-RIZ (PR) homology domain and a variable number of zinc finger motifs. 	PRDM		hgnc.genegroup:1399	
1198	Ras association domain family		RASSF		so:0005855	
1199	Glutamate ionotropic receptor kainate type subunits	Kainate receptors, or KARs, are ionotropic receptors that respond to the neurotransmitter glutamate. They were first identified as a distinct receptor type through their selective activation by the agonist kainate, a drug first isolated from the red alga Digenea simplex. KARs are less understood than AMPA and NMDA receptors, the other ionotropic glutamate receptors. Postsynaptic kainate receptors are involved in excitatory neurotransmission. Presynaptic kainate receptors have been implicated in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism.	GRIK		hgnc.genegroup:284	
12	Vesicle associated membrane proteins	Vesicle associated membrane proteins (VAMP) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.	VAMP		hgnc.genegroup:1124	
1200	Glutamate ionotropic receptor AMPA type subunits		GRIA		hgnc.genegroup:284	
1201	Glutamate ionotropic receptor NMDA type subunits	The N-methyl-D-aspartate receptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and ion channel protein found in nerve cells. It is activated when glutamate and glycine (or D-serine ) bind to it, and when activated it allows positively charged ions to flow through the cell membrane.  The NMDA receptor is very important for controlling synaptic plasticity and memory function. The NMDAR is a specific type of ionotropic glutamate receptor.  The NMDA receptor is named this because the agonist molecule N -methyl-D-aspartate (NMDA) binds selectively to it, and not to other glutamate receptors.	GRIN		hgnc.genegroup:284	
1202	Glutamate ionotropic receptor delta type subunits		GRID		hgnc.genegroup:284	
1203	Sodium voltage-gated channel alpha subunits	Sodium channels are voltage-gated sodium-selective ion channels present in the membrane of most excitable cells. Sodium channels comprise of one pore-forming α subunit, which may be associated with either one or two beta subunits. Alpha-subunits consist of four homologous domains (I–IV), each containing six transmembrane segments (S1–S6) and a pore-forming loop. The positively charged fourth transmembrane segment (S4) acts as a voltage sensor and is involved in channel gating. 			hgnc.genegroup:184	
1204	Sodium voltage-gated channel beta subunits	Sodium channels are voltage-gated sodium-selective ion channels present in the membrane of most excitable cells. Sodium channels comprise of one pore-forming alpha subunit, which may be associated with either one or two beta subunits. Auxiliary beta1, beta2, beta3 and beta4 subunits consist of a large extracellular N-terminal domain, a single transmembrane segment and a shorter cytoplasmic domain.			hgnc.genegroup:184	
1205	DASH family				so:0005855	
1208	ATPase Na+/K+ transporting subunits		ATP1		hgnc.genegroup:414	
1209	ATPases Ca2+ transporting		ATP2		hgnc.genegroup:414	
1210	ATPase phospholipid transporting				hgnc.genegroup:414	
1211	ATPase H+/K+ transporting				hgnc.genegroup:414	
1212	ATPase copper transporting		ATP7		hgnc.genegroup:414	
1213	ATPase orphan transporters		ATP13		hgnc.genegroup:414	
1215	Transmembrane BAX inhibitor motif containing		TMBIM		so:0005855	
1216	Transcription elongation factor A like family		TCEAL		so:0005855	
1217	Brain expressed X-linked family		BEX		so:0005855	
1218	LIM domain containing	LIM domains are protein structural domains, composed of two contiguous zinc finger domains, separated by a two- amino acid residue hydrophobic linker.  They are named after their initial discovery in the proteins L in11, I sl-1 & M ec-3.  LIM-domain containing proteins have been shown to play roles in cytoskeletal organisation, organ development and oncogenesis. LIM-domains mediate protein:protein interactions that are critical to cellular processes. LIM domains have highly divergent sequences, apart from certain key residues. The sequence divergence allow a great many different binding sites to be grafted onto the same basic domain. The conserved residues are those involved in zinc binding or the hydrophobic core of the protein. The sequence signature of LIM domains is as follows: - 2-4 -- 13-19 --- 2-4 ----- 2-4 -- 13-20 -C- 2-4 -     LIM domain organisation   LIM domains frequently occur in multiples, as seen in proteins such as TES, LMO4, and can also be attached to other domains in order to confer a binding or targeting function upon them, such as LIM-kinase. The LIM superclass of genes have been classified into 14 classes: ABLIM, CRP, ENIGMA, EPLIN, LASP, LHX, LMO, LIMK, LMO7, MICAL, PXN, PINCH, TES, and ZYX. Six of these classes (i.e., ABLIM, MICAL, ENIGMA, ZYX, LHX, LM07) originated in the stem lineage of animals, and this expansion is thought to have made a major contribution to the origin of animal multicellularity.  LIM domains are also found in various bacterial lineages where they are typically fused to a metallopeptidase domain. Some versions show fusions to an inactive P-loop NTPase at their N-terminus and a single transmembrane helix. These domain fusions suggest that the prokaryotic LIM domains are likely to regulate protein processing at the cell membrane. The domain architectural syntax is remarkable parallel to those of the prokaryotic versions of the B-box zinc finger and the AN1 zinc finger domains. 			hgnc.genegroup:26	
1219	Troponin complex subunits	Troponin is a complex of three regulatory proteins ( troponin C, troponin I, and troponin T ) that is integral to muscle contraction  in skeletal muscle and cardiac muscle, but not smooth muscle. Discussions of troponin often pertain to its functional characteristics  and/or to its usefulness as a diagnostic marker  or therapeutic target  for various heart disorders in particular as a highly specific marker for myocardial infarction or heart muscle cell death.	TNN		so:0005855	
1220	PDZ domain containing	The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses  and animals.  Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. PDZ is an acronym combining the first letters of three proteins — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) — which were first discovered to share the domain.  PDZ domains have previously been referred to as DHR (Dlg homologous region)  or GLGF ( glycine - leucine -glycine- phenylalanine ) domains.  Proteins with these domains help hold together and organize signaling complexes at cellular membranes. Protein domains, connected by intrinsically disordered flexible linker regions, induce long-range allostery via protein domain dynamics.  PDZ domains also play a highly significant role in the anchoring of cell surface receptors (such as CFTR  and FZD7 ) to the actin cytoskeleton via mediators like NHERF and ezrin.  In general PDZ domains bind to a short region of the C-terminus of other specific proteins. These short regions bind to the PDZ domain by beta sheet augmentation. This means that the beta sheet in the PDZ domain is extended by the addition of a further beta strand from the tail of the binding partner protein. 	PDZ		so:0005855	
1221	H/ACA ribonucleoprotein complex		NOLA		so:0005855	
1223	Crumbs complex				so:0005855	
1224	Scribble complex				so:0005855	
1225	UTPb subcomplex				hgnc.genegroup:1484	
1226	LY6/PLAUR domain containing		LYPD		so:0005855	
1227	Phospholipase A and acyltransferase family		PLAAT		hgnc.genegroup:1692	
1229	Translocase of outer mitochondrial membrane complex		TOMM		so:0005855	
1230	BEACH domain containing 				so:0005855	
1231	Bromodomain and extra-terminal domain family				so:0005855	
1232	Bromodomain containing	A bromodomain is an approximately 110 amino acid protein domain that recognizes acetylated lysine residues, such as those on the N-terminal tails of histones. Bromodomains, as the “readers” of lysine acetylation, are responsible in transducing the signal carried by acetylated lysine residues and translating it into various normal or abnormal phenotypes.  Their affinity is higher for regions where multiple acetylation sites exist in proximity. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. The domain itself adopts an all-α protein fold, a bundle of four alpha helices each separated by loop regions of variable lengths that form a hydrophobic pocket that recognizes the acetyl lysine.  	BRD		so:0005855	
1233	MRH domain containing 				so:0005855	
1234	C3 and PZP like, alpha-2-macroglobulin domain containing		CPAMD		so:0005855	
1235	Diacylglycerol O-acyltransferase 2 family		DGAT2		so:0005855	
1236	ASAP complex				so:0005855	
1238	Exon junction complex				hgnc.genegroup:1510|hgnc.genegroup:1964	
1239	Transmembrane 9 superfamily members		TM9SF		so:0005855	
1240	Tubulin polymerization promoting proteins		TPPP		so:0005855	
1241	Arrestins		ARR		so:0005855	
1243	EMSY complex				so:0005855	
1244	USH2 complex 				so:0005855	
1246	DAN family		DAND		so:0005855	
1247	DNA ligases		LIG		so:0005855	
1248	PAR bZIP family				hgnc.genegroup:506	
1249	Proline rich and Gla domain containing		PRRG		so:0005855	
1250	Gla domain containing				so:0005855	
1252	Spectrin repeat containing nuclear envelope family		SYNE		so:0005855	
1253	Scavenger receptors	Scavenger receptors are a group of receptors that recognize modified low-density lipoprotein  (LDL) by oxidation or acetylation. This naming is based on a function of cleaning (scavenging): Scavenger receptors widely recognize and take up macromolecules that have a negative charge, like modified LDL.	SCAR		so:0005855	
1254	NF-kappa B complex subunits	NF-kappaB ( nuclear factor kappa-light-chain-enhancer of activated B cells ) is a protein complex that controls transcription of DNA, cytokine production and cell survival. NF-kappaB is found in almost all animal cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet irradiation, oxidized LDL, and bacterial or viral antigens. NF-kappaB plays a key role in regulating the immune response to infection (kappa light chains are critical components of immunoglobulins). Incorrect regulation of NF-kappaB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection, and improper immune development. NF-kappaB has also been implicated in processes of synaptic plasticity and memory.     			so:0005855	
1255	Sm spliceosomal proteins	Sm and like-Sm (LSm) proteins belong to an ancient family of RNA-binding proteins represented in all three domains of life. Members of this family form ring complexes on specific sets of target RNAs and have critical roles in their biogenesis, function and turnover. These proteins are a part of several small nucleolar ribonucleoprotein complexes (snRNPs) involved in pre-mRNA splicing.  	SNRP		hgnc.genegroup:2045|hgnc.genegroup:1503|hgnc.genegroup:1499|hgnc.genegroup:1502|hgnc.genegroup:1501|hgnc.genegroup:1521	
1256	Fos transcription factor family		FOS		hgnc.genegroup:1258	
1257	Jun transcription factor family		JUN		hgnc.genegroup:1258	
1258	AP-1 transcription factor 				so:0005855	
1259	SNAG transcriptional repressors				so:0005855	
1260	RGK type GTPase family				hgnc.genegroup:389	
1261	Zinc fingers C2H2C-type				hgnc.genegroup:26	
1263	MBT domain containing				so:0005855	
1264	Interleukin 6 type cytokine family				so:0005855	
1265	Protein phosphatase 2 modulatory subunits				so:0005855	
1266	Protein phosphatase 2 scaffold subunits		PPP2R1		so:0005855	
1267	VEGF family		VEGF		hgnc.genegroup:542	
1268	ERCC excision repair associated		ERCC		hgnc.genegroup:1269	
1269	Nucleotide excision repair				so:0005855	
1275	Signal transduction and activation of RNA metabolism family		KHDRBS		so:0005855	
1276	Transcription and export complex 2				so:0005855	
1277	BCL2 homology region 3 (BH3) only	The BH3-only subset of the Bcl-2 family of proteins contain only a single BH3-domain. The BH3-only members play a key role in promoting apoptosis. The BH3-only family members are Bim, Bid, BAD and others. Various apoptotic stimuli induce expression and/or activation of specific BH3-only family members, which translocate to the mitochondria and initiate Bax/Bak-dependent apoptosis.			hgnc.genegroup:1057	
1278	SPARC family				hgnc.genegroup:863	
1279	SIBLING family				hgnc.genegroup:2245	
1280	Super elongation complex	The super elongation complex (SEC) consists of the RNA polymerase II (Pol II) elongation factors eleven-nineteen Lys-rich leukaemia (ELL) proteins, positive transcription elongation factor b (P-TEFb) and several frequent mixed lineage leukaemia (MLL) translocation partners. It is one of the most active P-TEFb-containing complexes required for rapid transcriptional induction in the presence or absence of paused Pol II. The SEC was found to regulate the transcriptional elongation checkpoint control (TECC) stage of transcription, and misregulation of this stage is associated with cancer pathogenesis. 			so:0005855	
1281	P-TEFb complex subunits	The positive transcription elongation factor, P-TEFb, plays an essential role in the regulation of transcription by RNA polymerase II (Pol II) in eukaryotes. Immediately following initiation Pol II becomes trapped in promoter proximal paused positions on the majority of human genes. P-TEFb is a cyclin dependent kinase that can phosphorylate the DRB sensitivity inducing factor (DSIF) and negative elongation factor (NELF), as well as the carboxyl terminal domain of the large subunit of Pol II and this causes the transition into productive elongation leading to the synthesis of mRNAs. P-TEFb is regulated in part by a reversible association with the 7SK snRNP. Treatment of cells with the P-TEFb inhibitors DRB or flavopidirol leads to loss of mRNA production and ultimately cell death.			hgnc.genegroup:1280	
1282	Membrane associated progesterone receptor family				so:0005855	
1283	YEATS domain containing	The YEATS family are named after the genes first found to share this domain: 'YNK7', `ENL', `AF-9', and `TFIIF small subunit'. All these proteins are thought to have a transcription stimulatory activity.			so:0005855	
1285	NudC family		NUDC		so:0005855	
1287	I-BAR domain containing	I-BAR modules preferentially bind to membrane surfaces of a negative curvature. I-BARs are also capable of deforming membranes and inducing plasma membrane protrusions			hgnc.genegroup:1292	
1288	F-BAR domain containing 	The F-BAR domain, also known as the extended FCH domain (EFC) in PCH family proteins includes the FCH domain and CC region and is only weakly similar to the BAR domain. By sequence alignment, structural, biochemical and cell biological studies, it has been shown that the EFC is actually an extended BAR domain, and that F-BAR domains share similar properties with BAR domains. The F-BAR domain plays a role in dimerization and membrane phospholipid binding.			hgnc.genegroup:1292	
1289	N-BAR domain containing	The BAR-domain homodimer displays a crescent shape that binds to the membrane bilayer with its concave side. In addition, an N-terminal amphipathic helix is thought to insert into the membrane like a “wedge”, thereby inducing membrane buckling.			hgnc.genegroup:1292	
1290	PX-BAR domain containing	PX domain proteins bind phosphoinositides and participate in membrane remodeling and trafficking events.			hgnc.genegroup:1292	
1291	BAR-PH domain containing				hgnc.genegroup:682|hgnc.genegroup:1292	
1292	AH/BAR superfamily				so:0005855	
1293	FERM domain containing	In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin ) is a widespread protein module involved in localising proteins to the plasma membrane.  FERM domains are found in a number of cytoskeletal -associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found.  			so:0005855	
1294	SPOUT methyltransferase domain containing				hgnc.genegroup:1398	
1295	PRELI domain containing		PRELID		so:0005855	
1296	TIR domain containing				so:0005855	
1298	C-type lectin domain containing	A C-type lectin (CLEC) is a type of carbohydrate-binding protein domain known as a lectin.  The C-type designation is from their requirement for calcium for binding.  Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis.	CLEC		so:0005855	
1299	BCH domain containing 				so:0005855	
130	Aminoacyl tRNA synthetases	An aminoacyl tRNA synthetase ( aaRS ) is an enzyme that catalyzes the esterification of a specific amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In other words, aminoacyl tRNA synthetase simply attaches the appropriate, or 'cognate,' amino acid onto the corresponding tRNA. This is sometimes called 'charging' or 'loading' the tRNA with the amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide, according to the genetic code.			so:0005855	
1300	MIA family		MIA		so:0005855	
1301	Large ribosomal subunit biogenesis complex	This complex contains the mammalian homologs of the budding yeast Rix1 complex.  It links arginine methylation to desumoylation and is important for ribosomal maturation.    			hgnc.genegroup:1729	
1302	Adenosine deaminase family				so:0005855	
1303	Adenosine deaminases acting on RNA		ADA		hgnc.genegroup:1302	
1305	NuRD complex subunits	In the field of molecular biology, the Mi-2NuRD was the only known protein complex coupling chromatin remodeling ATPase and chromatin deacetylation enzymatic functions.  The NuRD complex contains seven subunits: the histone deacetylase core proteins HDAC1 and HDAC2, the histone-binding proteins RbAp46 and RbAp48, the metastasis-associated proteins MTA1 (or MTA2 / MTA3 ), the methyl-CpG-binding domain protein MBD3 (or MBD2 ) and the chromodomain-helicase-DNA-binding protein CHD3 (aka Mi-2alpha) or CHD4 (aka Mi-2beta). The histone deacetylases HDAC1 and HDAC2 and the histone binding proteins RbAp48 and RbAp46 form a core complex shared between NuRD and Sin3-histone deacetylase complexes.   Overexpression of Mbd3, a subunit of NuRD, inhibits induction of iPSCs. Depletion of Mbd3, on the other hand, improves reprogramming efficiency,   that results in deterministic and synchronized iPS cell reprogramming (near 100% efficiency within seven days from mouse and human cells).  			hgnc.genegroup:2102	
1306	SIN3 histone deacetylase complex subunits	Mammalian genomes encode two homologs of SIN3 (SIN3A/B), which associate individually with HDAC1 and HDAC2, RBBP4 and RBBP7, SDS3, and the SIN3-associated proteins SAP18 and SAP30 to form the core SIN3 complex. Different studies have identified additional interaction partners including MeCP2 (methyl-CpG-binding protein), RBP1 (RB-binding protein), BRMS1 (breast cancer metastasis suppressor), ING1/2 (inhibitor of growth), SAP25, SAP130, and SAP180, as well as the histone demethylase RBP2/KDM5A (Hayakawa and Nakayama, 2011 and Kadamb et al., 2013).			hgnc.genegroup:2102	
1309	BTG/Tob family	The mammalian BTG/Tob family gene products have anti-proliferative ability and are characterised by a conserved BTG domain. Tob subfamily members have the most extensive C-terminal regions. The BTG domain mediates interactions with the highly similar Caf1a (CNOT7) and Caf1b (CNOT8) catalytic subunits of the Ccr4-Not deadenylase complex. Overexpression of BTG/Tob proteins is associated with the inhibition of G1 to S-phase cell cycle progression and decreased cell proliferation in a variety of cell types.			so:0005855	
131	Aminoacyl tRNA synthetases, Class I				hgnc.genegroup:130	
1311	Alpha arrestins		ARRDC		hgnc.genegroup:1241	
1312	Classical arrestins		ARR		hgnc.genegroup:1241	
1313	KEOPS complex				so:0005855	
1314	Leucine zipper tumor suppressor family		LZTS		so:0005855	
1315	Pregnancy specific glycoproteins		PSG		hgnc.genegroup:1317|hgnc.genegroup:594	
1316	Nuclear exosome targeting complex	The Nuclear Exosome Targeting (NEXT) complex is a key cofactor of the mammalian nuclear exosome in the removal of Promoter Upstream Transcripts (PROMPTs) and potentially aberrant forms of other noncoding RNAs, such as snRNAs. NEXT displays preference for U-rich pyrimidine sequences and this RNA binding is mediated by the RNA recognition motif (RRM) of the RBM7 subunit.			so:0005855	
1317	Carcinoembryonic antigen family				so:0005855	
1318	Non-canonical poly(A) polymerases	Polyadenylation of mitochondrial RNAs in higher eukaryotic organisms have diverse effects on their function and metabolism. Polyadenylation completes the UAA stop codon of a majority of mitochondrial mRNAs in mammals, regulates the translation of the mRNAs, and has diverse effects on their stability.   The addition of a poly(A) tail is catalyzed by poly(A) polymerases (PAPs). Nuclear PAPs that are involved in the 3′-end processing of pre-mRNAs have been studied extensively over the years. More recently, a collection of non-canonical PAPs (ncPAPs) has been identified, which are involved in polyadenylation in other organelles (as well as in the nucleus). Some of these ncPAPs have relaxed base selectivity and can also synthesize oligo- or poly-uridylate tails, and hence are also known as poly(U) polymerases (PUPs) or terminal uridylate transferases (TUTs or TUTases).			so:0005855	
132	Aminoacyl tRNA synthetases, Class II				hgnc.genegroup:130	
1320	TTT complex	In response to DNA damage, cells activate a complex signal transduction network called the DNA damage response (DDR).  TTI1 (Tel two-interacting protein 1) and TTI2 are highly conserved regulators of the DDR in mammals, protect cells from spontaneous DNA damage and are required for the establishment of the intra-S and G2/M checkpoints.   TTI1 and TTI2 exist in multiple complexes, including a 2-MDa complex with TEL2 (telomere maintenance 2), called the Triple T complex, and phosphoinositide-3-kinase-related protein kinases (PIKKs) such as ataxia telangiectasia-mutated (ATM). The components of the TTT complex are mutually dependent on each other, and act as critical regulators of PIKK abundance and checkpoint signaling.			so:0005855	
1321	M14 carboxypeptidases	A carboxypeptidase ( EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. (Contrast with an aminopeptidase, which cleaves peptide bonds at the other end of the protein.) Humans, animals, and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation.	CP		so:0005855	
1322	MIS12 kinetochore complex	During mitosis, the spindle checkpoint senses kinetochores not properly attached to spindle microtubules and prevents precocious sister-chromatid separation and aneuploidy. The constitutive centromere-associated network (CCAN) at inner kinetochores anchors the KMN network consisting of Knl1, the Mis12 complex (Mis12C), and the Ndc80 complex (Ndc80C) at outer kinetochores.   			hgnc.genegroup:1574	
1324	STEAP family		STEAP		so:0005855	
1325	Synapsins	The synapsins are a family of proteins that have long been implicated in the regulation of neurotransmitter release at synapses. Specifically, they are thought to be involved in regulating the number of synaptic vesicles available for release via exocytosis at any one time.  Synapsins are present in invertebrates and vertebrates and are somewhat homologous across evaluated vertebrates. Current studies suggest the following hypothesis for the role of synapsin: synapsins bind synaptic vesicles to components of the cytoskeleton which prevents them from migrating to the presynaptic membrane and releasing neurotransmitter. During an action potential, synapsins are phosphorylated by PKA (cAMP dependent protein kinase), releasing the synaptic vesicles and allowing them to move to the membrane and release their neurotransmitter. Gene knockout studies in mice (where the mouse is unable to produce synapsin) have had some surprising results. Mice lacking all three synapsins are prone to seizures, and experience learning defects.  These results suggest that while synapsins are not essential for synaptic function, they do serve an important modulatory role. Conversely, studies using transgenic mice in which neuronal signaling is abolished in specific circuitries showed that synaptic activity regulates, but is not essential to maintain, the expression of these proteins. 	SYN		so:0005855	
1326	Cavins	Caveolae are specialized plasma membrane domains that form flask-shaped invaginations. They are involved in cell signalling and transport and have been shown to critically regulate metabolism and vascular permeability and blood pressure. The organization and functions of caveolae are mediated by coat proteins called caveolins (Caveolin1-3) and cavins (Cavin1-4).	CAVIN		so:0005855	
1328	BRCA1 A complex	This complex is critical for BRCA1 recruitment to the sites of DNA damage.			so:0005855	
1329	SRCAP complex	The SRCAP complex remodels chromatin by catalyzing the incorporation of H2AZ-H2B dimers into nucleosomes.  The SRCAP complex also plays a role in DSB resection and HR, hence contributing to cell survival upon exposure to DNA damage-inducing agents. 			so:0005855	
1330	casein kinase 1 family		CSNK		so:0005855	
1331	WASH complex	This is an actin-regulating complex that is recruited to endosomes by interactions with the retromer complex and plays a role in endosomal sorting.			so:0005855	
1332	MTOR complex 1	mTORC1, also known as mammalian target of rapamycin complex 1 or mechanistic target of rapamycin complex 1, is a protein complex that functions as a nutrientredox sensor and controls protein synthesis.    This complex embodies the classic functions of mTOR, namely as a nutrient/energy/redox sensor and controller of protein synthesis.   The activity of this complex is regulated by rapamycin, insulin, growth factors, phosphatidic acid, certain amino acids and their derivatives (e.g. L -leucine and β-hydroxy β-methylbutyric acid ), mechanical stimuli, and oxidative stress.     The role of mTORC1 is to activate translation of proteins. In order for cells to grow and proliferate by manufacturing more proteins, the cells must ensure that they have the resources available for protein production. Thus, for protein production, and therefore mTORC1 activation, cells must have adequate energy resources, nutrient availability, oxygen abundance, and proper growth factors in order for mRNA translation to begin. 			so:0005855	
1333	MTOR complex 2	mTOR Complex 2 ( mTORC2 ) is a protein complex that regulates cellular metabolism as well as the cytoskeleton. 			so:0005855	
1334	Shelterin complex	Shelterin (also called telosome ) is a protein complex known to protect telomeres in many eukaryotes from DNA repair mechanisms, as well as regulate telomerase activity. In mammals and other eukaryotes, telomeric DNA consists of double- and single-stranded TTAGGG repeats and a single-stranded, G-rich overhang. Subunits of shelterin bind to these regions and induce the formation of a t-loop, a cap structure that deters DNA-damage-sensing machinery from mistakenly repairing telomeres. The absence of shelterin causes telomere uncapping and thereby activates damage-signaling pathways that may lead to non-homologous end joining (NHEJ), homology directed repair (HDR),  senescence, or apoptosis. 			so:0005855	
1335	BRCA1 B complex	The BRCA1-B complex is involved in DNA replication stress-induced checkpoint and DNA interstrand crosslink (ICL) repair			so:0005855	
1336	BRCA1 C complex	 BRCA1 forms a complex with  RBBP8 and MRN (MRE11/RAD50/NBN) in a cell cycle-dependent manner during S and G2 phase of the cell cycle through the BRCT domains of BRCA1 binding to phosphorylated S327, a CDK phosphorylation site of RBBP8 in a phospho-SPxF motif. The <a href='http://www.genenames.org/cgi-bin/genefamilies/set/1344'>MRN complex</a> also has other functions not related to its role in the BRCA1 C complex.  RBBP8  is required for DNA end resection at the initial step of homologous recombination (HR) dependent DSB repair CTIP promotes DNA end resection by interacting and stimulating the nuclease activity of the MRN complex. The complex formation of BRCA1-RBBP8-MRN is important for facilitating DSB resection to generate single-stranded DNA that is needed for HR-mediated DSB repair.  			so:0005855	
1337	TIM22 complex				so:0005855	
1338	Chromosomal passenger complex				so:0005855	
1339	Checkpoint clamp complex				so:0005855	
1340	Ripoptosome				so:0005855	
1341	Apoptosome	The apoptosome is a large quaternary protein structure formed in the process of apoptosis. Its formation is triggered by the release of cytochrome c from the mitochondria in response to an internal (intrinsic) or external (extrinsic) cell death stimulus. Stimuli can vary from DNA damage and viral infection to developmental cues such as those leading to the degradation of a tadpole's tail. In mammalian cells, once cytochrome c is released, it binds to the cytosolic protein Apaf-1 to facilitate the formation of apoptosome. An early biochemical study suggests a two-to-one ratio of cytochrome c to apaf-1 for apoptosome formation. However, recent structural studies suggest the cytochrome c to apaf-1 ratio is one-to-one. It has also been shown that the nucleotide dATP as third component binds to apaf-1, however its exact role is still debated. The mammalian apoptosome had never been crystallized, but a human APAF-1/cytochrome-c apoptosome has been imaged at lower (2 nm ) resolution by cryogenic transmission electron microscopy 10 years ago,  revealing a wheel-like particle with 7-fold symmetry. Recently, a medium resolution (9.5 Ångström) structure of human apoptosome was also solved by cryo-electron microscopy, which allows unambiguous inference for positions of all the APAF-1 domains (CARD, NBARC and WD40) and cytochrome c. There is also now a crystal structure of the monomeric, inactive Apaf-1 subunit (PDB 3SFZ).   Once formed, the apoptosome can then recruit and activate the inactive pro-caspase-9. Once activated, this initiator caspase can then activate effector caspases and trigger a cascade of events leading to apoptosis.			so:0005855	
1342	Death inducing signaling complex 	The death-inducing signaling complex or DISC is a multi-protein complex formed by members of the 'death receptor' family of apoptosis -inducing cellular receptors.  A typical example is FasR, which forms the DISC upon trimerization as a result of its ligand ( FasL ) binding. The DISC is composed of the death receptor, FADD, and caspase 8. It transduces a downstream signal cascade resulting in apoptosis. The Fas ligands, or cytotoxicity-dependent APO-1-associated proteins, physically associate with APO-1 (also known as the Fas receptor, or CD95), a tumor necrosis factor containing a functional death domain. This association leads to the formation of the DISC, thereby inducing apoptosis.  The entire process is initiated when the cell registers the presence of CD95L, the cognate ligand for APO-1.  Upon binding, the CAP proteins and procaspase-8 (composed of FLICE, MACH, and Mch5) bind to CD95 through death domain and death effector domain interactions. Procaspase-8 activation is thought to occur through a dimerization process with other procaspase-8 molecules, known as an induced proximity model. The CAP proteins associate only with the oligomerized version of APO-1 when forming the complex. The CAP1 are CAP2 proteins are also known as FADD/MORT1, an adaptor molecule with a death domain. CAP4 is also called FLICE, a cysteine protease with two death effector domains.  CAP3 is the prodomain of FLICE generated during proteolytic activation.  Once the DISC assembles, it allows APO-1 signaling to occur, which triggers cell death. In order to do this, downstream targets such as FLICE must be activated. In its inactive state, FLICE's two death domains are thought to bind together and prevent its activation. Once APO-1 aggregates within the cytosol, it recruits FADD, CAP3, and FLICE to the receptor, where FLICE is modified into several active subunits, which have the ability to cleave a variety of substrates. This proteolytic activity then results in a cascade of caspase activation, and ultimately cell death. This apoptotic activity is critical for tissue homeostasis and immune function. APO-1-mediated apoptosis can be inhibited by a variety of factors, including the viral caspase inhibitors CrmA and p35, as well as viral FLICE-inhibitory proteins known as v-FLIPs. When in the presence of APO-1, v-FLIPs preferentially bind and prevent procaspase-8 from being recruited; as such, apoptosis is stalled. Interestingly, humans have a homolog for v-FLIP known as c-FLIP, which occurs in two endogenous forms (c-FLIPL (long) and c-FLIPS (short)). These are similar in structure to procaspase-8, but lack the amino acids necessary for caspase-8 catalytic activity. It is thought that c-FLIP may be involved in modulating the immune system, as c-FLIPS is upregulated upon stimulation of the T cell receptor. Furthermore, as high expression of FLIP is known to promote tumor growth, these inhibitor molecules play a role in cancer proliferation. The DISC has been implicated as a possible drug development target for various cancers, including leukemia, glioma, and colon cancer. In glioma cells, the effects of TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) have been shown to induce DISC-mediated apoptosis. Specifically, TRAIL works by activating two death receptors, DR4 and DR5; these bind to FADD, which then interacts with caspase-8 to assemble the DISC. Tumor cells show varying sensitivity to TRAIL modulated apoptosis, depending on the presence of the antiapoptotic FLIP proteins.  Additionally, studies in leukemia have indicated that the histone deacetylase inhibitor LAQ824 increases apoptosis by decreasing the expression levels of the c-FLIPs.  As such, these inhibitors are promising targets for anti-cancer therapy.			so:0005855	
1343	CST complex	The CST complex localizes specifically to single-stranded telomeric DNA, including the telomeric overhang. In yeast this complex is involved in chromosome end capping and telomere length regulation. The capping properties of CST may be dispensable in vertebrates in vivo due to the presence of the shelterin complex, which also caps chromosome ends.   There is evidence to suggest that the CST complex  rescues stalled replication forks under conditions of replication stress.  			so:0005855	
1344	MRN complex	The MRN complex (MRX complex in yeast) is a protein complex consisting of Mre11, Rad50 and Nbs1 (also known as Nibrin  in humans and as Xrs2 in yeast). In eukaryotes, the MRN/X complex plays an important role in the initial processing of double-strand DNA breaks prior to repair by homologous recombination or non-homologous end joining. The MRN complex binds avidly to double-strand breaks both in vitro and in vivo and may serve to tether broken ends prior to repair by non-homologous end joining or to initiate resection prior to repair by homologous recombination. The MRN complex also participates in activating the checkpoint kinase ATM in response to DNA damage.   Production of short single-strand oligonucleotides by Mre11 endonuclease activity has been implicated in ATM activation by the MRN complex. 			so:0005855	
1345	tRNA splicing ligase complex	tRNA maturation involves an intron splicing and an exon ligation step. The product of RTCB is the catalytic subunit of the human tRNA ligation complex. Full enzymatic activity of RTCB depends on guanylation, which is provided by the co-factor ZBTB8OS (archease) working in cooperation with DDX1. 			so:0005855	
1346	JmjC hydroxylases	The protein products of these genes catalyze the oxidation of proteins (for TYW5 a tRNA) to stable hydroxylated products. JmjC hydroxylases in general appear to have more open binding sites than the KDMs and bind their target residues primarily through main and side chain hydrogen bonds, rather than the principally hydrophobic interactions used by KDMs. 			hgnc.genegroup:1368	
1347	Polycomb repressive complex 2	The Polycomb Repressive Complex 2 (PRC2) is a key chromatin modifier involved in the maintenance of transcriptional silencing. The proteins encoded by EZH1 and EZH2 are the two paralogous enzymatic subunits of the complex and the proteins encoded by SUZ12 and EED are strictly required for their enzymatic activity. The RBBP4/7 paralogs, which are believed to contribute to nucleosome binding, are also part of other chromatin regulatory complexes.			so:0005855	
1348	Transcription and export complex 1 subunits	The TREX complex couples transcription elongation by RNA polymerase II to mRNA export, moving along the gene with the elongating polymerase during transcription. It acts as a binding platform for the protein product of NXF1 (nuclear RNA export factor 1). TREX subunits are also involved in piRNA transcription and biogenesis. The TREX complex also helps prevent R-loop formation during transcription.  			so:0005855	
135	Zinc fingers GRF-type	These genes encode proteins that contain Glycine-arginine-phenylalanine (GRF)-type zinc fingers (GRF-ZFs), 45- to 50-residue domains with a conserved GRxF motif. GRF-ZFs are widely distributed throughout eukaryotes in proteins that are involved in DNA damage response (DDR), transcriptional regulation, and RNA metabolism. GRF-ZFs are nucleic acid interaction modules and in several cases these motifs have been shown to enhance enzymatic activity.  This domain comprises a three-stranded anti-parallel β-sheet that folds into a crescent-shaped claw-like structure (5U6Z). A single bound Zn(2+) ion plays a central structural role in this domain, and is coordinated with tetrahedral geometry by a 'CHCC' sequence motif.	ZGRF		hgnc.genegroup:26	
1350	S100 fused type protein family	The S100 fused type protein (SFTP) family or fused gene family encompasses genes which are mainly expressed in stratified epithelia and play a role in epithelial homeostasis. Like S100 proteins, SFTPs contain two calcium-binding EF-hand motifs. These proteins are associated with cytoplasmic intermediate filaments as well as minor components of the CE. Due to their homologous structure they are also known as filaggrin-like proteins.			hgnc.genegroup:1354	
1352	Cornified envelope precursor family	As it name implies, the cornified envelope (CE) precursor family includes genes that encode the proteins forming the CE. The CE is a cross-linked matrix that surrounds terminally differentiated squamous keratinocytes after a process known as cornification. CE precursor proteins are cross-linked by transglutaminases. The ratio of CE precursor proteins varies from tissue to tissue. In the epidermis, the most abundant CE component is loricrin (65-70%), while involucrin is a minor component (<5%).			hgnc.genegroup:1354	
1353	Small proline rich proteins	SPRR genes encode proteins that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo and are a class of cornified envelope precursor proteins. The structure of the central segments of the encoded proteins are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus *K*PEP**. 	SPRR		hgnc.genegroup:1354	
1354	Epidermal differentiation complex	The epidermal differentiation complex ( EDC ) is a gene complex comprising over fifty genes encoding proteins involved in the terminal differentiation and cornification of keratinocytes, the primary cell type of the epidermis. In humans, the complex is located on a 1.9 Mbp stretch within chromosome 1q 21.   The proteins encoded by EDC genes are closely related in terms of function, and evolutionarily they belong to three distinct gene families : the cornified envelope precursor family, the S100 protein family and the S100 fused type protein (SFTP) family.  It has been hypothesized that the clustering of EDC genes occurred due to duplication events which were evolutionarily favored during the adaptation to terrestrial environments.   EDC proteins have been involved in a variety of skin disorders including ichthyosis vulgaris, atopic dermatitis and psoriasis. 			so:0005855	
1355	Cysteine rich secretory protein family	Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins.  They are a subgroup of the CRISP, antigen 5 and Pr-1 ( CAP ) protein superfamily and are substantially implicated in the functioning of the mammalian reproductive system.  CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels. 	CRISP		hgnc.genegroup:1356	
1356	CAP superfamily	The CAP superfamily ( cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP)) is a large superfamily of secreted proteins that are produced by a wide range of organisms, including prokaryotes and non- vertebrate eukaryotes.    Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility ; as tumour suppressor or pro- oncogenic genes in tissues including the prostate ; and in cell-cell adhesion during fertilisation.   The overall protein structural conservation within the CAP superfamily results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences.  			so:0005855	
1358	GLIPR family 		GLIPR		hgnc.genegroup:1356	
1359	Beta-gamma crystallins	In anatomy, a crystallin is a water-soluble structural protein found in the lens and the cornea of the eye accounting for the transparency of the structure.  It has also been identified in other places such as the heart, and in aggressive breast cancer tumors.   Since it has been shown that lens injury may promote nerve regeneration, crystallin has been an area of neural research. So far, it has been demonstrated that crystallin beta B2 (CRYBB2) may be a neurite -promoting factor. 	CRYB, CRYG		so:0005855	
136	Zinc fingers CXXC-type	This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to non-methylated CpG dinucleotides. The domain is characterised by two CGXCXXC repeats. The RecQ helicase has a single repeat that also binds to zinc, but this has not been included in this family. The DNA binding interface has been identified by NMR (<a href='https://pubmed.ncbi.nlm.nih.gov/9207790/'>PMID: 9207790</a>).	CXXC		hgnc.genegroup:26	
1360	Beta-gamma crystallin domain containing	The proteins encoded by these genes contain six beta-gamma crystallin like domains encoded in exons arranged like those in beta crystallin genes. The proteins encoded by these genes do not serve as crystallins.			hgnc.genegroup:1359	
1361	NineTeen complex	NTC/Prp19C was discovered as a complex that functions in splicing and more specifically during the catalytic activation of the spliceosome. More recent work revealed that NTC/Prp19C plays a role in transcription elongation in Saccharomyces cerevisiae and in genome maintenance in higher eukaryotes.			hgnc.genegroup:1510|hgnc.genegroup:1507|hgnc.genegroup:1508|hgnc.genegroup:1516	
1363	NURF complex	Nucleosome Remodeling Factor (NURF) is an ATP-dependent chromatin remodeling complex that catalyzes nucleosome sliding in order to regulate gene transcription. It contains an ISWI ATPase (SMARCA1), making it part of the ISWI family of chromatin remodeling complexes. NURF is highly conserved among eukaryotes and is involved in transcriptional regulation of developmental genes.			so:0005855	
1366	Integrator complex	The Integrator complex associates with phosphorylated RNA polymerase II (RNAPII). This complex processes the 3′ end of the U-rich small nuclear RNA (snRNA).  	INTS		so:0005855	
1368	Iron (II) and 2-oxoglutarate dependent oxygenases				so:0005855	
1369	Doublecortin superfamily		DCDC		so:0005855	
137	Zinc fingers 3CxxC-type	These genes encode proteins containing a domain with several pairs of CxxC motifs, referred to as 3CxxC-type zinc finger which is found in 3CxxC-type zinc finger proteins, such as zygote arrest protein 1 (ZAR1) and its homologues, ZAR1-like proteins, and receptor-transporting proteins 1-5 (RTP1-5). Only one pair of cysteines is associated with a highly conserved histidine residue.	Z3CXXC		hgnc.genegroup:26	
1371	STRIPAK complex				so:0005855	
1372	C1q and TNF related 		C1QTNF		hgnc.genegroup:1641	
1373	Hedgehog signaling molecule family				so:0005855	
1374	TLC domain containing	The TLC domain is also known as the TRAM/LAG1/CLN8 homology domain (IPR006634). InterPro describes the domain and family members as follows:  TLC is a protein domain with at least 5 transmembrane alpha-helices. Lag1p and Lac1p [yeast proteins] are essential for acyl-CoA-dependent ceramide synthesis [PMID: 11694577], TRAM1 is a subunit of the translocon and the CLN8 gene is mutated in Northern epilepsy syndrome. Proteins containing this domain may possess multiple functions such as lipid trafficking, metabolism, or sensing. Trh homologues [e.g. the CERS class homeobox class family in humans] possess additional homeobox domains [PMID: 9872981].			so:0005855	
1375	BRISC complex	The BRCC36 isopeptidase complex (BRISC) is a Deubiquitinating enzyme (DUB) that is specific for lysine 63-linked ubiquitin hydrolysis. The BRISC complex regulates the assembly of the mitotic spindle by deubiquitinating the essential spindle assembly factor nuclear mitotic apparatus (NuMA). 			so:0005855	
1376	MINDY deubiquitinases	MINDY family DUBs are highly selective at cleaving K48-linked polyUb, a signal that targets proteins for degradation.	MINDY		hgnc.genegroup:996	
1377	Haloacid dehalogenase like hydrolase domain containing		HDHD		so:0005855	
1378	Mitochondrially encoded ribosomal RNAs		MT-RNR		hgnc.genegroup:848|hgnc.genegroup:1975	
1379	Cytoplasmic ribosomal RNAs				hgnc.genegroup:848	
1380	5S ribosomal RNAs	The 5S ribosomal RNA (5S rRNA) is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life (bacteria, archaea, and eukaryotes), with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation velocity in an ultracentrifuge, which is measured in Svedberg units (S). 	RNA5S		hgnc.genegroup:1379	
1381	Ribosomal 45S RNA clusters	The genes encoding the rRNA components of the ribosome are organized as tandem rDNA repeating units, designated RNR1 through RNR5, in the p12 region of chromosomes 13, 14, 15, 21 and 22. Each rDNA unit encodes a 45S rRNA which serves as the precursor for an 18S, 5.8S and 28S rRNA. The number of rDNA repeating units varies between individuals and from chromosome to chromosome, although usually 30 to 40 repeats are found on each chromosome. [Note that the clusters are extremely difficult to sequence and are therefore not represented on the reference genome assembly. This is why the chromosomal location for each cluster includes the term 'not on reference assembly']	RNR		hgnc.genegroup:1379	
1382	45S pre-ribosomal RNAs	The sequences coding for ribosomal RNAs are present as rDNA repeating units, designated RNR1 through RNR5, in the p12 region of chromosomes 13, 14, 15, 21 and 22. A 45S rRNA which serves as the precursor for the 18S, 5.8S and 28S rRNA, is transcribed from each rDNA unit by RNA polymerase I. The number of rDNA repeating units varies between individuals and from chromosome to chromosome, although usually 30 to 40 repeats are found on each chromosome. [Note that the clusters are extremely difficult to sequence and are therefore not represented on the reference genome assembly. Each gene symbol below is representative of one 45S pre-ribosomal RNA repeat unit per repeat cluster]	RNA45S		hgnc.genegroup:1381	
1383	18S ribosomal RNAs	18 S ribosomal RNA (abbreviated 18S rRNA) is a part of the ribosomal RNA. The S in 18S represents Svedberg units. 18S rRNA is a component of the small eukaryotic ribosomal subunit (40S). 18S rRNA is the structural RNA for the small component of eukaryotic cytoplasmic ribosomes, and thus one of the basic components of all eukaryotic cells. It is the eukaryotic nuclear homologue of 16S ribosomal RNA in Prokaryotes and mitochondria. 	RNA18S		hgnc.genegroup:1382	
1384	5.8S ribosomal RNAs	In molecular biology the 5.8S ribosomal RNA (5.8S rRNA) is a non-coding RNA component of the large subunit of the eukaryotic ribosome and so plays an important role in protein translation. It is transcribed by RNA polymerase I as part of the 45S precursor that also contains 18S and 28S rRNA. Its function is thought to be in ribosome translocation.  It is also known to form covalent linkage to the p53 tumour suppressor protein.	RNA5-8S		hgnc.genegroup:1382	
1385	28S ribosomal RNAs	28S ribosomal RNA is the structural ribosomal RNA (rRNA) for the large component, or large subunit (LSU) of eukaryotic cytoplasmic ribosomes, and thus one of the basic components of all eukaryotic cells.  It is the eukaryotic nuclear homologue of the prokaryotic 23S and mitochondrial 16S ribosomal RNAs.	RNA28S		hgnc.genegroup:1382	
1387	Mitochondrial complex I assembly complex				hgnc.genegroup:645	
1388	Src family tyrosine kinases	Src family kinase is a family of non-receptor tyrosine kinases that includes nine members: Src, Yes, Fyn, and Fgr, forming the SrcA subfamily, Lck, Hck, Blk, and Lyn in the SrcB subfamily, and Frk in its own subfamily. Frk has homologs in invertebrates such as flies and worms, and Src homologs exist in organisms as diverse as unicellular choanoflagellates, but the SrcA and SrcB subfamilies are specific to vertebrates. Src family kinases contain six conserved domains: a N-terminal myristoylated segment, a SH2 domain, a SH3 domain, a linker region, a tyrosine kinase domain, and C-terminal tail  Src family kinases interact with many cellular cytosolic, nuclear and membrane proteins, modifying these proteins by phosphorylation of tyrosine residues. A number of substrates have been discovered for these enzymes.  Deregulation, including constitutive activation or over expression, may contribute to the progression of cellular transformation and oncogenic activity 			hgnc.genegroup:1458	
139	G protein-coupled receptors	Receptors which transduce extracellular signals across the cell membrane. At the external side they receive a ligand (a photon in the case of opsins), and at the cytosolic side they activate a guanine nucleotide-binding (G) protein. These receptors are hydrophobic proteins that cross the membrane seven times.			hgnc.genegroup:2054	
1390	Linear ubiquitin chain assembly complex 				so:0005855	
1391	RBR E3 ubiquitin ligases				so:0005855	
1392	Elongin complex	The Elongin complex is  a positive regulator of RNA polymerase II and and increases the rate of elongation by suppressing transient pausing along the DNA template. It is composed of a transcriptionally active subunit (A) and two regulatory subunits (B and C). The Elongin BC complex enhances the transcriptional activity of Elongin A.   The Elongin BC complex also acts as an adaptor connecting cullins and SOCS box proteins.  	ELO		so:0005855	
1393	KICSTOR complex				so:0005855	
1394	GATOR1 subcomplex				hgnc.genegroup:1396	
1395	GATOR2 subcomplex				hgnc.genegroup:1396	
1396	GATOR complex				so:0005855	
1397	Peptidoglycan recognition proteins		PGLYRP		so:0005855	
1398	Methyltransferase families				so:0005855	
1399	SET domain containing		SET		hgnc.genegroup:1398	
14	Wiskott-Aldrich Syndrome protein family				so:0005855	
140	G protein-coupled receptors, Class A rhodopsin-like	Rhodopsin-like receptors are a family of proteins that comprise the largest group of G protein-coupled receptors.			hgnc.genegroup:139	
1400	Seven-beta-strand methyltransferase motif containing				hgnc.genegroup:1398	
1401	R2TP complex				so:0005855	
1402	Zyxin family				hgnc.genegroup:1218	
1403	Ajuba family				hgnc.genegroup:1218	
1404	Scavenger receptor cysteine rich domain containing				so:0005855	
1405	CBM complex				so:0005855	
1406	RELT family		REL		so:0005855	
1407	Myocardin family				so:0005855	
1408	Glutamine amidotransferase class 1 domain containing		GATD		so:0005855	
1409	Retrotransposon Gag like		RTL		hgnc.genegroup:1411	
141	Olfactory receptors	Olfactory receptors expressed in the cell membranes of olfactory receptor neurons are responsible for the detection of odor molecules. Activated olfactory receptors are the initial player in a signal transduction cascade which ultimately produces a nerve impulse which is transmitted to the brain. These receptors are members of the class A rhodopsin-like family of G protein-coupled receptors (GPCRs).   The olfactory receptors form a multigene family consisting of around 800 genes in humans and 1400 genes in mice. 	OR		hgnc.genegroup:140	
1410	Ig-like cell adhesion molecule family	Immunoglobulin superfamily CAMs ( IgSF CAMs ) are a class of cell adhesion molecules.  They are either homophilic or heterophilic and bind integrins or different IgSF CAMs.			so:0005855	
1411	Gag like LTR retrotransposon derived genes				hgnc.genegroup:2296	
1412	Envelope ERV derived genes				hgnc.genegroup:2296	
1413	Glycoside hydrolase family 31				hgnc.genegroup:1650	
1414	IgCAM CXADR-related subfamily				hgnc.genegroup:1410	
1415	DNA transposon derived genes				hgnc.genegroup:1416	
1416	Transposable element derived genes				so:0005855	
1418	Heparin binding growth factor family				hgnc.genegroup:1147	
1419	m6A methyltransferase complex	N6-methyladenosine modification in mRNA influences mRNA splicing, export, localization, translation, and stability. The m6A writer complex is located in the nuclear speckle, and catalyses the transfer of methyl groups from S-adenosylmethionine (SAM) to the specific adenines on the target RNAs. METTL3 and METTL14 are the catalytic subunits in this complex.  			so:0005855	
1420	WTAP complex				so:0005855	
1421	ROCO family		ROCO		so:0005855	
1423	Endosome-associated recycling protein (EARP) complex				so:0005855	
1424	Golgi associated retrograde protein (GARP) complex				so:0005855	
1425	G protein subunits alpha	This family consists of the G protein alpha subunit, which acts as a weak GTPase. G protein classes are defined based on the sequence and function of their alpha subunits, which in mammals fall into several sub-types: G(S)alpha, G(Q)alpha, G(I)alpha, transducin and G(12)alpha; there are also fungal and plant classes of alpha subunits. The alpha subunit consists of two domains: a GTP-binding domain and a helical insertion domain ( INTERPRO ). The GTP-binding domain is homologous to Ras-like small GTPases, and includes switch regions I and II, which change conformation during activation. The switch regions are loops of alpha-helices with conformations sensitive to guanine nucleotides. The helical insertion domain is inserted into the GTP-binding domain before switch region I and is unique to heterotrimeric G proteins. This helical insertion domain functions to sequester the guanine nucleotide at the interface with the GTP-binding domain and must be displaced to enable nucleotide dissociation.	GNA		hgnc.genegroup:1431	
1426	G protein subunits alpha, group s	This family consists of the G protein alpha subunit group S (stimulatory) which transduces signals from various cell surface receptors to the cAMP-generating enzyme adenylyl cyclase. The G alpha-S subunit is encoded by GNAS, a complex imprinted gene that uses multiple promoters to generate several gene products.			hgnc.genegroup:1425	
1427	G protein subunits alpha, group q	This family consists of the G protein alpha-Q subunit, which includes both G alpha-Q and G alpha-11. G alpha-Q proteins are widely expressed, toxin-insensitive proteins that couple various receptors to the effector enzyme phospholipase C (PLC), causing the release of calcium from internal stores via calcium channel activation.			hgnc.genegroup:1425	
1428	G protein subunits alpha, group i	This family consists of the G protein alpha subunit group I (inhibitory), which includes G alpha-I, G alpha-O, G alpha-T and G alpha-Z. G alpha-I proteins were originally identified by their receptor-mediated inhibition of the cAMP-generating enzyme adenylyl cyclase.	GNAI		hgnc.genegroup:1425	
1429	G protein subunits alpha, group 12/13	This family consists of the alpha-12 group of G proteins, which includes both alpha-12 group of G proteins and alpha-13 group of G proteins. G alpha-12 and G alpha-13 are ubiquitously expressed and can induce many cellular responses, including phospholipase C-epsilon activation, phospholipase D activation, cytoskeletal change, oncogenic response, apoptosis, MAP kinase activation and Na/H-exchange activation			hgnc.genegroup:1425	
1430	G protein subunits beta	Guanine nucleotide binding proteins (G proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha, beta and gamma. This entry consists of the G protein beta subunit, which assumes a barrel-shaped beta-propeller structure containing WD-40 repeats preceded by an N-terminal alpha helix. The beta subunit forms a stable dimer with the gamma subunit. The alpha subunit only contacts the beta subunit in the dimer, lying on the opposite face from the gamma subunit.	GNB		hgnc.genegroup:1431	
1431	Heterotrimeric G proteins	'G protein' usually refers to the membrane-associated heterotrimeric G proteins, sometimes referred to as the 'large' G proteins (as opposed to the subclass of smaller, monomeric small GTPases). These proteins are activated by G protein-coupled receptors and are made up of alpha, beta and gamma subunits,  the latter two referred to as the beta-gamma complex			so:0005855	
1432	G protein subunits gamma	Guanine nucleotide binding proteins (G proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha, beta and gamma. The specific combination of subunits in heterotrimeric G proteins affects not only which receptor it can bind to, but also which downstream target is affected, providing the means to target specific physiological processes in response to specific external stimuli. G proteins carry lipid modifications on one or more of their subunits to target them to the plasma membrane and to contribute to protein interactions. This entry represents the G protein gamma subunit.	GNG		hgnc.genegroup:1431	
1436	Actin related proteins				so:0005855	
1437	M1 metallopeptidases	These genes encode zinc dependent metallopeptidases in which two of the zinc ligands are histidines in a 'HEXXH' motif. The M1 family contains exopeptidases that act at the free N-terminus of polypeptides.			hgnc.genegroup:2104	
1438	M3 metallopeptidase family	These genes encode zinc dependent metallopeptidases in which two of the zinc ligands are histidines in a 'HEXXH' motif. This family includes intracellular oligopeptidases.			so:0005855	
1439	M13 metallopeptidases	These genes encode zinc dependent metallopeptidases in which two of the zinc ligands are histidines in a 'HEXXH' motif. 			so:0005855	
1440	M16 metallopeptidases	These genes encode zinc dependent metallopeptidases in which two of the zinc ligands are histidines in a 'HXXEH' motif. 			so:0005855	
1442	M24 metallopeptidase family	The exopeptidases in this family require cocatalytic ions of cobalt or manganese. 			so:0005855	
1443	M20 metallopeptidases	These genes encode zinc dependent metallopeptidases that require cocatalytic metal ions.			so:0005855	
1444	M28 metallopeptidases	These genes encode zinc dependent metallopeptidases that require cocatalytic metal ions. This family contains both aminopeptidases and carboxypeptidases.			so:0005855	
1445	M19 metallopeptidases	These genes encode zinc dependent metallopeptidases that require cocatalytic metal ions.			so:0005855	
1446	M38 metallopeptidases				so:0005855	
1448	Hyaluronidases		HYAL		hgnc.genegroup:1650	
1449	Cleavage stimulation factor subunits	Cleavage stimulatory factor or cleavage stimulation factor (CstF or CStF) is a heterotrimeric protein, made up of the proteins CSTF1 (55 kDa ), CSTF2 (64kDa) and CSTF3 (77kDa), totalling about 200 kDa. It is involved in the cleavage of the 3' signaling region from a newly synthesized pre- messenger RNA (mRNA) molecule. CstF is recruited by cleavage and polyadenylation specificity factor (CPSF) and assembles into a protein complex on the 3' end to promote the synthesis of a functional polyadenine tail, which results in a mature mRNA molecule ready to be exported from the cell nucleus to the cytosol for translation. The amount of CstF in a cell is dependent on the phase of the cell cycle, increasing significantly during the transition from G0 phase to S phase in mouse fibroblast and human splenic B cells. 	CSTF		so:0005855	
1450	Cleavage and polyadenylation specific factor subunits	CPSF defines the specificity of pre-mRNA 3′ processing by recognizing the PAS. CPSF also plays important roles in transcription coupling, as it is recruited to the transcription initiation complex and accompanies RNAP II throughout the transcription process.			so:0005855	
1451	Kleisins				so:0005855	
1452	Condensin I subunits				hgnc.genegroup:1454	
1453	Condensin II subunits				hgnc.genegroup:1454	
1454	Condensin subunits				so:0005855	
1455	Ferritin chains	Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including algae, bacteria, higher plants, and animals. In humans, it acts as a buffer against iron deficiency and iron overload.  Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body, hence serum ferritin is used as a diagnostic test for iron-deficiency anemia.  Ferritin is a globular protein complex consisting of 24 protein subunits forming a nanocage with multiple metal–protein interactions.  It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. Ferritin that is not combined with iron is called apoferritin.			so:0005855	
1457	Tec family tyrosine kinases				hgnc.genegroup:1458	
1458	Non-receptor tyrosine kinases	Non-receptor tyrosine kinases (nRTKs) are cytoplasmic enzymes that are responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation). These enzymes regulate many cellular functions by switching on or switching off other enzymes in a cell. Unlike the receptor tyrosine kinases (RTKs), the second subgroup of tyrosine kinases, the non-receptor tyrosine kinases are cytoplasmic enzymes. Thirty-two non-receptor tyrosine kinases have been identified in human cells ( EC 2.7.10.2 ). Non-receptor tyrosine kinases regulate cell growth, proliferation, differentiation, adhesion, migration and apoptosis, and they are critical components in the regulation of the immune system.			so:0005855	
1459	Jak family tyrosine kinases		JAK		hgnc.genegroup:1458	
1460	Csk family tyrosine kinases				hgnc.genegroup:1458	
1461	Fes family tyrosine kinases				hgnc.genegroup:1458	
1463	Abl family tyrosine kinases		ABL		hgnc.genegroup:1458	
1464	Syk family tyrosine kinases				hgnc.genegroup:1458	
1466	Nucleoredoxin family		NXN		so:0005855	
1468	Glutaredoxin domain containing		GLRX		so:0005855	
1469	Microsomal glutathione S-transferases		MGST		hgnc.genegroup:1470	
147	Olfactory receptors, family 1		OR1		hgnc.genegroup:141	
1470	Glutathione S-transferases	Glutathione S -transferases ( GSTs ), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal — also known as MAPEG — proteins.    Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function.  The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions. GSTs can constitute up to 10% of cytosolic protein in some mammalian organs.   GSTs catalyse the conjugation of GSH — via a sulfhydryl group — to electrophilic centers on a wide variety of substrates in order to make the compounds more water-soluble.   This activity detoxifies endogenous compounds such as peroxidised lipids and enables the breakdown of xenobiotics. GSTs may also bind toxins and function as transport proteins, which gave rise to the early term for GSTs, ligandin.  			so:0005855	
1471	Tetraspan junctional complex superfamily				so:0005855	
1473	Clarins		CLRN		hgnc.genegroup:1471	
1474	Tetraspan vesicle membrane proteins				hgnc.genegroup:1471	
1475	Synaptogyrins		SYNGR		hgnc.genegroup:1474|hgnc.genegroup:1626	
1476	Synaptophysins		SYP		hgnc.genegroup:1474	
1477	eNoSC complex	Glucose deprivation reduces rRNA synthesis. An energy-dependent change in the NAD+/NADH ratio regulates the eNoSC complex, allowing it to couple the changing energy status with the level of rRNA transcription by regulating the epigenetic status of rRNA clusters. eNoSC promotes the restoration of energy balance and protects cells from energy deprivation-induced apoptosis. 			so:0005855	
1478	Calcium homeostasis modulators	These genes encode ion channel proteins that are regulated by membrane voltage and extracellular Ca2+ concentration. A CALHM1 channel is a hexamer of CALHM1 monomers.  CALHM genes are expressed in primate taste buds, exclusively in type II cells.	CALHM		hgnc.genegroup:1471	
1481	MSL histone acetyltransferase complex				so:0005855	
1482	NSL histone acetyltransferase complex				so:0005855	
1483	UTPa subcomplex				hgnc.genegroup:1484	
1484	SSU processome	The small subunit (SSU) processome is a large ribonucleoprotein (RNP) in eukaryotes required for the assembly of the SSU of the ribosome as well as for the maturation of the 18S rRNA. 			hgnc.genegroup:1729	
1485	U3 small nucleolar ribonucleoprotein				hgnc.genegroup:1484	
1486	MPP10 subcomplex				hgnc.genegroup:1484	
1487	CAP and C-type lectin domain containing		CLEC18		hgnc.genegroup:1356	
1489	LHFPL tetraspan proteins		LHFPL		hgnc.genegroup:1471	
149	Olfactory receptors, family 2		OR2		hgnc.genegroup:141	
1490	UTPc subcomplex				hgnc.genegroup:1484	
1491	Cilia and flagella associated		CFAP		so:0005855	
1492	Armadillo like helical domain containing		ARMH		so:0005855	
1493	Clathrin/coatomer adaptor, adaptin-like, N-terminal domain containing				hgnc.genegroup:1492	
1494	Pumilio homology domain containing		PUM		hgnc.genegroup:1492	
1495	TOG domain containing				hgnc.genegroup:1492	
1497	TSC complex				so:0005855	
1498	NTC associated proteins				so:0005855	
1499	U1 small nuclear ribonucleoprotein	The U1 snRNP complex  is involved in pre-mRNA splicing events, playing an integral part in splice-site selection and spliceosome assembly. U1 snRNP may also regulate transcript length and the directionality of transcription via competition with components of the polyadenylation machinery. 			hgnc.genegroup:1504|hgnc.genegroup:1507|hgnc.genegroup:1522	
150	Olfactory receptors, family 3		OR3		hgnc.genegroup:141	
1500	SMN complex	The SMN complex is essential for the biogenesis of spliceosomal snRNP particles, which are required for splicing of nuclear pre-mRNAs. Through its binding to specific sequences in the snRNAs, the SMN complex surveys the correct identity of the target RNAs and facilitates snRNP assembly.			so:0005855	
1501	U2 small nuclear ribonucleoprotein 	 The U2 snRNP complex  is involved in pre-mRNA splicing events. U2 snRNP plays a role in the recognition of the 3 prime splice site and the branch site in introns.			hgnc.genegroup:1504|hgnc.genegroup:1510|hgnc.genegroup:1507|hgnc.genegroup:1508|hgnc.genegroup:1516	
1502	U4/U6 small nuclear ribonucleoprotein particle	In order for U6 snRNA to enter into functional spliceosomes, it must first interact with U4 snRNA through an extensive base-pair interaction in a di-snRNP. Of the five snRNAs, U6 is the most likely to play a direct role in catalysis since it associates with the 5′ splice site of the pre-mRNA in the active core of functional spliceosomes (PMID:20659011)			hgnc.genegroup:1506	
1503	U5 small nuclear ribonucleoprotein	The U5 snRNP complex  is involved in pre-mRNA splicing events. Of the six U5 snRNP-specific proteins, three are NTPases. DDX23 and SNRNP200 are members of the DEXD/H box family and EFTUD2  is the sole GTPase identified in the spliceosome to date. The NTPases of the U5 snRNP are involved in the critical switch in which U1 is replaced by U6 at the 5 prime splice site.			hgnc.genegroup:1506|hgnc.genegroup:1520	
1504	Spliceosomal A complex	The spliceosomal A complex is an intermediate complex in the assembly of a spliceosome.  The entry of the U2 snRNP to the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1522'>E complex</a> defines the branch-point and leads to the formation of the A complex. The A complex associates with the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1506'>U4/U6.U5 tri-snRNP</a> to generate the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1507'>B complex</a>.   			hgnc.genegroup:1518	
1505	LSm proteins		LSM		hgnc.genegroup:1506	
1506	tri-snRP complex	The U4/U6.U5 triple complex is the largest intermediate subcomplex on the assembly pathway for the human spliceosome. 			hgnc.genegroup:1507	
1507	Spliceosomal B complex	The spliceosomal B complex is an intermediate complex in the assembly of a spliceosome.   The <a href='/cgi-bin/genefamilies/set/1504' target='_blank'>spliceosomal A complex</a> associates with the U4/U6.U5 tri-snRNP to generate the B complex.  The B complex remains catalytically inactive until it undergoes extensive compositional and conformational rearrangements, including the dissociation of U1 and U4, resulting in the formation of the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1508'>Bact complex</a>. This is converted into a catalytically active spliceosome  (designated B*) by the action of the RNA helicase DHX16. The B* complex catalyses the first step of splicing, generating the cleaved 5' exon and intron-3' exon lariat intermediates and forming the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1510'>C complex</a>.			hgnc.genegroup:1518	
1508	Spliceosomal Bact complex	Although all snRNPs are present in the <a href=''>B complex</a>, it is still catalytically inactive and requires major conformational and compositional rearrangements (i.e., activation) in order to become competent to facilitate the first transesterification step of splicing. During spliceosome activation U1 and U4 are destabilized or released, giving rise to the activated spliceosome (i.e., the Bact complex). Subsequently, after a structural rearrangement is catalyzed by the DExH/D-box protein Prp2, the catalytically activated spliceosome (B* complex) is formed. The B* complex catalyses the first step of splicing, generating the cleaved 5' exon and intron-3' exon lariat intermediates, and at this stage the <a href=''>spliceosomal C complex</a> is generated.  			hgnc.genegroup:1518	
151	Olfactory receptors, family 4		OR4		hgnc.genegroup:141	
1510	Spliceosomal C complex	After additional RNP rearrangements, the C complex catalyses the second step of splicing, resulting in the ligation of the 5' and 3' exons and release of the intron in the form of a lariat.			hgnc.genegroup:1518	
1511	Calcium channel auxiliary gamma subunits	Voltage-dependent calcium channels ( VDCCs ) are a group of voltage-gated ion channels found in the membrane of excitable cells ( e.g., muscle, glial cells, neurons, etc.) with a permeability to the calcium ion Ca 2+.   These channels are slightly permeable to sodium ions, so they are also called Ca 2+ -Na + channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions.  At physiologic or resting membrane potential, VDCCs are normally closed. They are activated ( i.e., opened) at depolarized membrane potentials and this is the source of the 'voltage-dependent' epithet. The concentration of calcium (Ca 2+ ions) is normally several thousand times higher outside of the cell than inside. Activation of particular VDCCs allows Ca 2+ to rush into the cell, which, depending on the cell type, results in activation of calcium-sensitive potassium channels, muscular contraction,  excitation of neurons, up-regulation of gene expression, or release of hormones or neurotransmitters. VDCCs have been immunolocalized in the zona glomerulosa of normal and hyperplastic human adrenal, as well as in aldosterone -producing adenomas (APA), and in the latter T-type VDCCs correlated with plasma aldosterone levels of patients.  Excessive activation of VDCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium activates enzymes which, at high enough levels, can degrade essential cellular structures.	CACNG		hgnc.genegroup:253|hgnc.genegroup:1471	
1512	Calcium voltage-gated channel alpha1 subunits	Voltage-dependent calcium channels ( VDCCs ) are a group of voltage-gated ion channels found in the membrane of excitable cells ( e.g., muscle, glial cells, neurons, etc.) with a permeability to the calcium ion Ca 2+.   These channels are slightly permeable to sodium ions, so they are also called Ca 2+ -Na + channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions.  At physiologic or resting membrane potential, VDCCs are normally closed. They are activated ( i.e., opened) at depolarized membrane potentials and this is the source of the 'voltage-dependent' epithet. The concentration of calcium (Ca 2+ ions) is normally several thousand times higher outside of the cell than inside. Activation of particular VDCCs allows Ca 2+ to rush into the cell, which, depending on the cell type, results in activation of calcium-sensitive potassium channels, muscular contraction,  excitation of neurons, up-regulation of gene expression, or release of hormones or neurotransmitters. VDCCs have been immunolocalized in the zona glomerulosa of normal and hyperplastic human adrenal, as well as in aldosterone -producing adenomas (APA), and in the latter T-type VDCCs correlated with plasma aldosterone levels of patients.  Excessive activation of VDCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium activates enzymes which, at high enough levels, can degrade essential cellular structures.	CACNA1		hgnc.genegroup:253	
1514	Calcium voltage-gated channel auxiliary alpha2delta subunits	Voltage-dependent calcium channels ( VDCCs ) are a group of voltage-gated ion channels found in the membrane of excitable cells ( e.g., muscle, glial cells, neurons, etc.) with a permeability to the calcium ion Ca 2+.   These channels are slightly permeable to sodium ions, so they are also called Ca 2+ -Na + channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions.  At physiologic or resting membrane potential, VDCCs are normally closed. They are activated ( i.e., opened) at depolarized membrane potentials and this is the source of the 'voltage-dependent' epithet. The concentration of calcium (Ca 2+ ions) is normally several thousand times higher outside of the cell than inside. Activation of particular VDCCs allows Ca 2+ to rush into the cell, which, depending on the cell type, results in activation of calcium-sensitive potassium channels, muscular contraction,  excitation of neurons, up-regulation of gene expression, or release of hormones or neurotransmitters. VDCCs have been immunolocalized in the zona glomerulosa of normal and hyperplastic human adrenal, as well as in aldosterone -producing adenomas (APA), and in the latter T-type VDCCs correlated with plasma aldosterone levels of patients.  Excessive activation of VDCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium activates enzymes which, at high enough levels, can degrade essential cellular structures.	CACNA2D		hgnc.genegroup:253	
1515	Calcium voltage-gated channel auxiliary beta subunits	Voltage-gated calcium channels (VGCCs), also known as voltage-dependent calcium channels (VDCCs), are a group of voltage-gated ion channels found in the membrane of excitable cells (e.g., muscle, glial cells, neurons, etc.) with a permeability to the calcium ion Ca2+. These channels are slightly permeable to sodium ions, so they are also called Ca2+-Na+ channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions. At physiologic or resting membrane potential, VGCCs are normally closed. They are activated (i.e., opened) at depolarized membrane potentials and this is the source of the 'voltage-gated' epithet. The concentration of calcium (Ca2+ ions) is normally several thousand times higher outside the cell than inside. Activation of particular VGCCs allows a Ca2+ influx into the cell, which, depending on the cell type, results in activation of calcium-sensitive potassium channels, muscular contraction, excitation of neurons, up-regulation of gene expression, or release of hormones or neurotransmitters. VGCCs have been immunolocalized in the zona glomerulosa of normal and hyperplastic human adrenal, as well as in aldosterone-producing adenomas (APA), and in the latter T-type VGCCs correlated with plasma aldosterone levels of patients. Excessive activation of VGCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium activates enzymes which, at high enough levels, can degrade essential cellular structures.	CACNB		hgnc.genegroup:253	
1516	Spliceosomal P complex	The spliceosomal P complex is a large stable splicing complex that forms after the spliceosomal <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1510'>C complex</a> but before mRNA release.  			hgnc.genegroup:1518	
1517	SF3b complex	SF3b is a multi-protein complex which recognizes the branch point adenosine of pre-mRNA as part of a larger U2 snRNP or U11/U12 di-snRNP in the dynamic spliceosome machinery.			hgnc.genegroup:1501|hgnc.genegroup:1521	
1518	Major spliceosome	A spliceosome is a large and complex molecular machine found primarily within the splicing speckles of the cell nucleus of eukaryotic cells. The spliceosome is assembled from snRNAs and protein complexes. The spliceosome removes introns from a transcribed pre-mRNA, a type of primary transcript. This process is generally referred to as splicing.			so:0005855	
152	Olfactory receptors, family 5		OR5		hgnc.genegroup:141	
1520	Minor spliceosome	U12-type introns are a minor subgroup of introns, distinct from the major or U2-type introns. U12-type introns are present in most eukaryotes but only account for less than 0.5% of all introns in any given genome. They are processed by a specific U12-dependent spliceosome, which is similar to, but distinct from, the major spliceosome. The U11, U12 and U4atac/U6atac snRNPs are functional analogs of the U1, U2 and U4/U6 snRNPs in the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1518'>major spliceosome</a>.			so:0005855	
1521	U11/U12 di-snRNP	The U11/U12 di-snRNP forms part of the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1520'>minor spliceosome complex</a>.  U11 and U12 snRNPs bind U12-type pre-mRNAs as a preformed di-snRNP complex, simultaneously recognizing the 5' splice site and branchpoint sequence. Thus, within the U12-type prespliceosome, U11/U12 components form a molecular bridge connecting both ends of the intron. 			hgnc.genegroup:1520	
1522	Spliceosomal E complex	The assembly of the spliceosome occurs in a stepwise manner.  First, U1 snRNP is bound to the 5′SS of the pre-mRNA together with various proteins generating complex E.   The SF1 encoded protein recognizes the branch point sequence (BPS) at the 3' splice site during the formation of early complex E thereby pre-bulging the BPS adenosine, thought to facilitate subsequent base-pairing of the U2 snRNA with the BPS. U2AF2 interacts with SF1 and recruits the U2 snRNP to the spliceosome.   The entry of the U2 snRNP defines the branch-point and leads to the formation of the <a href='https://www.genenames.org/cgi-bin/genefamilies/set/1504'>A complex</a>.			hgnc.genegroup:1518	
1528	Ribosomal 45S rRNA genes outside of clusters	These 45S pre-ribosomal RNA genes, and the 18S, 28S and 5.8S rRNA which may be processed from each 45S rRNA shown below, are found outside of the 13p12, 14p12, 15p12, 21p12 and 22p12 rRNA clusters that are the sites of rRNA transcription in the nucleolus. Therefore it is not certain whether these genes would be transcribed into functional rRNA molecules. To denote this, each gene symbol has the letter 'N' before its numerical identifier.			hgnc.genegroup:1379	
1529	Gasdermins		GSDM		so:0005855	
153	Olfactory receptors, family 6		OR6		hgnc.genegroup:141	
1530	VPS-C complexes	The Vps-C complexes CORVET (class C core vacuole/endosome tethering) and HOPS (homotypic fusion and protein sorting) are found on endosomes and lysosomes, where they control membrane trafficking pathways.			so:0005855	
1531	HOPS complex	The HOPS tethering complex regulates late-endosomal tethering and shares several subunits with the CORVET complex that regulates early endosomal tethering. The membrane-targeting module in HOPS binds RILP (Rab interacting lysosomal protein). VPS11 acts as a molecular switch that binds either the CORVET complex specific TGFBRAP1 or HOPS specific VPS39/RILP thereby allowing selective targeting of these tethering complexes to early- or late endosomes to time fusion events in the endo/lysosomal pathway. 	VPS		hgnc.genegroup:1530	
1532	CORVET complex	The CORVET tethering complex regulates early-endosomal tethering and shares several subunits with the HOPS complex that regulates late endosomal tethering. VPS11 acts as a molecular switch that binds either the CORVET complex specific TGFBRAP1, or HOPS specific VPS39/RILP thereby allowing selective targeting of these tethering complexes to early- or late endosomes to time fusion events in the endo/lysosomal pathway. 			hgnc.genegroup:1530	
1534	Mitochondrial RNase P complex	Metazoans have two RNase P enzymes: a nuclear RNA-based RNase P and a mitochondrial PRORP (protein-only RNase P).  Human mitochondrial RNase P consists of three subunits and lacks an RNA component. RNase P enzymes are metal ion-dependent endonucleases: hydrolases that catalyze site-specific phosphodiester bond hydrolysis primarily within pre-tRNA.			so:0005855	
1535	B9 domain containing	The B9 domain-containing proteins are found only in organisms that form cilia and all B9 proteins are involved in ciliary functions in both C. elegans and vertebrates.			hgnc.genegroup:823	
1536	DOCK family Rho GEFs	Zizimin proteins belong to the Dock (Dedicator of Cytokinesis) superfamily of Guanine nucleotide Exchange Factor (GEF) proteins. This family of proteins plays a role in the regulation of Rho family small GTPases. Together the Rho family of small GTPases and the Dock/Zizimin proteins play a vital role in a number of cell processes including cell migration, apoptosis, cell division and cell adhesion. 	DOCK		hgnc.genegroup:823|hgnc.genegroup:1958	
1537	NT-C2 domain containing	The NT-C2 domain is found in several microfilament/actin and endocytosis related proteins.  			hgnc.genegroup:823	
1538	FASTK mitochondrial RNA binding family		FASTK		so:0005855	
1539	p120 catenin family				hgnc.genegroup:1544	
154	Olfactory receptors, family 7		OR7		hgnc.genegroup:141	
1540	Catenins				so:0005855	
1541	Plakophilins		PKP		hgnc.genegroup:1544	
1542	Beta catenins		CTNNB		hgnc.genegroup:1540	
1543	Alpha catenins		CTNNA		hgnc.genegroup:1540	
1544	Delta catenins				hgnc.genegroup:1540	
1545	MKS complex				so:0005855	
1546	NPHP complex				so:0005855	
1547	Pyruvate dehydrogenase complex		PDH		so:0005855	
1549	TCF/LEF transcription factor family	The TCF/LEF family is a group of transcription factors which bind to DNA through a high mobility group domain. They are involved in the Wnt signaling pathway, where they recruit the coactivator beta-catenin to enhancer elements of genes they target. They can also recruit members of the Groucho family of corepressors. 			so:0005855	
155	Olfactory receptors, family 8		OR8		hgnc.genegroup:141	
1552	TIM23 complex	Tim17 and Tim23 form the core of the complex onto which all other subunits assemble.  Complete translocation into the matrix is mediated by the import motor of the TIM23 complex, also referred to as PAM (presequence translocase-associated motor). mtHsp70 (encoded by HSPA1A, HSPA1B and HSPA1L,) is the central component of the import motor. Its ATP-dependent action, regulated by the J and J-like proteins DNAJC19 (aliases: Tim14/Pam18) and Tim16/Pam16 and the nucleotide exchange factor GRPEL1 (yeast ortholog Mge1), drives translocation of proteins across the inner membrane.  			so:0005855	
1555	SF3a complex		SF3A		hgnc.genegroup:1501	
1556	Retriever complex				so:0005855	
1557	CCC complex				so:0005855	
1558	WRAD complex	SET1-family enzymes are only fully active in the context of a multi-subunit complex, which includes a protein module comprised of WDR5, RbBP5, ASH2L and DPY-30 (WRAD). These proteins bind in close proximity to the catalytic SET domain of SET1-family enzymes and stimulate H3K4 methyltransferase activity. The mechanism by which WRAD promotes catalysis involves elements of allosteric control and possibly the utilization of a second H3K4 methyltransferase active site present within WRAD itself. WRAD components also engage in physical interactions that recruit SET1-family proteins to target sites on chromatin.			so:0005855	
1559	Ski2 like RNA helicases				hgnc.genegroup:500	
156	Olfactory receptors, family 9		OR9		hgnc.genegroup:141	
1561	CTLH complex	The yeast homologue of this complex (the GID complex) functions as an E3 ubiquitin ligase that targets enzymes of the gluconeogenesis pathway. While the CTLH complex E3 ubiquitin ligase activity and substrates still remain to be characterized, the high level of conservation between the complexes in yeast and mammals infers that the CTLH complex could also serve to promote the degradation of specific substrates through ubiquitination.  With the exception of ARMC8, a striking feature is the shared presence of LisH and CTLH domains amongst the complex members.			so:0005855	
1562	NSP adaptor proteins				so:0005855	
1564	WBP1/VOPP1 family				so:0005855	
1568	WIPI family		WIPI		so:0005855	
1569	Purinosome				so:0005855	
157	Olfactory receptors, family 10		OR10		hgnc.genegroup:141	
1573	NDC80 kinetochore complex 				hgnc.genegroup:1574	
1574	KMN network				so:0005855	
1575	KNL1 complex				hgnc.genegroup:1574	
1576	Constitutive centromere associated network				so:0005855	
1579	DAZ RNA binding protein family 		DAZ		so:0005855	
158	WWC family		WWC		so:0005855	
1582	Neurexins	Neurexin (NRXN) is a presynaptic protein that helps to connect neurons at the synapse. They are located mostly on the presynaptic membrane and contain a single transmembrane domain. The extracellular domain interacts with proteins in the synaptic cleft, most notably neuroligin, while the intracellular cytoplasmic portion interacts with proteins associated with exocytosis. Neurexin and neuroligin 'shake hands,' resulting in the connection between the two neurons and the production of a synapse. Neurexins mediate signaling across the synapse, and influence the properties of neural networks by synapse specificity. Neurexins were discovered as receptors for α-latrotoxin, a vertebrate-specific toxin in black widow spider venom that binds to presynaptic receptors and induces massive neurotransmitter release. In humans, alterations in genes encoding neurexins are implicated in autism and other cognitive diseases, such as Tourette syndrome and schizophrenia.  	NRXN		so:0005855	
1583	Neuroligins	Neuroligin (NLGN), a type I membrane protein, is a cell adhesion protein on the postsynaptic membrane that mediates the formation and maintenance of synapses between neurons. Neuroligins act as ligands for β-Neurexins, which are cell adhesion proteins located presynaptically. Neuroligin and β-neurexin 'shake hands,' resulting in the connection between two neurons and the production of a synapse. Neuroligins also affect the properties of neural networks by specifying synaptic functions, and they mediate signalling by recruiting and stabilizing key synaptic components. Neuroligins interact with other postsynaptic proteins to localize neurotransmitter receptors and channels in the postsynaptic density as the cell matures. Additionally, neuroligins are expressed in human peripheral tissues and have been found to play a role in angiogenesis. In humans, alterations in genes encoding neuroligins are implicated in autism and other cognitive disorders.	NRLGN		so:0005855	
1584	MYST type domain containing lysine acetyltransferases	There are five MYST histone acetyltransferases in mammals. They are defined by their MYST histone acetyltransferase catalytic domain. This domain contains an acetyl-coenzyme A binding domain and an unusual C2HC-type zinc finger. 	KAT		hgnc.genegroup:486	
1585	Neurotrophins		NTF		hgnc.genegroup:542	
1586	GDNF family ligands				hgnc.genegroup:542	
1587	Repulsive guidance molecule family	The repulsive guidance molecule (RGM) family function as co-receptors that enhance cellular responses to BMP ligands.  RGM family members are differentially expressed in a wide range of tissues, and have been suggested to have diverse biologic roles ranging from repulsive axonal guidance, neural tube closure, neuronal differentiation, cell survival, axonal regeneration after injury, immunity, inflammation, and iron homeostasis regulation.			so:0005855	
1588	PI4KA lipid kinase complex	The first step in PM phosphoinositide synthesis is the conversion of phosphatidylinositol (PI) to PI4P, the precursor of PI(4,5)P2 and PI(3,4,5)P3 This conversion is catalyzed by the PI4KIIIα complex.			so:0005855	
159	Olfactory receptors, family 11		OR11		hgnc.genegroup:141	
1596	PIK3C3 complex subunits	The Beclin1–class III phosphatidylinositol 3-kinase (PI3KC3) complex produces an autophagy-specific pool of phosphatidylinositol 3-phosphate (PI3P). Inhibition of the activity or loss of the lipid kinase components inhibits autophagy. BECN1 interacts with a number of proteins, forming multiple functionally distinct complexes, and this allows Beclin1 to respond to different signals regulating autophagy.			so:0005855	
1598	Interferon induced transmembrane protein family	Interferon inducible transmembrane proteins have diverse roles, including the control of cell proliferation, promotion of homotypic cell adhesion, protection against viral infection, promotion of bone matrix maturation and mineralisation, and mediating germ cell development.	IFITM		so:0005855	
16	Cadherins	Cadherins are calcium-dependent transmembrane proteins that generally mediate cell-cell adhesion or cell-cell recognition and are characterized by the presence of at least two consecutive extracellular cadherin-specific motifs, called cadherin repeats, with conserved calcium-binding amino acid residues.			so:0005855	
160	Olfactory receptors, family 12		OR12		hgnc.genegroup:141	
1600	Dispanins	This is a family of transmembrane proteins with a common two TM structure. 			so:0005855	
1601	Junctophilins	Junctophilins (JPHs) are members of a junctional membrane complex protein family important for the physical approximation of plasmalemmal and sarcoplasmic/endoplasmic reticulum membranes. As such, JPHs facilitate signal transduction in excitable cells between plasmalemmal voltage-gated calcium channels and intracellular calcium release channels.	JPH		so:0005855	
1602	Matrilins	Marilins mediate interactions between macromolecular components of the extracellular matrix, e.g., collagens and proteoglycans. They are composed of von Willebrand factor type A and epidermal growth factor-like domains and the subunits oligomerize via coiled-coil domains.	MATN		so:0005855	
1603	Enolases		ENO		so:0005855	
1604	BAF complex				hgnc.genegroup:2091	
1605	PBAF complex				hgnc.genegroup:2091	
1606	GBAF complex				hgnc.genegroup:2091	
1607	Myozenins		MYOZ		so:0005855	
1608	PTF1 complex				so:0005855	
1609	Myogenic regulatory family		MYF		so:0005855	
161	Ligand gated ion channels	Ligand-gated ion channels (LGICs) are a group of transmembrane ion channel proteins which open to allow ions such as Na +, K +, Ca 2+, or Cl - to pass through the membrane in response to the binding of a chemical messenger (i.e. a ligand ),  such as a neurotransmitter. These proteins are typically composed of at least two different domains: a transmembrane domain which includes the ion pore, and an extracellular domain which includes the ligand binding location (an allosteric binding site). This modularity has enabled a 'divide and conquer' approach to finding the structure of the proteins (crystallising each domain separately). The function of such receptors located at synapses is to convert the chemical signal of presynaptically released neurotransmitter directly and very quickly into a postsynaptic electrical signal. Many LGICs are additionally modulated by allosteric ligands, by channel blockers, ions, or the membrane potential. LGICs are classified into three superfamilies which lack evolutionary relationship: Cys-loop receptors, Ionotropic glutamate receptors and ATP-gated channels. 			hgnc.genegroup:294	
1610	Ciliogenesis and planar polarity effector complex subunits	The CPLANE multiprotein complex is essential for the assembly of IFT-A particles and intraflagellar transport. 	CPLANE		so:0005855	
1613	Metallo-beta-lactamase fold containing family	The metallo-β-lactamase (MBL) superfamily constitutes a group of proteins found in all domains of life that share a characteristic αββα fold with the ability to bind transition metal ions. Such metal binding sites may have divalent transition metal ions like Zn(II), Fe(II)/Fe(III) and Mn(II), and are located at the bottom of a wide cleft able to accommodate diverse substrates. The name was adopted after the first members of the superfamily to be studied experimentally: a group of zinc-dependent hydrolytic enzymes conferring bacterial resistance to β-lactam antibiotics.   Proteins belonging to the MBL superfamily usually combine at least one MBL domain with additional domains that provide different functions, such as substrate recognition or binding to other polypeptides, in a modular fashion. Thus, MBL superfamily members grasp the metal-assisted water-activation ability of the MBL domain in order to perform a wide variety of hydrolytic reactions. 			so:0005855	
1614	MBL domain containing glyoxalase 2 subfamily				hgnc.genegroup:1613	
1615	MBL fold containing DNA/RNA interacting subfamily				hgnc.genegroup:1613	
1616	Mitochondrial contact site and cristae organizing system subunits		MICOS		hgnc.genegroup:1683	
1617	LIMK/TESK kinase family	LIM-kinases and related TESKs specifically phosphorylate cofilin at Ser-3 and thereby inhibit the actin binding, severing, and depolymerizing activities of cofilin.			so:0005855	
1619	Terminal nucleotidyltransferases		TENT		so:0005855	
162	Olfactory receptors, family 13		OR13		hgnc.genegroup:141	
1620	Albuminoid family				so:0005855	
1622	divergent protein kinase domain family		DIPK		so:0005855	
1623	RAB11 binding domain containing		RAB11FIP		so:0005855	
1624	Small NF90 (ILF3) associated RNAs		SNAR		hgnc.genegroup:475	
1625	AGC family kinases				so:0005855	
1626	MARVEL domain containing				so:0005855	
1627	Axonemal dynein assembly factors	This comprises a group of genes encoding cytoplasmic factors that are involved in axonemal dynein pre-assembly.	DNAAF		so:0005855	
1629	Neuregulins		NRG		so:0005855	
163	Olfactory receptors, family 14		OR14		hgnc.genegroup:141	
1630	Calmodulin dependent protein kinases		CAMK		so:0005855	
1631	OOSP family		OOSP		so:0005855	
1632	My-T-BRC complex				so:0005855	
1633	Chromatin accessibility complex				so:0005855	
1634	Tip60/Nua4 histone acetyltransferase complex subunits				so:0005855	
1636	Granule associated serine proteases of immune defence				so:0005855	
1637	Golgi associated kinase family		GASK		so:0005855	
1638	Complement system activation components				hgnc.genegroup:492	
1639	Complement system regulators and receptors				hgnc.genegroup:492	
164	Olfactory receptors, family 51		OR51		hgnc.genegroup:141	
1641	C1q domain containing				so:0005855	
1642	Hexosaminidases		HEX		hgnc.genegroup:1650	
1643	TNK family tyrosine kinases				hgnc.genegroup:1458	
1644	PTK2 family tyrosine kinases				hgnc.genegroup:1458	
1645	PTK6 family tyrosine kinases				hgnc.genegroup:1458	
1646	Early B-cell factors		EBF		so:0005855	
1647	Clathrin subunits	Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by Barbara Pearse in 1976. It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle. This is how clathrin gets its name, from the Latin clathratus meaning like a lattice. Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation. The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection.			so:0005855	
1648	Amylases alpha	α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi.	AMY		hgnc.genegroup:1650	
1649	Neuraminidases	Neuraminidase enzymes are glycoside hydrolase enzymes that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologues are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologues have been described  in the human genome (see NEU1, NEU2, NEU3, NEU4).	NEU		hgnc.genegroup:1650	
165	Olfactory receptors, family 52		OR52		hgnc.genegroup:141	
1650	Glycoside hydrolase family	Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms  (e.g.,  viral neuraminidases) and in normal cellular function  (e.g.,  trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.			so:0005855	
1651	Heparanases		HPSE		hgnc.genegroup:1650	
1652	Glycoside hydrolase family 1				hgnc.genegroup:1650	
1653	Alpha-L-fucosidases		FUCA		hgnc.genegroup:1650	
1654	Galactosidases beta		GLB		hgnc.genegroup:1650	
1655	Galactosidases alpha		GLA		hgnc.genegroup:1650	
1656	Shieldin complex		SHLD		so:0005855	
1657	Family with sequence similarity 230		FAM230		so:0005855	
1658	INHAT complex				so:0005855	
1659	SET complex				so:0005855	
166	Olfactory receptors, family 55		OR55		hgnc.genegroup:141	
1660	Cysteine rich transmembrane BMP regulators		CRIM		so:0005855	
1661	Chordin family		CHRD		so:0005855	
1662	Inhibin subunits		INH		hgnc.genegroup:1932	
1663	Glutamyl-tRNA amidotransferase subunits				so:0005855	
1664	Transforming growth factor beta family		TGFB		hgnc.genegroup:1932	
1665	Pseudouridine synthases				so:0005855	
1666	Oxoglutarate dehydrogenase family		OGDH		so:0005855	
1667	Flavin containing monooxygenases		FMO		so:0005855	
1668	Myosin light chain kinase family		MYLK		so:0005855	
1669	Basigin family 				hgnc.genegroup:594	
167	Olfactory receptors, family 56		OR56		hgnc.genegroup:141	
1670	Adaptor related protein complexes		AP		hgnc.genegroup:1961	
1671	Adaptor related protein complex 1		AP1		hgnc.genegroup:1670	
1672	Adaptor related protein complex 2		AP2		hgnc.genegroup:1670	
1673	Adaptor related protein complex 3		AP3		hgnc.genegroup:1670	
1674	Adaptor related protein complex 4		AP4		hgnc.genegroup:1670	
1675	Adaptor related protein complex 5		AP5		hgnc.genegroup:1670	
1676	7SK snRNP complex	In molecular biology 7SK is an abundant small nuclear RNA found in metazoans.   It plays a role in regulating transcription by controlling the positive transcription elongation factor P-TEFb. 7SK is found in a small nuclear ribonucleoprotein complex (snRNP) with a number of other proteins that regulate the stability and function of the complex.			hgnc.genegroup:1281	
1677	Wnt enhanceosome complex	The nuclear endpoint of the Wnt/β-catenin signalling cascade is marked by the Wnt enhanceosome, a multiprotein complex. The Wnt enhanceosome enables β-catenin to gain access to target genes, to relieve their transcriptional repression by members of the TLE family.			so:0005855	
1679	EMAP like		EML		so:0005855	
168	Amine receptors	Biogenic amine receptor are a variety of neurotransmitter receptors that are sensitive to biogenic amine neurotransmitters. They belong to the G protein-coupled receptor (GPCR) family of transmembrane receptors, specifically within GPCR 'Family A' ( Rhodopsin -like receptors).			hgnc.genegroup:140	
1680	TLE family		TLE		so:0005855	
1681	Cytoplasmic transfer RNA pseudogenes				hgnc.genegroup:842	
1682	Metaxins		MTX		hgnc.genegroup:1685	
1683	Mitochondrial intermembrane space bridging complex 	Mitochondrial inner membrane folds into cristae, which significantly increase its surface and are important for mitochondrial function. The stability of cristae depends on the mitochondrial contact site (MICOS) complex. In human mitochondria, the inner membrane MICOS complex interacts with the outer membrane sorting and assembly machinery (SAM) complex, to form the mitochondrial intermembrane space bridging complex (MIB).			so:0005855	
1684	Subcortical maternal complex				so:0005855	
1685	Mitochondrial sorting and assembly machinery complex	The SAM complex is an evolutionary conserved machinery, involved in the sorting and assembly of β-barrel proteins into the outer mitochondrial membrane.			hgnc.genegroup:1683	
1687	Endoribonucleases				so:0005855	
1688	MicroRNA non-coding host genes	Long non-coding RNA genes that contain a microRNA gene in either an intron or an exon on the same strand are assigned the format [microRNA gene symbol]HG e.g. MIR22HG for ‘MIR22 host gene’. 	MIR#HG		hgnc.genegroup:1690|hgnc.genegroup:788	
1689	Notch receptors	The Notch signaling pathway is a highly conserved cell signaling system present in most multicellular organisms. Mammals possess four different notch receptors, referred to as NOTCH1, NOTCH2, NOTCH3, and NOTCH4. The notch receptor is a single-pass transmembrane receptor protein. It is a hetero-oligomer composed of a large extracellular portion, which associates in a calcium-dependent, non-covalent interaction with a smaller piece of the notch protein composed of a short extracellular region, a single transmembrane-pass, and a small intracellular region.Notch signaling promotes proliferative signaling during neurogenesis, and its activity is inhibited by Numb to promote neural differentiation. It plays a major role in the regulation of embryonic development.	NOTCH		hgnc.genegroup:403	
169	Adrenoceptors	The adrenergic receptors (or adrenoceptors ) are a class of G protein-coupled receptors that are targets of the catecholamines, especially norepinephrine (noradrenaline) and epinephrine (adrenaline). Many cells possess these receptors, and the binding of a catecholamine to the receptor will generally stimulate the sympathetic nervous system. The sympathetic nervous system is responsible for the fight-or-flight response, which includes widening the pupils of the eye, mobilizing energy, and diverting blood flow from non-essential organs to skeletal muscle.	ADR		hgnc.genegroup:168	
1690	MicroRNA host genes	In the human genome over half of microRNA genes are hosted by other genes, either in the introns, or to a lesser extent, the exons. Such microRNA host genes can be either protein-coding or non-coding.			so:0005855	
1691	MicroRNA protein coding host genes	These protein coding genes host microRNA genes in their introns or exons.			hgnc.genegroup:1690	
1692	LRAT domain containing 				so:0005855	
1693	Macro domain containing				so:0005855	
1695	SWC tripartite complex				so:0005855	
1696	MicroRNA MIR1/206 family				hgnc.genegroup:476	
1697	MicroRNA MIRLET7 family				hgnc.genegroup:476	
1698	MicroRNA MIR9 family				hgnc.genegroup:476	
1699	Deoxyribonucleoside kinases				so:0005855	
170	5-hydroxytryptamine receptors, G protein-coupled		HTR		hgnc.genegroup:168|hgnc.genegroup:171	
1700	MicroRNA MIR10/100 family	The miR-10 microRNA precursor is a short non-coding RNA gene involved in gene regulation.  It is part of an RNA gene family which contains miR-10, miR-51, miR-57, miR-99 and miR-100.  miR-10, miR-99 and miR-100 have now been predicted or experimentally confirmed in a wide range of species.			hgnc.genegroup:476	
1701	MicroRNA MIR29 family				hgnc.genegroup:476	
1702	MicroRNA MIR34/449 family				hgnc.genegroup:476	
1703	MicroRNA MIR17 family				hgnc.genegroup:476	
1704	MicroRNA MIR19 family				hgnc.genegroup:476	
1705	MicroRNA MIR25/92 family				hgnc.genegroup:476	
1706	MicroRNA MIR124 family		MIR124		hgnc.genegroup:476	
1708	MicroRNA MIR133 family	mir-133 is a type of non-coding RNA called a microRNA that was first experimentally characterised in mice. Homologues have since been discovered in several other species including invertebrates such as the fruitfly Drosophila melanogaster. Each species often encodes multiple microRNAs with identical or similar mature sequence.  For example, in the human genome there are three known miR-133 genes: miR-133a-1, miR-133a-2 and miR-133b found on chromosomes 18, 20 and 6 respectively. The mature sequence is excised from the 3' arm of the hairpin. miR-133 is expressed in muscle tissue and appears to repress the expression of non-muscle genes.	MIR133		hgnc.genegroup:476	
1709	MicroRNA MIR141/200 family	The miR-8 microRNA precursor (homologous to miR-141, miR-200, miR-236), is a short non-coding RNA gene involved in gene regulation. miR-8 in Drosophila melanogaster is expressed from the 3' arm of related precursor hairpins (represented here), along with miR-200, miR-236, miR-429 and human and mouse homolog miR-141. Members of this precursor family have now been predicted or experimentally confirmed in a wide range of species. The bounds of the precursors are predicted based on conservation and base pairing and are not generally known. The miR-200 family is highly conserved in bilaterian animals, with miR-8 as the sole homolog in Drosophila. This species has accordingly been used heavily in work looking to uncover the biological function of the miR-200 family. miR-8 has been observed at all developmental stages of the embryo, and is present in cultured S2 cells of D. melanogaster.  Its expression has been seen to be strongly upregulated in larvae and this expression then sustained through to adulthood.			hgnc.genegroup:476	
171	5-hydroxytryptamine receptors	The serotonin receptors, also known as 5-hydroxytryptamine receptors or 5-HT receptors, are a group of G protein-coupled receptors ( GPCRs ) and ligand-gated ion channels ( LGICs ) found in the central and peripheral nervous systems.  They mediate both excitatory and inhibitory neurotransmission. The serotonin receptors are activated by the neurotransmitter serotonin, which acts as their natural ligand. The serotonin receptors modulate the release of many neurotransmitters, including glutamate, GABA, dopamine, epinephrine / norepinephrine, and acetylcholine, as well as many hormones, including oxytocin, prolactin, vasopressin, cortisol, corticotropin, and substance P, among others. The serotonin receptors influence various biological and neurological processes such as aggression, anxiety, appetite, cognition, learning, memory, mood, nausea, sleep, and thermoregulation. The serotonin receptors are the target of a variety of pharmaceutical drugs, including many antidepressants, antipsychotics, anorectics, antiemetics, gastroprokinetic agents, antimigraine agents, hallucinogens, and entactogens. The serotonin receptors are known to regulate longevity  and behavioral aging  in the nematode, Caenorhabditis elegans.	HTR		so:0005855	
1710	MicroRNA MIR219 family	In molecular biology, the microRNA miR-219 was predicted in vertebrates by conservation between human, mouse and pufferfish and cloned in pufferfish.  It was later predicted and confirmed experimentally in Drosophila. Homologs of miR-219 have since been predicted or experimentally confirmed in a wide range of species, including the platyhelminth Schmidtea mediterranea, several arthropod species and a wide range of vertebrates (MIPF0000044).  The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known.  In this case, the mature sequence is excised from the 5' arm of the hairpin. miR-219 has also been linked with NMDA receptor signalling in humans by targeting CaMKIIγ (a kind of protein kinase dependent to calcium and calmodulin) expression. And it has been suggested that deregulation of this miRNA can lead to the expression of mental disorders such as schizophrenia. miR-219 can also regulate Recent findings show that miR-219 is linked with Tau toxicity, suggesting that miR-219 is involved in neurodegenerative disease, such as Alzheimer's disease, Parkinson's disease etc.	MIR219		hgnc.genegroup:476	
1711	MicroRNA MIR23 family				hgnc.genegroup:476	
1712	MicroRNA MIR128 family		MIR128		hgnc.genegroup:476	
1713	MicroRNA MIR130 family	In molecular biology, miR-130 microRNA precursor is a small non-coding RNA that regulates gene expression. This microRNA has been identified in mouse (MI0000156, MI0000408), and in human (MI0000448, MI0000748). miR-130 appears to be vertebrate-specific miRNA and has now been predicted or experimentally confirmed in a range of vertebrate species (MIPF0000034). Mature microRNAs are processed from the precursor stem-loop by the Dicer enzyme. In this case, the mature sequence is excised from the 3' arm of the hairpin. It has been found that miR-130 is upregulated in a type of cancer called hepatocellular carcinoma. It has been shown that miR-130a is expressed in the hematopoietic stem/progenitor cell compartment but not in mature blood cells.			hgnc.genegroup:476	
1714	MicroRNA MIR132/212 family				hgnc.genegroup:476	
1716	MicroRNA MIR146 family	miR-146 is a family of microRNA precursors found in mammals, including humans. The ~22 nucleotide mature miRNA sequence is excised from the precursor hairpin by the enzyme Dicer. This sequence then associates with RISC which effects RNA interference.miR-146 is primarily involved in the regulation of inflammation and other process that function in the innate immune system. Loss of functional miR-146 (and mir-145) could predispose an individual to suffer from chromosome 5q deletion syndrome. miR-146 has also been reported to be highly upregulated in osteoarthritis cartilage, and could be involved in its pathogenesis. mir-146 expression is associated with survival in triple negative breast cancer.	MIR146		hgnc.genegroup:476	
1717	MicroRNA MIR148/152 family	In molecular biology, miR-148 is a microRNA whose expression has been demonstrated in human (MI0000253), mouse (MI0000550), rat (MI0000616) and zebrafish (MI0002015).  miR-148 has also been predicted in chicken (MI0001189). These predicted hairpin precursor sequence are related to those of miR-152, which has been expressed in mouse (MI0000174) and is predicted in human (MI0000462).The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known.  In this case, the mature sequence is excised from the 3' arm of the hairpin.			hgnc.genegroup:476	
1718	MicroRNA MIR181 family	In molecular biology miR-181 microRNA precursor is a small non-coding RNA molecule. MicroRNAs (miRNAs) are transcribed as ~70 nucleotide precursors and subsequently processed by the RNase-III type enzyme Dicer to give a ~22 nucleotide mature product. In this case the mature sequence comes from the 5' arm of the precursor. They target and modulate protein expression by inhibiting translation and / or inducing degradation of target messenger RNAs. This new class of genes has recently been shown to play a central role in malignant transformation. miRNA are downregulated in many tumors and thus appear to function as tumor suppressor genes. The mature products miR-181a, miR-181b, miR-181c or miR-181d are thought to have regulatory roles at posttranscriptional level, through complementarity to target mRNAs. miR-181 which has been predicted or experimentally confirmed in a wide number of vertebrate species  as rat, zebrafish, and in the pufferfish (see below) (MIPF0000007).	MIR181		hgnc.genegroup:476	
1719	MicroRNA MIR192/215 family	The miR-192 microRNA precursor (homologous to miR-215), is a short non-coding RNA gene involved in gene regulation. miR-192 and miR-215 have now been predicted or experimentally confirmed in mouse and human.microRNAs are transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a ~22 nucleotide product.  In this case the mature sequence comes from the 5' arm of the precursor.  The mature products are thought to have regulatory roles through complementarity to mRNA.mir-192 and mir-215 are thought to be positive regulators of p53, a human tumour suppressor. They are also overexpressed in gastric cancer, and could be used as biomarkers or therapeutic targets. It has also been suggested that mir-192 could be used as a biomarker for drug-induced liver damage.			hgnc.genegroup:476	
172	5-hydroxytryptamine receptors, ionotropic 		HTR3		hgnc.genegroup:171|hgnc.genegroup:161	
1720	MicroRNA MIR194 family	In molecular biology, miR-194 microRNA precursor is a small non-coding RNA gene that regulated gene expression. Its expression has been verified in mouse (MI0000236, MI0000733) and in human (MI0000488, MI0000732). mir-194 appears to be a vertebrate-specific miRNA and has now been predicted or experimentally confirmed in a range of vertebrate species (MIPF0000055). The mature microRNA is processed from the longer hairpin precursor by the Dicer enzyme. In this case, the mature sequence is excised from the 5' arm of the hairpin.	MIR194		hgnc.genegroup:476	
1721	MicroRNA MIR196 family	miR-196 is a non-coding RNA called a microRNA that has been shown to be expressed in human (MI0000238, MI0000279) and mouse (MI0000552, MI0000553).  miR-196 appears to be a vertebrate specific microRNA and has now been predicted or experimentally confirmed in a wide range of vertebrate species (MIPF0000031). In many species the miRNA appears to be expressed from intergenic regions in HOX gene clusters. The hairpin precursors are predicted based on base pairing and cross-species conservation—their extents are not known.  In this case the mature sequence is excised from the 5' arm of the hairpin. It has been suggested that a rare SNP (rs11614913) that overlaps has-mir-196a2 has been found to be associated with non-small cell lung carcinoma.	MIR196		hgnc.genegroup:476	
1722	MicroRNA MIR199 family	The miR-199 microRNA precursor is a short non-coding RNA gene involved in gene regulation. miR-199 genes have now been predicted or experimentally confirmed in mouse, human and a further 21 other species. microRNAs are transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a ~22 nucleotide product. The mature products are thought to have regulatory roles through complementarity to mRNA.	MIR199		hgnc.genegroup:476	
1723	MicroRNA MIR203 family	In molecular biology miR-203 is a short non-coding RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms, such as translational repression and Argonaute-catalyzed messenger RNA cleavage. miR-203 has been identified as a skin-specific microRNA, and it forms an expression gradient that defines the boundary between proliferative epidermal basal progenitors and terminally differentiating suprabasal cells. It has also been found upregulated in psoriasis and differentially expressed in some types of cancer.	MIR203		hgnc.genegroup:476	
1724	MicroRNA MIR204/211 family				hgnc.genegroup:476	
1725	MicroRNA MIR208 family		MIR208		hgnc.genegroup:476	
1726	MicroRNA MIR218 family	miR-218 microRNA precursor is a small non-coding RNA that regulates gene expression by antisense binding. miR-218 appears to be a vertebrate specific microRNA and has now been predicted and experimentally confirmed in a wide range of vertebrate species. The extents of the hairpin precursors are not known.  In this case the mature sequence in excised from the 5'arm of the hairpin. miR-218 is specifically expressed by mammalian motor neurons during embryonic development into adulthood, and motor neurons lacking expression of miR-218  exhibit hyperexcitability, neuromuscular junction failure, and neurodegeneration, as demonstrated by knockout mouse models.The involvement of miR-218 in cancer has also been investigated. miR-218, along with miR-585, has been found to be silenced by DNA methylation in oral squamous cell carcinoma. It is also downregulated in Nasopharyngeal carcinoma, with artificially-induced expression serving to slow tumour growth. miR-218 has also been found to have tumour suppressing qualities in bladder cancer cells. miR-218 expression was associated with overall survival in breast cancer datasets.	MIR218		hgnc.genegroup:476	
1727	MicroRNA MIR451 family		MIR451		hgnc.genegroup:476	
1729	Ribosomal biogenesis factors				so:0005855	
173	Cholinergic receptors nicotinic subunits	Nicotinic acetylcholine receptors, or nAChRs, are cholinergic receptors that form ligand-gated ion channels in the plasma membranes of certain neurons and on the presynaptic and postsynaptic sides of the neuromuscular junction. As ionotropic receptors, nAChRs are directly linked to ion channels and do not use second messengers (as metabotropic receptors do). Nicotinic acetylcholine receptors are the best-studied of the ionotropic receptors.  Like the other type of acetylcholine receptor - muscarinic acetylcholine receptor (mAChR) - nAChR is triggered by the binding of the neurotransmitter acetylcholine (ACh). Just as muscarinic receptors are named such because they are also activated by muscarine, nicotinic receptors can be opened not only by acetylcholine but also by nicotine —hence the name 'nicotinic.'   In insects, the cholinergic system is limited to the central nervous system. In contrast, neuronal receptors are found in both the central nervous system and the peripheral nervous system of mammals. Mammalian neuromuscular receptors are found in the neuromuscular junctions of somatic muscles ; stimulation of these receptors causes muscular contraction.	CHRN		hgnc.genegroup:175|hgnc.genegroup:161	
1732	PeBoW complex	The PeBoW complex is essential for cell proliferation and maturation of the large ribosomal subunit in mammalian cells.			hgnc.genegroup:1301	
1733	Dehydrodolichyl diphosphate synthase 				so:0005855	
1734	Stomatin family		STOM		so:0005855	
1736	MicroRNA MIR7 family		MIR7		hgnc.genegroup:476	
1737	MicroRNA MIR15/16 family				hgnc.genegroup:476	
1738	MicroRNA MIR24 family	The miR-24 microRNA precursor is a small non-coding RNA molecule that regulates gene expression.  microRNAs are transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a mature ~22 nucleotide product.  In this case the mature sequence comes from the 3' arm of the precursor. The mature products are thought to have regulatory roles through complementarity to mRNA. miR-24 is conserved in various species, and is clustered with miR-23 and miR-27, on human chromosome 9  and 19. Recently, miR-24 has been shown to suppress expression of two crucial cell cycle control genes, E2F2 and Myc in hematopoietic differentiation and also to promote keratinocyte differentiation by repressing actin-cytoskeleton regulators PAK4, Tsk5 and ArhGAP19.	MIR24		hgnc.genegroup:476	
1739	MicroRNA MIR26 family	The miR-26 microRNA is a small non-coding RNA that is involved in regulating gene expression. The miR-26 family is composed of miR-26a-1, miR-26a-2 and miR-26b located in chromosomes 3, 12 and 2, respectively. Pre-miR-26 with stem-loop structure is processed into mature miR-26 by a series of enzymes of intranuclear and intracytoplasm. The mature miRNA of miR-26a-1 and miR-26a-2 possesses the same sequence, with the exception of 2 different nucleotides in mature miR-26b. miR-26 appears to be a vertebrate specific microRNA and has now been predicted or experimentally validated in many vertebrate species (MIPF0000043). 	MIR26		hgnc.genegroup:476	
1740	MicroRNA MIR27 family		MIR27		hgnc.genegroup:476	
1741	MicroRNA MIR30 family	miR-30 microRNA precursor is a small non-coding RNA that regulates gene expression. Animal microRNAs are transcribed as pri-miRNA (primary miRNA) of varying length which in turns are processed in the nucleus by Drosha into ~70 nucleotide stem-loop precursor called pre-miRNA (precursor miRNA) and subsequently processed by the Dicer enzyme to give a mature ~22 nucleotide product. In this case the mature sequence comes from both the 3' (miR-30) and 5' (mir-97-6) arms of the precursor. The products are thought to have regulatory roles through complementarity to mRNA.A screen of 17 miRNAs that have been predicted to regulate a number of breast cancer associated genes found variations in the microRNAs. miR-17 and miR-30c-1, these patients were noncarriers of BRCA1 or BRCA2 mutations, lending the possibility that familial breast cancer may be caused by variation in these miRNAs.Members of the miR-30 family have been found to be highly expressed in heart cells.	MIR30		hgnc.genegroup:476	
1742	MicroRNA MIR33 family	miR-33 is a family of microRNA precursors, which are processed by the Dicer enzyme to give mature microRNAs. miR-33 is found in several animal species, including humans. In some species there is a single member of this family which gives the mature product mir-33. In humans there are two members of this family called mir-33a and mir-33b, which are located in intronic regions within two protein-coding genes for Sterol regulatory element-binding proteins (SREBP-2 and SREBP-1) respectively.	MIR33		hgnc.genegroup:476	
1743	Interferon regulatory factors 		IRF		so:0005855	
1744	CDK activating kinase complex				hgnc.genegroup:1745	
1745	General transcription factor IIH complex subunits	Transcription factor II Human (Transcription Factor II H; TFIIH) is an important protein complex, having roles in transcription of various protein-coding genes and DNA nucleotide excision repair (NER) pathways. TFIIH first came to light in 1989 when general transcription factor-δ or basic transcription factor 2 was characterized as an indispensable transcription factor in vitro. This factor was also isolated from yeast and finally named as TFIIH in 1992.TFIIH consists of ten subunits, 7 of which (ERCC2/XPD, ERCC3/XPB, GTF2H1/p62, GTF2H4/p52, GTF2H2/p44, GTF2H3/p34 and GTF2H5/TTDA) form the core complex. The cyclin activating kinase-subcomplex (CDK7, MAT1, and cyclin H) is linked to the core via the XPD protein  Two of the subunits, ERCC2/XPD and ERCC3/XPB, have helicase and ATPase activities and help create the transcription bubble.  In a test tube these subunits are only required for transcription if the DNA template is not already denatured or if it is supercoiled. Two other TFIIH subunits, CDK7 and cyclin H, phosphorylate serine amino acids on the RNA polymerase II C-terminal domain and possibly other proteins involved in the cell cycle. Next to a vital function in transcription initiation, TFIIH is also involved in nucleotide excision repair.	GTF2H		hgnc.genegroup:565	
1746	General transcription factor IIE complex subunits	Transcription factor II E (TFIIE) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex. It is a tetramer of two alpha and two beta chains and interacts with TAF6/TAFII80, ATF7IP, and varicella-zoster virus IE63 protein.TFIIE recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. Transcription factor II E is encoded by the GTF2E1 and GTF2E2 genes.  TFIIE is thought to be involved in DNA melting at the promoter: it contains a zinc ribbon motif that can bind single stranded DNA.	GTF2E		hgnc.genegroup:565	
1747	General transcription factor IIIC complex subunits		GTF3C		hgnc.genegroup:565	
1748	General transcription factor IIA complex subunits	Transcription factor TFIIA is a nuclear protein involved in the RNA polymerase II-dependent transcription of DNA.  TFIIA is one of several general (basal) transcription factors (GTFs) that are required for all transcription events that use RNA polymerase II.  Other GTFs include TFIID, a complex composed of the TATA binding protein TBP and TBP-associated factors (TAFs), as well as the factors TFIIB, TFIIE, TFIIF, and TFIIH.  Together, these factors are responsible for promoter recognition and the formation of a transcription preinitiation complex (PIC) capable of initiating RNA synthesis from a DNA template.	GTF2A		hgnc.genegroup:565	
1749	Depalmitoylases				so:0005855	
175	Cholinergic receptors	An acetylcholine [cholinergic] receptor (abbreviated AChR) is an integral membrane protein that responds to the binding of acetylcholine, a neurotransmitter.			so:0005855	
1750	General transcription factor IIF complex subunits	Transcription factor IIF (TFIIF) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex.Transcription factor IIF is encoded by the GTF2F1, GTF2F2, and GTF2F2L genes.TFIIF binds to RNA Polymerase II when the enzyme is already unbound to any other transcription factor, thus avoiding it from contacting DNA outside the promoter. Furthermore, TFIIF stabilizes the RNA polymerase II while it's contacting TBP and TFIIB.	GTF2F		hgnc.genegroup:565	
1751	FA core complex				so:0005855	
1752	IPT domain containing	The IPT (Ig-like, plexins, transcription factors) domain has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. The Ron tyrosine kinase receptor shares with the members of its subfamily (Met and Sea) a unique functional feature: the control of cell dissociation, motility, and invasion of extracellular matrices (scattering).			so:0005855	
1753	MicroRNA MIR101 family	miR-101 microRNA precursor is a small non-coding RNA  that regulates gene expression. Expression of miR-101 has been validated in both human (MI0000103, MI0000739) and mouse (MI0000148). This microRNA appears to be specific to the vertebrates and has now been predicted or confirmed in a wide range of vertebrate species (MIPF0000046). The precursor microRNA is a stem-loop structure of about 70 nucleotides in length that is processed by the Dicer enzyme to form the 21-24 nucleotide mature microRNA.  In this case the mature sequence is excised from the 3' arm of the hairpin. Survival analysis shows that hsa-miR-101 is associated with survival in multiple breast cancer datasets.			hgnc.genegroup:476	
1754	MicroRNA MIR103/107 family	The miR-103 microRNA precursor (homologous to miR-107), is a short non-coding RNA gene involved in gene regulation. miR-103 and miR-107 have now been predicted or experimentally confirmed in human.microRNAs are transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a ~22 nucleotide product.  In this case the mature sequence comes from the 5' arm of the precursor.  The mature products are thought to have regulatory roles through complementarity to mRNA.mir-103 and mir-107 were noted as being upregulated in obese mice and were subsequently found to have a key role in insulin sensitivity. This led to a suggestion that these microRNAs represent potential targets for the treatment of type 2 diabetes.mir-103 has also been linked with chronic pain and intestinal cell proliferation.Recently, miR-103-3p was shown to target the 5' untranslated region (5' UTR) of GPRC5A's mRNA in pancreatic cancer. This is one of only a handful of known instances where a miRNA targets the 5' UTR of a mRNA.			hgnc.genegroup:476	
1756	MicroRNA MIR129 family	The miR-129 microRNA precursor is a small non-coding RNA molecule that regulates gene expression. This microRNA was first experimentally characterised in mouse and homologues have since been discovered in several other species, such as humans, rats and zebrafish. The mature sequence is excised by the Dicer enzyme from the 5' arm of the hairpin. It was elucidated by Calin et al. that miR-129-1 is located in a fragile site region of the human genome near a specific site, FRA7H in chromosome 7q32, which is a site commonly deleted in many cancers. miR-129-2 is located in 11p11.2.	MIR129		hgnc.genegroup:476	
1757	MicroRNA MIR135 family	The miR-135 microRNA precursor is a small non-coding RNA that is involved in regulating gene expression.  It has been shown to be expressed in human, mouse and rat.  miR-135 has now been predicted or experimentally confirmed in a wide range of vertebrate species (MIPF0000028). Precursor microRNAs are ~70 nucleotides in length and are processed by the Dicer enzyme to produce the shorter 21-24 nucleotide mature sequence.   In this case the mature sequence is excised from the 5' arm of the hairpin.	MIR135		hgnc.genegroup:476	
1758	MicroRNA MIR138 family	miR-138 is a family of microRNA precursors found in animals, including humans. MicroRNAs are typically transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a ~22 nucleotide product. The excised region or, mature product, of the miR-138 precursor is the microRNA mir-138. miR-138 has been used as an example of the post-transcriptional regulation of miRNA, due to the finding that while the precursor is expressed ubiquitously, the mature product is found only in specific cell types.	MIR138		hgnc.genegroup:476	
1759	MicroRNA MIR153 family		MIR153		hgnc.genegroup:476	
176	Zinc activated channels	Zinc-activated ion channel (ZAC), is a human protein encoded by the ZACN gene. ZAC forms a cation-permeable ligand-gated ion channel of the 'Cys-loop' superfamily. The ZAC gene is present in humans and dogs, but no ortholog is thought to exist in the rat or mouse genomes.	ZACN		hgnc.genegroup:161	
1760	MicroRNA MIR190 family		MIR190		hgnc.genegroup:476	
1761	MicroRNA MIR193 family		MIR193		hgnc.genegroup:476	
1762	MicroRNA MIR365 family		MIR365		hgnc.genegroup:476	
1763	MicroRNA MIR216 family		MIR216		hgnc.genegroup:476	
1764	MicroRNA MIR302 family		MIR302		hgnc.genegroup:476	
1765	MicroRNA MIR551 family		MIR551		hgnc.genegroup:476	
1766	MicroRNA MIR105 family		MIR105		hgnc.genegroup:476	
1767	MicroRNA MIR95 family				hgnc.genegroup:476	
1768	MicroRNA MIR147 family		MIR147		hgnc.genegroup:476	
1769	MicroRNA MIR154 family				hgnc.genegroup:476	
177	Ion channels	Ion channels are pore-forming membrane proteins whose functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by gating the flow of ions across the cell membrane, controlling the flow of ions across secretory and epithelial cells, and regulating cell volume. Ion channels are present in the membranes of all cells. Ion channels are considered to be one of the two traditional classes of ionophoric proteins, with the other class known as ion transporters (including the sodium-potassium pump, sodium-calcium exchanger, and sodium-glucose transport proteins, amongst others).  Study of ion channels ( channelomics ) often includes biophysics, electrophysiology and pharmacology, utilizing techniques including voltage clamp, patch clamp, immunohistochemistry, and RT-PCR.			so:0005855	
1770	MicroRNA MIR379 family				hgnc.genegroup:476	
1771	MicroRNA MIR329 family				hgnc.genegroup:476	
1773	MicroRNA MIR500 family				hgnc.genegroup:476	
1775	MicroRNA MIR374 family		MIR374		hgnc.genegroup:476	
1776	RISC loading complex subunits	The RNA-induced silencing complex, or RISC, is a multiprotein complex, specifically a ribonucleoprotein, which functions in gene silencing via a variety of pathways at the transcriptional and translational levels. Using single-stranded RNA (ssRNA) fragments, such as microRNA (miRNA), or double-stranded small interfering RNA (siRNA), the complex functions as a key tool in gene regulation. The single strand of RNA acts as a template for RISC to recognize complementary messenger RNA (mRNA) transcript. Once found, one of the proteins in RISC, Argonaute, activates and cleaves the mRNA. This process is called RNA interference (RNAi) and it is found in many eukaryotes; it is a key process in defense against viral infections, as it is triggered by the presence of double-stranded RNA (dsRNA).			so:0005855	
1777	MicroRNA MIR376 family		MIR376		hgnc.genegroup:476	
1778	MicroRNA MIR378 family		MIR378		hgnc.genegroup:476	
1779	MicroRNA MIR371 family				hgnc.genegroup:476	
178	Voltage-gated ion channels	Voltage-gated ion channels are a class of transmembrane ion channels that are activated by changes in electrical membrane potential near the channel; these types of ion channels are especially critical in neurons, but are common in many types of cells. They have a crucial role in excitable neuronal and muscle tissues, allowing a rapid and co-ordinated depolarization in response to triggering voltage change. Found along the axon and at the synapse, voltage-gated ion channels directionally propagate electrical signals.			hgnc.genegroup:294	
1780	MicroRNA MIR515 family				hgnc.genegroup:476	
1787	B-WICH chromatin-remodelling complex subunits	The chromatin-remodelling complex B-WICH specifically activates RNA polymerase III transcription of the 5S rRNA and 7SL genes.			so:0005855	
1788	MicroRNA MIR506 family				hgnc.genegroup:476	
1789	MicroRNA MIR450 family		MIR450		hgnc.genegroup:476	
179	Sodium channels	Sodium channels are integral membrane proteins that form ion channels, conducting sodium ions ( Na +) through a cell's plasma membrane.  They are classified according to the trigger that opens the channel for such ions, i.e. either a voltage-change ('Voltage-gated,' 'voltage-sensitive,' or 'voltage-dependent' sodium channel also called 'VGSCs' or 'Nav channel') or a binding of a substance (a ligand ) to the channel (ligand-gated sodium channels). In excitable cells such as neurons, myocytes, and certain types of glia, sodium channels are responsible for the rising phase of action potentials.			hgnc.genegroup:292	
1790	MicroRNA MIR486 family		MIR486		hgnc.genegroup:476	
1791	Serine beta lactamase family				so:0005855	
1792	Paralemmins		PALM		so:0005855	
1793	SCAR/WAVE complex	The WAVE regulatory complex (WRC) is a five-subunit protein complex in the Wiskott-Aldrich syndrome protein (WASP) family involved in the formation of the actin cytoskeleton through interaction with the Arp2/3 complex. The holocomplex comprises WAVE1 (also known as WASF1), CYFIP1, ABI2, Nap1 and HSPC300 in its canonical form, or orthologues of these.			so:0005855	
1796	MicroRNA MIR888 family				hgnc.genegroup:476	
1798	MicroRNA MIR891 family		MIR891		hgnc.genegroup:476	
1799	MicroRNA MIR544 family		MIR544		hgnc.genegroup:476	
18	Major cadherins	All members of the major cadherin (CDH) gene family encode proteins with an ectodomain comprising at least five consecutive cadherin repeats showing high sequence conservation within the family. The family includes the “classical” type I and type II cadherin genes, encoding proteins with a single transmembrane domain and a cytoplasmic domain containing two conserved motifs for binding to members of the armadillo protein family. Further, the family includes type-III, type-IV and desmosomal cadherins, often encoding longer ectodomains with additional motifs, a single transmembrane domain and a cytoplasmic domain containing at least one conserved motif for armadillo protein binding. Finally, the family includes Flamingo/CELSR genes encoding proteins, which typically have a longer ectodomain, a seven-pass membrane domain and an unrelated cytoplasmic domain compared to other cadherins. These subfamilies are phylogenetically grouped together in one major cadherin branch.	CDH		hgnc.genegroup:16	
180	Cholinergic receptors muscarinic	Muscarinic receptors, or mAChRs, are acetylcholine receptors that form G protein-receptor complexes in the cell membranes of certain neurons  and other cells. They play several roles, including acting as the main end-receptor stimulated by acetylcholine released from postganglionic fibers in the parasympathetic nervous system. Muscarinic receptors were named as such because they are more sensitive to muscarine than to nicotine. Their counterparts are nicotinic acetylcholine receptors (nAChRs), receptor ion channels that are also important in the autonomic nervous system. Many drugs and other substances (for example pilocarpine and scopolamine ) manipulate these two distinct receptors by acting as selective agonists or antagonists.	CHRM		hgnc.genegroup:175|hgnc.genegroup:168	
1800	MicroRNA MIR550 family		MIR550		hgnc.genegroup:476	
1801	Cyclin and CBS domain divalent metal cation transport mediators		CNNM		so:0005855	
1802	I kappa B kinases				so:0005855	
1803	MicroRNA MIR28/151 family				hgnc.genegroup:476	
1804	MicroRNA MIR320 family	In molecular biology mir-320 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. The biogenesis of miR-320 is different from the canonical Microprocessor-dependent miRNAs. The pre-miR-320 is transcribed directly as a precursor microRNA hairpin and thus contains a 5' m7G-cap.  	MIR320		hgnc.genegroup:476	
1805	MicroRNA MIR188/532 family				hgnc.genegroup:476	
1806	MicroRNA MIR548 family				hgnc.genegroup:476	
1807	MicroRNA MIR663 family	In molecular biology mir-663 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms.	MIR663		hgnc.genegroup:476	
1808	Diphthamide biosynthesis genes		DPH		so:0005855	
1809	MicroRNA MIR664 family		MIR664		hgnc.genegroup:476	
181	Dopamine receptors	Dopamine receptors are a class of G protein-coupled receptors that are prominent in the vertebrate central nervous system (CNS). The neurotransmitter dopamine is the primary endogenous ligand for dopamine receptors. Dopamine receptors are implicated in many neurological processes, including motivation, pleasure, cognition, memory, learning, and fine motor control, as well as modulation of neuroendocrine signaling. Abnormal dopamine receptor signaling and dopaminergic nerve function is implicated in several neuropsychiatric disorders. Thus, dopamine receptors are common neurologic drug targets; antipsychotics are often dopamine receptor antagonists while psychostimulants are typically indirect agonists of dopamine receptors.	DRD		hgnc.genegroup:168	
1810	MicroRNA MIR1255 family		MIR1255		hgnc.genegroup:476	
1811	Histidine triad superfamily				so:0005855	
1812	CAMSAP family		CAMSAP		so:0005855	
1813	ELMO domain containing		ELMOD		so:0005855	
1814	Family with sequence similarity 83 		FAM83		so:0005855	
1815	KCTD family		KCTD		so:0005855	
1816	Bivalent Mical/EHBP Rab binding domain containing		BMERB		so:0005855	
1817	IKK complex	The IκB kinase (IKK) is an enzyme complex that is involved in propagating the cellular response to inflammation.The IκB kinase enzyme complex is part of the upstream NF-κB signal transduction cascade.  The IκBα (inhibitor of kappa B) protein inactivates the NF-κB transcription factor by masking the nuclear localization signals (NLS) of NF-κB proteins and keeping them sequestered in an inactive state in the cytoplasm.  Specifically, IKK phosphorylates the inhibitory IκBα protein. This phosphorylation results in the dissociation of IκBα from NF-κB. NF-κB, which is now free, migrates into the nucleus and activates the expression of at least 150 genes; some of which are anti-apoptotic.			so:0005855	
1819	Variant U1 small nuclear RNAs		RNVU1		hgnc.genegroup:849	
182	Calcium channels	A calcium channel is an ion channel which displays selective permeability to calcium ions. It is sometimes synonymous as voltage-dependent calcium channel, although there are also ligand-gated calcium channels.			hgnc.genegroup:292	
1820	ZUP1 deubiquitinase		ZUP		hgnc.genegroup:996	
1821	Ectonucleotide pyrophosphatase/phosphodiesterase family		ENPP		so:0005855	
1822	Ectonucleoside triphosphate diphosphohydrolase family				so:0005855	
1823	Pentatricopeptide repeat containing		PTCD		so:0005855	
1824	B7 family	B7 is a type of peripheral membrane protein found on activated antigen presenting cells (APC) that, when paired with either a CD28 or CD152 (CTLA-4) surface protein on a T cell, can produce a costimulatory signal or a coinhibitory signal to enhance or decrease the activity of a MHC-TCR signal between the APC and the T cell, respectively. Binding of the B7 of APC to CTLA-4 of T-cells causes inhibition of the activity of T-cells. There are two major types of B7 proteins: B7-1 or CD80, and B7-2 or CD86. However, it is not known if they differ significantly from each other. CD28 and CTLA-4 each interact with both B7-1 and B7-2.			so:0005855	
1825	Guanylate binding proteins		GBP		so:0005855	
1826	Microtubule associated protein RP/EB family 		MAPRE		so:0005855	
1827	Profilins	Profilin is an actin-binding protein involved in the dynamic turnover and restructuring of the actin cytoskeleton.   It is found in all eukaryotic organisms in most cells. Profilin is important for spatially and temporally controlled growth of actin microfilaments, which is an essential process in cellular locomotion and cell shape changes. This restructuring of the actin cytoskeleton is essential for processes such as organ development, wound healing, and the hunting down of infectious intruders by cells of the immune system. Profilin also binds sequences rich in the amino acid proline in diverse proteins. While most profilin in the cell is bound to actin, profilins have over 50 different binding partners. Many of those are related to actin regulation, but profilin also seems to be involved in activities in the nucleus such as mRNA splicing.Profilin binds some variants of membrane phospholipids (phosphatidylinositol (4,5)-bisphosphate and inositol trisphosphate). The function of this interaction is the sequestration of profilin in an 'inactive' form, from where it can be released by action of the enzyme phospholipase C. Profilin is the major allergen present in birch, grass, and other pollen and is found in Toxoplasma gondii  as an essential part of host cell invasion. It is the specific pathogen-associated molecular pattern (PAMP) of TLR11.	PFN		so:0005855	
1828	SLIT and NTRK like family		SLITRK		so:0005855	
1829	TAFA chemokine like family		TAFA		so:0005855	
183	Potassium channels	In the field of cell biology, potassium channels are the most widely distributed type of ion channel and are found in virtually all living organisms.  They form potassium -selective pores that span cell membranes. Furthermore potassium channels are found in most cell types and control a wide variety of cell functions.	KCN		hgnc.genegroup:292	
1830	Tweety family		TTYH		so:0005855	
1831	Torsins		TOR		hgnc.genegroup:413	
1832	Thioesterase superfamily		THEM		so:0005855	
1833	SSX family		SSX		so:0005855	
1834	SPANX family				so:0005855	
1835	Small nucleolar RNA protein coding host genes	These protein coding genes host snoRNA genes in their introns.			hgnc.genegroup:1838	
1836	IGF like family		IGFL		so:0005855	
1837	Chymotrypsin like elastases		CELA		so:0005855	
1838	Small nucleolar RNA host genes	In the human genome, most snoRNA genes are located within the introns of other 'host' genes. Such snoRNA host genes can be either protein-coding or non-coding.			so:0005855	
1839	Small nucleolar RNA non-coding host genes	Long non-coding genes that host snoRNA genes in either an intron or an exon on the same strand are named with the root symbol SNHG for ‘small nucleolar RNA host gene’, followed by a sequential number e.g. SNHG1 for 'small nucleolar RNA host gene 1'. 	SNHG		hgnc.genegroup:1838|hgnc.genegroup:788	
184	Sodium voltage-gated channels		SCN		hgnc.genegroup:179|hgnc.genegroup:178	
1840	Inter-alpha-trypsin inhibitor heavy chains		ITIH		so:0005855	
1841	LGI family		LGI		so:0005855	
1842	NDRG family		NDRG		so:0005855	
1844	XAGE family		XAGE		so:0005855	
1845	GAGE family		GAGE		so:0005855	
1846	PAGE family		PAGE		so:0005855	
1847	SAGE family		SAGE		so:0005855	
1848	BAGE family		BAGE		so:0005855	
1849	CT antigen family 45		CT45		so:0005855	
185	Sodium channels epithelial		SCNN		hgnc.genegroup:179	
1850	CT antigen family 47		CT47		so:0005855	
1851	CSAG family		CSAG		so:0005855	
1853	Mitochondrial iron-sulfur assembly components				hgnc.genegroup:1854	
1854	Iron-sulfur assembly components				so:0005855	
1855	Nectins and nectin-like molecules	Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion.Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue.			hgnc.genegroup:1410	
1856	Golgin related				hgnc.genegroup:1084	
1857	Tim17 family				so:0005855	
1858	MicroRNA MIR1302 family		MIR1302		hgnc.genegroup:476	
1859	MicroRNA MIR1184 family		MIR1184		hgnc.genegroup:476	
186	Cation channels sperm associated 	The cation channels of sperm also known as Catsper channels or CatSper, are ion channels that are related to the two-pore channels and distantly related to TRP channels. The four members of this family form voltage-gated Ca 2+ channels that seem to be specific to sperm. As sperm encounter the more alkaline environment of the female reproductive tract, CatSper channels become activated by the altered ion concentration. These channels are required for proper fertilization.  The study of these channels has been slow because they do not traffic to the cell membrane in many heterologous systems.	CATSPER		hgnc.genegroup:178|hgnc.genegroup:182	
1860	MicroRNA MIR1233 family		MIR1233		hgnc.genegroup:476	
1861	MicroRNA MIR1244 family		MIR1244		hgnc.genegroup:476	
1863	MicroRNA MIR1285 family		MIR1285		hgnc.genegroup:476	
1864	MicroRNA MIR1289 family		MIR1289		hgnc.genegroup:476	
1865	MicroRNA MIR1972 family		MIR1972		hgnc.genegroup:476	
1866	MicroRNA MIR3118 family		MIR3118		hgnc.genegroup:476	
1867	MicroRNA MIR3156 family		MIR3156		hgnc.genegroup:476	
1868	MicroRNA MIR3179 family		MIR3179		hgnc.genegroup:476	
1869	MicroRNA MIR3180 family		MIR3180		hgnc.genegroup:476	
187	Histamine receptors	The histamine receptors are a class of G protein-coupled receptors with histamine as their endogenous ligand. There are four known histamine receptors:  H 1 receptor H 2 receptor H 3 receptor H 4 receptor	HRH		hgnc.genegroup:168	
1870	MicroRNA MIR3198 family		MIR3198		hgnc.genegroup:476	
1871	MicroRNA MIR3648 family		MIR3648		hgnc.genegroup:476	
1872	MicroRNA MIR3670 family		MIR3670		hgnc.genegroup:476	
1874	MicroRNA MIR3680 family		MIR3680		hgnc.genegroup:476	
1875	NCoR/SMRT transcriptional repression complex subunits				hgnc.genegroup:2102	
1876	Signal recognition particle	The signal recognition particle (SRP) is an abundant, cytosolic, universally conserved ribonucleoprotein (protein-RNA complex) that recognizes and targets specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes.			so:0005855	
1877	Low confidence cytoplasmic transfer RNAs	These cytoplasmic tRNAs are not included in the high confidence set at the Genomic tRNA database. They may have low tRNAscan feature scores and may possibly be repeat elements or pseudogenes.			hgnc.genegroup:842	
1878	General transcription factor IID complex subunits 	Transcription factor II D (TFIID) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex. RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells. It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins.  Before the start of transcription, the transcription Factor II D (TFIID) complex binds to the TATA box in the core promoter of the gene.	TAF		hgnc.genegroup:565	
1879	General transcription factor IIIB complex subunits 				hgnc.genegroup:565	
188	Trace amine receptors	Trace amine-associated receptors, abbreviated TAAR and otherwise known as trace amine receptors, abbreviated TAR or TA, are a class of G protein-coupled receptors identified in 2001.   These receptors have gained considerable interest in academic and pharmaceutical industry research as putative endogenous receptors for trace amines, metabolic derivatives of classical biogenic amines and the psychostimulants amphetamine and methamphetamine.    In 2004 it was shown that in mammals TAAR1 is probably also a receptor for thyronamines, decarboxylated and deiodinated metabolites of the thyroid hormones, while the mouse mTAAR2 -€“ mTAAR9 receptors are most probably olfactory receptors for volatile amines.	TAAR		hgnc.genegroup:168	
1880	Runt-related transcription factors	Runt-related transcription factor 1 (RUNX1) also known as acute myeloid leukemia 1 protein (AML1) or core-binding factor subunit alpha-2 (CBFA2) is a protein that in humans is encoded by the RUNX1 gene. RUNX1 is a transcription factor that regulates the differentiation of hematopoietic stem cells into mature blood cells.  In addition it plays a major role in the development of the neurons that  transmit pain. It belongs to the Runt-related transcription factor (RUNX) family of genes which are also called core binding factor-α (CBFα). RUNX proteins form a heterodimeric complex with CBFβ which confers increased DNA binding and stability to the complex. Chromosomal translocations involving the RUNX1 gene are associated with several types of leukemia including M2 AML. Mutations in RUNX1 are implicated in cases of breast cancer.	RUNX		so:0005855	
1881	IQSEC ArfGEF family		IQSEC		hgnc.genegroup:1945	
1882	MAB21 family		MAB21		so:0005855	
1883	Thioredoxin domain containing 		TXNDC		so:0005855	
1885	HECT and RLD domain containing E3 ubiquitin protein ligases		HERC		hgnc.genegroup:1959	
1887	Atlastins		ATL		so:0005855	
1888	Fibrillins		FBN		so:0005855	
1889	Filamins		FLN		so:0005855	
189	Chemokine receptors	Chemokine receptors are cytokine receptors found on the surface of certain cells that interact with a type of cytokine called a chemokine.  There have been 19 distinct chemokine receptors described in mammals. Each has a 7- transmembrane (7TM) structure and couples to G-protein for signal transduction within a cell, making them members of a large protein family of G protein-coupled receptors. Following interaction with their specific chemokine ligands, chemokine receptors trigger a flux in intracellular calcium (Ca 2+ ) ions ( calcium signaling ). This causes cell responses, including the onset of a process known as chemotaxis that traffics the cell to a desired location within the organism. Chemokine receptors are divided into different families, CXC chemokine receptors, CC chemokine receptors, CX3C chemokine receptors and XC chemokine receptors that correspond to the 4 distinct subfamilies of chemokines they bind.			hgnc.genegroup:140	
1891	BAG6 complex	The Bag6 complex is involved in tail-anchored protein targeting and various protein quality-control pathways in the cytosol as well as regulating transcription and histone methylation in the nucleus. 			hgnc.genegroup:1914	
1893	Dolichyl-phosphate mannosyltransferase subunits		DPM		so:0005855	
1894	KDEL endoplasmic reticulum protein retention receptors		KDELR		so:0005855	
1895	Fibroblast growth factor family		FGF		so:0005855	
1896	Glycoprotein hormone subunits				so:0005855	
1898	R-spondin family		RSPO		hgnc.genegroup:542	
1899	WNK lysine deficient protein kinases		WNK		so:0005855	
19	Protocadherins	The protocadherin (PCDH) gene family encodes proteins with an ectodomain comprising six or seven cadherin repeats with high sequence conservation within the family and weaker homology to the cadherin repeats of members of the major cadherin family. Further, protocadherins have a single transmembrane domain and a distinct, protocadherin-specific, cytoplasmic domain. Protocadherins can be further subdivided into clustered and non-clustered protocadherins on the basis of particular genomic organizations.	PCDH		hgnc.genegroup:16	
1900	AKT kinases	Protein kinase B (PKB), also known as Akt, is a serine/threonine-specific protein kinase that plays a key role in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription and cell migration.	AKT		hgnc.genegroup:1625	
1901	Tachykinin precursors		TAC		hgnc.genegroup:1902	
1902	Neuropeptides				hgnc.genegroup:542	
1903	Aldolases	Aldolase A (ALDOA, or ALDA), also known as fructose-bisphosphate aldolase, is an enzyme that in humans is encoded by the ALDOA gene on chromosome 16. The protein encoded by this gene is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. Alternative splicing and alternative promoter usage results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 3 and 10. [provided by RefSeq, Aug 2011]	ALDO		so:0005855	
1908	Endothelins		EDN		hgnc.genegroup:1902	
1909	Contactins		CNTN		hgnc.genegroup:1410|hgnc.genegroup:555	
1910	Lysosome associated membrane proteins		LAMP		so:0005855	
1911	ER membrane protein complex subunits		EMC		so:0005855	
1912	Guided entry of tail-anchored proteins complex subunits	Get3/TRC40 function requires an ER receptor, which in yeast consists of the Get1/Get2 heterotetramer and in mammals of the WRB protein (now approved as GET1 in human), homologous to yeast Get1, in combination with CAML (calcium-modulating cyclophilin ligand), which is not homologous to Get2. 	GET		hgnc.genegroup:1915	
1914	GET4-GET5 transmembrane domain recognition complex subunits	In yeast, Get4 and Get5 escort tail-anchored proteins to Get3. In mammals, BAG6, (which lacks a yeast equivalent) is additionally required to enable an otherwise similar TA protein transfer process.			hgnc.genegroup:1915	
1915	Guided entry of tail-anchored proteins associated factors	The GET (guided entry of tail-anchored proteins)/TRC (transmembrane recognition complex) pathway for tail-anchored protein targeting to the endoplasmic reticulum (ER) has been characterized in detail in yeast and is thought to function similarly in mammals.			so:0005855	
1916	Activating signal cointegrator 1 complex		ASCC		so:0005855	
1917	COPI coat complex		COP		hgnc.genegroup:1961	
1918	Transmembrane and tetratricopeptide repeat containing		TMTC		so:0005855	
1921	AH domain containing				hgnc.genegroup:1292	
1923	AH/BAR family Rho GTPase activating proteins				hgnc.genegroup:721|hgnc.genegroup:1292	
1924	BAR and Dbl domain containing				hgnc.genegroup:1292	
1925	Prolyl 3-hydroxylase family		P3H		so:0005855	
1926	Isocitrate dehydrogenases	Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms: IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.	IDH		so:0005855	
1927	Pepsinogens	Pepsin is an endopeptidase that breaks down proteins into smaller peptides (that is, a protease). It is produced in the stomach and is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site.It is one of three principal proteases in the human digestive system, the other two being chymotrypsin and trypsin. During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Pepsin's proenzyme, pepsinogen, is released by the chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin.  			hgnc.genegroup:1928	
1928	Peptidase family A1	Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin.Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin and archaean preflagellin have been described.Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral duplication. Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. Each domain contributes a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. The presence and position of disulfide bridges are other conserved features of aspartic peptidases.			so:0005855	
1929	Superoxide dismutases		SOD		so:0005855	
1931	NRZ tethering complex	The yeast Dsl1 complex, which comprises Dsl1, Tip20, and Sec39/Dsl3, has been shown to participate, as a vesicle-tethering complex, in retrograde trafficking from the Golgi apparatus to the endoplasmic reticulum. Its metazoan counterpart NRZ complex, which comprises NAG, RINT1, and ZW10, is also involved in Golgi-to-ER retrograde transport, but each component of the complex has diverse cellular functions including endosome-to-Golgi transport, cytokinesis, cell cycle checkpoint, autophagy, and mRNA decay. 			so:0005855	
1932	Transforming growth factor beta superfamily				hgnc.genegroup:542	
1933	RZZ complex	The spindle assembly checkpoint (SAC) ensures proper chromosome segregation by delaying anaphase onset in response to unattached kinetochores. Checkpoint signalling requires the kinetochore localization of the Mad1-Mad2 complex that in more complex eukaryotes depends on the Rod-Zwilch-ZW10 (RZZ) complex. 			so:0005855	
1935	H1 histones	Histone H1 is one of the five main histone protein families which are components of chromatin in eukaryotic cells. Though highly conserved, it is nevertheless the most variable histone in sequence across species.	H1		hgnc.genegroup:864	
1936	H2A histones	Histone H2A is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells.	H2A		hgnc.genegroup:864	
1937	H2B histones	Histone H2B is one of the 4 main histone proteins involved in the structure of chromatin in  eukaryotic cells. Featuring a main globular domain and long N-terminal and C-terminal tails, H2B is involved with the structure of the nucleosomes.	H2B		hgnc.genegroup:864	
1938	H3 histones	Histone H3 is one of the five main histone proteins involved in the structure of chromatin in  eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. The term 'Histone H3' alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.	H3		hgnc.genegroup:864	
1939	H4 histones	Histone H4 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H4 is involved with the structure of the nucleosome of the 'beads on a string' organization. Histone proteins are highly post-translationally modified. Covalently bonded modifications include acetylation and methylation of the N-terminal tails. These modifications may alter expression of genes located on DNA associated with its parent histone octamer. Histone H4 is an important protein in the structure and function of chromatin, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.	H4		hgnc.genegroup:864	
1940	CCM adhesion complex	The three CCM proteins can exist in a trimeric complex, and each of these essential multi-domain adaptor proteins also interacts with a range of signaling, cytoskeletal and adaptor proteins, presumably accounting for their roles in a range of basic cellular processes including cell adhesion, migration, polarity and apoptosis.			so:0005855	
1941	Calmodulin binding transcription activators 		CAMTA		so:0005855	
1942	Caveolins		CAV		so:0005855	
1943	TACC family		TACC		so:0005855	
1944	Negative elongation factor complex members		NELF		so:0005855	
1945	Sec7 family				so:0005855	
1946	Cytohesins		CYTH		hgnc.genegroup:1945	
1947	ARFGEF family		ARFGEF		hgnc.genegroup:1945	
1948	Pleckstrin and Sec7 domain containing		PSD		hgnc.genegroup:1945	
1950	Heterogeneous nuclear ribonucleoproteins	Heterogeneous nuclear ribonucleoproteins (hnRNPs) are complexes of RNA and protein present in the cell nucleus during gene transcription and subsequent post-transcriptional modification of the newly synthesized RNA (pre-mRNA). The presence of the proteins bound to a pre-mRNA molecule serves as a signal that the pre-mRNA is not yet fully processed and therefore not ready for export to the cytoplasm. Since most mature RNA is exported from the nucleus relatively quickly, most RNA-binding protein in the nucleus exist as heterogeneous ribonucleoprotein particles. After splicing has occurred, the proteins remain bound to spliced introns and target them for degradation. hnRNPs are also integral to the 40s subunit of the ribosome and therefore important for the translation of mRNA in the cytoplasm. However, hnRNPs also have their own nuclear localization sequences (NLS) and are therefore found mainly in the nucleus. Though it is known that a few hnRNPs shuttle between the cytoplasm and nucleus, immunofluorescence microscopy with hnRNP-specific antibodies shows nucleoplasmic localization of these proteins with little staining in the nucleolus or cytoplasm. This is likely because of its major role in binding to newly transcribed RNAs. High-resolution immunoelectron microscopy has shown that hnRNPs localize predominantly to the border regions of chromatin, where it has access to these nascent RNAs.The proteins involved in the hnRNP complexes are collectively known as heterogeneous ribonucleoproteins. They include protein K and polypyrimidine tract-binding protein (PTB), which is regulated by phosphorylation catalyzed by protein kinase A and is responsible for suppressing RNA splicing at a particular exon by blocking access of the spliceosome to the polypyrimidine tract. hnRNPs are also responsible for strengthening and inhibiting splice sites by making such sites more or less accessible to the spliceosome.  Cooperative interactions between attached hnRNPs may encourage certain splicing combinations while inhibiting others.	HNRNP		so:0005855	
1951	Glycosylphosphatidylinositol transamidase complex				so:0005855	
1956	Pantothenate kinase family		PANK		so:0005855	
1957	TMEM8 family		TMEM8		so:0005855	
1958	Rho guanine nucleotide exchange factors	Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP).  A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase.			so:0005855	
1959	HECT domain containing				so:0005855	
196	Complement component GPCRs				hgnc.genegroup:140	
1960	COPII coat complex				hgnc.genegroup:1961	
1961	Protein coat complexes				so:0005855	
1962	SMG1 complex				hgnc.genegroup:1963	
1963	SURF complex				so:0005855	
1964	DECID complex				so:0005855	
1967	Steroid 5-alpha reductase family		SRD5A		so:0005855	
1968	SUN family	SUN proteins are type-II transmembrane proteins with nuclear-oriented N-termini and lumenal C-termini. Named for SUN domain family members (Sad1p, Unc-84) they all share a conserved SUN domain at the C-terminus of the lumenal domain. This lumenal region of SUN proteins also includes an extended coiled-coil domain. The nucleoplasmic domain of SUN proteins is structurally less characterized, but at least in some mammalian family members, has been shown to be capable of nuclear localization independent of the rest of the protein.	SUN		hgnc.genegroup:2005	
1969	Contactin associated protein family		CNTNAP		hgnc.genegroup:1582	
1970	CREB3 transcription factor family		CREB3		hgnc.genegroup:506	
1971	Shroom family		SHROOM		so:0005855	
1972	Mitochondrial genome		MT-		so:0005855	
1973	Mitochondrially encoded regions				hgnc.genegroup:1972	
1974	Mitochondrially encoded protein coding genes				hgnc.genegroup:1972	
1975	Mitochondrially encoded RNAs				hgnc.genegroup:1972	
1976	Mitochondrially encoded long non-coding RNAs				hgnc.genegroup:1975	
1978	IFT-A complex	 Intraflagellar transport (IFT)-A and -B complexes mediate retrograde and anterograde ciliary protein trafficking, respectively. The IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located. 			hgnc.genegroup:615	
1979	IFT-B complex	IFT52 is a key component of the IFT-B complex and ensures the interaction of the two subcomplexes, IFT-B1 and IFT-B2.			hgnc.genegroup:615	
198	Formyl peptide receptors	The formyl peptide receptors (FPR) belong to a class of G protein-coupled receptors involved in chemotaxis.  These receptors were originally identified by their ability to bind N-formyl peptides such as N -formylmethionine produced by the degradation of either bacterial or host cells.  Hence formyl peptide receptors are involved in mediating immune cell response to infection. These receptors may also act to suppress the immune system under certain conditions.  The close phylogenetical relation of signaling in chemotaxis and olfaction was recently proved by detection formyl peptide receptor like proteins as a distinct family of vomeronasal organ chemosensors in mice	FPR		hgnc.genegroup:140	
1980	IFT-B1 complex	The IFT-B1 complex consists of 9-10 stably associated core subunits.	IFT		hgnc.genegroup:1979	
1981	IFT-B2 complex	Thought to be peripheral components of the IFT‐B complex, IFT172, 80, 57, 54, and 20 form a stable sub‐complex (IFT‐B2). IFT‐B2 interacts with tubulin/microtubules and connects them to the core IFT‐B1 complex through interaction with IFT88/52.	IFT		hgnc.genegroup:1979	
1983	Tenascins		TN		hgnc.genegroup:554|hgnc.genegroup:555	
1984	Ras related GTP binding proteins		RRAG		hgnc.genegroup:358	
1985	Nuclear factor I family		NFI		so:0005855	
1986	Long intergenic non-protein coding RNAs	The HGNC defines long intergenic non-protein coding (LINC) RNAs as long non-coding RNA genes that do not overlap on either strand, or share a bidirectional promoter with, a protein coding gene and do not host either snoRNA or microRNA genes. These lincRNA genes are assigned the root symbol LINC# for ‘long intergenic non-protein coding RNA’ followed by a unique 5-digit number e.g. LINC00115.	LINC		hgnc.genegroup:788	
1987	Antisense RNAs	The HGNC defines antisense RNAs as long non-coding RNA genes that are on the opposite strand of the genomic span of a protein coding gene, including the intronic and UTR regions of the opposite protein coding gene. Please note this nomenclature is not intended to suggest that there is a shared function between the protein coding gene and antisense RNA. Antisense lncRNA genes are assigned the format [protein coding gene symbol]-AS + sequential number e.g. ABCA9-AS1 for 'ABCA9 antisense RNA 1'.			hgnc.genegroup:788	
1988	Overlapping transcripts	The HGNC defines overlapping transcripts as long non-coding RNA genes that overlap a protein coding gene on the same strand. These lncRNA genes are assigned the format [protein coding gene symbol]-OT + sequential number e.g. ACER2-OT1 for 'ACER2 3' UTR overlapping transcript'.			hgnc.genegroup:788	
1989	Intronic transcripts	The HGNC defines intronic transcripts as long non-coding RNA genes that are located within an intron on the SAME strand as a protein coding gene. These lncRNA genes are assigned the format  [protein coding gene symbol]-IT + sequential number e.g. AKT2-IT1 for 'AKT2 intronic transcript 1'.			hgnc.genegroup:788	
199	Glycoprotein hormone receptors				hgnc.genegroup:140	
1990	Divergent transcripts	The HGNC defines divergent transcripts as long non-coding RNA genes that are within 300-500 nucleotides of a protein coding gene on the opposite strand. These lncRNA genes are named with the format [protein coding gene symbol]-DT  e.g. DHX33-DT for ‘DHX33 divergent transcript’.   			hgnc.genegroup:788	
1992	Long non-coding RNAs with non-systematic symbols				hgnc.genegroup:788	
1993	Long non-coding RNAs with FAM root symbol	Homologous long non-coding RNA genes may be named together using the root symbol FAM# for 'family with sequence similarity'. Note that this root symbol is also used for protein coding families - this gene groups shows only the non-coding genes named with the FAM# root.	FAM		hgnc.genegroup:788	
1994	Large subunit mitochondrial ribosomal proteins		MRPL		hgnc.genegroup:646	
1996	Small subunit mitochondrial ribosomal proteins		MRPS		hgnc.genegroup:646	
1997	HIRA histone chaperone complex subunits				so:0005855	
1998	minichromosome maintenance 2-7 complex	The eukaryotic minichromosome maintenance 2-7 complex is the core of the inactive MCM replication licensing complex and the catalytic core of the Cdc45-MCM-GINS replicative helicase. 			hgnc.genegroup:1999	
1999	CMG helicase complex	The CMG (Cdc45-MCM-GINS) complex is the eukaryotic replicative helicase, the enzyme that unwinds double-stranded DNA at replication forks. 			so:0005855	
20	Clustered protocadherins				hgnc.genegroup:19	
200	Hydroxycarboxylic acid receptors		HCAR		hgnc.genegroup:140	
2002	APC membrane recruitment proteins		AMER		so:0005855	
2003	Atrophins				so:0005855	
2005	Linker of nucleoskeleton and cytoskeleton complex subunits	The LINC complex (Linker of Nucleoskeleton and Cytoskeleton) is a protein complex associated with both inner and outer membranes of the nucleus. It is composed of SUN-domain proteins and KASH-domain proteins. The SUN-domain proteins are associated with both nuclear lamins and chromatin and cross the inner nuclear membrane. They interact with the KASH domain proteins in the perinuclear (lumen) space between the two membranes. The KASH domain proteins cross the outer nuclear membrane and interact with actin filaments, microtubule filaments (through dynein and kinesin motors), intermediate filaments (through spectrin), centrosomes and cytoplasmic organelles. The number of SUN-domain and KASH-domain proteins increased in evolution.			so:0005855	
2006	Formins				so:0005855	
2007	R2SP complex				so:0005855	
201	Lipid like receptors				hgnc.genegroup:140	
2010	KASH domain containing	KASH domains are conserved C-terminal protein regions less than ~30 amino acids. KASH is an acronym for Klarsicht, ANC-1, Syne Homology. KASH domains always follow a transmembrane domain.  Most proteins containing KASH domains are thought to be involved in the positioning of the nucleus in the cell.  KASH domains interact with proteins containing SUN domains in the space between the outer and inner nuclear membranes to bridge the nuclear envelope, and may transfer force from the nucleoskeleton to the cytoplasmic cytoskeleton and enable mechanosensory roles in cells.  KASH proteins are thought to largely localize to the outer nuclear membrane, although there are reports of inner nuclear membrane localization of some KASH protein isoforms.			hgnc.genegroup:2005	
2012	FHF complex	The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex) 			so:0005855	
2019	Outer dynein arm docking complex subunits	The outer dynein arm-docking complex (ODA-DC), which was first identified in the green alga Chlamydomonas reinhardtii, is a protein complex that mediates the binding of axonemal dynein and doublet microtubules. 	ODAD		so:0005855	
202	Cannabinoid receptors	The cannabinoid receptors are a class of cell membrane receptors under the G protein-coupled receptor superfamily.   As is typical of G protein-coupled receptors, the cannabinoid receptors contain seven transmembrane spanning domains.  Cannabinoid receptors are activated by three major groups of ligands, endocannabinoids (produced by the mammalian body), plant cannabinoids (such as THC, produced by the cannabis plant) and synthetic cannabinoids (such as HU-210 ). All of the endocannabinoids and plant cannabinoids are lipophilic, i.e. fat soluble, compounds. There are currently two known subtypes, termed CB 1 and CB 2.  The CB 1 receptor is expressed mainly in the brain ( central nervous system or 'CNS'), but also in the lungs, liver and kidneys. The CB 2 receptor is expressed mainly in the immune system and in hematopoietic cells. Mounting evidence suggests that there are novel cannabinoid receptors  that is, non-CB 1 and non-CB 2, which are expressed in endothelial cells and in the CNS. In 2007, the binding of several cannabinoids to a G protein-coupled receptor (GPCR) in the brain was described.  The protein sequences of CB 1 and CB 2 receptors are about 44% similar.  When only the transmembrane regions of the receptors are considered, amino acid similarity between the two receptor subtypes is approximately 68%.  In addition, minor variations in each receptor have been identified. Cannabinoids bind reversibly and stereo-selectively to the cannabinoid receptors. Subtype selective cannabinoids have been developed which theoretically may have advantages for treatment of certain diseases such as obesity.	CNR		hgnc.genegroup:201	
2020	Type II transmembrane serine proteases				hgnc.genegroup:738	
2021	IQ motif containing GTPase activating protein family		IQGAP		so:0005855	
2022	Oxoglutarate dehydrogenase complex				so:0005855	
2023	Procollagen-lysine,2-oxoglutarate 5-dioxygenase family		PLOD		so:0005855	
2025	3-hydroxyacyl-CoA dehydratase family		HACD		so:0005855	
2028	Dynein 1 complex subunits	Cytoplasmic dynein-1 is a major microtubule-based motor critical for cell division. Dynein is essential for the formation and positioning of the mitotic spindle as well as the transport of various cargos in the cell.	DYNC1		hgnc.genegroup:538	
2029	Dynein 2 complex subunits	The motor protein that powers the movement of the particles from the tip of the flagellum to the base (retrograde IFT) is called cytoplasmic dynein 1b in Chlamydomonas and cytoplasmic dynein 2 in vertebrates.	DYNC2		hgnc.genegroup:538	
203	Free fatty acid receptors	The free fatty acid receptor is a G-protein coupled receptor which binds free fatty acids.  There are four variants of the receptor, each encoded by a separate gene ( FFAR1, FFAR2, FFAR3, FFAR4).	FFAR		hgnc.genegroup:201	
2030	ADP-ribosyltransferase family		ART		so:0005855	
2031	Dyneins, axonemal outer arm complex subunits				hgnc.genegroup:536	
2032	Dyneins, axonemal inner arm I1/f complex subunits				hgnc.genegroup:536	
2033	Dishevelled binding antagonist of beta catenin family		DACT		so:0005855	
2035	DNA cross-link repair family		DCLRE1		hgnc.genegroup:1615	
2036	Radical S-adenosylmethionine domain containing				hgnc.genegroup:1398	
2037	Argonaute RISC component family		AGO		hgnc.genegroup:408	
2038	Piwi like RNA-mediated gene silencing family		PIWIL		hgnc.genegroup:408	
2039	Myosin light chains, class 1				hgnc.genegroup:657|hgnc.genegroup:863	
204	Leukotriene receptors				hgnc.genegroup:201	
2040	Myosin light chains, class 2				hgnc.genegroup:657|hgnc.genegroup:863	
2042	CREC family				hgnc.genegroup:863	
2044	 Mitochondrial translation release factor family		MTRF		so:0005855	
2045	U11 small nuclear ribonucleoprotein	A ribonucleoprotein complex that contains small nuclear RNA U11, a heptameric ring of Sm proteins, as well as several proteins that are unique to the U11 snRNP, most of which remain associated with the U11 snRNA both while the U11 snRNP is free or assembled into a series of spliceosomal complexes.			so:0005855	
2046	Axonemal radial spoke subunits 	The radial spoke is a multi-unit protein structure found in the axonemes of eukaryotic cilia and flagella. Although experiments have determined the importance of the radial spoke in the proper function of these organelles, its structure and mode of action remain poorly understood.	RSPH		so:0005855	
2047	Methylcrotonyl-CoA carboxylase subunits	Methylcrotonyl-CoA carboxylase (MCCC) is a heteromultimeric complex that is composed of two subunits which are encoded by distinct genes.	MCCC		so:0005855	
2048	Transcription factor AP-2 family		TFAP2		so:0005855	
2049	Tet methylcytosine dioxygenase family		TET		so:0005855	
205	Lysophosphatidic acid receptors		LPAR		hgnc.genegroup:201	
2050	Adducin family		ADD		so:0005855	
2051	TNRC6 adaptor family		TNRC6		so:0005855	
2052	PARN exonuclease family				so:0005855	
2053	ATPase F1/V1 alpha/A and beta/B subunit family	The ATP synthase F1 domain and V-ATPase V1 domain alpha/A and beta/B subunits are encoded by homologous genes, shown together here.			so:0005855	
2054	7TM proteins				so:0005855	
2055	TLDc domain containing	The TLDc domain is a highly conserved protein motif present in several mammal proteins that share a protective function against oxidative stress.	TLDC		so:0005855	
2056	7BS protein lysine methyltransferases				hgnc.genegroup:2058	
2057	7BS protein arginine methyltranferases				hgnc.genegroup:2058	
2058	7BS protein methyltransferases				hgnc.genegroup:1400	
2059	7BS DNA/RNA methyltransferases				hgnc.genegroup:1400	
206	Sphingosine 1-phosphate receptors		S1PR1		hgnc.genegroup:201	
2060	7BS C5-cytosine DNA/RNA methyltransferases				hgnc.genegroup:2059	
2061	7BS N6-adenosine DNA/RNA methyltransferases				hgnc.genegroup:2059	
2062	7BS 2'O-ribose DNA/RNA methyltransferases				hgnc.genegroup:2059	
2063	7BS small molecule methyltransferases				hgnc.genegroup:1400	
2065	Homocysteine methyltransferases				hgnc.genegroup:1398	
2066	7BS orphan methyltransferases				hgnc.genegroup:1400	
2067	Apelin receptor				hgnc.genegroup:220	
2068	Nuclear receptor subfamily 0 group B		NR0B		hgnc.genegroup:71	
2069	Retinoic acid receptors		RAR		hgnc.genegroup:71	
207	Prostaglandin receptors				hgnc.genegroup:201	
2070	Thyroid hormone receptors		THR		hgnc.genegroup:71	
2071	Peroxisome proliferator activated receptors		PPAR		hgnc.genegroup:71	
2072	Nuclear receptor subfamily 1 group D		NR1D		hgnc.genegroup:71	
2073	Nuclear receptor subfamily 2 group C		NR2C		hgnc.genegroup:71	
2074	Nuclear receptor subfamily 2 group E		NR2E		hgnc.genegroup:71	
2075	Nuclear receptor subfamily 2 group F		NR2F		hgnc.genegroup:71	
2076	Nuclear receptor subfamily 3 group C		NR3C		hgnc.genegroup:71	
2077	Estrogen receptors		ESR		hgnc.genegroup:71	
2078	Estrogen related receptors		ESRR		hgnc.genegroup:71	
2079	Nuclear receptor subfamily 4 group A		NR4A		hgnc.genegroup:71	
208	Platelet activating factor receptor	The platelet-activating factor receptor is a G-protein coupled receptor which binds platelet-activating factor. The PAF receptor shows structural characteristics of the rhodopsin (MIM 180380) gene family and binds platelet-activating factor (PAF). PAF is a phospholipid (1-0-alkyl-2-acetyl-sn-glycero-3-phosphorylcholine) that has been implicated as a mediator in diverse pathologic processes, such as allergy, asthma, septic shock, arterial thrombosis, and inflammatory processes.[supplied by OMIM]   	PTAFR		hgnc.genegroup:201	
2080	Nuclear receptor subfamily 5 group A		NR5A		hgnc.genegroup:71	
2081	Nuclear receptor subfamily 6 group A		NR6A		hgnc.genegroup:71	
2082	RAR related orphan receptors		ROR		hgnc.genegroup:71	
2083	Nuclear receptor subfamily 1 group H		NR1H		hgnc.genegroup:71	
2084	Nuclear receptor subfamily 1 group I		NR1I		hgnc.genegroup:71	
2085	Hepatocyte nuclear factor 4 family		HNF4		hgnc.genegroup:71	
2086	Retinoid X receptors		RXR		hgnc.genegroup:71	
209	Melatonin receptors	A melatonin receptor is a G protein-coupled receptor (GPCR) which binds melatonin. Three types of melatonin receptor have been cloned. The MT 1 (or Mel 1A or MTNR1A) and MT 2 (or Mel 1B or MTNR1B) receptor subtypes are present in humans and other mammals, while an additional melatonin receptor subtype MT 3 (or Mel 1C or MTNR1C) has been identified in amphibia and birds.	MTNR		hgnc.genegroup:140	
2091	SWI/SNF related BAF chromatin remodeling complexes				so:0005855	
2092	Glucosylceramidases		GBA		so:0005855	
2093	2'-5'-oligoadenylate synthetase family	In molecular biology, 2'-5'-oligoadenylate synthetase (2-5A synthetase) is an enzyme (EC 2.7.7.84) that reacts to interferon signal. It is an antiviral enzyme that counteracts viral attack by degrading RNAs, both viral and host. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease (RNASEL), resulting in degradation of viral RNA and inhibition of virus replication.The C-terminal half of 2'-5'-oligoadenylate synthetase, also referred to as domain 2 of the enzyme, is largely alpha-helical and homologous to a tandem ubiquitin repeat. It carries the region of enzymatic activity between at the extreme C-terminal end.	OAS		so:0005855	
2098	Peptidase family A28 				so:0005855	
2099	Peptidase family A22				so:0005855	
21	Non-clustered protocadherins				hgnc.genegroup:19	
210	Nucleotide like receptors				hgnc.genegroup:140	
2101	Cleavage factor Im complex subunits				so:0005855	
2102	Class I HDAC complexes	HDAC1, 2 and 3 form the catalytic subunit of multiprotein complexes to mediate gene transcription although HDAC8 is fully active in isolation. HDAC1 and HDAC2 form the catalytic core of multiple corepressor complexes, including NuRD (nucleosome remodeling and deacetylase), Sin3 (switch intensive 3)  CoREST (corepressor of RE1-silencing transcription) and MiDAC (mitotic deacetylase), while HDAC3 forms the key component of the SMRT/NCoR (silencing mediator of retinoic acid and thyroid hormone receptors/nuclear receptor corepressor) complex. As part of these complexes, the HDACs become maximally activated and are targeted to specific regions of chromatin.			so:0005855	
2103	MiDAC complex subunits				hgnc.genegroup:2102	
2104	Metallopeptidases	A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal.  An example of this would be ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline.			so:0005855	
2105	M48 metallopeptidase family				hgnc.genegroup:2104	
2106	M49 metallopeptidase family				hgnc.genegroup:2104	
2107	M54 metallopeptidase family				hgnc.genegroup:2104	
2108	M76 metallopeptidase family				hgnc.genegroup:2104	
2109	Peptidase family C1				so:0005855	
211	Adenosine receptors	The adenosine receptors (or P1 receptors ) are a class of purinergic receptors, G protein-coupled receptors  with adenosine as endogenous ligand.	ADORA		hgnc.genegroup:210	
2111	Glyoxalase domain containing 	VOC members are metalloenzymes highly divergent in sequence and biological functions, but universally share the use of the βαβββ structural motif (also known as the glyoxylase fold) to build a divalent metal-containing active site. VOC enzymes catalyze a range of chemical reactions including isomerization, epimerization, oxidative C-C bond cleavage and nucleophilic substitution 			so:0005855	
2115	Ferredoxin family		FDX		so:0005855	
2116	Aminoacyl tRNA synthetase complex interacting multifunctional proteins		AIMP		so:0005855	
2117	Tubulin polyglutamylase complex subunits		TPGS		so:0005855	
2118	Leiomodins		LMOD		hgnc.genegroup:1140	
2119	SKI complex subunits				so:0005855	
212	Purinergic receptors	Purinergic receptors, also known as purinoceptors, are a family of plasma membrane molecules that are found in almost all mammalian tissues.  Broadly, purinergic receptors and signaling have been implicated in learning and memory, locomotor and feeding behavior, and sleep.  More specifically, these receptors are involved in several cellular functions, including proliferation and migration of neural stem cells, vascular reactivity, apoptosis and cytokine secretion.  These functions have not been well characterized and the effect of the extracellular microenvironment on their function is also poorly understood. The term purinergic receptor was originally introduced to illustrate specific classes of membrane receptors that mediate relaxation of gut smooth muscle as a response to the release of ATP (P2 receptors) or adenosine (P1 receptors). P2 receptors have further been divided into five subclasses: P2X, P2Y, P2Z, P2U, and P2T. To distinguish P2 receptors further, the subclasses have been divided into families of metabotropic (P2Y, P2U, and P2T) and ionotropic receptors (P2X and P2Z).	P2R		so:0005855	
2120	Fc receptors				so:0005855	
2124	Eukaryotic translation initiation factor 2 alpha kinases		EIF2AK		so:0005855	
2125	Zinc fingers PCLO-type	Piccolo zinc fingers were found to interact with the dual prenylated rab3A and VAMP2/Synaptobrevin II receptor PRA1. There are eight conserved cysteines in Piccolo-type zinc fingers, suggesting that they coordinate two zinc ligands.			hgnc.genegroup:26	
2126	SCF complex core subunits				hgnc.genegroup:1171	
2127	PAS domain containing		PASD		so:0005855	
2128	MIF4G domain containing proteins				so:0005855	
2129	MD-2 related lipid recognition domain containing				so:0005855	
213	P2Y receptors		P2RY		hgnc.genegroup:212|hgnc.genegroup:210	
2130	GIY-YIG endonuclease domain containing		GIYD		so:0005855	
2131	SIK family kinases		SIK		hgnc.genegroup:2133	
2132	Microtubule affinity regulating kinases		MARK		hgnc.genegroup:2133	
2133	PRKAA related kinases				so:0005855	
2134	Protein kinase AMP-activated catalytic subunit alphas		PRKAA		hgnc.genegroup:2133	
2135	BR serine/threonine kinases		BRSK		hgnc.genegroup:2133	
2136	NUAK family kinases		NUAK		hgnc.genegroup:2133	
2137	MELK family kinases		MELK		hgnc.genegroup:2133	
2139	Zinc fingers TRAF-type	This entry represents TRAF-type zinc finger domains. Some of the proteins that have this domain are mammalian signal transducers associated with the cytoplasmic domain of the 75kDa tumour necrosis factor receptor <a href='https://pubmed.ncbi.nlm.nih.gov/11607847/'>PMID: 11607847</a>. A heterocomplex, homodimer or heterodimer of TRAF1 and TRAF2, binds to the N-terminal of the inhibitor of apoptosis proteins 1 and 2 (IAPS) and recruits them to the tumour necrosis factor receptor 2. 			hgnc.genegroup:26	
214	Purinergic receptors P2X	P2X receptors are a family of cation-permeable ligand gated ion channels that open in response to the binding of extracellular adenosine 5'-triphosphate ( ATP ). They belong to a larger family of receptors known as the purinergic receptors. P2X receptors are present in a diverse array of organisms including humans, mouse, rat, rabbit, chicken, zebrafish, bullfrog, fluke, and amoeba. 	P2RX		hgnc.genegroup:212|hgnc.genegroup:161	
2140	Phosphorylase kinase subunits		PHK		so:0005855	
2141	Bridge-like lipid transfer protein family		BLTP		so:0005855	
2142	Serine hydroxymethyltransferase family		SHMT		so:0005855	
2144	Protein kinase A subunits	In cell biology, protein kinase A (PKA) is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase (AMP-activated protein kinase).			so:0005855	
2147	Lysophospholipid acyltransferases	Phospholipids can be produced by several metabolic routes, and a key reaction that utilizes lysophospholipids and acyl-CoAs as substrates to produce phospholipids is catalyzed by a class of enzymes called lysophospholipid acyltransferases (LPLATs). Based on their primary structures, these LPLATs are divided into two families, the 1-acylglycerol-3-phosphate O-acyltransferase (AGPAT) and the membrane bound O-acyltransferase (MBOAT) families. These two families also contain non-LPLAT members.			so:0005855	
2148	Alpha-2-macroglobulin family				hgnc.genegroup:1234	
215	Opsin receptors	Opsins are a group of light-sensitive 35–55 kDa membrane-bound G protein-coupled receptors of the retinylidene protein family found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade.	OPN		hgnc.genegroup:140	
2150	Teneurin transmembrane protein family		TENM		so:0005855	
2151	thymocyte selection associated high mobility group box family		TOX		so:0005855	
2152	Solute carrier family 12		SLC12		hgnc.genegroup:752	
2153	Solute carrier family 39 		SLC39		hgnc.genegroup:752	
2154	Solute carrier family 1		SLC1		hgnc.genegroup:752	
2155	Solute carrier family 2		SLC2		hgnc.genegroup:752	
2156	Solute carrier family 3		SLC3		hgnc.genegroup:752	
2157	Solute carrier family 4		SLC4		hgnc.genegroup:752	
2158	Solute carrier family 5		SLC5		hgnc.genegroup:752	
2159	Solute carrier family 6		SLC6		hgnc.genegroup:752	
216	Prokineticin receptors	The prokineticin receptor is a G protein-coupled receptor which binds the peptide hormone prokineticin. There are two variants each encoded by a different gene ( PROKR1, PROKR2 ).  These receptors mediate gastrointestinal smooth muscle contraction and angiogenesis.	PROKR		hgnc.genegroup:140	
2160	Solute carrier family 7		SLC7		hgnc.genegroup:752	
2161	Solute carrier family 8		SLC8		hgnc.genegroup:752	
2162	Solute carrier family 9		SLC9		hgnc.genegroup:752	
2163	Solute carrier family 10		SLC10		hgnc.genegroup:752	
2164	Solute carrier family 11		SLC11		hgnc.genegroup:752	
2165	Solute carrier family 13		SLC13		hgnc.genegroup:752	
2166	Solute carrier family 14		SLC14		hgnc.genegroup:752	
2167	Solute carrier family 15		SLC15		hgnc.genegroup:752	
2168	Solute carrier family 16		SLC16		hgnc.genegroup:752	
2169	Solute carrier family 17		SLC17		hgnc.genegroup:752	
217	Relaxin family peptide receptors		RXFP		hgnc.genegroup:140	
2170	Solute carrier family 18		SLC18		hgnc.genegroup:752	
2171	Solute carrier family 19		SLC19		hgnc.genegroup:752	
2172	Solute carrier family 20		SLC20		hgnc.genegroup:752	
2173	Solute carrier family 22		SLC22		hgnc.genegroup:752	
2174	Solute carrier family 23		SLC23		hgnc.genegroup:752	
2175	Solute carrier family 24		SLC24		hgnc.genegroup:752	
2176	Solute carrier family 25		SLC25		hgnc.genegroup:752	
2177	Solute carrier family 26		SLC26		hgnc.genegroup:752	
2178	Solute carrier family 27		SLC27		hgnc.genegroup:752	
2179	Solute carrier family 28		SLC28		hgnc.genegroup:752	
218	Chemerin receptors		CMKLR		hgnc.genegroup:140	
2180	Solute carrier family 29		SLC29		hgnc.genegroup:752	
2181	Solute carrier family 30		SLC30		hgnc.genegroup:752	
2182	Solute carrier family 31		SLC31		hgnc.genegroup:752	
2183	Solute carrier family 32		SLC32		hgnc.genegroup:752	
2184	Solute carrier family 33		SLC33		hgnc.genegroup:752	
2185	Solute carrier family 34		SLC34		hgnc.genegroup:752	
2186	Solute carrier family 35		SLC35		hgnc.genegroup:752	
2187	Solute carrier family 36		SLC36		hgnc.genegroup:752	
2188	Solute carrier family 38		SLC38		hgnc.genegroup:752	
2189	Solute carrier family 37		SLC37		hgnc.genegroup:752	
219	F2R receptors	Protease-activated receptors are a subfamily of related G protein-coupled receptors that are activated by cleavage of part of their extracellular domain. They are highly expressed in platelets, but also on endothelial cells, myocytes and neurons.	F2R		hgnc.genegroup:140	
2190	Solute carrier family 40		SLC40		hgnc.genegroup:752	
2191	Solute carrier family 41		SLC41		hgnc.genegroup:752	
2192	Solute carrier family 42		SLC42		hgnc.genegroup:752	
2193	Solute carrier family 43		SLC43		hgnc.genegroup:752	
2194	Solute carrier family 44		SLC44		hgnc.genegroup:752	
2195	Solute carrier family 45		SLC45		hgnc.genegroup:752	
2196	Solute carrier family 46		SLC46		hgnc.genegroup:752	
2197	Solute carrier family 47		SLC47		hgnc.genegroup:752	
2198	Solute carrier family 48		SLC48		hgnc.genegroup:752	
2199	Solute carrier family 49		SLC49, FLVCR		hgnc.genegroup:752	
220	Peptide receptors	A subclass of 'G protein-coupled receptors, Class A rhodopsin-like receptors' that bind peptide ligands via the transmembrane helices and the extracellular loops of the receptor.			hgnc.genegroup:140	
2200	Solute carrier family 50		SLC50		hgnc.genegroup:752	
2202	Solute carrier family 52		SLC52		hgnc.genegroup:752	
2203	Solute carrier family 53		SLC53		hgnc.genegroup:752	
2204	Solute carrier family 54, mitochondrial pyruvate carriers		SLC54, MPC		hgnc.genegroup:752	
2205	Solute carrier family 55, LETM mitochondrial cation/proton exchangers		SLC55, LETM		hgnc.genegroup:752	
2206	Solute carrier family 57, NIPA-like magnesium transporters		SLC57, NIPA		hgnc.genegroup:752	
2207	Solute carrier family 58		SLC58		hgnc.genegroup:752	
2208	Solute carrier family 59		SLC59		hgnc.genegroup:752	
2209	Solute carrier family 60		SLC60, MFSD4		hgnc.genegroup:752	
221	Angiotensin receptors	The angiotensin receptors are a class of G protein-coupled receptors with angiotensin II as their ligands. They are important in the renin-angiotensin system : they are responsible for the signal transduction of the vasoconstricting stimulus of the main effector hormone, angiotensin II.	AGTR		hgnc.genegroup:220	
2210	Solute carrier family 61		SLC61, MFSD5		hgnc.genegroup:752	
2211	Solute carrier family 62		SLC62, ANKH		hgnc.genegroup:752	
2212	Solute carrier family 63, sphingosine phosphate transporters		SLC63, SPNS		hgnc.genegroup:752	
2213	Solute carrier family 64		SLC64, TMEM165		hgnc.genegroup:752	
2214	Solute carrier family 65, NPC-type cholesterol transporters		SLC65, NPC1		hgnc.genegroup:752	
2215	Solute carrier family 66		SLC66		hgnc.genegroup:752	
2216	Solute carrier organic anion transporter family		SLCO		hgnc.genegroup:752	
2217	Dispatched RND transporter family 		DISP		so:0005855	
2219	Transmembrane protein 14 family		TMEM14		so:0005855	
222	Bombesin receptors				so:0005855	
2223	Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex				so:0005855	
2224	Tubulin gamma complex component family		TUBGCP		so:0005855	
2226	NHERF family PDZ scaffold proteins		NHERF		so:0005855	
2229	TSNAXIP1 domain containing				so:0005855	
223	Bradykinin receptors	The bradykinin receptor family is a group of G-protein coupled receptors whose principal ligand is the protein bradykinin. There are two Bradykinin receptors: the B 1 receptor and the B 2 receptor.	BDKR		hgnc.genegroup:220	
2230	YTH domain containing N6-methyladenosine readers		YTH		so:0005855	
2231	Thrombospondin family		THBS		so:0005855	
2232	Isthmin family		ISM		so:0005855	
2234	Methionine adenosyltransferase family		MAT		so:0005855	
2239	STAG family cohesin complex components		STAG		so:0005855	
224	Cholecystokinin receptors	Cholecystokinin receptors or CCK receptors are a group of G-protein coupled receptors which bind the peptide hormones cholecystokinin (CCK) or gastrin. There are two different subtypes CCK A and CCK B which are ~50% homologous : Various cholecystokinin antagonists have been developed and are used in research, although the only drug of this class that has been widely marketed to date is the anti-ulcer drug proglumide. 			hgnc.genegroup:220	
2240	Nebulin family				so:0005855	
2241	Gfo/Idh/MocA-like oxidoreductase domain containing	The Gfo/Idh/MocA protein family members have very low sequence identity but the 3D structures of the proteins are very similar, consisting of two main domains: an N-terminal dinucleotide-binding domain containing a typical Rossmann fold3 and a C-terminal α/β-domain participating in substrate binding and oligomerisation. [Note the BLVRA gene included here encodes a protein with the N-terminal, but not C-terminal domain].			so:0005855	
2242	Basonuclin zinc finger proteins		BNC		so:0005855	
2243	Prokineticin family		PROK		so:0005855	
2244	Prominin family		PROM		so:0005855	
2245	Secretory calcium-binding phosphoprotein family				so:0005855	
2246	FERRY complex subunits				so:0005855	
2247	Fibrillar collagens		COL		hgnc.genegroup:490	
2248	Fibril associated collagens with interrupted triple helices		COL		hgnc.genegroup:490	
2249	Network forming collagens		COL		hgnc.genegroup:490	
225	Endothelin receptors		EDNR		hgnc.genegroup:220	
2250	Membrane associated collagens with interrupted triple helices		COL		hgnc.genegroup:2251	
2251	Transmembrane collagens		COL		hgnc.genegroup:490	
2252	Multiplexin collagens		COL		hgnc.genegroup:490	
2253	EPS8 signaling adaptor family		EPS8		so:0005855	
2258	Flavoproteins	Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes. Flavoproteins have either FMN (flavin mononucleotide) or FAD (flavin adenine dinucleotide) as a prosthetic group or as a cofactor. The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). About 5-10% of flavoproteins have a covalently linked FAD. Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. Flavoproteins are mainly located in the mitochondria. Of all flavoproteins, 90% perform redox reactions and the other 10% are transferases, lyases, isomerases, ligases.			so:0005855	
2259	VCP-Ufd1-Npl4 complex subunits				so:0005855	
226	Galanin receptors	The galanin receptor is a G protein-coupled receptor, or metabotropic receptor which binds galanin. Galanin receptors can be found throughout the peripheral and central nervous systems and the endocrine system. So far three subtypes are known to exist: GAL-R1, GAL-R2, and GAL-R3. The specific function of each subtype remains to be fully elucidated, although as of 2009 great progress is currently being made in this respect with the generation of receptor subtype-specific knockout mice,  and the first selective ligands for galanin receptor subtypes. Selective galanin agonists are anticonvulsant,  while antagonists produce antidepressant and anxiolytic effects in animals,   so either agonist or antagonist ligands for the galanin receptors may be potentially therapeutic compounds in humans.	GALR		hgnc.genegroup:220	
2261	Ceramide synthases		CERS		so:0005855	
2262	MAF bZIP transcription factor family 		MAF		hgnc.genegroup:506	
2263	Small MAF bZIP transcription factor family				hgnc.genegroup:2262	
2264	Large MAF bZIP transcription factor family				hgnc.genegroup:2262	
2265	Mitofusin family		MFN		so:0005855	
2269	NHS family		NHS		so:0005855	
227	Gonadotropin releasing hormone receptors	The gonadotropin-releasing hormone receptor (GNRHR), also known as the luteinizing hormone releasing hormone receptor ( LHRHR ), is a member of the seven-transmembrane, G-protein coupled receptor (GPCR) family. It is expressed on the surface of pituitary gonadotrope cells as well as lymphocytes, breast, ovary, and prostate. This receptor is a 60 kDa G protein-coupled receptor and resides primarily in the pituitary and is responsible for eliciting the actions of LHRH after its release from the hypothalamus. Upon activation, the LHRHr stimulates tyrosine phosphatase and elicits the release of LH from the pituitary. Evidence exists showing the presence of LHRH and its receptor in extrapituitary tissues as well as a role in progression of some cancers.	GNRHR		hgnc.genegroup:220	
2274	Solute carrier family 51		SLC51		hgnc.genegroup:752	
2279	Canonical Notch ligands	 The canonical Notch ligands are members of the Delta/Serrate/Lag-1 (DSL) family of proteins. When they bind to Notch receptors this induces a conformational change (regulated intramembrane proteolysis) in the receptor, freeing its Notch intracellular domain (NICD). The NICD can then translocate to the nucleus and promote gene transcription.  			so:0005855	
228	Hypocretin receptors		HCRTR		hgnc.genegroup:220	
2280	DREAM complex subunits	The dimerization partner, RB-like, E2F and multi-vulval class B (DREAM) complex is a protein complex responsible for the regulation of cell cycle-dependent gene expression. The complex is evolutionarily conserved, although some of its components vary from species to species. In humans, the key proteins in the complex are RBL1 (p107) and RBL2 (p130), both of which are homologs of RB (p105) and bind repressive E2F transcription factors E2F4 and E2F5; DP1, DP2 and DP3, dimerization partners of E2F; and MuvB, which is a complex of LIN9/37/52/54 and RBBP4.			so:0005855	
2281	MuvB complex subunits	MuvB complexes are key to regulating the cell-division cycle. The MuvB complex can form part of the transcriptional repressor complex DREAM, or part of the activator complexes MMB and FOXM1-MuvB.  When cells are not actively dividing, the DREAM complex represses G1/S and G2/M genes. The expression of mitotic genes in the G2/M stage of the cell cycle can be regulated by MuvB activator complexes which include either the oncogenic transcription factor B-MYB or FOXM1.			hgnc.genegroup:2280|hgnc.genegroup:2282|hgnc.genegroup:2283	
2282	MMB complex subunits				so:0005855	
2283	FOXM1-MMB complex subunits				so:0005855	
2285	Zinc fingers A20-type	This gene group represents genes encoding proteins with the zinc finger domain found in TNFAIP3, also known as A20. A20 is an inhibitor of cell death that inhibits NF-kappaB activation via the tumour necrosis factor receptor associated factor pathway <a href='https://pubmed.ncbi.nlm.nih.gov/17449604/'>(PMID: 17449604)</a>. The zinc finger domains appear to mediate self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.			hgnc.genegroup:26	
2286	RNA binding fox-1 homologs	The RNA-binding Fox-1 homolog (RBFOX) proteins represent an ancient family of splicing factors, conserved through evolution. All members share an RNA recognition motif (RRM), and a particular affinity for the GCAUG signature in target RNA molecules.	RBFOX		so:0005855	
2288	Chymotrypsins		CTR		so:0005855	
2289	Mitochondrial transcription initiation complex subunits				hgnc.genegroup:2290	
2290	Mitochondrial nucleoid associated proteins				so:0005855	
2291	ELAV like RNA binding protein family		ELAVL		so:0005855	
2293	Proteins encoded by multiple genes	This group lists protein coding genes that encode a protein that is identical to that encoded by another gene or genes. The list was constructed from a set of UniProt accessions that are associated with multiple genes. The list is limited to genes on the current reference assembly and excludes proteins encoded by read-through transcripts. Genes that encode the same protein share root symbols. Note the H3C root is associated with two different proteins - one encoded by a cluster of genes on 6p22.1 and the other by a cluster of three genes on 1q21.2 (H3C13-15).			so:0005855	
2295	LAR (PTPRF) protein receptor tyrosine phosphatase family 				so:0005855	
2296	Retrotransposon derived genes				hgnc.genegroup:1416	
2297	Integrase like retrotransposon derived				hgnc.genegroup:2296	
2300	Regulins				so:0005855	
2302	TSPYL family		TSPYL		hgnc.genegroup:2305	
2303	TSPY family		TSPY		hgnc.genegroup:2305	
2304	Nucleosome assembly protein 1 like family		NAP1L		hgnc.genegroup:2305	
2305	Nucleosome assembly protein superfamily				so:0005855	
2307	Storkhead boxes		STOX		so:0005855	
2308	SH3 and cysteine rich domain family		STAC		so:0005855	
2309	Sprouty related EVH1 domain containing 		SPRED		so:0005855	
2310	Sprouty RTK signaling antagonist family		SPRY		so:0005855	
2312	SplA/ryanodine receptor domain and SOCS box containing family		SPSB		so:0005855	
2313	ZU5 domain containing 				so:0005855	
2314	Olfactomedin domain containing 		OLFM		so:0005855	
2315	Neurexophilins		NXPH		hgnc.genegroup:2317	
2316	Neurexophilin and PC-esterase domain containing		NXPE		hgnc.genegroup:2317	
2317	Neurexophilin domain containing		NXP		so:0005855	
2318	Complexins	Complexin (also known as synaphin) refers to a one of a small set of eukaryotic cytoplasmic neuronal proteins which binds to the  SNARE protein complex (SNAREpin) with a high affinity. These are called synaphin 1 and 2. In the presence of Ca2+, the transport vesicle protein synaptotagmin displaces complexin, allowing the SNARE protein complex to bind the transport vesicle to the presynaptic membrane. Complexin acts as both an inhibitor and a facilitator of synaptic vesicle fusion and neurotransmitter release. In one conformation, it clamps SNAREpin complexes, preventing vesicle fusion, while in a different conformation it releases the SNAREpins, allowing synaptotagmin to trigger fusion.  Whereas complexin is not necessary for synaptic vesicle exocytosis, it does increase neurotransmitter release by 60–70% as demonstrated by complexin gene knockout in mice. A number of human neurological diseases have been linked to a deficiency of complexin. Synaphin can promote exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.	CPLX		so:0005855	
2319	Pecanex family		PCNX		so:0005855	
2320	Canopy FGF signaling regulators		CNPY		so:0005855	
2321	RAS guanyl releasing proteins		RASGRP		so:0005855	
2322	Reticulons	Reticulons (RTNs in vertebrates and reticulon-like proteins or RNTls in other eukaryotes) are a group of evolutionary conservative proteins residing predominantly in endoplasmic reticulum, primarily playing a role in promoting membrane curvature. In addition, reticulons may play a role in nuclear pore complex formation, vesicle formation, and other processes yet to be defined. They have also been linked to oligodendrocyte roles in inhibition of neurite outgrowth. Some studies link RTNs with Alzheimer's disease and amyotrophic lateral sclerosis.All eukaryotes studied so far carry RTN genes in their genomes. The reticulons are absent only in archaea and bacteria. Mammals have four reticulon genes, RTN1, RTN2, RTN3, RTN4. Plants possess a greater number of reticulon isoforms, with 21 having been identified in the commonly used model organism Arabidopsis thaliana.The genes possess a number of exons and introns and are accordingly spliced into many isoforms. C-terminal region of RTNs contains a highly conservative reticulon homology domain (RHD) while other parts of the protein may vary even within a single organism.A peculiar feature of RTN4's isoform RTN4A (Nogo-A) is its ability to inhibit axonal growth. This reticulon subform is curiously absent in fish, a taxon known for the heightened ability of its CNS to regenerate after injury. Transmembrane 33 (TMEM33) exogenously suppresses reticulon 4C function and therefore may play a role in dictating membrane curvature through inhibition of reticulon function.	RTN		so:0005855	
2323	Golgi associated RAB2 interactor family		GARIN		so:0005855	
2324	Leucine rich repeats and calponin homology domain containing		LRCH		so:0005855	
2326	Cornichon family		CNIH		so:0005855	
2327	Angiopoietins	Angiopoietin is part of a family of vascular growth factors that play a role in embryonic and postnatal angiogenesis. Angiopoietin signaling most directly corresponds with angiogenesis, the process by which new arteries and veins form from preexisting blood vessels. Angiogenesis proceeds through sprouting, endothelial cell migration, proliferation, and vessel destabilization and stabilization. They are responsible for assembling and disassembling the endothelial lining of blood vessels. Angiopoietin cytokines are involved with controlling microvascular permeability, vasodilation, and vasoconstriction by signaling smooth muscle cells surrounding vessels.  Angiopoietin-1 is critical for vessel maturation, adhesion, migration, and survival. Angiopoietin-2, on the other hand, promotes cell death and disrupts vascularization. Yet, when it is in conjunction with vascular endothelial growth factors, or VEGF, it can promote neo-vascularization.	ANGPT		so:0005855	
2328	LysM domain containing		LYSMD		so:0005855	
2329	DEP domain containing				so:0005855	
235	Melanin concentrating hormone receptors	Two Melanin-concentrating hormone receptors ( MCHR ) have recently been characterized: MCH-R1 and MCH-R2. These two receptors share approximately 38% homology.	MCHR		hgnc.genegroup:220	
236	Melanocortin receptors	Melanocortin receptors are members of the rhodopsin family of 7-transmembrane G protein-coupled receptors. There are five known members of the melanocortin receptor system  each with differing specificities for melanocortins :   MC1R. MC1R is associated with pigmentation genetics. MC2R. MC2R is also known as the ACTH receptor or corticotropin receptor because it is specific for ACTH alone. MC3R. MC3R MC4R. Defects in MC4R are a cause of autosomal dominant obesity, accounting for 6% of all cases of early-onset obesity.  MC5R. MC5R  These receptors are inhibited by endogenous inverse agonists agouti signalling peptide and agouti-related peptide, and activated by synthetic (i.e. afamelanotide ) and endogenous agonist melanocyte-stimulating hormones.			hgnc.genegroup:220	
239	Neuromedin U receptors	The neuromedin U receptors are two G-protein coupled receptors which bind the neuropeptide hormones neuromedin U and neuromedin S. There are two subtypes of the neuromedin U receptor, each encoded by a separate gene ( NMUR1, NMUR2 ).	NMUR		hgnc.genegroup:220	
24	Cadherin related	The cadherin-related (CDHR) genes do not fit into the major cadherin or protocadherin families as they are phylogenetically clearly separated. The encoded proteins comprise at least two typical, consecutive cadherin motifs, but often more than the typical members of the cadherin and protocadherin families. Their overall domain organization differs from the members of the major cadherin family and the protocadherin family, and includes different and unique cytoplasmic domains.	CDHR		hgnc.genegroup:16	
240	Neuropeptide FF receptors	The neuropeptide FF receptors are members of the G-protein coupled receptor superfamily of integral membrane proteins which bind the pain modulatory neuropeptides AF and FF. The Neuropeptide FF receptor family is a member of the G protein-coupled receptor superfamily containing two subtypes, NPFF1 and NPFF2, which exhibit a high affinity for Neuropeptide FF (NPFF) peptides. NPFF1 is broadly distributed in the central nervous system with the highest levels found in the limbic system and the hypothalamus. NPFF2 is present in high density, particularly in mammals in the superficial layers of the spinal cord where it is involved in nociception and modulation of opioid functions These receptors participate to the modulation of opioid receptor function in the brain and spinal cord, and can either reduce or increase opioid receptor function depending which tissue they are released in, reflecting a complex role for neuropeptide FF in pain responses. 	NPFFR		hgnc.genegroup:220	
241	Neuropeptide S receptor	The neuropeptide S receptor ( NPSR ) is a member of the G-protein coupled receptor superfamily of integral membrane proteins  which binds neuropeptide S (NPS).  It was formerly an orphan receptor, GPR154, until the discovery of neuropeptide S as the endogenous ligand. In the CNS, activation of the NPSR by NPS promotes arousal and anxiolytic -like effects.  In addition, mututations in NPSR have been linked to a susceptibility to asthma. Hence NPSR has also been called GPRA (G protein-coupled receptor for asthma susceptibility). Activation of NPSR in the airway epithelium has a number of effects including upregulation of matrix metalloproteinases which are involved in the pathogenesis of asthma.  This gene is a member of the G protein-coupled receptor 1 family and encodes a plasma membrane protein. Increased expression of this gene in ciliated cells of the respiratory epithelium and in bronchial smooth muscle cells is associated with asthma. Mutations in this gene have also been associated with this disease. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.	NPSR		hgnc.genegroup:220	
242	Neuropeptides B and W receptors		NPBWR		hgnc.genegroup:220	
243	Neuropeptide Y receptors	Neuropeptide Y receptors are a class of G-protein coupled receptors which are activated by the closely related peptide hormones neuropeptide Y, peptide YY and pancreatic polypeptide. These receptors are involved in the control of a diverse set of behavioral processes including appetite, circadian rhythm, and anxiety.    Activated neuropeptide receptors release the G i subunit from the heterotrimeric G protein complex. The G i subunit in turn inhibits the production of the second messenger cAMP from ATP.			hgnc.genegroup:220	
244	Neurotensin receptors		NTSR		hgnc.genegroup:220	
245	Opioid receptors	Opioid receptors are a group of G protein-coupled receptors with opioids as ligands.  The endogenous opioids are dynorphins, enkephalins, endorphins, endomorphins and nociceptin. The opioid receptors are ~40% identical to somatostatin receptors (SSTRs). Opiate receptors are distributed widely in the brain, and are found in the spinal cord and digestive tract.	OPR		hgnc.genegroup:220	
247	Two pore segment channels	This small family of 2 members putatively forms cation-selective ion channels. They are predicted to contain two KV-style six-transmembrane domains, suggesting they form a dimer in the membrane. These channels are closely related to CatSper channels and, more distantly, to TRP channels.	TPCN		hgnc.genegroup:178|hgnc.genegroup:182	
249	Transient receptor potential cation channels	Transient receptor potential channels (TRP channels) are a group of ion channels located mostly on the plasma membrane of numerous human and animal cell types. There are about 28 TRP channels that share some structural similarity to each other.  These are grouped into two broad groups: Group 1 includes TRPC ( 'C' for canonical), TRPV ('V' for vanilloid), TRPM ('M' for melastatin), TRPN, and TRPA. In group 2, there are TRPP ('P' for polycystic) and TRPML ('ML' for mucolipin). Many of these channels mediate a variety of sensations like the sensations of pain, hotness, warmth or coldness, different kinds of tastes, pressure, and vision. In the body, some TRP channels are thought to behave like microscopic thermometers and used in animals to sense hot or cold. Some TRP channels are activated by molecules found in spices like garlic ( allicin ), chilli pepper ( capsaicin ), wasabi ( allyl isothiocyanate ); others are activated by menthol, camphor, peppermint, and cooling agents; yet others are activated by molecules found in cannabis (i.e., THC, CBD and CBN ). Some act as sensors of osmotic pressure, volume, stretch, and vibration. These ion channels are relatively non-selectively permeable to cations, including sodium, calcium and magnesium. TRP channels were initially discovered in trp -mutant strain of the fruit fly Drosophila. Later, TRP channels were found in vertebrates where they are ubiquitously expressed in many cell types and tissues. Most TRP channels are composed of 6 membrane -spanning helices with intracellular N- and C-termini. Mammalian TRP channels are activated and regulated by a wide variety of stimuli and are expressed throughout the body.	TRP		hgnc.genegroup:178	
250	Cyclic nucleotide gated channels	Cyclic nucleotide-gated ion channels or CNG channels are ion channels that function in response to the binding of cyclic nucleotides. CNG channels are nonselective cation channels that are found in the membranes of various tissue and cell types, and are significant in sensory transduction as well as cellular development. Their function can be the result of a combination of the binding of cyclic nucleotides (cGMP and cAMP) and either a depolarization or a hyperpolarization event. Initially discovered in the cells that make up the retina of the eye, CNG channels have been found in many different cell types across both the animal and the plant kingdoms. CNG channels have a very complex structure with various subunits and domains that play a critical role in their function. CNG channels are significant in the function of various sensory pathways including vision and olfaction, as well as in other key cellular functions such as hormone release and chemotaxis.	CNG		hgnc.genegroup:178	
253	Calcium voltage-gated channel subunits	Voltage-dependent calcium channels ( VDCC ) are a group of voltage-gated ion channels found in the membrane of excitable cells ( e.g., muscle, glial cells, neurons, etc.) with a permeability to the calcium ion Ca 2+.  These channels are slightly permeable to sodium ions, so they are also called Ca 2+ -Na + channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions.  At physiologic or resting membrane potential, VDCCs are normally closed. They are activated ( i.e., opened) at depolarized membrane potentials and this is the source of the 'voltage-dependent' epithet. The concentration of calcium (Ca 2+ ions) is normally several thousand times higher outside of the cell than inside. Activation of particular VDCCs allows Ca 2+ to rush into the cell, which, depending on the cell type, results in activation of calcium-sensitive potassium channels, muscular contraction, excitation of neurons, up-regulation of gene expression, or release of hormones or neurotransmitters. Excessive activation of VDCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium activates enzymes which, at high enough levels, can degrade essential cellular structures.	CACN		hgnc.genegroup:178|hgnc.genegroup:182	
254	Hydrogen voltage gated channels		HVCN		hgnc.genegroup:178	
255	Potassium calcium-activated channels	Calcium-activated potassium channels are divided into BK [KCNMA1] channels, IK [KCNN4] channels, and SK [KCNN1-3] channels based on their conductance (big, intermediate, and small conductance).			hgnc.genegroup:178|hgnc.genegroup:183	
257	Somatostatin receptors		SSTR		hgnc.genegroup:220	
258	Tachykinin receptors	There are three known mammalian tachykinin receptors. All are members of the 7 transmembrane G-protein coupled receptor family and induce the activation of phospholipase C, producing inositol triphosphate (so called G q-coupled).	TACR		hgnc.genegroup:220	
259	Arginine vasopressin and oxytocin receptors	The actions of vasopressin are mediated by stimulation of tissue-specific G protein-coupled receptors (GPCRs) called vasopressin receptors that are classified into V1, V2 and V3 subtypes.  These three subtypes differ in localization, function and signal transduction mechanisms. 	AVPR		hgnc.genegroup:220	
26	Zinc fingers	A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions in order to stabilize the fold. Originally coined to describe the finger-like appearance of a hypothesized structure from Xenopus laevis transcription factor IIIA, the zinc finger name has now come to encompass a wide variety of differing protein structures.  Proteins that contain zinc fingers ( zinc finger proteins ) are classified into several different structural families. Unlike many other clearly defined supersecondary structures such as Greek keys or beta hairpins, there are a number of unique types of zinc fingers, each with a unique three-dimensional architecture. A particular zinc finger protein's class is determined by this three-dimensional structure, but it can also be recognized based on the primary structure of the protein or the identity of the ligands coordinating the zinc ion. In spite of the large variety of these proteins, however, the vast majority typically function as interaction modules that bind DNA, RNA, proteins, or other small, useful molecules, and variations in structure serve primarily to alter the binding specificity of a particular protein. Since their original discovery and the elucidation of their structure, these interaction modules have proven ubiquitous in the biological world. In addition, zinc fingers have become extremely useful in various therapeutic and research capacities. Engineering zinc fingers to have an affinity for a specific sequence is an area of active research, and zinc finger nucleases and zinc finger transcription factors are two of the most important applications of this to be realized to date.			so:0005855	
262	G protein-coupled receptors, Class A orphans	This set contains class A 'orphan' G protein coupled receptors where the endogenous ligand(s) is not known.			hgnc.genegroup:140	
263	G protein-coupled receptors, Class B secretin-like				hgnc.genegroup:139	
264	Vasoactive intestinal peptide family receptors 				hgnc.genegroup:263	
265	Calcitonin receptors	The calcitonin receptor (CT) is a G protein-coupled receptor that binds the peptide hormone calcitonin and is involved in maintenance of calcium homeostasis, particularly with respect to bone formation and metabolism.   CT works by activating the G-proteins G s and G q often found on osteoclasts, on cells in the kidney, and on cells in a number of regions of the brain.  It may also affect the ovaries in women and the testes in men. The function of the CT receptor protein is modified through its interaction with Receptor activity-modifying proteins (RAMPs), forming the multimeric amylin receptors AMY 1 (CT + RAMP1), AMY 2 (CT + RAMP2), and AMY 3 (CT+ RAMP3).	CALCR		hgnc.genegroup:263	
266	Corticotropin releasing hormone receptors		CRHR		hgnc.genegroup:263	
269	Glucagon receptor family				hgnc.genegroup:263	
27	ANP32 acidic nuclear phosphoproteins		ANP32		so:0005855	
270	Parathyroid hormone receptors	There are two known parathyroid hormone receptors in mammals termed PTH1R and PTH2R. These receptors bind parathyroid hormone and are members of the GPCR family of transmembrane proteins.  parathyroid hormone 1 receptor (PTH1R) is the classical PTH receptor, is expressed in high levels in bone and kidney and regulates calcium ion homeostasis through activation of adenylate cyclase and phospholipase C.    parathyroid hormone 2 receptor (PTH2R) is expressed primarily in the central nervous system, pancreas, testis, and placenta.			hgnc.genegroup:263	
274	Potassium voltage-gated channels	Voltage-gated potassium channels are transmembrane channels specific for potassium and sensitive to voltage changes in the cell's membrane potential. During action potentials, they play a crucial role in returning the depolarized cell to a resting state.			hgnc.genegroup:178|hgnc.genegroup:183	
275	G protein-coupled receptors, Class C metabotropic glutamate/pheromone	The class C G-protein-coupled receptors (IPR000337) are a class of G-protein coupled receptors that include the metabotropic glutamate receptors (IPR000162) and several additional receptors.  Family C GPCRs have a large extracellular N-terminus which binds the orthosteric (endogenous) ligand. The shape of this domain is often likened to a clam. Several allosteric ligands to these receptors have been identified and these bind within the seven transmembrane region.			hgnc.genegroup:139	
276	Potassium inwardly rectifying channel subfamily J	Inwardly rectifying potassium channels ( Kir, IRK ) are a specific subset of potassium selective ion channels. To date, seven subfamilies have been identified in various mammalian cell types  and they are also found in plants.  They are the targets of multiple toxins, and malfunction of the channels has been implicated in several diseases.	KCNJ		hgnc.genegroup:183	
277	Potassium two pore domain channel subfamily K 	The two-pore-domain potassium channel a family of 15 members form what is known as 'leak channels' which possess Goldman-Hodgkin-Katz (open) rectification. These channels are regulated by several mechanisms including oxygen tension, pH, mechanical stretch, and G-proteins.  Their name is derived from the fact that the alpha subunits consist of four transmembrane segments, each containing two pore loops. As such, they structurally correspond to two inward-rectifier alpha subunits and thus form dimers in the membrane.	KCNK		hgnc.genegroup:178|hgnc.genegroup:183	
278	Chloride channels	Chloride channels are a superfamily of poorly understood ion channels consisting of approximately 13 members. Chloride channels display a variety of important physiological and cellular roles that include regulation of pH, volume homeostasis, organic solute transport, cell migration, cell proliferation and differentiation. Based on sequence homology the chloride channels can be subdivided into a number of groups. The importance of one such group, the CLC family of chloride channels, can be seen from the diseases that develop when the channel does not function normally. This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three CLC subfamilies are found in animals. CLC-1 ( P35523 ) is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two CBS domains. Chloride channels are also important for maintaining safe ion concentrations within plant cells.			hgnc.genegroup:292	
279	Calcium sensing receptors	The calcium-sensing receptor (CaSR) is a Class C G-protein coupled receptor which senses extracellular levels of calcium ion. In the parathyroid gland, the calcium-sensing receptor controls calcium homeostasis by regulating the release of parathyroid hormone (PTH).			hgnc.genegroup:275	
28	Zinc fingers C2H2-type	The Cys2His2-like fold group is by far the best-characterized class of zinc fingers and are extremely common in mammalian transcription factors. These domains adopt a simple ββα fold and have the amino acid Sequence motif:  X2-Cys-X2,4-Cys-X12-His-X3,4,5-His	ZNF		hgnc.genegroup:26	
280	Gamma-aminobutyric acid type B receptor subunits	GABA B receptors (GABA BR) are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA) that are linked via G-proteins to potassium channels.  The changing potassium concentrations hyperpolarize the cell at the end of an action potential. The reversal potential the GABA B-mediated IPSP is -100 mV, which is much more hyperpolarized than the GABA A IPSP. GABA B receptors are found in the central and peripheral autonomic nervous system.	GABBR		hgnc.genegroup:275|hgnc.genegroup:562	
281	Glutamate metabotropic receptors	The metabotropic glutamate receptors, or mGluR s, are a type of glutamate receptor that are active through an indirect metabotropic process. They are members of the group C family of G-protein-coupled receptors, or GPCRs.  Like all glutamate receptors, mGluRs bind with glutamate, an amino acid that functions as an excitatory neurotransmitter.	GRM		hgnc.genegroup:275|hgnc.genegroup:282	
282	Glutamate receptors	Glutamate receptors are synaptic receptors located primarily on the membranes of neuronal cells. Glutamate (glutamic acid) is abundant in the human body, but particularly in the nervous system and especially prominent in the human brain where it is the body's most prominent neurotransmitter, the brain's main excitatory neurotransmitter, and also the precursor for GABA, the brain's main inhibitory neurotransmitter.  Glutamate receptors are responsible for the glutamate-mediated postsynaptic excitation of neural cells, and are important for neural communication, memory formation, learning, and regulation. Glutamate receptors are implicated in a number of neurological conditions. Their central role in excitotoxicity and prevalence in the central nervous system has been linked or speculated to be linked to many neurodegenerative diseases, and several other conditions have been further linked to glutamate receptor gene mutations or receptor autoantigen /antibody activity.			so:0005855	
283	Sodium leak channels, non selective		NALCN		hgnc.genegroup:179	
284	Glutamate ionotropic receptors	The ability of synapses to modify their synaptic strength in response to activity is a fundamental property of the nervous system and may be an essential component of learning and memory. There are four classes of ionotropic glutamate receptors, namely NMDA receptor, AMPA receptor, Delta receptor and kainate receptors. They are believed to play critical roles in synaptic plasticity. At many synapses in the brain, transient activation of NMDA receptors leads to a persistent modification in the strength of synaptic transmission mediated by AMPA receptors and kainate receptors can act as the induction trigger for long-term changes in synaptic transmission.	GRI		hgnc.genegroup:282|hgnc.genegroup:161	
285	G protein-coupled receptors, Class C orphans	This set contains class C 'orphan' G protein coupled receptors where the endogenous ligand(s) is not known.			hgnc.genegroup:275	
286	G protein-coupled receptors, Class F frizzled	Frizzled is a family of G protein-coupled receptor proteins that serve as receptors in the Wnt signaling pathway and other signaling pathways.	FZD		hgnc.genegroup:139	
287	Ryanodine receptors	Ryanodine receptors ( RyRs ) form a class of intracellular calcium channels in various forms of excitable animal tissue like muscles and neurons. It is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells.	RYR		hgnc.genegroup:161|hgnc.genegroup:182	
288	Pannexins	Pannexins (from Greek 'pan' all, and from Latin 'nexus' connection) are a family of vertebrate proteins identified by their homology to the invertebrate innexins. While innexins are responsible for forming gap junctions in invertebrates, the pannexins have been shown to predominantly exist as large transmembrane channels connecting the intracellular and extracellular space, allowing the passage of ions and small molecules between these compartments (such as ATP and sulforhodamine B). 	PANX		hgnc.genegroup:1471	
289	Taste receptors	A taste receptor is a type of receptor which facilitates the sensation of taste. When food or other substances enter the mouth, molecules interact with saliva and are bound to taste receptors in the oral cavity and other locations. Molecules which give a sensation of taste are considered 'sapid'.			hgnc.genegroup:139	
290	Acid sensing ion channel subunits	Acid-Sensing Ion Channels (ASICs) are neuronal voltage-insensitive cationic channels activated by extracellular protons. ASIC proteins are a subfamily of the ENaC/Deg superfamily of ion channels. To date five proteins of the ASIC family have been identified that arise from four genes, ASIC1, ASIC2, ASIC3, and ASIC4. ASIC1a, 1b and 2a, 2b are splice variants. ASICs are trimeric and can be made up of different combinations of subunits. ASIC2b is non functional on its own but modulates channel activity when participating in heteromultimers. ASIC4 has no known function. All ASICs are expressed in the peripheral nervous system while ASIC1a, 2a, 2b and 4 are expressed in the central nervous system. ASICs are Na+ permeable with ASIC1a showing low Ca++ permeability.	ASIC		hgnc.genegroup:179|hgnc.genegroup:294	
291	Vomeronasal receptors	Pheromones have evolved in all animal phyla, to signal sex and dominance status, and are responsible for stereotypical social and sexual behaviour among members of the same species. In mammals, these chemical signals are believed to be detected primarily by the vomeronasal organ (VNO), a chemosensory organ located at the base of the nasal septum.  The VNO is present in most amphibia, reptiles and non-primate mammals but is absent in birds, adult catarrhine monkeys and apes. An active role for the human VNO in the detection of pheromones is disputed; the VNO is clearly present in the fetus but appears to be atrophied or absent in adults. Three distinct families of putative pheromone receptors have been identified in the vomeronasal organ (V1Rs, V2Rs and V3Rs). All are G protein-coupled receptors but are only distantly related to the receptors of the main olfactory system, highlighting their different role.  The V1 receptors share between 50 and 90% sequence identity but have little similarity to other families of G protein-coupled receptors. They appear to be distantly related to the mammalian T2R bitter taste receptors and the rhodopsin-like GPCRs. A number of human V1 receptor homologues have also been found. The majority of these human sequences are pseudogenes but an apparently functional receptor has been identified that is expressed in the human olfactory system.	VN1R, VN2R		hgnc.genegroup:139	
292	Ion channels by channel type				hgnc.genegroup:177	
293	Adiponectin receptors	Similar to G protein-coupled receptors (GPCRs), ADIPOR1 also possesses 7 transmembrane domains. However ADIPOR1 is orientated oppositely to GPCRs in the membrane (i.e., cytoplasmic N-terminus, extracellular C-terminus) and does not associate with G proteins.	ADIPOR		so:0005855	
294	Ion channels by gating mechanism				hgnc.genegroup:177	
297	Inositol 1,4,5-triphosphate receptors	Inositol trisphosphate receptor ( InsP3R ) is a membrane glycoprotein complex acting as a Ca 2+ channel activated by inositol trisphosphate (InsP3). InsP3R is very diverse among organisms, and is necessary for the control of cellular and physiological processes including cell division, cell proliferation, apoptosis, fertilization, development, behavior, learning and memory.  Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca 2+ from intracellular store sites. There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca 2+ signals characterized by complex patterns relative to both space and time. For example, Ca 2+ waves and oscillations.  The InsP3 receptor was first purified from rat cerebellum by neuroscientists Surachai Supattapone and Solomon Snyder at Johns Hopkins University School of Medicine.	ITPR		hgnc.genegroup:182|hgnc.genegroup:161	
3	Fascin family		FSCN		so:0005855	
301	Chloride calcium-activated channels				hgnc.genegroup:278	
302	Chloride voltage-gated channels		CLCN		hgnc.genegroup:278	
304	Porins	Membrane protein which in a multimeric form constitutes a water-filled transmembrane channel (a pore). This pore allows the passage of ions and numerous other, non-specific molecules through the membrane. Found in the mitochondrial and plastid outer membrane of eukaryotes, in many Gram-negative bacteria, at least some Corynebacterineae, archaea and in sea anemones.			hgnc.genegroup:292	
305	Aquaporins	Aquaporins are integral membrane proteins from a larger family of major intrinsic proteins (MIP) that form pores in the membrane of biological cells. Genetic defects involving aquaporin genes have been associated with several human diseases.  The 2003 Nobel Prize in Chemistry was awarded jointly to Peter Agre for the discovery of aquaporins,  and Roderick MacKinnon for his work on the structure and mechanism of potassium channels. The plasma membranes of a variety of different animal and plant cells contain aquaporins through which water can flow more rapidly inside the cell than by diffusing through the phospholipid bilayer.	AQP		hgnc.genegroup:304	
306	Voltage dependent anion channels	Voltage-dependent anion channels are a class of porin ion channel located on the outer mitochondrial membrane. There is debate as to whether or not this channel is expressed in the cell surface membrane.    This major protein of the outer mitochondrial membrane of eukaryotes forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules.   The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. VDAC facilitates the exchange of ions and molecules between mitochondria and cytosol and is regulated by the interactions with other proteins and small molecules.	VDAC		hgnc.genegroup:304	
307	Chloride intracellular channels		CLIC		hgnc.genegroup:278	
309	Chloride channels, ATP-gated CFTR		CFTR		hgnc.genegroup:278|hgnc.genegroup:161	
310	7TM uncharacterized proteins	These genes encode proteins that are predicted to encode seven transmembrane regions, but they do not fall into any specific class of G protein-coupled receptor and ligands for the putative 'receptors' have not been identified.			hgnc.genegroup:2054	
314	Gap junction proteins	Connexins, or gap junction proteins, are a family of structurally related transmembrane proteins that assemble to form vertebrate gap junctions (an entirely different family of proteins, the innexins, form gap junctions in invertebrates).  Each gap junction is composed of two hemichannels, or connexons, which are themselves each constructed out of six connexin molecules. Gap junctions are essential for many physiological processes, such as the coordinated depolarization of cardiac muscle, proper embryonic development, and the conducted response in microvasculature. For this reason, mutations in connexin-encoding genes can lead to functional and developmental abnormalities.	GJ		hgnc.genegroup:292|hgnc.genegroup:1471	
320	Receptor kinases				so:0005855	
321	Receptor tyrosine kinases	Receptor tyrosine kinases (RTKs), a family of cell-surface receptors, which transduce signals to polypeptide and protein hormones, cytokines and growth factors are key regulators of critical cellular processes, such as proliferation and differentiation, cell survival and metabolism, cell migration and cell cycle control. In the human genome, 58 RTKs have been identified, which fall into 20 families. All RTKs display an extracellular ligand binding domain, a single transmembrane helix, a cytoplasmic region containing the protein tyrosine kinase activity (occasionally split into two domains by an insertion, termed the kinase insertion), with juxta-membrane and C-terminal regulatory regions. Agonist binding to the extracellular domain evokes dimerization, and sometimes oligomerization, of RTKs (a small subset of RTKs forms multimers even in the absence of activating ligand). This leads to autophosphorylation in the tyrosine kinase domain in a trans orientation, serving as a site of assembly of protein complexes and stimulation of multiple signal transduction pathways, including phospholipase C-γ, mitogen-activated protein kinases and phosphatidylinositol 3-kinase.			hgnc.genegroup:320	
343	Transmembrane guanylate cyclases	Membrane bound guanylyl cyclases include an external ligand-binding domain (e.g., for peptide hormones such as BNP and ANP), a transmembrane domain, and an internal catalytic domain homologous to adenylate cyclases.	GUCY2		hgnc.genegroup:819	
344	Receptor serine/threonine kinase family		RSTK		hgnc.genegroup:320	
345	Type 1 receptor serine/threonine kinases				hgnc.genegroup:344	
346	Type 2 receptor serine/threonine kinases				hgnc.genegroup:344	
348	Immunoglobulins	Immunoglobulins (IG) or antibodies are antigen receptors of the B cells of the adaptive immune response, acquired by jawed vertebrates (or gnathostomata) more than 450 million years ago and found in all extant jawed vertebrate species from fishes to humans. IG are anchored in the membrane of a B cell as part of a signaling B cell receptor (BcR = membrane IG+CD79) or are secreted by plasmocytes. IG recognize antigens in their native (unprocessed) form. IG are made of two identical heavy (H) chains and two identical light (kappa or lambda) chains, encoded by genes located in three major loci: the IG heavy (IGH) locus at 14q32.33, IG kappa (IGK) locus at 2p11.2 and IG lambda (IGL) locus at 22q11.2. Genes outside of these major loci are orphons. There are four IG gene types, variable (V), diversity (D) (only for IGH), joining (J) and constant (C) genes which contribute to the IG chain synthesis. The variable domain at the N-terminal end of each IG chain results from a V-(D)-J rearrangement whereas the remaining of the chain, or constant region, is encoded by a C gene. The combinatorial and junctional diversity together with IG somatic hypermutations create a huge diversity of 1012 specific IG per individual, the limiting factor being only the number of B cells that an organism is genetically programmed to prod	IG		so:0005855	
349	Immunoglobulin heavy locus at 14q32.33	The IGH locus is at 14q32.33 and contains IGHV (variable) genes, IGHD (diversity) genes, IGHJ (joining) genes, and IGHA, IGHG, IGHD, IGHE and IGHM constant genes. 	IGH		hgnc.genegroup:886	
350	Immunoglobulin heavy (IGH) orphons	These are IGH genes that are found outside of the 14q32.33 IGH locus and therefore cannot form part of an immunoglobulin-encoding gene.			hgnc.genegroup:886	
351	Immunoglobulin kappa locus at 2p11.2	The human IGK locus is at 2p11.2 and contains IGKV (variable) genes, IGKJ (joining) genes and one IGKC (constant) gene. Most individuals have two clusters of the IGKV genes resulting from a duplication.  The clusters are designated as either proximal or distal to the IGKC gene.  Genes from the distal cluster are denoted with a “D” in the symbol while those without a “D” are located in the proximal cluster.	IGK		hgnc.genegroup:887	
352	Immunoglobulin kappa (IGK) orphons	These are IGK genes that are found outside of the 2p11.2 IGK locus and therefore cannot form part of an immunoglobulin-encoding gene.			hgnc.genegroup:887	
353	Immunoglobulin lambda locus at 22q11.2	The IGL locus is at 22q11.2 and contains IGLV (variable) genes, IGLJ (joining) genes and IGLC (constant) genes.	IGL		hgnc.genegroup:888	
354	Immunoglobulin lambda (IGL) orphons	These are IGL genes that are found outside of the 22q11.2 IGL locus and therefore cannot form part of an immunoglobulin-encoding gene.			hgnc.genegroup:888	
356	Adenylate kinases	Adenylate kinases are abundant phosphotransferases that catalyze the interconversion of adenine nucleotides and thus regulate the adenine nucleotide ratios in different intracellular compartments.	AK		so:0005855	
357	ARF GTPase family	ADP Ribosylation Factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family proteins are ubiquitous in eukaryotic cells, and six highly conserved members of the family have been identified in mammalian cells. Although ARFs are soluble, they generally associate with membranes because of N-terminus myristoylation. They function as regulators of vesicular traffic and actin remodelling. The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic. They are the founding members of a growing family that includes Arl (Arf-like), Arp [ARFRP] (Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins.			hgnc.genegroup:358	
358	Ras small GTPase superfamily	The Ras superfamily is a protein superfamily of small GTPases, which are all related, to a degree, to the Ras protein subfamily (the key human members of which are KRAS, NRAS, and HRAS ). There are more than a hundred proteins in the Ras superfamily.			so:0005855	
360	Wnt family	The Wnt protein family includes a large number of cysteine-rich glycoproteins. The Wnt proteins activate signal transduction cascades via three different pathways, the canonical Wnt pathway, the noncanonical planar cell polarity (PCP) pathway, and the noncanonical Wnt/Ca2+ pathway.	WNT		hgnc.genegroup:542	
361	WAP four-disulfide core domain containing		WFDC		so:0005855	
362	WD repeat domain containing		WDR		so:0005855	
363	UDP glucuronosyltransferases		UGT		hgnc.genegroup:424	
364	UBX domain containing		UBXN		so:0005855	
365	U-box domain containing		UBOX		so:0005855	
366	Ubiquitin specific peptidases		USP		hgnc.genegroup:996	
367	Vestigial like family		VGLL		so:0005855	
368	Variable charge X/Y family	The VCX/Y genes encode small and highly charged proteins of unknown function. The presence of a putative bipartite nuclear localization signal suggests that VCX/Y members are nuclear proteins.	VCX, VCY		so:0005855	
370	T cell receptors	T cell receptors (TR) are antigen receptors of the T cells of the adaptive immune response, acquired by jawed vertebrates (or gnathostomata) more than 450 million years ago and found in all extant jawed vertebrate species from fishes to humans. TR are anchored in the membrane of a T cell as part of the signaling T cell receptor (TcR = TR+CD3). TR alpha/beta recognize processed antigens, which are presented as peptides by the highly polymorphic major histocompatibility (MH, in humans HLA for human leukocyte antigens) proteins, whereas TR gamma/delta recognize nonpeptidic antigens. TR are made of two chains, alpha and beta, or gamma and delta, encoded by genes located in four major loci: the TR alpha (TRA) at 14q11.2, TR beta (TRB) at 7q34, TR gamma (TRG) at 7p14 and TR delta (TRD) at 14q11.2. Genes outside of these major loci are orphons. There are four TR gene types, variable (V), diversity (D) (for TRB and TRD), joining (J) and constant (C) genes which contribute to the TR chain synthesis. The variable domain at the N-terminal end of each TR chain results from a V-(D)-J rearrangement whereas the remaining of the chain, or constant region, is encoded by a C gene. The combinatorial and junctional diversity creates a huge potential diversity of 1012 specific TR per individual, the limiting factor being only the number of T cells that an organism is genetically programmed to produce.	TR		so:0005855	
371	T cell receptor alpha locus at 14q11.2	The TRA locus at 14q11.2 contains TRAV (variable) genes, TRAJ (joining) genes and one TRAC (constant) gene.	TRA		hgnc.genegroup:370	
372	T cell receptor beta locus at 7q34	The TRB locus at 7q34 contains TRBV (variable) genes, TRBD (diversity) genes, TRBJ (joining) genes and TRBC (constant) genes.	TRB		hgnc.genegroup:889	
373	T cell receptor beta (TRB) orphons	These are TRB genes that are found outside of the 7q34 TRB locus and therefore cannot form part of a T cell receptor-encoding gene.			hgnc.genegroup:889	
374	T cell receptor delta locus at 14q11.2	The TRD locus at 14q11.2 contains TRDV (variable) genes, TRDD (diversity) genes, TRDJ (joining) genes and one TRDC (constant) gene.	TRD		hgnc.genegroup:370	
375	T cell receptor gamma locus at 7p14	The TRG locus at 7p14 contains TRGV (variable) genes, TRGJ (joining) genes and TRGC (constant) genes.	TRG		hgnc.genegroup:370	
388	RAB, member RAS oncogene GTPases	The Rab family of proteins is a member of the Ras superfamily of monomeric G proteins. Rab GTPases regulate many steps of membrane traffic, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.	RAB		hgnc.genegroup:358	
389	RAS type GTPase family	The RAS family is a subset of the RAS small GTPase superfamily.  The family includes the proto-oncogenes HRAS, NRAS and KRAS.	RAS		hgnc.genegroup:358	
39	Actin related protein 2/3 complex subunits		ARPC		so:0005855	
390	Rho family GTPases	The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic organisms including yeasts and some plants. Three members of the family have been studied a great deal: Cdc42, Rac1, and RhoA. All G proteins are 'molecular switches', and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions.	RHO		hgnc.genegroup:358	
391	RAN family GTPases		RAN		hgnc.genegroup:358	
392	Miro like atypical Rho GTPases	Mitochondrial Rho proteins (Miro-1, Q8IXI2 [encoded by RHOT1] and Miro-2, Q8IXI1 [encoded by RHOT2]), are atypical Rho GTPases. They have a unique domain organisation, with tandem GTP-binding domains and two EF hand domains (PF00036), that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.			hgnc.genegroup:358	
394	RAB like GTPases		RABL		hgnc.genegroup:358	
395	ArfGAPs	The ArfGAPs are GTPase activating proteins for the ARF (ADP-ribosylation factor) GTPases.			so:0005855	
396	A-kinase anchoring proteins	The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell.	AKAP		so:0005855	
397	Alcohol dehydrogenases	Alcohol dehydrogenases ( ADH ) ( EC 1.1.1.1 ) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD + to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD +.	ADH		so:0005855	
398	Aldehyde dehydrogenases	Aldehyde dehydrogenases ( EC 1.2.1.3 ) are a group of enzymes that catalyse the oxidation (dehydrogenation) of aldehydes. To date, nineteen ALDH genes have been identified within the human genome. These genes participate in a wide variety of biological processes including the detoxification of exogenously and endogenously generated aldehydes.	ALDH		so:0005855	
399	Aldo-keto reductases		AKR		so:0005855	
4	Abhydrolase domain containing		ABHD		so:0005855	
40	Acyl-CoA synthetase family		ACS		so:0005855	
400	Alkaline ceramidases	Alkaline ceramidases (EC 3.5.1.23) catalyse the following reaction: N-acylsphingosine + H(2)O <=> a carboxylate + sphingosine.	ACER		so:0005855	
401	Alkylation repair homologs	Members of this family are homologous to AlkB, an E.coli enzyme that repairs alkylated DNA and RNA.The 9 human homologs are all members of the alpha-ketoglutarate and FE(II)-dependent dioxygenase superfamily. 	ALKBH		so:0005855	
402	Anaphase promoting complex 	This article refers to the cell-cycle regulatory complex, APC/C. For the tumor suppressor APC, in which mutations lead to colon cancer, see Adenomatous polyposis coli. Anaphase-Promoting Complex (also called the cyclosome or APCC is a large complex of 11-13 subunit proteins, including a cullin (Apc2) and RING (Apc11) subunit much like SCF. Other parts of the APC/C still have unknown functions, but are highly conserved.  It was the discovery of the APC/C (and SCF ) and their key role in eukaryotic cell reproduction that established once and for all the importance of ubiquitin -mediated proteolysis in eukaryotic cell biology. Once perceived as a system exclusively involved in removing damaged protein from the cell, ubiquitination and subsequent protein degradation by the proteasome is now perceived as a universal regulatory mechanism for signal transduction whose importance approaches that of protein phosphorylation. In 2014, the APC/C was mapped in 3D at a resolution of less than a nanometre, which also uncovered its secondary structure. Researchers have claimed this finding could transform the understanding of cancer and reveal new binding sites for future cancer drugs.  	ANAPC		so:0005855	
403	Ankyrin repeat domain containing	Protein containing at least one ANK repeat, a conserved domain of approximately 33 amino acids, that was originally identified in ankyrin. It has been described as an L-shaped structure consisting of a beta-hairpin and two alpha-helices. Many ankyrin repeat regions are known to function as protein-protein interaction domains.	ANKRD		so:0005855	
404	Annexins	Annexin is a common name for a group of cellular proteins. They are mostly found in eukaryotic organisms (animal, plant and fungi). In humans, the annexins are found inside the cell. However some annexins (Annexin A1, Annexin A2, and Annexin A5) have also been found outside the cellular environment, for example, in blood. How the annexins are transported out of the cell into the blood is a mystery because they lack a signal peptide necessary for proteins to be transported out of the cell.  Annexin is also known as lipocortin. Lipocortins suppress phospholipase A2. Increased expression of the gene coding for annexin-1 is one of the mechanisms by which glucocorticoids (such as cortisol ) inhibit inflammation.	ANXA		so:0005855	
405	Apolipoproteins	Protein or apolipoprotein associated with High-Density Lipoproteins (HDL), a class of proteins involved in lipid (cholesterol, phospholipids and triacylglycerol) metabolism in the body fluids. HDL are formed in the liver and are involved in reverse cholesterol transport, the transport of cholesterol from peripherical tissues to the liver. Apolipoproteins are proteins which are specifically associated with lipoproteins, which is not the case for all the proteins associated with HDL or with the other lipoprotein classes.	APO		so:0005855	
406	Apolipoprotein B mRNA editing enzyme catalytic subunits	APOBEC ('apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like') is a family of evolutionary conserved proteins. A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalytic domain. More specifically, the catalytic domain is a zinc dependent cytidine deaminase domain and is essential for cytidine deamination. RNA editing by APOBEC-1 requires homodimerisation and this complex interacts with RNA binding proteins to form the editosome.	APOBEC		so:0005855	
407	Arachidonate lipoxygenases	Lipoxygenases ( EC 1.13.11.- ) are a family of iron -containing enzymes that catalyse the dioxygenation of polyunsaturated fatty acids in lipids containing a cis,cis-1,4- pentadiene structure. It catalyses the following reaction:  fatty acid + O 2 = fatty acid hydroperoxide  Lipoxygenases are found in plants, animals and fungi. Products of lipoxygenases are involved in diverse cell functions.	ALOX		so:0005855	
408	Argonaute/PIWI family				so:0005855	
409	Armadillo repeat containing	Armadillo repeat is the name of a characteristic, repetitive amino acid sequence found in β-catenin and many other proteins, like α-importin, plakoglobin,or adenomatous polyposis coli (APC). Its name derives from the historical name of the β-catenin gene in the fruitfly Drosophila: where they were first discovered. Armadillo repeats are approximately 40 amino acids long and proteins that contain them usually have many tandemly repeated copies. These tandem repeats usually fold together to form a single, rigid protein domain called the armadillo (ARM) domain. Because ARM domains can consist of a variable number of repeats, they are a good example of solenoid protein domains. The best characterized example of armadillo domains is found in β-catenin. β-catenin is a protein involved in linking cadherin cell adhesion proteins to the cytoskeleton, but the Armadillo repeat is found in a wide range of proteins with other functions. This type of protein domain is important in transducing WNT signals during embryonic development.	ARMC		hgnc.genegroup:1492	
41	Acyl-CoA thioesterases		ACOT		hgnc.genegroup:1832	
410	Sulfatases	Sulfatases EC 3.1.6. are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters.	ARS		so:0005855	
412	ATPases	This family page represents all types of ATPases found in human.  V-type and F-type ATPases are both rotor protein complexes and are related in structure and function.  The V-type ATPase hydrolyses ATP to pump protons across membranes while the F-type ATPase couples proton transfer to synthesis of ATP from ADP.  The AAA and P-type families are unrelated and comprise many individual members.  The AAA ATPase family hydrolyse ATP to obtain energy for a diverse variety of biological processes.  P-type ATPases use the energy from ATP hydrolysis to pump ions across cellular membranes.			so:0005855	
413	AAA ATPases	AAA or AAA+ is an abbreviation for ATPases Associated with diverse cellular Activities. They share a common conserved module of approximately 230 amino acid residues. This is a large, functionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases, which exert their activity through the energy-dependent remodeling or translocation of macromolecules.  AAA proteins couple chemical energy provided by ATP hydrolysis to conformational changes which are transduced into mechanical force exerted on a macromolecular substrate.  AAA proteins are functionally and organizationally diverse, and vary in activity, stability, and mechanism.  Members of the AAA family are found in all organisms  and they are essential for many cellular functions. They are involved in processes such as DNA replication, protein degradation, membrane fusion, microtubule severing, peroxisome biogenesis, signal transduction and the regulation of gene expression.	ATAD		hgnc.genegroup:412	
414	P-type ATPases	The P-type ATPases, also known as E1-E2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. They are alpha-helical bundle primary transporters referred to as P-type ATPases because they catalyze auto- (or self-) phosphorylation of a key conserved aspartate residue within the pump. In addition, they all appear to interconvert between at least two different conformations, denoted by E1 and E2. Most members of this transporter family are specific for the pumping of a large array of cations, however one subfamily is involved in flipping phospholipids to maintain the asymmetric nature of the biomembrane. Prominent examples of P-type ATPases are the sodium-potassium pump (Na +,K +-ATPase), the plasma membrane proton pump (H +-ATPase), the proton-potassium pump (H +,K +-ATPase), and the calcium pump (Ca 2+ -ATPase).			hgnc.genegroup:412	
415	V-type ATPase subunits	Vacuolar-type H +-ATPase ( V-ATPase ) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms.  V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells.	ATP6V		hgnc.genegroup:412	
417	ATP binding cassette transporters	ATP-binding cassette transporters ( ABC transporters ) are members of a protein superfamily that is one of the largest and most ancient families with representatives in all extant phyla from prokaryotes to humans.  ABC transporters are transmembrane proteins that utilize the energy of adenosine triphosphate (ATP) binding and hydrolysis to carry out certain biological processes including translocation of various substrates across membranes and non-transport-related processes such as translation of RNA and DNA repair.  They transport a wide variety of substrates across extra- and intracellular membranes, including metabolic products, lipids and sterols, and drugs. Proteins are classified as ABC transporters based on the sequence and organization of their ATP-binding cassette (ABC) domain(s). ABC transporters are involved in tumor resistance, cystic fibrosis and a range of other inherited human diseases along with both bacterial (prokaryotic) and eukaryotic (including human) development of resistance to multiple drugs.	ABC		so:0005855	
418	AT-rich interaction domain containing	In molecular biology, the ARID domain (AT-rich interaction domain; also known as BRIGHT domain))  is a protein domain that binds to DNA. ARID domain-containing proteins are found in fungi and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure.  The basic structure of the ARID domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini. 	ARID		so:0005855	
419	Baculoviral IAP repeat containing	The inhibitor of apoptosis domain - also known as IAP repeat, Baculovirus Inhibitor of apoptosis protein Repeat, or BIR - is a structural motif found in proteins with roles in apoptosis, cytokine production, and chromosome segregation. Proteins containing BIR are known as inhibitor of apoptosis proteins (IAPs), or BIR-containing proteins (BIRPs or BIRCs), and include BIRC1 (NAIP), BIRC2 (cIAP1), BIRC3 (cIAP2), BIRC4 (xIAP), BIRC5 (survivin) and BIRC6.  BIR domains belong to the zinc-finger domain family and characteristically have a number of invariant amino acid residues, including 3 conserved cysteines and one conserved histidine, which coordinate a zinc ion.  They are typically composed of 4-5 alpha helices and a three-stranded beta sheet.	BIRC		so:0005855	
42	SCAN domain containing				hgnc.genegroup:1411	
420	Basic helix-loop-helix proteins	A basic helix-loop-helix (bHLH) is a protein structural motif that characterizes a family of transcription factors. The motif is characterized by two α-helices connected by a loop. In general, transcription factors including this domain are dimeric, each with one helix containing basic amino acid residues that facilitate DNA binding.	BHLH		so:0005855	
422	BEN domain containing		BEND		so:0005855	
423	Beta-1,3-glucuronyltransferases	Beta-1,3-glucuronyltransferases (EC 2.4.1.135) catalyse the following reaction: UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein <=> UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.	B3GAT		hgnc.genegroup:424	
424	Glycosyltransferases	Enzymes that catalyze the transfer of glycosyl (sugar) residues to an acceptor, both during degradation (cosubstrates= water or inorganic phosphate) and during biosynthesis of polysaccharides, glycoproteins and glycolipids. In biosynthetic glycosyl transfers, the common activated monomeric sugar intermediate is a nucleoside diphosphate sugar.			so:0005855	
425	Beta 4-glycosyltransferases				hgnc.genegroup:424	
426	Beta 3-glycosyltransferases				hgnc.genegroup:424	
427	Glycosyl transferases group 1 domain containing				hgnc.genegroup:424	
428	Glycosyltransferase family 2				hgnc.genegroup:424	
429	Glycosyltransferase family 6				hgnc.genegroup:424	
430	Dolichyl D-mannosyl phosphate dependent mannosyltransferases	This functional set of mannosyltransferases all use dolichyl D-mannosyl phosphate (dol-P-Man) as a sugar donor.			hgnc.genegroup:424	
431	Exostosin glycosyltransferase family		EXT		hgnc.genegroup:424	
433	Polypeptide N-acetylgalactosaminyltransferases	In enzymology, a polypeptide N-acetylgalactosaminyltransferase ( EC 2.4.1.41 ) is an enzyme that catalyzes the chemical reaction  UDP-N-acetyl-D-galactosamine + polypeptide UDP + N-acetyl-D-galactosaminyl-polypeptide  Thus, the two substrates of this enzyme are UDP-N-acetyl-D-galactosamine and polypeptide, whereas its two products are UDP and N-acetyl-D-galactosaminyl-polypeptide. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. This enzyme participates in o-glycan biosynthesis and glycan structures - biosynthesis 1. It has 2 cofactors : manganese, and calcium.	GALNT		hgnc.genegroup:424	
434	Fucosyltransferases	A fucosyltransferase is an enzyme that transfers an L- fucose sugar from a GDP-fucose ( guanosine diphosphate -fucose) donor substrate to an acceptor substrate. The acceptor substrate can be another sugar such as the transfer of a fucose to a core GlcNAc ( N-acetylglucosamine ) sugar as in the case of N-linked glycosylation, or to a protein, as in the case of O -linked glycosylation produced by O -fucosyltransferase. There are various fucosyltransferases in mammals, the vast majority of which, are located in the Golgi apparatus. The O -fucosyltransferases have recently been shown to localize to the endoplasmic reticulum (ER). Some of the proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins. Galactoside 3(4)-L-fucosyltransferase ( EC 2.4.1.65 ) belongs to the Lewis blood group system and is associated with Le(a/b) antigen.	FUT		hgnc.genegroup:424	
435	Mannosyl-glycoprotein N-acetylglucosaminyltransferases		MGAT		hgnc.genegroup:424	
436	Glycosyltransferase family 8				hgnc.genegroup:424	
437	Glycogen phosphorylases	Glycogen phosphorylase is one of the phosphorylase enzymes ( EC 2.4.1.1 ). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.	PYG		hgnc.genegroup:424	
438	Sialyltransferases	Sialyltransferases are a subset of glycosyltransferases that catalyze the transfer of sialic acid (Sia) residues from an activated sugar donor (CMP-βNeu5Ac, CMP-βNeu5Gc, CMP-βKdn) to the hydroxyl group at the terminal non reducing position of Gal, GlcNAc, GalNAc or Sia monosaccharides of glycoconjugate acceptors (glycoproteins or glycolipids) leading to the formation of α2-3, α2-6 or α2-8 glycosidic linkages. Animal sialyltransferases are gathered in a unique group of the CAZy classification (GT#29). Within this group, four families are distinguished based on the glycosidic linkage formed and the monosaccharide acceptor (ST3Gal, ST6Gal, ST6GalNAc and ST8Sia).			hgnc.genegroup:424	
439	Collagen beta(1-O)galactosyltransferases		COLGALT		hgnc.genegroup:424	
440	UDP-glucose glycoprotein glucosyltransferases		UGGT		hgnc.genegroup:424	
441	Glucosaminyl (N-acetyl) transferases/xylosyltransferases		GCNT, XYLT		hgnc.genegroup:424	
442	Alpha 1,4-glycosyltransferases				hgnc.genegroup:424	
443	Glycosyltransferase family 90		POGLUT		hgnc.genegroup:424	
444	STT3 oligosaccharyltransferase catalytic subunits		STT3		hgnc.genegroup:424	
445	Oligosaccharyltransferase complex subunits	Oligosaccharyltransferase or OST ( EC 2.4.1.119 ) is a membrane protein complex that transfers a 14- sugar oligosaccharide from dolichol to nascent protein. It is a type of glycosyltransferase. The sugar Glc 3Man 9GlcNAc 2 (where Glc= Glucose, Man= Mannose, and GlcNAc= N-acetylglucosamine ) is attached to an asparagine (Asn) residue in the sequence Asn-X- Ser or Asn-X- Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N -linked glycosylation pathway.	OST		so:0005855	
446	O-linked N-acetylglucosaminyltransferases				hgnc.genegroup:424	
447	Alpha-1,3-glucosyltransferases				hgnc.genegroup:424	
448	Alpha-1,2-glucosyltransferases		ALG10		hgnc.genegroup:424	
449	UDP-N-acetylglucosaminyltransferase subunits				hgnc.genegroup:424	
450	UDP-glucose ceramide glucosyltransferases				hgnc.genegroup:424	
452	Biogenesis of lysosomal organelles complex 1 subunits	BLOC-1 or biogenesis of lysosome-related organelles complex 1 is a ubiquitously expressed multisubunit protein complex. BLOC-1 is required for normal biogenesis of specialized organelles of the endosomal -lysosomal system, such as melanosomes and platelet dense granules.	BLOC1S		so:0005855	
454	Blood group antigens	Protein belonging to the set of cell surface antigens found chiefly, but not solely, on blood cells. More than fifteen different blood group systems are recognised in humans. In most cases the antigenic determinant resides in the carbohydrate chains of membrane glycoproteins or glycolipids.			so:0005855	
455	Bone morphogenetic proteins	Bone morphogenetic proteins ( BMPs ) are a group of growth factors also known as cytokines and as metabologens. Originally discovered by their ability to induce the formation of bone and cartilage, BMPs are now considered to constitute a group of pivotal morphogenetic signals, orchestrating tissue architecture throughout the body.  The important functioning of BMP signals in physiology is emphasized by the multitude of roles for dysregulated BMP signalling in pathological processes. Cancerous disease often involves misregulation of the BMP signalling system. Absence of BMP signalling is, for instance, an important factor in the progression of colon cancer,  and conversely, overactivation of BMP signalling following reflux-induced esophagitis provokes Barrett's esophagus and is thus instrumental in the development of adenocarcinoma in the proximal portion of the gastrointestinal tract.	BMP		hgnc.genegroup:1932	
456	BPI fold containing		BPIF		so:0005855	
457	BRICHOS domain containing	The BRICHOS family consists of a variety of proteins linked to major diseases, each containing a 100 amino acid BRICHOS domain that is thought to have a chaperone function.	BRICD		so:0005855	
458	Butyrophilins	Butyrophilin is a family of proteins. Butyrophilin (Btn) genes constitute a subgroup of at least 10 genes in the Ig superfamily identified in human, mouse, cow, goat and other species.  The eponymous Btn gene (BTN1A1 in humans; Btn1a1 in mouse) is highly expressed in the secretory epithelium of the mammary gland during lactation. Other homologues are predominantly expressed in skeletal muscle and the intestine and erythroid cells. In contrast, BTN2A1 and 2 and BTN3A1, 2, and 3 are widely expressed in many tissues, suggesting that the structural domains of Btn proteins may have both universal and tissue-specific functions.	BTN		so:0005855	
459	S100 calcium binding proteins	The S-100 proteins (often styled without the hyphen, S100) are a family of low-molecular-weight proteins found in vertebrates and characterized by two calcium-binding sites that have helix-loop-helix ('EF-hand type') conformation. There are at least 21 different S-100 proteins. Their name is derived from the fact that these proteins are soluble in 100%, i.e. saturated ammonium sulfate at neutral pH. They are encoded by a family of genes whose symbols use the S100 prefix, for example, S100A1, S100A2, S100A3.	S100		hgnc.genegroup:1354	
46	1-acylglycerol-3-phosphate O-acyltransferases		AGPAT		so:0005855	
460	Carbonic anhydrases	The carbonic anhydrases (or carbonate dehydratases ) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs rather slowly in the absence of a catalyst.  The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. One of the functions of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues.	CA		so:0005855	
461	Carboxylesterases	In enzymology, a carboxylesterase or carboxylic-ester hydrolase ( EC 3.1.1.1 ) is an enzyme that catalyzes a chemical reaction of the form  a carboxylic ester + H 2O an alcohol + a carboxylate  Thus, the two substrates of this enzyme are carboxylic ester and H 2O, whereas its two products are alcohol and carboxylate. 	CES		so:0005855	
463	Paraoxonases	Paraoxonases are a group of enzymes involved in the hydrolysis of organophosphates.	PON		so:0005855	
464	Lipases	A lipase is an enzyme that catalyzes the hydrolysis of fats (lipids).	LIP		so:0005855	
465	Arylacetamide deacetylase family		AADAC		so:0005855	
466	Patatin like phospholipase domain containing		PNPLA		so:0005855	
467	Phospholipases	A phospholipase is an enzyme that hydrolyzes phospholipids  into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C and D, distinguished by the type of reaction which they catalyze:  Phospholipase A  Phospholipase A1 - cleaves the SN-1 acyl chain. Phospholipase A2 - cleaves the SN-2 acyl chain, releasing arachidonic acid.   Phospholipase B - cleaves both SN-1 and SN-2 acyl chains ; this enzyme is also known as a lysophospholipase. Phospholipase C - cleaves before the phosphate, releasing diacylglycerol and a phosphate-containing head group. Phospholipase Cs play a central role in signal transduction, releasing the second messenger inositol triphosphate. Phospholipase D - cleaves after the phosphate, releasing phosphatidic acid and an alcohol.  Types C and D are considered phosphodiesterases. Phospholipase A2 acts on the intact lecithin molecule and hydrolyses the fatty acid esterified to the second carbon atom. The resulting products are lysolecithin and a fatty acid. Phospholipase A2 is an enzyme present in the venom of bees and viper snakes.			so:0005855	
468	Caspases	Caspases, or cysteine-aspartic proteases or cysteine-dependent aspartate-directed proteases are a family of cysteine proteases that play essential roles in apoptosis (programmed cell death), necrosis, and inflammation. Caspases are essential in cells for apoptosis, or programmed cell death, in development and most other stages of adult life, and have been termed 'executioner' proteins for their roles in the cell. Some caspases are also required in the immune system for the maturation of lymphocytes. Failure of apoptosis is one of the main contributions to tumour development and autoimmune diseases; this, coupled with the unwanted apoptosis that occurs with ischemia or Alzheimer's disease, has stimulated interest in caspases as potential therapeutic targets since they were discovered in the mid-1990s.	CASP		so:0005855	
469	Cas scaffold proteins		CASS		so:0005855	
47	ADAM metallopeptidase domain containing		ADAM		hgnc.genegroup:901	
470	Cathepsins	Cathepsins ( Ancient Greek kata- 'down' and hepsein 'boil'; abbreviated CTS ) are proteases ( enzymes that degrades proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are distinguished by their substrate specificities.	CTS		hgnc.genegroup:2109	
471	CD molecules	The cluster of differentiation (cluster of designation) (often abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules providing targets for immunophenotyping of cells. In terms of physiology, CD molecules can act in numerous ways, often acting as receptors or ligands (the molecule that activates a receptor) important to the cell. A signal cascade is usually initiated, altering the behavior of the cell (see cell signaling). Some CD proteins do not play a role in cell signaling, but have other functions, such as cell adhesion. 	CD		so:0005855	
473	Cyclins	Cyclins are a family of proteins that control the progression of cells through the cell cycle by activating cyclin-dependent kinase (Cdk) enzymes.	CCN		so:0005855	
475	Non-coding RNAs	A non-coding RNA (ncRNA) is a functional RNA molecule that is not translated into a protein. Less-frequently used synonyms are non-protein-coding RNA (npcRNA), non-messenger RNA (nmRNA) and functional RNA (fRNA). The term small RNA (sRNA) is often used for short bacterial ncRNAs. The DNA sequence from which a non-coding RNA is transcribed is often called an RNA gene. Non-coding RNA genes include highly abundant and functionally important RNAs such as transfer RNA (tRNA) and ribosomal RNA (rRNA), as well as RNAs such as snoRNAs, microRNAs, siRNAs, snRNAs, exRNAs, and piRNAs and the long ncRNAs that include examples such as Xist and HOTAIR (see here for a more complete list of ncRNAs). The number of ncRNAs encoded within the human genome is unknown, however recent transcriptomic and bioinformatic studies suggest the existence of thousands of ncRNAs., but see  Since many of the newly identified ncRNAs have not been validated for their function, it is possible that many are non-functional.			so:0005855	
476	MicroRNAs	A microRNA (abbr. miRNA) is a small non-coding RNA molecule (ca. 22 nucleotides ) found in plants, animals, and some viruses, which functions in transcriptional and post-transcriptional regulation of gene expression. Encoded by eukaryotic nuclear DNA in plants and animals and by viral DNA in certain viruses whose genome is based on DNA, miRNAs function via base-pairing with complementary sequences within mRNA molecules. As a result, these mRNA strands are silenced because they can no longer be translated into proteins by ribosomes, and such complexes are often actively disassembled by the cell ('target degradation').  The human genome may encode over 1000 miRNAs,  which may target about 60% of mammalian genes and are abundant in many human cell types.  	MIR		hgnc.genegroup:475	
478	Transfer RNAs	A Transfer RNA (abbreviated tRNA and archaically referred to as sRNA abbreviating soluble RNA) is an adaptor molecule composed of RNA, typically 73 to 94 nucleotides in length, that serves as the physical link between the nucleotide sequence of nucleic acids ( DNA and RNA ) and the amino acid sequence of proteins. It does this by carrying an amino acid to the protein synthetic machinery of a cell ( ribosome ) as directed by a three-nucleotide sequence ( codon ) in a messenger RNA (mRNA). As such, tRNAs are a necessary component of protein translation, the biological synthesis of new proteins according to the genetic code. The specific nucleotide sequence of an mRNA specifies which amino acids are incorporated into the protein product of the gene from which the mRNA is transcribed, and the role of tRNA is to specify which sequence from the genetic code corresponds to which amino acid.  One end of the tRNA matches the genetic code in a three-nucleotide sequence called the anticodon. The anticodon forms three base pairs with a codon in mRNA during protein biosynthesis. The mRNA encodes a protein as a series of contiguous codons, each of which is recognized by a particular tRNA. On the other end of the tRNA is a covalent attachment to the amino acid that corresponds to the anticodon sequence. Each type of tRNA molecule can be attached to only one type of amino acid, so each organism has many types of tRNA (in fact, because the genetic code contains multiple codons that specify the same amino acid, there are many tRNA molecules bearing different anticodons which also carry the same amino acid). 	TR		hgnc.genegroup:475	
480	CDC like kinases	CLK family members have shown to interact with, and phosphorylate, serine / arginine -rich (SR) proteins of the spliceosomal complex, which is a part of the regulatory mechanism that enables the SR proteins to control RNA splicing.	CLK		so:0005855	
481	CDGSH iron sulfur domain containing		CISD		so:0005855	
482	Charged multivesicular body proteins		CHMP		so:0005855	
483	Chemokine ligands	Chemokines (Greek -kinos, movement) are a family of small cytokines, or signaling proteins secreted by cells. Their name is derived from their ability to induce directed chemotaxis in nearby responsive cells; they are chemo tactic cyto kines. Proteins are classified as chemokines according to shared structural characteristics such as small size (they are all approximately 8-10 kilodaltons in size), and the presence of four cysteine residues in conserved locations that are key to forming their 3-dimensional shape. However, these proteins have historically been known under several other names including the SIS family of cytokines, SIG family of cytokines, SCY family of cytokines, Platelet factor-4 superfamily or intercrines. Some chemokines are considered pro- inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria, but none have been described for other invertebrates. Chemokines have been classified into four main subfamilies : CXC, CC, CX3C and XC. All of these proteins exert their biological effects by interacting with G protein -linked transmembrane receptors called chemokine receptors, that are selectively found on the surfaces of their target cells.	CCL		hgnc.genegroup:542	
484	Chromatin modifying enzymes				so:0005855	
485	Lysine demethylases		KDM		hgnc.genegroup:1368|hgnc.genegroup:484	
486	Lysine acetyltransferases		KAT		hgnc.genegroup:484	
487	Lysine methyltransferases		KMT		hgnc.genegroup:484|hgnc.genegroup:1398	
488	Claudins	Claudins are a family of proteins that are the most important components of the tight junctions, where they establish the paracellular barrier that controls the flow of molecules in the intercellular space between the cells of an epithelium. They have four transmembrane domains, with the N-terminus and the C-terminus in the cytoplasm.	CLDN		hgnc.genegroup:1471	
489	Coiled-coil-helix-coiled-coil-helix domain containing proteins		CHCHD		so:0005855	
490	Collagens	Protein which contains one or more collagen-like domain. Collagen is a fibrous protein found in vertebrates, the major element of skin, bone, tendon, cartilage, blood vessels and teeth. It forms insoluble fibres of high tensile strength and which contains the unusual amino acids hyroxyproline and hydroxylysine. It is rich in glycine but lacks cysteine and tryptophan, and has an unusually regular amino-acid domain.	COL		so:0005855	
491	Collectins	Collectins (collagen-containing C-type lectins) are a part of the innate immune system. They form a family of collagenous Ca 2+ -dependent defense lectins, which are found in animals. Collectins are soluble pattern recognition receptors (PRRs). Their function is to bind to oligosaccharide structure or lipids which are on the surface of microorganisms. Like other PRRs they bind pathogen-associated molecular patterns (PAMPs) and also danger-associated molecular patterns (DAMPs) of oligosaccharide origin. Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis or inhibition of microbial growth. Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells.	COLEC		so:0005855	
492	Complement system	The complement system helps or '€œcomplements'€ the ability of antibodies and phagocytic cells to clear pathogens from an organism. It is part of the immune system called the innate immune system  that is not adaptable and does not change over the course of an individual's lifetime. However, it can be recruited and brought into action by the adaptive immune system. The complement system consists of a number of small proteins found in the blood, in general synthesized by the liver, and normally circulating as inactive precursors (pro-proteins). When stimulated by one of several triggers, proteases in the system cleave specific proteins to release cytokines and initiate an amplifying cascade of further cleavages. The end-result of this activation cascade is massive amplification of the response and activation of the cell-killing membrane attack complex. Over 30 proteins and protein fragments make up the complement system, including serum proteins, serosal proteins, and cell membrane receptors. They account for about 5% of the globulin fraction of blood serum and can serve as opsonins.			so:0005855	
493	Components of oligomeric golgi complex		COG		so:0005855	
495	Coronins	Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis.  Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to man.	CORO		so:0005855	
496	Cyclin dependent kinases	Cyclin-dependent kinases (CDKs) are a family of protein kinases first discovered for their role in regulating the cell cycle. They are also involved in regulating transcription, mRNA processing, and the differentiation of nerve cells.  They are present in all known eukaryotes, and their regulatory function in the cell cycle has been evolutionarily conserved. In fact, yeast cells can proliferate normally when their CDK gene has been replaced with the homologous human gene.  CDKs are relatively small proteins, with molecular weights ranging from 34 to 40 kDa, and contain little more than the kinase domain.  By definition, a CDK binds a regulatory protein called a cyclin. Without cyclin, CDK has little kinase activity; only the cyclin-CDK complex is an active kinase. CDKs phosphorylate their substrates on serines and threonines, so they are serine-threonine kinases.  The consensus sequence for the phosphorylation site in the amino acid sequence of a CDK substrate is PX, where S/T* is the phosphorylated serine or threonine, P is proline, X is any amino acid, K is lysine, and R is arginine	CDK		so:0005855	
497	Cytochrome b561	Cytochrome b561 is an integral membrane protein responsible for electron transport, binding two heme groups non-covalently.  It is a family of ascorbate -dependent oxidoreductase enzymes. 	CYB561		so:0005855	
498	DDB1 and CUL4 associated factors		DCAF		so:0005855	
499	DEAD-box helicases	DEAD box proteins are involved in an assortment of metabolic processes that typically involve RNAs, but in some cases also other nucleic acids. They are highly conserved in nine motifs and can be found in both prokaryotes and eukaryotes, but not all. Many organisms, including humans, contain DEAD-box helicases, which are involved in RNA metabolism.	DDX		hgnc.genegroup:1168	
50	ADAM metallopeptidases with thrombospondin type 1 motif		ADAMTS		hgnc.genegroup:901	
500	DEAH-box helicases		DHX		hgnc.genegroup:1168	
501	Defensins	Families of microbicidal and cytotoxic peptides. Defensins have antibacterial, antifungal and antiviral properties. Defensins kills cells by forming voltage-regulated multimeric channels in the susceptible cell's membrane.			so:0005855	
502	Defensins, alpha	Alpha defensins are a family of mammalian defensin peptides. Defensins are 2-6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses,  containing three pairs of intramolecular disulfide bonds. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. Alpha-defensins, which have been identified in humans, monkeys and several rodent species, are particularly abundant in neutrophils, certain macrophage populations and Paneth cells of the small intestine. 	DEFA		hgnc.genegroup:501	
503	Defensins, beta	Beta defensins are a family of mammalian defensins. The beta defensins are antimicrobial peptides implicated in the resistance of epithelial surfaces to microbial colonization. Defensins are 2-6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses,  containing three pairs of intramolecular disulfide bonds. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. Every mammalian species explored thus far has beta-defensins. In cows, as many as 13 beta-defensins exist in neutrophils. However, in other species, beta-defensins are more often produced by epithelial cells lining various organs (e.g. the epidermis, bronchial tree and genitourinary tract. Human, rabbit and guinea-pig beta-defensins, as well as human beta-defensin-2 (hBD2), induce the activation and degranulation of mast cells, resulting in the release of histamine and prostaglandin D2.	DEFB		hgnc.genegroup:501	
504	DENN domain containing		DENND		so:0005855	
505	Dishevelled segment polarity proteins		DVL		so:0005855	
506	Basic leucine zipper proteins	The Basic Leucine Zipper Domain ( bZIP domain ) is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors.			so:0005855	
508	Forkhead boxes	FOX (Forkhead box) proteins are a family of transcription factors that play important roles in regulating the expression of genes involved in cell growth, proliferation, differentiation, and longevity. Many FOX proteins are important to embryonic development.  FOX proteins also have pioneering transcription activity by being able to bind condensed chromatin during cell differentiation processes.  The defining feature of FOX proteins is the forkhead box, a sequence of 80 to 100 amino acids forming a motif that binds to DNA. This forkhead motif is also known as the winged helix due to the butterfly-like appearance of the loops in the protein structure of the domain.  Forkhead genes are a subgroup of the helix-turn-helix class of proteins.	FOX		so:0005855	
510	High mobility group	High-Mobility Group or HMG is a group of chromosomal proteins that are involved in the regulation of DNA-dependent processes such as transcription, replication, recombination, and DNA repair.	HMG		so:0005855	
511	Canonical high mobility group				hgnc.genegroup:510	
512	Non-canonical high mobility group				hgnc.genegroup:510	
516	Homeoboxes	Protein which contains at least one homeobox, a conserved sequence originally detected, on the nucleotide level, in many of the genes which give rise to homeotic and segmentation mutants in Drosophila. The homeobox, also termed homeodomain, consists of about 60 amino acids and is involved in DNA-binding.			so:0005855	
517	ANTP class homeoboxes				hgnc.genegroup:516	
518	HOXL subclass homeoboxes				hgnc.genegroup:517	
519	NKL subclass homeoboxes and pseudogenes				hgnc.genegroup:517	
521	PRD class homeoboxes and pseudogenes				hgnc.genegroup:516	
522	LIM class homeoboxes				hgnc.genegroup:516|hgnc.genegroup:1218	
523	POU class homeoboxes and pseudogenes		POU		hgnc.genegroup:516	
524	HNF class homeoboxes				hgnc.genegroup:516	
525	SINE class homeoboxes		SIX		hgnc.genegroup:516	
526	TALE class homeoboxes and pseudogenes				hgnc.genegroup:516	
527	CUT class homeoboxes and pseudogenes				hgnc.genegroup:516	
528	PROS class homeoboxes		PROX		hgnc.genegroup:516	
529	ZF class homeoboxes and pseudogenes				hgnc.genegroup:516	
53	Adenylate cyclases	The adenylate cyclases break ATP down into 3',5'-cyclic AMP and diphosphate.	ADCY		so:0005855	
530	CERS class homeoboxes		CERS		hgnc.genegroup:1374|hgnc.genegroup:516	
532	Myb/SANT domain containing				so:0005855	
533	Helix-turn-helix CENPB type domain containing				so:0005855	
534	ETS transcription factor family				so:0005855	
535	DNA polymerases	Enzyme that catalyzes DNA synthesis by addition of deoxyribonucleotide units to a DNA chain using DNA as a template. They can also possess exonuclease activity and therefore function in DNA repair.	POL		so:0005855	
536	Dyneins, axonemal	Axonemal dyneins come in multiple forms that contain either one, two or three non-identical heavy chains (depending upon the organism and location in the cilium). Each heavy chain has a globular motor domain with a doughnut-shaped structure believed to resemble that of other AAA proteins, a coiled coil 'stalk' that binds to the microtubule, and an extended tail (or 'stem') that attaches to a neighboring microtubule of the same axoneme. Each dynein molecule thus forms a cross-bridge between two adjacent microtubules of the ciliary axoneme.	DNA		hgnc.genegroup:537	
537	Dyneins	Dynein is a motor protein (also called molecular motor or motor molecule) in cells which converts the chemical energy contained in ATP into the mechanical energy of movement. Dynein transports various cellular cargo by 'walking' along cytoskeletal microtubules towards the minus-end of the microtubule, which is usually oriented towards the cell center. Thus, they are called 'minus-end directed motors.' This form of transport is known as retrograde transport. In contrast, kinesins, which are motor proteins that move toward the microtubules' plus end, are called plus-end directed motors.			so:0005855	
538	Dyneins, cytoplasmic	Cytoplasmic dynein, which has a molecular mass of about 1.5 megadaltons (MDa), contains approximately twelve polypeptide subunits: two identical 'heavy chains', 520 kDa in mass, which contain the ATPase activity and are thus responsible for generating movement along the microtubule; two 74 kDa intermediate chains which are believed to anchor the dynein to its cargo; four 53–59 kDa intermediate chains; and several light chains which are less understood.	DYN		hgnc.genegroup:537	
539	Elongator acetyltransferase complex 		ELP		so:0005855	
540	EMI domain containing	In molecular biology, the EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine -rich protein domain of around 75 amino acids. The EMI domain is most often found at the N terminus of metazoan extracellular proteins that are forming or are compatible with multimer formation.  It is found in association with other domains, such as C1q, laminin-type EGF-like, collagen-like, FN3, WAP, ZP or FAS1.  It has been suggested that the EMI domain could be a protein-protein interaction module, as the EMI domain of EMILIN-1 was found to interact with the C1q domain of EMILIN-2. 			so:0005855	
542	Receptor ligands				so:0005855	
543	Engulfment and cell motility proteins	ELMO (Engulfment and Cell Motility) is a family of related proteins (~82 kDa) involved in intracellular signalling networks. These proteins have no intrinsic catalytic activity and instead function as adaptors which can regulate the activity of other proteins through their ability to mediate protein-protein interactions.	ELMO		hgnc.genegroup:1492|hgnc.genegroup:1813	
544	Exonucleases	Enzyme that degrades DNA or RNA by progressively splitting off single nucleotides from one end of the chain.			so:0005855	
546	Ephrins	Ephrins also known as ephrin ligands or Eph family receptor interacting proteins are a family of proteins that serve as the ligands of the ephrin receptor. Ephrin receptors in turn compose the largest known subfamily of receptor protein-tyrosine kinases (RTKs). Since ephrin ligands (ephrins) and Eph receptors (Ephs) are both membrane-bound proteins, binding and activation of Ephepherin signaling regulates a variety of biological processes during embryonic development including the guidance of axon growth cones, formation of tissue boundaries,  cell migration, and segmentation. Additionally, Eph/epherin signaling has recently been identified to play a critical role in the maintenance of several processes during adulthood including long-term potentiation, angiogenesis, and stem cell differentiation.	EFN		hgnc.genegroup:542	
547	Exportins		XPO		hgnc.genegroup:1492	
548	FA complementation groups		FANC		so:0005855	
550	Fatty acid binding protein family		FABP		hgnc.genegroup:632	
552	Fatty acid hydroxylase domain containing				so:0005855	
553	Fatty acid desaturases	A fatty acid desaturase is an enzyme that removes two hydrogen atoms from a fatty acid, creating a carbon /carbon double bond.	FADS		so:0005855	
554	Fibrinogen C domain containing				so:0005855	
555	Fibronectin type III domain containing				so:0005855	
556	Fibulins	Fibulin (FY-beau-lin) (now known as Fibulin-1 FBLN1 ) is the prototypic member of a multigene family, currently with seven members. Fibulin-1 is a calcium-binding glycoprotein. In vertebrates, fibulin-1 is found in blood and extracellular matrices. In the extracellular matrix, fibulin-1 associates with basement membranes and elastic fibers. The association with these matrix structures is mediated by its ability to interact with numerous extracellular matrix constituents including fibronectin, proteoglycans, laminins and tropoelastin. In blood, fibulin-1 binds to fibrinogen and incorporates into clots. Fibulins are secreted glycoproteins that become incorporated into a fibrillar extracellular matrix when expressed by cultured cells or added exogenously to cell monolayers.  The five known members of the family share an elongated structure and many calcium-binding sites, owing to the presence of tandem arrays of epidermal growth factor-like domains. They have overlapping binding sites for several basement-membrane proteins, tropoelastin, fibrillin, fibronectin and proteoglycans, and they participate in diverse supramolecular structures. The amino-terminal domain I of fibulin consists of three anaphylatoxin -like (AT) modules, each approximately 40 residues long and containing four or six cysteines. The structure of an AT module was determined for the complement-derived anaphylatoxin C3a, and was found to be a compact alpha-helical fold that is stabilized by three disulphide bridges in the pattern Cys14, Cys25 and Cys36 (where Cys is cysteine). The bulk of the remaining portion of the fibulin molecule is a series of nine EGF-like repeats.	FBLN		so:0005855	
557	F-boxes	F-box proteins are proteins containing at least one F-box domain. The first identified F-box protein is one of three components of the SCF complex, which mediates ubiquitination of proteins targeted for degradation by the proteasome. F-box proteins have also been associated with cellular functions such as signal transduction and regulation of the cell cycle. In plants, many F-box proteins are represented in gene networks broadly regulated by microRNA -mediated gene silencing via RNA interference. In human cells, in high-iron condition, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2. The F-box domain is a protein structural motif of about 50 amino acids that mediates protein–protein interactions. It was first identified in cyclin F. The F-box motif interacts directly with the SCF protein Skp1, and F-box domains commonly exist in proteins in concert with other protein–protein interaction motifs such as leucine-rich repeats and WD repeats, which are thought to mediate interactions with SCF substrates.	FBX		hgnc.genegroup:1171	
558	F-box and leucine rich repeat proteins		FBXL		hgnc.genegroup:557	
559	F-box and WD repeat domain containing		FBXW		hgnc.genegroup:557	
56	IZUMO family		IZUMO		so:0005855	
560	F-boxes other	FBXO group members contain F-box domains and may contain other unrelated domains. The word 'other' is to distinguish this subgroup from the other two F-box subgroups: FBXW (members contain F-box domains and WD40 repeats) and FBXL (members contain F-box domains and leucine-rich repeats).	FBXO		hgnc.genegroup:557	
561	Fermitins	The [fermitin or] kindlin family of proteins each contain a bipartite FERM domain comprising four subdomains F0, F1, F2, and F3 that show homology with the FERM head (H) domain of the cytoskeletal Talin protein. Kindlins have been linked to Kindler syndrome, leukocyte adhesion deficiency, cancer and other acquired human diseases. They are essential in the organisation of focal adhesions that mediate cell-extracellular matrix junctions and are involved in other cellular compartments that control cell-cell contacts and nucleus functioning. Therefore they are responsible for cell to cell crosstalk via cell-cell contacts and integrin mediated cell adhesion through focal adhesion proteins and as specialised adhesion structures of hematopoietic cells they are also present in podosome's F actin surrounding ring structure.	FERMT		so:0005855	
562	Gamma-aminobutyric acid (GABA) receptors	The GABA receptors are a class of receptors that respond to the neurotransmitter gamma-aminobutyric acid (GABA), the chief inhibitory neurotransmitter in the vertebrate central nervous system. There are two classes of GABA receptors: GABA A and GABA B. GABA A receptors are ligand-gated ion channels (also known as ionotropic receptors), whereas GABA B receptors are G protein-coupled receptors (also known as metabotropic receptors ).			so:0005855	
563	Gamma-aminobutyric acid type A receptor subunits	The GABA A receptor (GABA AR) is an ionotropic receptor and ligand-gated ion channel. Its endogenous ligand is gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system. Upon activation, the GABA A receptor selectively conducts Cl-ˆ’ through its pore, resulting in hyperpolarization of the neuron. This causes an inhibitory effect on neurotransmission by diminishing the chance of a successful action potential occurring. The reversal potential of the GABA A-mediated IPSP in normal solution is -ˆ’70 mV, contrasting the GABA B IPSP.	GABR		hgnc.genegroup:161|hgnc.genegroup:562	
564	Gamma-glutamyltransferases	Gamma-glutamyl transferase or gamma-glutamyl transpeptidase ( EC 2.3.2.2 ) is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT  catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate ). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification.	GGT		so:0005855	
565	General transcription factors	General transcription factors (GTFs), also known as basal transcriptional factors, are a class of protein transcription factors that bind to specific sites on DNA to activate transcription. GTFs, RNA polymerase, and the mediator multiple protein complex constitute the basic transcriptional apparatus.  GTFs are also intimately involved in the process of gene regulation, and most are required for life.	GTF		so:0005855	
567	Soluble glutathione S-transferases		GST		hgnc.genegroup:1470	
568	Glycerol kinases	Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes the transfer of a phosphate from ATP to glycerol thus forming glycerol phosphate (ATP + glycerol <=> ADP + sn-glycerol 3-phosphate ). Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. This glycerol is instead shuttled to the liver via the blood where it is:	GK		so:0005855	
570	Proteoglycans	Protein containing one or more covalently linked and usually sulfated glycosaminoglycans, (e.g., chondroitin sulfate, dermatan sulfate, heparan sulfate, heparin, keratan sulfate). Glycosaminoglycans are polysaccharides made of repeating disaccharides (usually 40-100 times), which consist of uronic acid (or galactose) and hexosamines. Aggrecan, for example, is the major component in articular cartilage.			so:0005855	
571	Syndecans	Syndecans are single transmembrane domain proteins that are thought to act as coreceptors, especially for G protein-coupled receptors. These core proteins carry three to five heparan sulfate and chondroitin sulfate chains, which allow for interaction with a large variety of ligands including fibroblast growth factors, vascular endothelial growth factor, transforming growth factor -beta, fibronectin and antithrombin -1. Interactions between fibronectin and some syndecans can be modulated by the extracellular matrix protein tenascin C.	SDC		hgnc.genegroup:570	
572	Glypicans	Glypicans constitute one of the two major families of heparan sulfate proteoglycans, with the other major family being syndecans. Six glypicans have been identified in mammals, and are referred to as GPC1 through GPC6.	GPC		hgnc.genegroup:570	
573	Small leucine rich repeat proteoglycans				hgnc.genegroup:570	
574	Hyalectan proteoglycans	Lecticans, also known as hyalectans, are a family of proteoglycans (a type protein that is attached to chains of negatively charged polysaccharides ) that are components of the extracellular matrix. There are four members of the lectican family: aggrecan, brevican, neurocan, and versican. Lecticans interact with hyaluronan and tenascin-R to form a ternary complex. 			hgnc.genegroup:570	
575	Collagen proteoglycans				hgnc.genegroup:570	
578	GPN-loop GTPases		GPN		so:0005855	
579	G-patch domain containing		GPATCH		so:0005855	
58	Ring finger proteins	In molecular biology, a RING (Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a Cys 3 HisCys 4 amino acid motif which binds two zinc cations. This protein domain contains from 40 to 60 amino acids. Many proteins containing a RING finger play a key role in the ubiquitination pathway.	RNF		hgnc.genegroup:26	
580	GTPases, IMAP		GIMAP		so:0005855	
581	HAUS augmin like complex 		HAUS		so:0005855	
582	Heat shock proteins	Heat shock proteins (HSP) are a group of proteins induced by heat shock, the most prominent members of this group are a class of functionally related proteins involved in the folding and unfolding of other proteins. Their expression is increased when cells are exposed to elevated temperatures or other stress.  This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF).			so:0005855	
583	Heat shock 70kDa proteins	The 70 kilodalton heat shock proteins ( Hsp70 s) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress.	HSPA		hgnc.genegroup:582	
584	DNAJ (HSP40) heat shock proteins	In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans.	DNAJ		hgnc.genegroup:582	
585	Small heat shock proteins		HSPB		hgnc.genegroup:582	
586	Heat shock 90kDa proteins	Hsp90 ( heat shock protein 90 ) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species.  As their name implies, heat shock proteins protect cells when stressed by elevated temperatures. They account for 1-2% of total protein in unstressed cells. However, when cells are heated, the fraction of heat shock proteins increases to 4-€“6% of cellular proteins. 	HSP90		hgnc.genegroup:582	
587	Chaperonins	Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional form. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones. The energy to fold proteins is supplied by adenosine triphosphate (ATP).			hgnc.genegroup:582	
588	Histocompatibility complex	The major histocompatibility complex ( MHC ) is a set of cell surface molecules encoded by a large gene family in all vertebrates. MHC molecules mediate interactions of leukocytes, also called white blood cells (WBCs), which are immune cells, with other leukocytes or body cells. MHC determines compatibility of donors for organ transplant as well as one's susceptibility to an autoimmune disease via crossreacting immunization.	HLA		so:0005855	
589	Immunoglobulin superfamily domain containing	The immunoglobulin superfamily (IgSF) is a large group of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. Molecules are categorized as members of this superfamily based on shared structural features with immunoglobulins (also known as antibodies); they all possess a domain known as an immunoglobulin domain or fold. Members of the IgSF include cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins. They are commonly associated with roles in the immune system.			so:0005855	
59	Tripartite motif family		TRIM		so:0005855	
590	V-set domain containing	V-set domains are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families, including immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2), CD4, CD80, and CD86; in myelin membrane adhesion molecules; in junction adhesion molecules (JAM); in tyrosine-protein kinase receptors; and in the programmed cell death protein 1 (PD1).			hgnc.genegroup:589	
591	C1-set domain containing	C1-set domains are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system.			hgnc.genegroup:589	
592	C2-set domain containing	C2-set domains, which are Ig-like domains resembling the antibody constant domain. C2-set domains are found primarily in the mammalian T-cell surface antigens CD2 (Cluster of Differentiation 2), CD4 and CD80, as well as in vascular (VCAM) and intercellular (ICAM) cell adhesion molecules.			hgnc.genegroup:589	
593	I-set domain containing				hgnc.genegroup:589	
594	Immunoglobulin like domain containing				hgnc.genegroup:589	
595	INO80 complex 		INO80		so:0005855	
596	Importins	Importin is a type of protein that moves other protein molecules into the nucleus by binding to a specific recognition sequence, called the nuclear localization signal (NLS). Importin is classified as a karyopherin.  Importin has two subunits, importin alpha and importin beta. Members of the importin-beta family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha.	IPO		so:0005855	
597	Integrins	Protein of the integrin family of cell surface heterodimeric receptors that mediates dynamic cell-to-cell as well as cell-to-matrix adhesion. Integrins function as mechanochemical sensors and transducers able to change rapidly and reversibly their adhesive functions by modulating their ligand-binding affinity. Each subunit has a large N-terminal extracellular domain followed by a transmembrane domain and a short C-terminal cytoplasmic region. Some subclasses of integrins share a common beta chain while having different alpha chains.	ITG		so:0005855	
598	Interferons	Interferons (IFNs) are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites or tumor cells. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs belong to the large class of glycoproteins known as cytokines. Interferons are named after their ability to 'interfere' with viral replication within host cells. IFNs have other functions: they activate immune cells, such as natural killer cells and macrophages ; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes ; and they increase the ability of uninfected host cells to resist new infection by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. 	IFN		hgnc.genegroup:542	
599	Interferon receptors				so:0005855	
6	ZYG11 cell cycle regulator family		ZYG11		so:0005855	
60	Membrane associated ring-CH-type fingers		MARCHF		so:0005855	
601	Interleukins	Interleukins are a group of cytokines (secreted proteins and signaling molecules ) that were first seen to be expressed by white blood cells ( leukocytes ).  The function of the immune system depends in a large part on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency. The majority of interleukins are synthesized by helper CD4 T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T and B lymphocytes, and hematopoietic cells. Interleukin receptors on astrocytes in the hippocampus are also known to be involved in the development of spatial memories in mice.	IL		hgnc.genegroup:542	
602	Interleukin receptors	An interleukin receptor is a cytokine receptor for interleukins.			so:0005855	
607	Intermediate filaments	Intermediate filaments (IF) are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide and intermediate in size between microtubules and microfilaments. This family of protein includes cytokeratins, vimentin, desmin, glial fibrillary acidic protein, neurofilament proteins and nestin. All IF proteins are structurally similar in that they consist of: a central rod domain which is arranged in coiled-coiled alpha-helices, with at least two short characteristic interruptions; an N-terminal non-helical domain (head) of variable length; and an C-terminal domain (tail) which is also non-helical and shows extreme length variation between different IF proteins.			so:0005855	
608	Keratins, type I	These proteins are the most diverse among IFs and constitute type I (acidic) and type II (basic) IF proteins. The many isoforms are divided in two groups:      epithelial keratins (about 20) in epithelial cells     trichocytic keratins (about 13) (hair keratins), which make up hair, nails, horns and reptilian scales.  Regardless of the group, keratins are either acidic or basic. Acidic and basic keratins bind each other to form acidic-basic heterodimers and these heterodimers then associate to make a keratin filament.			hgnc.genegroup:1109	
609	Keratins, type II	These proteins are the most diverse among IFs and constitute type I (acidic) and type II (basic) IF proteins. The many isoforms are divided in two groups:      epithelial keratins (about 20) in epithelial cells (image to right)     trichocytic keratins (about 13) (hair keratins), which make up hair, nails, horns and reptilian scales.  Regardless of the group, keratins are either acidic or basic. Acidic and basic keratins bind each other to form acidic-basic heterodimers and these heterodimers then associate to make a keratin filament.			hgnc.genegroup:1109	
61	Polycomb group ring fingers	Polycomb-group proteins are a family of proteins first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place. Polycomb-group proteins are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies ( Drosophila melanogaster ).	PCGF		so:0005855	
610	Intermediate filaments Type III				hgnc.genegroup:607	
611	Intermediate filaments Type IV				hgnc.genegroup:607	
612	Lamins	Nuclear lamins (not to be confused with laminins ), also known as Class V intermediate filaments, are fibrous proteins providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with membrane-associated proteins to form the nuclear lamina on the interior of the nuclear envelope. They are involved in the breakdown and reformation of the nuclear envelope during mitosis, as well as the positioning of nuclear pores.	LMN		hgnc.genegroup:607	
613	Beaded filament structural proteins	The beaded filament structural proteins are components of the cytoskeleton in the eye lens.	BFSP		hgnc.genegroup:607	
614	Intermediate filament family orphans		IFFO		hgnc.genegroup:607	
615	Intraflagellar transport complexes	Intraflagellar transport or IFT is a bidirectional motility along axonemal microtubules that is essential for the formation ( ciliogenesis ) and maintenance of most eukaryotic cilia and flagella. It is thought to be required to build all cilia that assemble within a membrane projection from the cell surface.  The process of IFT has been best characterized in the biflagellate alga Chlamydomonas reinhardtii as well as the sensory cilia of the nematode Caenorhabditis elegans. It has been suggested based on localization studies that IFT proteins also function outside of cilia.			so:0005855	
616	Kallikreins	Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein ( KLKB1 ) has no known homologue, while tissue kallikrein-related peptidases ( KLKs ) encode a family of fifteen closely related serine proteases. These genes are localised to chromosome 19q13, forming the largest contiguous cluster of proteases within the human genome. Kallikreins are responsible for the coordination of various physiological functions including blood pressure, semen liquefaction and skin desquamation.	KLK		so:0005855	
617	Kelch like	Kelch proteins (and Kelch-like proteins) are a widespread group of proteins that contain multiple Kelch motifs. The kelch domain generally occurs as a set of five to seven kelch repeats that form a beta-propeller tertiary structure. Kelch-repeat beta-propellers are generally involved in protein-protein interactions, though the large diversity of domain architectures and limited sequence identity between kelch motifs make characterisation of the kelch superfamily difficult.	KLHL		so:0005855	
619	Keratin associated proteins		KRTAP		so:0005855	
620	Killer cell immunoglobulin like receptors	Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface proteins found on important cells of the immune system called natural killer (NK) cells. They regulate the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to detect virally infected cells or tumor cells that have a characteristic low level of Class I MHC on their surface. Most KIRs are inhibitory, meaning that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the ability to activate cells.  KIR molecules are highly polymorphic, meaning their gene sequences differ greatly between individuals, so that different individuals possess different arrays/repertoires of KIR genes.	KIR		hgnc.genegroup:594	
621	Killer cell lectin like receptors		KLR		so:0005855	
622	Kinesins	A kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule filaments, and are powered by the hydrolysis of ATP (thus kinesins are ATPases ). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo from the centre of the cell towards the periphery. This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the microtubules' minus end.	KIF		so:0005855	
623	KN motif and ankyrin repeat domain containing		KANK		hgnc.genegroup:403	
624	KLF transcription factors	The Kruppel-like family of transcription factors (KLFs) are a set of zinc finger DNA-binding proteins that regulate gene expression.	KLF		so:0005855	
625	La ribonucleoproteins		LARP		so:0005855	
626	Laminin subunits	Laminins are major proteins in the basal lamina (one of the layers of the basement membrane), a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion, as well as phenotype and survival.	LAM		so:0005855	
627	Late cornified envelope proteins		LCE		hgnc.genegroup:1353|hgnc.genegroup:1354	
628	Latent transforming growth factor beta binding proteins		LTBP		so:0005855	
629	Galectins	The LGALS genes encode soluble lectins that are referred to as the galectins, galactoside-binding lectins or S-type lectins.	LGALS		so:0005855	
63	Zinc fingers AN1-type	In molecular biology, the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1, a ubiquitin-like protein in Xenopus laevis.  The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.	ZFAND		hgnc.genegroup:26	
630	Leukocyte immunoglobulin like receptors	The leukocyte immunoglobulin-like receptors (LILR) are a family of receptors possessing extracellular immunoglobulin domains. They are also known as CD85, ILTs and LIR, and can exert immunomodulatory effects on a wide range of immune cells.  The human genes encoding these receptors are found in a gene cluster at chromosomal region 19q13.4.	LILR		hgnc.genegroup:594	
631	Lipocalins	The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids. They share limited regions of sequence homology and a common tertiary structure architecture.    This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosing an internal ligand binding site.  These proteins are found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants. Lipocalins have been associated with many biological processes, among them immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions.	LCN		hgnc.genegroup:632	
632	Calycin structural superfamily				so:0005855	
634	Low density lipoprotein receptors	The low-density lipoprotein receptor gene family codes for a class of structurally related cell surface receptors that fulfill diverse biological functions in different organs, tissues, and cell types.  The role that is most commonly associated with this evolutionarily ancient family is cholesterol homeostasis (maintenance of appropriate concentration of cholesterol). In humans, excess cholesterol in the blood is captured by low-density lipoprotein (LDL) and removed by the liver via endocytosis of the LDL receptor.	LRP		so:0005855	
635	LYR motif containing	This family of short proteins includes proteins from the NADH-ubiquinone oxidoreductase complex I. The family includes the B14 subunit from bovine NADH-ubiquinone oxidoreductase B14 subunit, and the B22 [NDUFB9] subunit from the human enzyme. The family has been named LYR after a highly conserved tripeptide motif close to the N terminus of these proteins.	LYRM		so:0005855	
636	Maestro heat like repeat containing 	Maestro family members are all related by homology and all contain HEAT repeats, or regions that are highly similar to HEAT repeats.	MROH		hgnc.genegroup:1492	
637	MAX dimerization proteins		MXD		so:0005855	
638	Metallothioneins	Metallothionein (MT) is a family of cysteine-rich, low molecular weight (MW ranging from 500 to 14000 Da ) proteins. They are localized to the membrane of the Golgi apparatus. MTs have the capacity to bind both physiological (such as zinc, copper, selenium ) and xenobiotic (such as cadmium, mercury, silver, arsenic ) heavy metals through the thiol group of its cysteine residues, which represents nearly the 30% of its amino acidic residues.  	MT		so:0005855	
639	Mitochondrial respiratory chain complexes				so:0005855	
64	Zinc fingers BED-type	In molecular biology the BED-type zinc finger domain is a protein domain which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain.	ZBED		hgnc.genegroup:26	
640	Mitochondrial complex I: NADH:ubiquinone oxidoreductase subunits	Complex I ( EC 1.6.5.3 ) (also referred to as NADH:ubiquinone oxidoreductase or, especially in the context of the human protein, NADH dehydrogenase (ubiquinone) ) is an enzyme of the respiratory chains of myriad organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and, in eukaryotes, it is located in the inner mitochondrial membrane. It is one of the 'entry enzymes' of oxidative phosphorylation in the mitochondria.			hgnc.genegroup:639	
641	Mitochondrial complex II: succinate dehydrogenase subunits	Succinate dehydrogenase or succinate-coenzyme Q reductase (SQR) or respiratory Complex II is an enzyme complex, bound to the inner mitochondrial membrane of mammalian mitochondria and many bacterial cells. It is the only enzyme that participates in both the citric acid cycle and the electron transport chain. In step 6 of the citric acid cycle, SQR catalyzes the oxidation of succinate to fumarate with the reduction of ubiquinone to ubiquinol. This occurs in the inner mitochondrial membrane by coupling the two reactions together.	SDH		hgnc.genegroup:639	
642	Mitochondrial complex III: ubiquinol-cytochrome c reductase complex subunits	The coenzyme Q : cytochrome c-oxidoreductase, sometimes called the cytochrome bc 1 complex, and at other times complex III, is the third complex in the electron transport chain ( EC 1.10.2.2 ), playing a critical role in biochemical generation of ATP ( oxidative phosphorylation ). Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial ( cytochrome b ) and the nuclear genomes (all other subunits). Complex III is present in the mitochondria of all animals and all aerobic eukaryotes and the inner membranes of most eubacteria.	UQCR		hgnc.genegroup:639	
643	Mitochondrial complex IV: cytochrome c oxidase subunits	The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1 ) is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes. It is the last enzyme in the respiratory electron transport chain of mitochondria (or bacteria) located in the mitochondrial (or bacterial) membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water, and in addition translocates four protons across the membrane, helping to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.	COX, MT-CO		hgnc.genegroup:639	
644	Mitochondrial complex V: ATP synthase subunits	ATP synthase ( EC 3.6.3.14 ) is an important enzyme that provides energy for the cell to use through the synthesis of adenosine triphosphate (ATP). ATP is the most commonly used 'energy currency' of cells from most organisms. It is formed from adenosine diphosphate (ADP) and inorganic phosphate (P i), and needs energy. The overall reaction sequence is: ADP + P = ATP, where ADP and P i are joined together by ATP synthase Energy is often released in the form of hydrogen ions ( H+ ), moving down an electrochemical gradient, such as from the lumen into the stroma of chloroplasts or from the inter-membrane space into the matrix in mitochondria.	ATP5, MT-ATP		hgnc.genegroup:639|hgnc.genegroup:412	
645	Mitochondrial respiratory chain complex assembly factors				so:0005855	
646	Mitochondrial ribosomal proteins		MRP		hgnc.genegroup:1054	
647	MOB kinase activators		MOB		so:0005855	
648	Mucins	Mucins are a family of high molecular weight, heavily glycosylated proteins ( glycoconjugates ) produced by epithelial tissues in most metazoans.  Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers.  They often take an inhibitory role.  Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms  and bone formation in vertebrates.  They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer.  Although some mucins are membrane -bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, most mucins are secreted onto mucosal surfaces or secreted to become a component of saliva.	MUC		so:0005855	
649	Myocyte enhancer factor 2 proteins	In the field of molecular biology, myocyte enhancer factor-2 ( Mef2 ) proteins are a family of transcription factors which through control of gene expression are important regulators of cellular differentiation and consequently play a critical role in embryonic development. In adult organisms, Mef2 proteins mediate the stress response in some tissues.  Mef2 proteins contain both MADS-box and Mef2 DNA-binding domains.	MEF2		so:0005855	
65	THAP domain containing	The THAP-type zinc finger (consensus: C-x(2,4)-C-x(35,50)-C-x(2)-H) is an ~90-residue domain restricted to animals, which is shared between the THAP family of cellular DNA-binding proteins, and transposases from mobile genomic parasites (<a href='https://pubmed.ncbi.nlm.nih.gov/12575992/'>PMID: 12575992</a>, <a href='https://pubmed.ncbi.nlm.nih.gov/12717420/'>PMID: 12717420</a>). THAP1, the prototype of the THAP family, possesses zinc-dependent sequence-specific DNA binding activity and recognizes a consensus DNA target sequence of 11 nucleotides (<a href='https://pubmed.ncbi.nlm.nih.gov/15863623/'>PMID: 15863623</a>). The THAP-type zinc finger can be found in one or more copies and can be associated with other domains, such as the C2H2-type zinc finger.  The structure of the THAP-type zinc finger reveals the presence between the C2CH zinc coordinating residues of a short antiparallel β-sheet interspersed by a long loop-helix-loop insertion. This loop-helix-loop motif has been shown to be essential for the identification of a number of critical residues for DNA recognition  (<a href='https://pubmed.ncbi.nlm.nih.gov/18073205/'>PMID: 18073205</a>).	THAP		hgnc.genegroup:26	
651	Mitogen-activated protein kinases	Mitogen-activated protein kinases also known as MAP kinases are serinetyrosine-specific protein kinases belonging to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. The closest relatives of MAPKs are the cyclin-dependent kinases (CDKs).  MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis - among many others.  MAP kinases are found in eukaryotes only, but they are fairly diverse and encountered in all animals, fungi and plants, and even in an array of unicellular eukaryotes.	MAPK		hgnc.genegroup:652	
652	Mitogen-activated protein kinase cascade				so:0005855	
653	Mitogen-activated protein kinase kinases	Mitogen-activated protein kinase kinase (also known as MAP2K, MEK, MAPKK) is a kinase enzyme which phosphorylates mitogen-activated protein kinase (MAPK).  MAP2K is classified as EC 2.7.12.2. 	MAP2K		hgnc.genegroup:652	
654	Mitogen-activated protein kinase kinase kinases	MAP kinase kinase kinase (or MAP3K or MEKK ) is a serine/threonine-specific protein kinase which acts upon MAP kinase kinase.	MAP3K		hgnc.genegroup:652	
655	Mitogen-activated protein kinase kinase kinase kinases	Mitogen-activated protein kinase kinase kinase kinase (MAP4K) is a family of proteins involved in cellular signal transduction. 	MAP4K		hgnc.genegroup:652	
656	Myosin heavy chains	Myosins comprise a family of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other eukaryotic motility processes. They are responsible for actin -based motility. The term was originally used to describe a group of similar ATPases found in striated and smooth muscle cells.  Following the discovery by Pollard and Korn of enzymes with myosin-like function in Acanthamoeba castellanii, a large number of divergent myosin genes have been discovered throughout eukaryotes. Thus, although myosin was originally thought to be restricted to muscle cells (hence, 'myo'), there is no single 'myosin' but rather a huge superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous. The structure and function of myosin is strongly conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba.			so:0005855	
657	Myosin light chains	Myosin light chains are distinct and have their own properties, distinct from the heavy chains. They are not considered 'myosins' but are components of the macromolecular complexes that make up the functional myosin enzymes.	MYL		so:0005855	
658	Myosin binding proteins		MYBP		hgnc.genegroup:555	
659	Na+/K+ transporting ATPase interacting		NKAIN		so:0005855	
66	Zinc fingers C2HC-type		ZC2HC		hgnc.genegroup:26	
660	N-alpha-acetyltransferase subunits		NAA		so:0005855	
661	Netrins	Netrins are a class of proteins involved in axon guidance. They are named after the Sanskrit word 'netr', which means 'one who guides.' Netrins are genetically conserved across nematode worms, fruitflies, frogs, mice, and humans. Structurally, netrin resembles the extracellular matrix protein laminin. 	NTN		so:0005855	
662	NBPF members		NBPF		so:0005855	
663	N-terminal EF-hand calcium binding proteins		NECAB		so:0005855	
664	NOP2/Sun RNA methyltransferase family		NSUN		hgnc.genegroup:2060	
665	Nuclear factors of activated T-cells 	Nuclear factor of activated T-cells ( NFAT ) is a general name applied to a family of transcription factors shown to be important in immune response. One or more members of the NFAT family is expressed in most cells of the immune system. NFAT is also involved in the development of cardiac, skeletal muscle, and nervous systems. The NFAT transcription factor family consists of five members NFATc1, NFATc2, NFATc3, NFATc4, and NFAT5. NFATc1 through NFATc4 are regulated by calcium signaling.	NFAT		so:0005855	
666	NLR family		NLR		so:0005855	
667	Nudix hydrolase family	The Nudix family is a protein family of phosphohydrolases.   Using water-mediated catalysis they break a phosphate bond in their substrate to create two products. There are two components to the Nudix family: the so-called Nudix fold of a beta sheet with alpha helices on each side and the Nudix motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is Isoleucine, Leucine, or Valine and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids.	NUDT		so:0005855	
668	ORAI calcium release-activated calcium modulators		ORAI		so:0005855	
669	OTU domain containing		OTU		hgnc.genegroup:996	
670	Oxysterol binding proteins	Oxysterol-binding proteins, or Oxysterol-binding protein related-proteins, or simply ORPs, are evolutionary related proteins involved in sterol synthesis and/or its regulation.  These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds oxysterols (oxygenated derivatives of cholesterol), cholesterol and phosphatidylinositol 4-phosphate (PI4P); yeast Osh1, a protein of 859 residues that plays a role in ergosterol synthesis; and yeast proteins HES1 and KES1, highly related proteins of 434 residues that seem to play a role in ergosterol synthesis	OSBP		so:0005855	
671	Paraneoplastic Ma antigens		PNMA		hgnc.genegroup:1411	
673	Parvins	The parvins are a family of proteins involved in linking integrins and associated proteins with intracellular pathways that regulate actin cytoskeletal dynamics and cell survival. 	PARV		so:0005855	
674	PATE family		PATE		so:0005855	
675	Paired boxes	Protein which contains a paired box domain, a conserved domain of about 120 amino acids, which is generally located in the N-terminal section of various proteins.	PAX		so:0005855	
676	Pellino E3 ubiquitin protein ligases		PELI		so:0005855	
677	Peptidyl arginine deiminases	This gene family encodes enzymes that catalyse the following reaction: Protein L-arginine + H(2)O <=> protein L-citrulline + NH(3). E.C. number 3.5.3.15	PADI		so:0005855	
678	Perilipins	Perilipin, also known as lipid droplet-associated protein or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.	PLIN		so:0005855	
679	Phosphatase and actin regulators		PHACTR		so:0005855	
680	Phosphatidylinositol glycan anchor biosynthesis		PIG		so:0005855	
681	Phosphodiesterases	A phosphodiesterase (PDE) is any enzyme that breaks a phosphodiester bond.  The cyclic nucleotide phosphodiesterases comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cAMP and cGMP. They regulate the localization, duration, and amplitude of cyclic nucleotide signaling within subcellular domains. PDEs are therefore important regulators of signal transduction mediated by these second messenger molecules.	PDE		so:0005855	
682	Pleckstrin homology domain containing	Pleckstrin homology domain (PH domain) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.    This domain can bind Phosphatidylinositol lipids within biological membranes (such as Phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate ),  and proteins such as the Betagamma-subunits of heterotrimeric G proteins, and protein kinase C. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.	PLEKH		so:0005855	
683	Plexins	A plexin is a protein which acts as a receptor for semaphorin. Plexin acts as a signal transduction molecule in the neuropilin-plexin receptor complex. Plexins also act as transduction factors for ITAM-DAP12-RANKL signalling pathway involved in osteoclastic differentiation.	PLXN		so:0005855	
684	Poly(ADP-ribose) polymerases	Poly (ADP-ribose) polymerase ( PARP ) is a family of proteins involved in a number of cellular processes involving mainly DNA repair and programmed cell death.	PARP		so:0005855	
685	POTE ankyrin domain containing		POTE		hgnc.genegroup:403	
686	PRAME family		PRAMEF		so:0005855	
687	Prenyltransferase alpha subunit repeat containing		PTAR		so:0005855	
690	Proteasome	Also known as the Proteasome endopeptidase complex (EC 3.4.25.1).  The complex is ATP-dependent and cleaves a wide range of peptide bonds.	PSM		so:0005855	
692	Protein disulfide isomerases	Protein disulfide isomerase or PDI is an enzyme in the endoplasmic reticulum in eukaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold.	PDI		so:0005855	
693	Protein phosphatase catalytic subunits	This family of enzymes removes phosphate groups from serine/threonine residues of proteins, thus reversing the action of serine/threonine kinase enzymes.  The enzymes listed here are related by homology and most require regulatory subunits to function.	PPP		hgnc.genegroup:814	
694	Protein phosphatase 1 regulatory subunits	PPP1R subunits (also known as PP1-interacting proteins, or PIPs) direct the substrate specificity of protein phosphatase 1 catalytic (PPP1C) subunits. The large number of PPP1Rs reflects the wide substrate range of the serine/threonine phosphatase holoenzymes.	PPP1R		so:0005855	
696	Protein phosphatase 2 regulatory subunits	PPP2R subunits direct the substrate specificity of protein phosphatase 2 catalytic (PPP2C) subunits.	PPP2R		so:0005855	
697	Protein phosphatase 3 regulatory subunits	PPP3R subunits direct the substrate specificity of protein phosphatase 3 catalytic (PPP3C) subunits.	PPP3R		so:0005855	
698	Protein phosphatase 4 regulatory subunits	PPP4R subunits direct the substrate specificity of the protein phosphatase 4 catalytic (PPP4C) subunit.	PPP4R		so:0005855	
699	Protein phosphatase 6 regulatory subunits	PPP6R subunits direct the substrate specificity of the protein phosphatase 6 catalytic (PPP6C) subunit.	PPP6R		so:0005855	
701	Protein phosphatases, Mg2+/Mn2+ dependent	The PPM family, which includes PP2C [PPM1] and pyruvate dehydrogenase phosphatase, are enzymes with Mn2+/Mg2+ metal ions that are resistant to classic inhibitors and toxins of the PPP family.	PPM		hgnc.genegroup:814	
702	HAD Asp-based protein phosphatases	The HAD phosphatase family are named after the bacterial enzyme haloacid dehydrogenase and employ an Asp-based catalytic mechanism.  This family represents HAD Asp-based protein phosphatases.			hgnc.genegroup:703|hgnc.genegroup:1083	
703	Protein phosphatases	A protein phosphatase is an enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein.			hgnc.genegroup:1076	
705	Class I classical Cys-based phosphatases	Class I phosphatases are grouped into the dual specificity phosphatases that can dephosphorylate tyrosine residues and also serine/threonine residues, and the protein tyrosine phosphatases that are subdivided into receptor and non-receptor types, which can dephosphorylate only tyrosine residues.			hgnc.genegroup:703	
71	Nuclear hormone receptors	In the field of molecular biology, nuclear receptors are a class of proteins found within cells that are responsible for sensing steroid and thyroid hormones and certain other molecules. In response, these receptors work with other proteins to regulate the expression of specific genes, thereby controlling the development, homeostasis, and metabolism of the organism. Nuclear receptors have the ability to directly bind to DNA and regulate the expression of adjacent genes, hence these receptors are classified as transcription factors.  The regulation of gene expression by nuclear receptors generally only happens when a ligand - a molecule that affects the receptor's behavior - is present. More specifically, ligand binding to a nuclear receptor results in a conformational change in the receptor, which, in turn, activates the receptor, resulting in up-regulation or down-regulation of gene expression. A unique property of nuclear receptors that differentiates them from other classes of receptors is their ability to directly interact with and control the expression of genomic DNA. As a consequence, nuclear receptors play key roles in both embryonic development and adult homeostasis. As discussed below, nuclear receptors may be classified according to either mechanism  or homology.	NR		hgnc.genegroup:26	
711	Dual specificity phosphatases	Dual-specificity phosphatase is a form of phosphatase that can act upon tyrosine or serine / threonine residues.  All [DUSPs] share a similar catalytic mechanism, by which a conserved cysteine residue forms a covalent intermediate with the phosphate group to be eliminated. The residues surrounding their calatytic core obey a rather strict consensus: His-Cys-x-x-x-x-x-Arg-Ser. The serine side chain and an additional conserved aspartate play a central role in the elimination of the Cys-linked intermediate, thus completing their enzymatic cycle.  The main difference between tyrosine-specific phosphatases and dual-specificity phosphatases lies in the width of the latter enzymes' catalytic pocket: thus they can accommodate phosphorylated serine or threonine side chains as well as phosphorylated tyrosines. 	DUSP		hgnc.genegroup:705	
712	Class II Cys-based phosphatases	LMW (low-molecular-weight) phosphatases, or acid phosphatases, act on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.  The class II PTPs contain only one member, low-molecular-weight phosphotyrosine phosphatase (LMPTP).			hgnc.genegroup:703	
713	Class III Cys-based CDC25 phosphatases		CDC25		hgnc.genegroup:703	
714	Pseudoautosomal regions	At either end of the X and Y chromosomes are homologous regions known as the pseudoautosomal regions (PARs). These two regions pair regularly at male meiosis and undergo recombination. PAR1 is at the tip of the short 'p' arms (Xp22 and Yp11) and PAR2 is at the tip of the long 'q' arms (Xq28 and Yq12). There has been a report of a third pseudoautosomal region (PAR3), but this remains uncorroborated (PMID: 23708688).			so:0005855	
715	Pseudoautosomal region 1		PAR1		hgnc.genegroup:714	
716	Pseudoautosomal region 2		PAR2		hgnc.genegroup:714	
717	Receptor accessory proteins		REEP		hgnc.genegroup:1144	
718	Receptor (G protein-coupled) activity modifying proteins		RAMP		so:0005855	
719	Receptor transporter proteins		RTP		so:0005855	
720	Regulators of G-protein signaling	RGS are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways.	RGS		so:0005855	
721	Rho GTPase activating proteins	Rho GTPase activating proteins (RhoGAPs or ARHGAPs) bind to and stimulate the GTPase activity of Rho family small GTPases.	ARHGAP		so:0005855	
722	Dbl family Rho GEFs	Rho guanine nucleotide exchange factors (RhoGEFs or ARHGEFs) activate Rho family small GTPases by catalysing the exchange of GDP for GTP.	ARHGEF		hgnc.genegroup:1958	
723	Ribonuclease A family	Ribonuclease A (RNase A) is a pancreatic ribonuclease that cleaves single-stranded RNA.	RNASE		so:0005855	
725	RNA binding motif containing		RBM		so:0005855	
726	RNA polymerase subunits	RNA polymerase (RNAP or RNApol), also known as DNA-dependent RNA polymerase, is an enzyme that produces primary transcript RNA.	POLR		so:0005855	
727	RNA pseudouridylate synthase domain containing		RPUSD		so:0005855	
728	S ribosomal proteins		RPS		hgnc.genegroup:1054	
729	L ribosomal proteins		RPL		hgnc.genegroup:1054	
73	Zinc fingers CCCH-type		ZC3H		hgnc.genegroup:26	
731	SAM and SH3 domain containing		SASH		so:0005855	
732	Septins	Septins are a group of highly conserved GTP binding proteins found in eukaryotes. In yeast cells, they build scaffolding to provide structural support during cell division and compartmentalize parts of the cell. Recent research in human cells suggests that septins build cages around bacterial pathogens, immobilizing the harmful microbes and preventing them from invading other cells.	SEPTIN		so:0005855	
733	Secreted frizzled-related proteins	The Secreted frizzled-related protein (SFRP) family consists of five secreted glycoproteins in humans (SFRP1, SFRP2, SFRP3 [FRZB], SFRP4, SFRP5) that act as extracellular signaling ligands. Each SFRP is around 300 amino acids in length and contains a cysteine-rich domain (CRD) that shares 30-50% sequence homology with the CRD of Frizzled (Fz) receptors. SFRPs are able to bind Wnt proteins and Fz receptors in the extracellular compartment. 	SFRP		so:0005855	
734	Secretoglobins		SCGB		so:0005855	
735	Secretory carrier membrane proteins		SCAMP		hgnc.genegroup:1474	
736	Semaphorins	Semaphorins are a class of secreted and membrane proteins that act as axonal growth cone guidance molecules. They primarily act as short-range inhibitory signals and signal through multimeric receptor complexes.	SEMA		so:0005855	
737	Serine and arginine rich splicing factors		SRSF		so:0005855	
738	Serine proteases	Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.	PRSS		so:0005855	
739	Serpin peptidase inhibitors	Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors).	SERPIN		so:0005855	
74	Zinc fingers CCHC-type	This fold group is defined by two short β-strands connected by a turn (zinc knuckle) followed by a short helix or loop and resembles the classical Cys2His2 motif with a large portion of the helix and β-hairpin truncated.	ZCCHC		hgnc.genegroup:26	
740	Serine peptidase inhibitors, Kazal type		SPINK		so:0005855	
741	SH2 domain containing				so:0005855	
742	Shisa family members		SHISA		so:0005855	
743	Short chain dehydrogenase/reductase superfamily	The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases.	SDR		so:0005855	
745	Sialic acid binding Ig like lectins	Siglecs (Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid. They are found primarily on the surface of immune cells and are a subset of the I-type lectins. There are 14 different mammalian Siglecs, providing an array of different functions based on cell surface receptor-ligand interactions.	SIGLECs		hgnc.genegroup:594|hgnc.genegroup:1410	
746	Solute carrier family 56, sideroflexins		SLC56, SFXN		hgnc.genegroup:752	
747	Signal regulatory proteins		SIRP		so:0005855	
748	SKI transcriptional corepressors				so:0005855	
75	Zinc fingers DBF-type	DBF4 contains an N-terminal BRCT domain and a C-terminal conserved region that could potentially coordinate one zinc atom, the DBF4-type zinc finger... which is important for the interaction with Cdc7 (<a href='https://pubmed.ncbi.nlm.nih.gov/8943332/'>PMID: 8943332</a>, <a href='https://pubmed.ncbi.nlm.nih.gov/8066465/'>PMID: 8066465</a>).	ZDBF		hgnc.genegroup:26	
750	SMAD family	SMADs are intracellular proteins that transduce extracellular signals from transforming growth factor beta ligands to the nucleus where they activate downstream gene transcription.	SMAD		so:0005855	
751	Small G protein signaling modulators		SGSM		so:0005855	
752	Solute carrier families	The solute carrier (SLC) group of membrane transport proteins include over 400 members organized into 66 families. Most members of the SLC group are located in the cell membrane.	SLC		so:0005855	
754	Sorting nexins	Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain (a phospholipid-binding motif) or through protein-protein interactions with membrane-associated protein complexes. Some members of this family have been shown to facilitate protein sorting.	SNX		so:0005855	
755	Sp transcription factors		SP		so:0005855	
756	Speedy/RINGO cell cycle regulator family		SPDY		so:0005855	
757	SRY-box transcription factors	SOX genes encode a family of transcription factors that bind to the minor groove in DNA, and belong to a super-family of genes characterized by a homologous sequence called the HMG-box (for high mobility group ). This HMG box is a DNA binding domain that is highly conserved throughout eukaryotic species. Homologues have been identified in insects, nematodes, amphibians, reptiles, birds and a range of mammals. However, HMG boxes can be very diverse in nature, with only a few amino acids being conserved between species. Sox genes are defined as containing the HMG box of a gene involved in sex determination called SRY, which resides on the Y-chromosome (Sox stands for Sry-related HMG box). There are 20 SOX genes present in humans and mice, and 8 present in Drosophila. Almost all Sox genes show at least 50% amino acid similarity with the HMG box in Sry. The family is divided into subgroups according to homology within the HMG domain and other structural motifs, as well as according to functional assays.  	SOX		so:0005855	
759	StAR related lipid transfer domain containing		STARD		so:0005855	
76	Zinc fingers DHHC-type		ZDHHC		hgnc.genegroup:26	
760	Sterile alpha motif domain containing		SAMD		so:0005855	
761	Structural maintenance of chromosomes proteins	SMC proteins represent a large family of ATPases that participate in many aspects of higher-order chromosome organization and dynamics.[1][2][3] SMC stands for Structural Maintenance of Chromosomes.	SMC		so:0005855	
762	Sulfotransferases, cytosolic		SULT		hgnc.genegroup:821	
763	Sulfotransferases, membrane bound	Sulfotransferases EC 2.8.2. are transferase enzymes that catalyze the transfer of a sulfo group (not a sulfate group) from a donor molecule to an acceptor alcohol or amine. The most common sulfo group donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In the case of alcohol as acceptor, the product is a sulfate (R-OSO3-), whereas an amine leads to a sulfo-amine (R-NH-SO3-). Both reactive groups for a sulfonation via sulfotransferases may be part of a protein, lipid, carbohydrate or steroid.			hgnc.genegroup:821	
764	Suppressors of cytokine signaling	SOCS (suppressor of cytokine signaling proteins) refers to a family of genes involved in inhibiting the JAK-STAT signaling pathway.	SOCS		so:0005855	
765	Synaptotagmins		SYT		hgnc.genegroup:823	
766	T-box transcription factors		TBX		so:0005855	
767	Tectonic proteins		TCTN		so:0005855	
768	Tetraspanins	Tetraspanins, also called tetraspans or the transmembrane 4 superfamily (TM4SF), have four transmembrane domains, intracellular N- and C-termini and two extracellular domains, one short (called the small extracellular domain or loop, SED/SEL or EC1) and one longer, typically 100 amino acid residues (the large extracellular domain/loop, LED/LEL or EC2).	TSPAN		so:0005855	
769	Tetratricopeptide repeat domain containing		TTC		so:0005855	
770	THO complex		THOC		hgnc.genegroup:1348	
772	Trafficking protein particle complex subunits		TRAPPC		so:0005855	
773	Transglutaminases	A transglutaminase is an enzyme that catalyzes the formation of an isopeptide bond between a free amine group (e.g., protein- or peptide-bound lysine ) and the acyl group at the end of the side chain of protein - or peptide -bound glutamine. The reaction also produces a molecule of ammonia. Such an enzyme is classified as EC 2.3.2.13. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis).	TGM		so:0005855	
774	Transmembrane and coiled-coil domain containing		TMCC		so:0005855	
776	tRNA-splicing endonuclease subunits		TSEN		so:0005855	
777	Tropomyosins	Tropomyosins are a large family of integral components of actin filaments that play a critical role in regulating the function of actin filaments in both muscle and nonmuscle cells. These proteins consist of rod-shaped coiled-coil hetero- or homo-dimers that lie along the α-helical groove of most actin filaments. Interaction occurs along the length of the actin filament, with dimers aligning in a head-to-tail fashion.	TPM		so:0005855	
778	Tubulins	Tubulin (tubul- + -in) is one of several members of a small family of globular proteins. The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The most common members of the tubulin family are α-tubulin and β-tubulin, the proteins that make up microtubules. Each has a molecular weight of approximately 55,000 Daltons. Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8.	TUB		so:0005855	
779	Tubulin tyrosine ligase family		TTL		so:0005855	
780	Tudor domain containing		TDRD		so:0005855	
781	Tumor necrosis factor superfamily	Tumor necrosis factors (or the TNF family) refer to a group of cytokines that can cause cell death (apoptosis).	TNFSF		hgnc.genegroup:542	
782	Tumor necrosis factor receptor superfamily	A tumor necrosis factor receptor (TNFR), or death receptor, is a trimeric cytokine receptor that binds tumor necrosis factors (TNF). 	TNFRSF		so:0005855	
783	Ubiquilin family	Ubiquilins contain a N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. They physically associate with both proteasomes and ubiquitin ligases, and thus are thought to functionally link the ubiquitination machinery to the proteasome to effect in vivo protein degradation.	UBQLN		so:0005855	
785	Ubiquitin protein ligase E3 component n-recognins		UBR		so:0005855	
788	Long non-coding RNAs	Long non-coding RNAs are defined as any genes that produce transcripts of over 200 nucleotides in length which do not appear to be translated. Wherever possible, the HGNC names these genes based on a key function or characteristic of the encoded RNA. Where no other information is available at the time of naming, we assign a systematic nomenclature as shown in the gene subgroups below.			hgnc.genegroup:475	
790	Adhesion G protein-coupled receptors	Adhesion GPCRs are structurally identified on the basis of a large extracellular region, similar to the Class B GPCR, but which is linked to the 7TM region by a 'stalk' motif containing a GPCR proteolytic site. The N-terminus often shares structural homology with proteins such as lectins and immunoglobulins, leading to the term adhesion GPCR.	ADGR		hgnc.genegroup:263	
8	Zona pellucida glycoproteins	There are four major zona pellucida glycoproteins, termed ZP1-4. ZP1, ZP3 and ZP4 bind to capacitated spermatozoa and induce the acrosome reaction. Successful fertilization depends on the ability of sperm to penetrate the extracellular matrix that surrounds the egg.	ZP		so:0005855	
805	ATP binding cassette subfamily A		ABCA		hgnc.genegroup:417	
806	ATP binding cassette subfamily B		ABCB		hgnc.genegroup:417	
807	ATP binding cassette subfamily C		ABCC		hgnc.genegroup:417	
808	ATP binding cassette subfamily D		ABCD		hgnc.genegroup:417	
809	ATP binding cassette subfamily E		ABCE		hgnc.genegroup:417	
81	Zinc fingers FYVE-type	The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two zinc ions  (<a href='https://pubmed.ncbi.nlm.nih.gov/8798641/'>PMID: 8798641</a>). The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. FYVE-type domains are divided into two known classes: FYVE domains that specifically bind to phosphatidylinositol 3-phosphate in lipid bilayers and FYVE-related domains of undetermined function (<a href='https://pubmed.ncbi.nlm.nih.gov/15576038/'>PMID: 15576038</a>).	ZFYVE		hgnc.genegroup:26	
810	ATP binding cassette subfamily F		ABCF		hgnc.genegroup:417	
811	ATP binding cassette subfamily G		ABCG		hgnc.genegroup:417	
812	Protein tyrosine phosphatases non-receptor type		PTPN		hgnc.genegroup:705	
813	Protein tyrosine phosphatases receptor type		PTPR		hgnc.genegroup:705	
814	Serine/threonine phosphatases				hgnc.genegroup:703	
816	Chitinases	Chitinases (EC 3.2.1.14, chitodextrinase, 1,4-beta-poly-N-acetylglucosaminidase, poly-beta-glucosaminidase, beta-1,4-poly-N-acetyl glucosamidinase, poly glycanohydrolase, (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin.  As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin  or dissolve and digest the chitin of fungi or animals.	CHI		hgnc.genegroup:1650	
817	Exosome complex	The exosome complex (or PM/Scl complex, often just called the exosome) is a multi-protein complex capable of degrading various types of RNA (ribonucleic acid) molecules. Exosome complexes are found in both eukaryotic cells and archaea, while in bacteria a simpler complex called the degradosome carries out similar functions. The core of the exosome contains a six-membered ring structure to which other proteins are attached. In eukaryotic cells, the exosome complex is present in the cytoplasm, nucleus and especially the nucleolus, although different proteins interact with the exosome complex in these compartments regulating the RNA degradation activity of the complex to substrates specific to these cell compartments. Substrates of the exosome include messenger RNA, ribosomal RNA, and many species of small RNAs. The exosome has an exoribonucleolytic function, meaning it degrades RNA starting at one end (the 3′ end in this case), and in eukaryotes also an endoribonucleolytic function, meaning it cleaves RNA at sites within the molecule. Several proteins in the exosome are the target of autoantibodies in patients with specific autoimmune diseases (especially the PM/Scl overlap syndrome ) and some antimetabolitic chemotherapies for cancer function by blocking the activity of the exosome. In addition, mutations in exosome component 3 cause pontocerebellar hypoplasia and spinal motor neuron disease.	EXOSC		so:0005855	
818	Syntaxins	Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis. 	STX		hgnc.genegroup:1124	
819	Guanylate cyclases	Guanylate cyclase ( EC 4.6.1.2, also known as guanylyl cyclase, guanyl cyclase, or GC) is a lyase enzyme.	GUCY		so:0005855	
82	GATA zinc finger domain containing	In molecular biology, GATA zinc fingers are zinc-containing domains found in a number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins). Some members of this class of zinc fingers specifically bind the DNA sequence (A/T)GATA(A/G) in the regulatory regions of genes., giving rise to the name of the domain. In these domains, a single zinc ion is coordinated by 4 cysteine residues. NMR studies have shown the core of the Znf to comprise 2 irregular anti-parallel beta-sheets and an alpha-helix, followed by a long loop to the C-terminal end of the finger. The N-terminal part, which includes the helix, is similar in structure, but not sequence, to the N-terminal zinc module of the glucocorticoid receptor DNA-binding domain. The helix and the loop connecting the 2 beta-sheets interact with the major groove of the DNA, while the C-terminal tail wraps around into the minor groove. Interactions between the Znf and DNA are mainly hydrophobic, explaining the preponderance of thymines in the binding site; a large number of interactions with the phosphate backbone have also been observed. Two GATA zinc fingers are found in GATA-family transcription factors. However, there are several proteins that only contain a single copy of the domain. It is also worth noting that many GATA-type Znfs (such as those found in the proteins GATAD2B and MTA1) have not been experimentally demonstrated to be DNA-binding domains. Furthermore, several GATA-type Znfs have been demonstrated to act as protein-recognition domains. For example, the N-terminal Znf of GATA1 binds specifically to a zinc finger from the transcriptional coregulator FOG1 (ZFPM1).	GATAD		hgnc.genegroup:26	
820	Soluble guanylate cyclases	Soluble guanylyl cyclase (sGC) is the only known receptor for nitric oxide, NO. It is soluble, i.e. completely intracellular. Most notably, this enzyme is involved in vasodilation. In humans, it is encoded by the genes GUCY1A1, GUCY1A2, GUCY1B2 and GUCY1B3. It is classified under EC number 4.6.1.2. 	GUCY1		hgnc.genegroup:819	
821	Sulfotransferases	Sulfotransferases (EC 2.8.2.-) are transferase enzymes that catalyze the transfer of a sulfo group (not a sulfate group) from a donor molecule to an acceptor alcohol or amine.  The most common sulfo group donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In the case of alcohol as acceptor, the product is a sulfate (R-OSO 3 -), whereas an amine leads to a sulfo-amine (R-NH-SO 3 -). Both reactive groups for a sulfonation via sulfotransferases may be part of a protein, lipid, carbohydrate or steroid. 			so:0005855	
822	Synaptotagmin like tandem C2 proteins	This family contains proteins with tandem C-terminal cytoplasmic C2 domains that are similar to those found in synaptotagmins, but the N-terminal parts of the proteins differ from the synaptotagmin family.			hgnc.genegroup:823	
823	C2 domain containing	A C2 domain is a protein structural domain involved in targeting proteins to cell membranes. The typical version (PKC-C2) has a beta-sandwich composed of 8 Beta-strands that co-ordinates two or three calcium ions, which bind in a cavity formed by the first and final loops of the domain, on the membrane binding face. Many other C2 domain families don't have calcium binding activity.  			so:0005855	
826	Multiple C2 and transmembrane domain containing		MCTP		so:0005855	
827	Extended synaptotagmins		ESYT		hgnc.genegroup:823	
828	Ferlin family		FER1L		hgnc.genegroup:823	
829	Copines	In molecular biology, copines is a name for the group of human proteins that includes members such as CPNE1, CPNE4, CPNE6, and CPNE8.  These are highly conserved, calcium-dependent membrane proteins found in a variety of eukaryotes.  The domain structure of these proteins suggests that they may have a role in membrane trafficking in some prokaryotes as well as eukaryotes. 	CPNE		hgnc.genegroup:823	
83	Zinc fingers HIT-type	This group contains genes that encode proteins with a HIT-type zinc finger, which contains 7 conserved cysteines and one histidine that can potentially coordinate two zinc atoms. It has been named after the first protein that originally defined the domain: the yeast HIT1 protein (<a href='https://pubmed.ncbi.nlm.nih.gov/8943332/'>PMID: 8943332</a> ). The HIT-type zinc finger displays some sequence similarities to the MYND-type zinc finger. The function of this domain is unknown but it is mainly found in nuclear proteins involved in gene regulation and chromatin remodeling.	ZNHIT		hgnc.genegroup:26	
830	C2 and RasGAP domain containing				hgnc.genegroup:823	
831	Phosphatidylinositol 3-kinase subunits	Phosphatidylinositol-4,5-bisphosphate 3-kinase (also called phosphatidylinositide 3-kinases, phosphatidylinositol-3-kinases, PI 3-kinases, PI(3)Ks, PI-3Ks or by the [HGNC] official stem symbol for the gene family, PI3K(s)) are a family of enzymes involved in cellular functions such as cell growth, proliferation, differentiation, motility, survival and intracellular trafficking, which in turn are involved in cancer. PI3Ks are a family of related intracellular signal transducer enzymes capable of phosphorylating the 3 position hydroxyl group of the inositol ring of phosphatidylinositol (PtdIns).  The pathway, with oncogene PIK3CA and tumor suppressor PTEN, is implicated in insensitivity of cancer tumors to insulin and IGF1, in calorie restriction.	PIK3C		hgnc.genegroup:823	
832	C2 domain containing phospholipases				hgnc.genegroup:823	
833	Regulating synaptic membrane exocytosis family		RIMS		hgnc.genegroup:823	
835	C2 domain containing protein kinases				hgnc.genegroup:823	
836	UNC13 homologs		UNC13		hgnc.genegroup:823	
837	C2 tensin-type domain containing				hgnc.genegroup:823	
838	C2 and WW domain containing				hgnc.genegroup:823	
84	Zinc fingers matrin-type	Genes encoding proteins that contain U1-type zinc finger domains, a family of C2H2-type zinc fingers present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins (a href='https://pubmed.ncbi.nlm.nih.gov/15312772/'>PMID: 15312772</a>, a href='https://pubmed.ncbi.nlm.nih.gov/9826776/'>PMID: 9826776</a>).	ZMAT		hgnc.genegroup:26	
841	Nuclear-encoded mitochondrial transfer RNAs		NMTR		hgnc.genegroup:478	
842	Cytoplasmic transfer RNAs		TR		hgnc.genegroup:478	
843	Mitochondrially encoded transfer RNAs		MT-T		hgnc.genegroup:478|hgnc.genegroup:1975	
844	Small nucleolar RNAs	Small nucleolar RNAs (snoRNAs) are a class of small RNA molecules that primarily guide chemical modifications of other RNAs, mainly ribosomal RNAs, transfer RNAs and small nuclear RNAs.			hgnc.genegroup:475	
845	Small nucleolar RNAs, C/D box	C/D box snoRNAs contain two short conserved sequence motifs, C (RUGAUGA) and D (CUGA), located near the 5' and 3' ends of the snoRNA, respectively. Short regions (~ 5 nucleotides) located upstream of the C box and downstream of the D box are usually base complementary and form a stem-box structure, which brings the C and D box motifs into close proximity. This stem-box structure has been shown to be essential for correct snoRNA synthesis and nucleolar localization.	SNORD		hgnc.genegroup:844	
846	Small nucleolar RNAs, H/ACA box	H/ACA box snoRNAs have a common secondary structure consisting of a two hairpins and two single-stranded regions termed a hairpin-hinge-hairpin-tail structure. H/ACA snoRNAs also contain conserved sequence motifs known as H box (consensus ANANNA) and the ACA box (ACA). Both motifs are usually located in the single-stranded regions of the secondary structure.	SNORA		hgnc.genegroup:844	
847	Small Cajal body-specific RNAs	Small Cajal body-specific RNAs (scaRNAs) are a class of small nucleolar RNAs (snoRNAs) that specifically localise to the Cajal body, a nuclear organelle involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs or snurps). ScaRNAs guide the modification ( methylation and pseudouridylation ) of RNA polymerase II transcribed spliceosomal RNAs U1, U2, U4, U5 and U12. The first scaRNA identified was U85.  It is unlike typical snoRNAs in that it is a composite CACA box snoRNAs and can guide both pseudouridylation and 2'-O-methylation. Not all scaRNAs are composite C/D and H/ACA box snoRNA and most scaRNAs are structurally and functionally indistinguishable from snoRNAs, directing ribosomal RNA (rRNA) modification in the nucleolus.	SCARNA		hgnc.genegroup:844	
848	Ribosomal RNAs	In molecular biology, ribosomal ribonucleic acid (rRNA) is the RNA component of the ribosome, and is essential for protein synthesis in all living organisms. It constitutes the predominant material within the ribosome, which is approximately 60% rRNA and 40% protein by weight. Ribosomes contain two major rRNAs and 50 or more proteins. The ribosomal RNAs form two subunits, the large subunit (LSU) and small subunit (SSU). The LSU rRNA acts as a ribozyme, catalyzing peptide bond formation. rRNA sequences are widely used for working out evolutionary relationships among organisms, since they are of ancient origin and are found in all known forms of life.			hgnc.genegroup:475	
849	Small nuclear RNAs	Small nuclear ribonucleic acid (snRNA), also commonly referred to as U-RNA, is a class of small RNA molecules that are found within the splicing speckles and cajal bodies of the cell nucleus in eukaryotic cells. The length of an average snRNA is approximately 150 nucleotides. They are transcribed by either RNA polymerase II or RNA polymerase III, and studies have shown that their primary function is in the processing of pre- messenger RNA ( hnRNA ) in the nucleus. They have also been shown to aid in the regulation of transcription factors (7SK RNA) or RNA polymerase II (B2 RNA), and maintaining the telomeres. 			hgnc.genegroup:475	
85	Zinc fingers MIZ-type	In molecular biology the MIZ-type zinc finger domain is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding ability of Msx2.  Other proteins containing this domain include the human pias family (protein inhibitor of activated STAT protein). The name MIZ is derived from M sx- i nteracting- z inc finger. The crystal structure of S. cerevisiae sumo e3 ligase siz1 containing this domain has been solved.	ZMIZ		hgnc.genegroup:26	
851	Piwi-interacting RNA clusters	Piwi-interacting RNA (piRNA) is the largest class of small non-coding RNA molecules expressed in animal cells.   piRNAs form RNA-protein complexes through interactions with piwi proteins. These piRNA complexes have been linked to both epigenetic and post-transcriptional gene silencing of retrotransposons and other genetic elements in germ line cells, particularly those in spermatogenesis.  They are distinct from microRNA (miRNA) in size (26-31 nt rather than 21-24 nt), lack of sequence conservation, and increased complexity.   It remains unclear how piRNAs are generated, but potential methods have been suggested, and it is certain their biogenesis pathway is distinct from miRNA and siRNA, while rasiRNAs are a piRNA subspecies. 	PIRC		hgnc.genegroup:475	
852	Vault RNAs	Many eukaryotic cells contain large ribonucleoprotein particles in the cytoplasm known as vaults.  The vault complex comprises the major vault protein (MVP), two minor vault proteins (VPARP [PARP4] and TEP1), and a variety of small untranslated RNA molecules. Given the association with the nuclear membrane and the location within the cell, vaults are thought to play roles in intracellular and nucleocytoplasmic transport processes.  Also, given that the structure and protein composition are highly conserved among species, it is believed that the roles vault plays are integral to eukaryotic function.	VTRNA		hgnc.genegroup:475	
853	RNAs, Ro60-associated Y	Y RNAs are small non-coding RNAs. They are components of the Ro60 ribonucleoprotein particle which is a target of autoimmune antibodies in patients with systemic lupus erythematosus.	RNY		hgnc.genegroup:475	
856	Potassium sodium-activated channel subfamily T 		KCNT		hgnc.genegroup:183	
857	Potassium calcium-activated channel subfamily M regulatory beta subunits	BK channels [potassium large conductance calcium activated channels] have a tetrameric structure. Each monomer of the channel-forming alpha subunit is the product of the KCNMA1 gene. Modulatory beta subunits (encoded by KCNMB1, KCNMB2, KCNMB3, or KCNMB4) can associate with the tetrametic channel.	KCNMB		so:0005855	
858	Potassium voltage-gated channel regulatory subunits	Beta subunits are auxiliary proteins that associate with alpha subunits, sometimes in a alpha4beta4 stoichiometry. These subunits do not conduct current on their own but rather modulate the activity of Kv [potassium voltage gated ion] channels.			so:0005855	
86	Zinc fingers MYM-type	MYM-type zinc fingers were identified in MYM family proteins <a href='https://pubmed.ncbi.nlm.nih.gov/9716603/'>PMID: 9716603</a>. Human protein ZMYM3 is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 (<a href='https://pubmed.ncbi.nlm.nih.gov/8817323/'>PMID: 8817323</a>). ZMYM2 is also involved in disease. In myeloproliferative disorders it is fused to FGF receptor 1 (<a href='https://pubmed.ncbi.nlm.nih.gov/9576949/'>PMID: 9576949</a>); in atypical myeloproliferative disorders it is rearranged (<a href='https://pubmed.ncbi.nlm.nih.gov/9694738/'>PMID: 9694738</a>.) Members of the family generally are involved in development.	ZMYM		hgnc.genegroup:26	
861	BTB domain containing		BTBD		so:0005855	
862	Cytochrome P450s	Cytochromes P450 (CYPs) belong to the superfamily of proteins containing a heme cofactor and, therefore, are hemoproteins. CYPs use a variety of small and large molecules as substrates in enzymatic reactions. They are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. The term P450 is derived from the spectrophotometric peak at the wavelength of the absorption maximum of the enzyme (450 nm) when it is in the reduced state and complexed with CO. CYP enzymes have been identified in all domains of life - animals, plants, fungi, protists, bacteria, archaea, and even in viruses.  However, the enzymes have not been found in E. coli.   More than 21,000 distinct CYP proteins are known.  	CYP		so:0005855	
863	EF-hand domain containing	The EF hand is a helix-loop-helix structural domain or motif found in a large family of calcium-binding proteins. The EF-hand motif contains a helix-loop-helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca 2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity. The EF-hand consists of two alpha helices linked by a short loop region (usually about 12 amino acids ) that usually binds calcium ions.			so:0005855	
864	Histones	In biology, histones are highly alkaline proteins found in eukaryotic cell nuclei that package and order the DNA into structural units called nucleosomes.   They are the chief protein components of chromatin, acting as spools around which DNA winds, and play a role in gene regulation. Without histones, the unwound DNA in chromosomes would be very long (a length to width ratio of more than 10 million to 1 in human DNA). For example, each human cell has about 1.8 meters of DNA, (~6 ft) but wound on the histones it has about 90 micrometers (0.09�mm) of chromatin, which, when duplicated and condensed during mitosis, result in about 120 micrometers of chromosomes. 			so:0005855	
865	Anoctamins		ANO		hgnc.genegroup:301	
866	Bestrophins		BEST		hgnc.genegroup:301	
867	Chloride channel accessory		CLCA		so:0005855	
868	Glycine receptors	The glycine receptor, or GlyR, is the receptor for the amino acid neurotransmitter glycine. GlyR is an ionotropic receptor that produces its effects through chloride current. It is one of the most widely distributed inhibitory receptors in the central nervous system and has important roles in a variety of physiological processes, especially in mediating inhibitory neurotransmission in the spinal cord and brainstem.	GLRA, GLRB		hgnc.genegroup:161	
87	Zinc fingers MYND-type	In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants.    The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif.  Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions.	ZMYND		hgnc.genegroup:26	
870	Minor histocompatibility antigens	Minor histocompatibility antigens (a.k.a. MHA) are receptors on the cellular surface of donated organs that are known to give an immunological response in some organ transplants.  They cause problems of rejection less frequently than those of the major histocompatibility complex (MHC). Minor histocompatibility antigens are due to normal proteins that are in themselves polymorphic in a given population. Even when a transplant donor and recipient are identical with respect to their major histocompatibility complex genes, the amino acid differences in minor proteins can cause the grafted tissue to be slowly rejected.			so:0005855	
871	Homer scaffold proteins 		HOMER		so:0005855	
88	PHD finger proteins	The PHD finger was discovered in 1993 as a Cys 4 -His-Cys 3 motif in the plant homeodomain (hence PHD) proteins HAT3.1 in Arabidopsis thaliana and maize ZmHox1a. The PHD finger motif resembles the metal binding RING domain (Cys 3 -His-Cys 4 ) and FYVE domain. It occurs as a single finger, but often in clusters of two or three, and it also occurs together with other domains, such as the chromodomain and the bromodomain.	PHF		hgnc.genegroup:26	
886	Immunoglobulin heavy		IGH		hgnc.genegroup:348	
887	Immunoglobulin kappa		IGK		hgnc.genegroup:348	
888	Immunoglobulin lambda		IGL		hgnc.genegroup:348	
889	T cell receptor beta		TRB		hgnc.genegroup:370	
89	Zinc fingers RANBP2-type 	This group represents genes encoding proteins with the zinc finger domain found in RanBP2 proteins. Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran binding protein 2 (RanBP2) is a 358kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import (<a href='https://pubmed.ncbi.nlm.nih.gov/12019565/'>PMID: 12019565</a>). RanBP2 contains multiple zinc fingers which mediate binding to RanGDP (<a href='https://pubmed.ncbi.nlm.nih.gov/10318915/'>PMID: 10318915</a>).	ZRANB		hgnc.genegroup:26	
890	Selenoproteins	In molecular biology a selenoprotein is any protein that includes a selenocysteine (Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Se-Cys.  Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Se-Cys residues, which are split into two domains, a longer N-terminal domain that contains 1 Se-Cys, and a shorter C-terminal domain that contains 9 Se-Cys. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.  	SELENO		so:0005855	
891	M10 matrix metallopeptidases	Matrix metalloproteinases (MMPs) are zinc -dependent endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. Collectively, these enzymes are capable of degrading all kinds of extracellular matrix proteins, but also can process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand ), and chemokine dispersion), differentiation, angiogenesis, apoptosis, and host defense. They were first described in vertebrates (1962),  including humans, but have since been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix, and their specific evolutionary DNA sequence.	MMP		hgnc.genegroup:901	
892	Tissue inhibitor of metallopeptidases	The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitors of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP1, TIMP2, TIMP3 and TIMP4.  Overall, all MMPs are inhibited by TIMPs once they are activated but the gelatinases (MMP-2 and MMP- ) can form complexes with TIMPs when the enzymes are in the latent form. The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP ( MMP-14 ), a membrane-anchored MMP. The role of the pro-MMP-9/TIMP-1 complex is still unknown.	TIMP		so:0005855	
894	Astacins	In molecular biology, the astacins are a family of metallopeptidases. These metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12A (astacin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA, and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH.  The astacin family of metalloendopeptidases (EC 3.4.24.21) encompasses a range of proteins found in hydra to humans, in mature and developmental systems.  Their functions include activation of growth factors, degradation of polypeptides, and processing of extracellular proteins.  The proteins are synthesised with N-terminal signal and pro-enzyme sequences, and many contain multiple domains C-terminal to the protease domain. They are either secreted from cells, or are associated with the plasma membrane. The astacin molecule adopts a kidney shape, with a deep active-site cleft between its N- and C-terminal domains.  The zinc ion, which lies at the bottom of the cleft, exhibits a unique penta-coordinated mode of binding, involving 3 histidine residues, a tyrosine and a water molecule (which is also bound to the carboxylate side chain of Glu93).  The N-terminal domain comprises 2 alpha-helices and a 5-stranded beta-sheet. The overall topology of this domain is shared by the archetypal zinc-endopeptidase thermolysin. Astacin protease domains also share common features with serralysins, matrix metalloendopeptidases, and snake venom proteases; they cleave peptide bonds in polypeptides such as insulin B chain and bradykinin, and in proteins such as casein and gelatin; and they have arylamidase activity. 			hgnc.genegroup:901	
895	MAP kinase phosphatases				hgnc.genegroup:711	
896	Atypical dual specificity phosphatases				hgnc.genegroup:711	
897	Pappalysins		PAPPA		hgnc.genegroup:901	
898	Slingshot protein phosphatases	There are three members of this family with broad specificity. They contain SH3-binding motifs as well as F-actin binding motifs, thus they are generally believed to play a role in the regulation of cytoskeletal rearrangements. In accordance with their proposed rule, proteins like ADF, cofilin and LIMK1 are slingshot substrates.	SSH		hgnc.genegroup:711	
899	Protein tyrosine phosphatase 4A family		PTP4A		hgnc.genegroup:711	
90	Zinc fingers SWIM-type	This entry represents the SWIM (SWI2/SNF2 and MuDR) zinc-binding domain, which is found in a variety of prokaryotic and eukaryotic proteins, such as mitogen-activated protein kinase kinase kinase 1 (or MEKK1). It is also found in the related protein MEX (MEKK1-related protein X), a testis-expressed protein that acts as an E3 ubiquitin ligase through the action of E2 ubiquitin-conjugating enzymes in the proteasome degradation pathway; the SWIM domain is critical for MEX ubiquitination (<a href='https://pubmed.ncbi.nlm.nih.gov/16522193/'>PMID: 16522193</a>). SWIM domains are also found in the homologous recombination protein Sws1 (<a href='https://pubmed.ncbi.nlm.nih.gov/16710300/'>PMID: 16710300</a>), as well as in several hypothetical proteins.	ZSWIM		hgnc.genegroup:26	
900	CDC14 phosphatases				hgnc.genegroup:711	
901	Metzincin metallopeptidases				hgnc.genegroup:2104	
902	PTEN protein phosphatases				hgnc.genegroup:711	
903	Myotubularins	Myotubularin domain represents a region within eukaryotic myotubularin-related proteins that is sometimes found with the GRAM domain IPR004182.	MTM		hgnc.genegroup:1146	
904	Membrane associated guanylate kinases	The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.  The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains.  The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule / actin based machinery and molecules involved in signal transduction. The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.			so:0005855	
905	Angiopoietin like family		ANGPTL		so:0005855	
906	CEA cell adhesion molecule family		CEACAM		hgnc.genegroup:1317	
907	CTAGE family		CTAGE		so:0005855	
908	Transferrins				so:0005855	
909	Cyclophilin peptidylprolyl isomerases	Cyclophilins are a family of proteins from vertebrates and other organisms that bind to cyclosporine, an immunosuppressant which is usually used to suppress rejection after internal organ transplants.  These proteins have peptidyl prolyl isomerase activity, which catalyzes the isomerization of peptide bonds from trans form to cis form at proline residues and facilitates protein folding. Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B and C, and natural killer cell cyclophilin-related protein.    Major isoforms have been found throughout the cell, including the ER, and some are even secreted.	PPI		hgnc.genegroup:921	
91	Zinc fingers ZZ-type	In molecular biology the ZZ-type zinc finger domain is a type of protein domain that was named because of its ability to bind two z inc ions.  These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains. These zinc fingers are thought to be involved in protein-protein interactions. The structure of the ZZ domain shows that it belongs to the family of cross-brace zinc finger motifs that include the PHD, RING, and FYVE domains.	ZZZ		hgnc.genegroup:26	
910	FKBP prolyl isomerases		FKBP		hgnc.genegroup:921	
911	Adhesion G protein-coupled receptors, subfamily A		ADGRA		hgnc.genegroup:790	
912	Adhesion G protein-coupled receptors, subfamily B		ADGRB		hgnc.genegroup:790	
913	Adhesion G protein-coupled receptors, subfamily C		ADGRC		hgnc.genegroup:790	
914	Adhesion G protein-coupled receptors, subfamily D		ADGRD		hgnc.genegroup:790	
915	Adhesion G protein-coupled receptors, subfamily E		ADGRE		hgnc.genegroup:790	
916	Adhesion G protein-coupled receptors, subfamily F		ADGRF		hgnc.genegroup:790	
917	Adhesion G protein-coupled receptors, subfamily G		ADGRG		hgnc.genegroup:790	
918	Adhesion G protein-coupled receptors, subfamily L		ADGRL		hgnc.genegroup:790	
919	Adhesion G protein-coupled receptors, subfamily V		ADGRV		hgnc.genegroup:790	
920	Parvulins		PIN		hgnc.genegroup:922	
921	Immunophilins	In molecular biology, immunophilins are endogenous cytosolic peptidyl-prolyl isomerases that interconvert  between the cis and trans positions. Immunophilins are targeted by immunosuppressive drugs such as Sirolimus (earlier rapamycin), cyclosporine, and tacrolimus. For these drugs in particular, known immunophilins such as cyclophilin catalyze the cis-trans isomerization of peptide bonds, particularly X-Pro peptide bonds. This isomerase activity can be inhibited by immunosuppressive drugs.			hgnc.genegroup:922	
922	Peptidylprolyl isomerases	Prolyl isomerase (also known as peptidylprolyl isomerase or PPIase ) is an enzyme ( EC 5.2.1.8 ) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline.  Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but proline's unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.			so:0005855	
925	Granins	Granin (chromogranin and secretogranin) is a protein family of regulated secretory proteins ubiquitously found in the cores of amine and peptide hormone and neurotransmitter dense-core secretory vesicles. 	SCG		so:0005855	
926	Rhomboid family	The rhomboid proteases are a family of enzymes that exist in almost all species. They are proteases : they cut the polypeptide chain of other proteins. This proteolytic cleavage is irreversible in cells, and an important type of cellular regulation. Although proteases are one of the earliest and best studied class of enzyme, rhomboids belong to a much more recently discovered type: the intramembrane proteases. What is unique about intramembrane proteases is that their active sites are buried in the lipid bilayer of cell membranes, and they cleave other transmembrane proteins within their transmembrane domains.  About 30% of all proteins have transmembrane domains, and their regulated processing often has major biological consequences. Accordingly, rhomboids regulate many important cellular processes, and may be involved in a wide range of human diseases.	RHB		so:0005855	
928	VPS9 domain containing				so:0005855	
929	Actins	Actins are globular multi-functional proteins that form microfilaments. An actin protein's mass is roughly 42- kDa and they are the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. They can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous) both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division.  Actins participate in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape. Many of these processes are mediated by extensive and intimate interactions of actin with cellular membranes.  In vertebrates, three main groups of actin isoforms, alpha, beta, and gamma have been identified. The alpha actins, found in muscle tissues, are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. 	ACT		so:0005855	
930	Progestin and adipoQ receptor family		PAQR		so:0005855	
931	GINS complex		GINS		hgnc.genegroup:1999	
932	COP9 signalosome 	COP9 (Constitutive photomorphogenesis 9) signalosome (CSN) is a protein complex with isopeptidase activity. It catalyses the hydrolysis of NEDD8 protein from the cullin subunit of Cullin-RING ubiquitin ligases (CRL). Therefore, it is responsible for CRL deneddylation – at the same time, it is able to bind denedyllated cullin-RING complex and retain them in deactivated form. COP9 signalosome thus serves as a sole deactivator of CRLs.  It was found in all eukaryotic organisms including human; it was first discovered in plants.   Human COP9 signalosome (total size ~350 kDa ) consists of 8 subunits - CSN1/COPS1, CSN2/COPS2, CSN3/COPS3, CSN4/COPS4, CSN5/COPS5, CSN6/COPS6, CSN7/COPS7A & COPS7B and CSN8/COPS8. All are essential for full function of the complex and mutation in some of them is lethal in mice. 	COPS		so:0005855	
933	G protein-coupled bile acid receptor	The G protein-coupled bile acid receptor 1 (GPBAR1) also known G-protein coupled receptor 19 (GPCR19), membrane-type receptor for bile acids (M-BAR) or TGR5, is a protein that in humans is encoded by the GPBAR1 gene. 	GPBAR		hgnc.genegroup:140	
934	G protein-coupled estrogen receptor		GPER		hgnc.genegroup:140	
935	Oxoglutarate receptor		OXGR		hgnc.genegroup:140	
936	Succinate receptor		SUCNR		hgnc.genegroup:140	
937	Histone deacetylase superfamily	Histone deacetylases (EC 3.5.1.98, HDAC) are a class of enzymes that remove acetyl groups (O=C-CH3) from an epsilon-N-acetyl lysine amino acid on a histone, allowing the histones to wrap the DNA more tightly. This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. Its action is opposite to that of histone acetyltransferase. HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins. 	HDAC, SIRT		so:0005855	
938	Sirtuins	Sirtuin or Sir2 proteins are a class of proteins that possess either mono-ADP-ribosyltransferase, or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity.  Sirtuins regulate important biological pathways in bacteria, archaea and eukaryotes. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2 ',  the gene responsible for cellular regulation in yeast. The term sirtuins is derived from the word 'sir-two-ins'. Sirtuins have been implicated in influencing a wide range of cellular processes like aging, transcription, apoptosis, inflammation  and stress resistance, as well as energy efficiency and alertness during low-calorie situations.  Sirtuins can also control circadian clocks and mitochondrial biogenesis. Yeast Sir2 and some, but not all, sirtuins are protein deacetylases. Unlike other known protein deacetylases, which simply hydrolyze acetyl - lysine residues, the sirtuin-mediated deacetylation reaction couples lysine deacetylation to NAD hydrolysis. This hydrolysis yields O-acetyl-ADP- ribose, the deacetylated substrate and nicotinamide, itself an inhibitor of sirtuin activity. The dependence of sirtuins on NAD links their enzymatic activity directly to the energy status of the cell via the cellular NAD:NADH ratio, the absolute levels of NAD, NADH or nicotinamide or a combination of these variables.	SIRT		hgnc.genegroup:937	
939	Plakins	The plakins are a family of cytolinkers characterized by a multimodular structure that enables them to function as versatile cross-linkers of the cytoskeleton. They connect the microfilament, microtubule (MT), and intermediate filament (IF) systems with each other and with junctional complexes in organelle and plasma membranes, thereby contributing to cell shape and polarity. They also act as scaffolds and adaptors for signaling proteins that modulate cytoskeletal dynamics or cell migration, differentiation, and stress responses.			so:0005855	
94	Zinc fingers PARP-type	The PARP-type zinc finger domains seem to bind specifically to single-stranded DNA and to act as a DNA nick sensor. DNA ligase III (<a href='https://pubmed.ncbi.nlm.nih.gov/7760816/'>PMID: 7760816</a>) contains, in its N-terminal section, a single copy of a zinc finger highly similar to those of PARP.			hgnc.genegroup:26	
940	Hemoglobin subunits	Hemoglobin; also spelled haemoglobin and abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates (with the exception of the fish family Channichthyidae ) as well as the tissues of some invertebrates. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the rest of the body (i.e. the tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism.	HB		so:0005855	
943	Dynactin subunits	Dynactin or Dynein activator complex is a multi-subunit protein found in eukaryotic cells that aids in bidirectional intracellular transport by binding to dynein and kinesin-2 and linking them to the organelle or vesicle to be transported.  	DCTN		so:0005855	
945	Selectins	The selectins (cluster of differentiation 62 or CD62) are a family of cell adhesion molecules (or CAMs). All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding.  Selectins bind to sugar moieties and so are considered to be a type of lectin, cell adhesion proteins that bind sugar polymers. 	SEL		so:0005855	
946	ENAH/VASPs	ENAH/VASPs are a family of closely related proteins involved in cell motility in vertebrate and invertebrate animals. ENAH/VASPs are modular proteins that are involved in actin polymerization, as well as interaction with other proteins. Within the cell, ENAH/VASP proteins are found at the leading edge of Lamellipodia and at the tips of filopodia. Ena, the founding member of the family was discovered in a Drosophila genetic screen for mutations that act as dominant suppressors of the abl non receptor tyrosine kinase. Invertebrate animals have one Ena homologue, whereas human and other mammals have three: ENAH, VASP and EVL.			so:0005855	
947	ADAMTS like		ADAMTSL		so:0005855	
948	Toll like receptors	Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single, membrane-spanning, non-catalytic receptors usually expressed in sentinel cells such as macrophages and dendritic cells, that recognize structurally conserved molecules derived from microbes. Once these microbes have breached physical barriers such as the skin or intestinal tract mucosa, they are recognized by TLRs, which activate immune cell responses. The TLRs include TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, TLR11, TLR12, and TLR13, though the latter 3 are not found in human. They received their name from their similarity to the protein coded by the toll gene identified in Drosophila in 1985 by Christiane Nüsslein-Volhard.  The researchers were so surprised that they spontaneously shouted out in German, ' Das ist ja toll! ' which translates as 'That's great!' 	TLR		hgnc.genegroup:1296	
949	Tektins	Tektins are cytoskeletal proteins found in cilia and flagella as structural components of outer doublet microtubules. They are also present in centrioles and basal bodies. They are polymeric in nature, and form filaments. They include TEKT1, TEKT2, TEKT3, TEKT4, TEKT5.	TEKT		so:0005855	
950	Gelsolin/villins				so:0005855	
951	Erythrocyte membrane protein band 4.1		EPB41		so:0005855	
952	SNAP complex 		SNAPC		so:0005855	
953	Peroxiredoxins	Peroxiredoxins (Prxs, EC 1.11.1.15 ) are a ubiquitous family of antioxidant enzymes that also control cytokine -induced peroxide levels and thereby mediate signal transduction in mammalian cells.  The physiological importance of peroxiredoxins is illustrated by their relative abundance (one of the most abundant proteins in erythrocytes after hemoglobin is peroxiredoxin 2).	PRDX		so:0005855	
954	Phospholipid scramblases	Scramblase is a protein responsible for the translocation of phospholipids between the two monolayers of a lipid bilayer of a cell membrane.    In humans, phospholipid scramblases (PLSCRs) constitute a family of five homologous proteins that are named as PLSCR1-PLSCR5. Scramblases are not members of the general family of transmembrane lipid transporters known as flippases. Scramblases are distinct from flippases and floppases. In fact, scramblases, flippases and floppases are three different types of enzymatic groups of phospholipid transportation enzymes.  The inner-leaflet facing the inside of the cell contains negatively charged amino-phospholipids and phosphatidylethanolamine. The outer-leaflet, facing the outside environment, contains phosphatidylcholine and sphingomyelin. Scramblase is an enzyme, present in the cell membrane, that can transport (scramble ) the negatively charged phospholipids from the inner-leaflet to the outer-leaflet, and vice versa.	PLSCR		so:0005855	
955	XK related family		XKR		so:0005855	
956	Prefoldin subunits	Prefoldin is a family of proteins used in protein folding complexes. It is classified as a heterohexameric molecular chaperone in both archaea and eukarya, including humans. A prefoldin molecule works as a transfer protein in conjunction with a molecule of chaperonin to form a chaperone complex and correctly fold other nascent proteins. One of prefoldin's main uses in eukarya is the formation of molecules of actin for use in the eukaryotic cytoskeleton.	PFDN		so:0005855	
957	Peroxins	Peroxin (or peroxisomal/peroxisome biogenesis factor ) is a protein found in peroxisomes. Deficiencies are associated with several peroxisomal disorders. Numerous peroxin proteins serve several functions including the recognition of cytoplasmic proteins that contain peroxisomal targeting signals (PTS) that tag them for transport by peroxisomal proteins to the peroxisome.	PEX		so:0005855	
958	Membrane spanning 4-domains		MS4		so:0005855	
959	Caspase recruitment domain containing	Caspase recruitment domains, or Caspase activation and recruitment domains ( CARDs ), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis. These domains mediate the formation of larger protein complexes via direct interactions between individual CARDs. CARD domains are found on a strikingly wide range of proteins, including helicases, kinases, mitochondrial proteins, caspases, and other cytoplasmic factors.	CARD		so:0005855	
96	Zinc fingers CW-type	These genes encode proteins with a CW-type zinc finger motif, named for its conserved cysteine and tryptophan residues. It is predicted to be a highly specialised mononuclear four-cysteine (C4) zinc finger that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including chromatin methylation status and early embryonic development. The domain is found exclusively in vertebrates, vertebrate-infecting parasites and higher plants.	ZCW		hgnc.genegroup:26	
960	Origin recognition complex 	In molecular biology, ORC or origin recognition complex is a multi-subunit DNA binding complex (6 subunits) that binds in all eukaryotes in an ATP-dependent manner to origins of replication. The subunits of this complex are encoded by the ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6 genes. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle. ORC directs DNA replication throughout the genome and is required for its initiation. ORC bound at replication origins serves as the foundation for assembly of the pre-replication complex (pre-RC), which includes Cdc6, Tah11 (aka Cdt1), and the Mcm2 - Mcm7 complex. Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase. Cell cycle -regulated phosphorylation of Orc2, Orc6, Cdc6, and MCM by the cyclin -dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocking reinitiation in G2 / M phase.     In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR). ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers. Both Orc1 and Orc5 bind ATP, though only Orc1 has ATPase activity.  The binding of ATP by Orc1 is required for ORC binding to DNA and is essential for cell viability.  The ATPase activity of Orc1 is involved in formation of the pre-RC. ATP binding by Orc5 is crucial for the stability of ORC as a whole. Only the Orc1-5 subunits are required for origin binding; Orc6 is essential for maintenance of pre-RCs once formed.  Interactions within ORC suggest that Orc2-3-6 may form a core complex. 	ORC		so:0005855	
961	NME/NM23 family		NME		so:0005855	
964	Cystatin superfamily	The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta strand.			so:0005855	
965	Cystatins, type 2		CST		hgnc.genegroup:964	
966	Cystatins, type 1		CST		hgnc.genegroup:964	
967	Cystatins, type 3				hgnc.genegroup:964	
968	Cystatins, type 4				hgnc.genegroup:964	
971	Histatins and statherin	Histatins are proteins found in saliva.  They are antimicrobial and antifungal proteins, and have been found to play a role in wound-closure.  A significant source of histatins is found in the serous fluid secreted by Ebner's glands, salivary glands at the back of the tongue. Here they offer some early defense against incoming microbes. The three major histatins are 1, 3, and 5. Histatin 2 is a degradation product of histatin 1, and all other histatins are degradation products of histatin 3. Therefore there are only two genes, HTN1 and HTN3. Histatins also precipitate tannins from solution - thus preventing alimentary adsorption. 	HTN		so:0005855	
972	Proline rich proteins 	Proline-rich proteins (PRPs) is a class of intrinsically unstructured proteins  (IUP) containing several repeats of a short proline-rich sequence. Many tannin -consuming animals secrete a tannin-binding protein ( mucin ) in their saliva. Tannin-binding capacity of salivary mucin is directly related to its proline content. Advantages in using salivary proline-rich proteins (PRPs) to inactivate tannins are: PRPs inactivate tannins to a greater extent than do dietary proteins; this results in reduced fecal nitrogen losses, PRPs contain non specific nitrogen and nonessential amino acids; this makes them more convenient for an animal to exploit rather than using up valuable dietary protein.  An example of this class of protein is IB5, a human parotid salivary protein known to bind with polyphenols (binding responsible for the astringency mouth feel).	PRB, PRH		so:0005855	
973	Proprotein convertase subtilisin/kexin family	Proprotein convertases are a family of proteins that activate other proteins. Many proteins are inactive when they are first synthesized, because they contain chains of amino acids that block their activity. Proprotein convertases remove those chains and activate the protein. The prototypical proprotein convertase is furin.  Proprotein convertases have medical significance, because they are involved in many important biological processes, such as cholesterol synthesis.  Compounds called proprotein convertase inhibitors can block their action, and block the target proteins from becoming active. Many proprotein convertases, especially furin and PACE4, are involved in pathological processes such as viral infection, inflammation, hypercholesterolemia, and cancer, and have been postulated as therapeutic targets for some of these diseases. 	PCSK		so:0005855	
974	Acyl-CoA dehydrogenase family	Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells. Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate.  Flavin adenine dinucleotide ( FAD ) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function. ACADs can be categorized into three distinct groups based on their specificity for short-, medium-, or long-chain fatty acid acyl-CoA substrates. While different dehydrogenases target fatty acids of varying chain length, all types of ACADs are mechanistically similar. Differences in the enzyme occur based on the location of the active site along the amino acid sequence.  ACADs are an important class of enzymes in mammalian cells because of their role in metabolizing fatty acids present in ingested food materials. This enzyme's action represents the first step in fatty acid metabolism (the process of breaking long chains of fatty acids into acetyl CoA molecules). Deficiencies in these enzymes are linked to genetic disorders involving fatty acid oxidation (i.e. metabolic disorders).  ACAD enzymes have been identified in animals (of which there are 9 major eukaryotic classes), as well as plants,  nematodes,  fungi,  and bacteria.  Five of these nine classes are involved in fatty acid β-oxidation (SCAD, MCAD, LCAD, VLCAD, and VLCAD2), and the other four are involved in branched chain amino acid metabolism (i3VD, i2VD, GD, and iBD). Most acyl-CoA dehydrogenases are α 4 homotetramers, and in two cases (for very long chain fatty acid substrates) they are α 2 homodimers. An additional class of acyl-CoA dehydrogenase was discovered that catalyzes α,β-unsaturation reactions with steroid-CoA thioesters in certain types of bacteria.   This class of ACAD was demonstrated to form α 2 β 2 heterotetramers, rather than the usual α 4 homotetramer, a protein architecture that evolved in order to accommodate a much larger steroid-CoA substrate.   ACADs are classified as EC 1.3.99.3.	ACAD		so:0005855	
975	Calpains	A calpain (EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium -dependent, non- lysosomal cysteine proteases ( proteolytic enzymes ) expressed ubiquitously in mammals and many other organisms. Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the calpain proteases, the small regulatory subunit CAPNS1, also known as CAPN4, and the endogenous calpain-specific inhibitor, calpastatin.	CAPN		so:0005855	
976	Chromobox family		CBX		so:0005855	
978	CKLF like MARVEL transmembrane domain containing		CMTM		hgnc.genegroup:1626	
979	COMM domain containing		COMMD		so:0005855	
981	Dynein regulatory complex		DRC		so:0005855	
982	E2F transcription factors	E2F is a group of genes that codifies a family of transcription factors (TF) in higher eukaryotes. Three of them are activators: E2F1, 2 and E2F3a. Six others act as suppressors: E2F3b, E2F4-8. All of them are involved in the cell cycle regulation and synthesis of DNA in mammalian cells. E2Fs as TFs bind to the TTTCCCGC (or slight variations of this sequence) consensus binding site in the target promoter sequence.	E2F		so:0005855	
983	Desumoylases				so:0005855	
984	SUMO specific peptidases		SENP		hgnc.genegroup:983	
986	Desumoylating isopeptidases		DESI		hgnc.genegroup:983	
987	Transcription factor Dp family	In molecular biology, transcription factor DP is a family of proteins which function as transcription factors. DP forms a heterodimer with E2F and regulates genes involved in cell cycle progression. The transcriptional activity of E2F is inhibited by the retinoblastoma protein which binds to the E2F-DP heterodimer [1] and negatively regulates the G1-S transition.	TFDP		so:0005855	
988	Ubiquitin specific peptidase like 		USPL		hgnc.genegroup:983	
989	Histone deacetylases, class I		HDAC		hgnc.genegroup:937	
990	Histone deacetylases, class II		HDAC		hgnc.genegroup:937	
991	Histone deacetylases, class IV		HDAC		hgnc.genegroup:937	
992	Histone deacetylases, class IIA		HDAC		hgnc.genegroup:990	
993	Histone deacetylases, class IIB		HDAC		hgnc.genegroup:990	
994	Pyrin domain containing	A pyrin domain is a protein domain and a subclass of protein motif known as the death fold; it allows a pyrin domain containing protein to interact with other proteins that contain a pyrin domain. It is also known as a PYD or PAAD/DAPIN domain, and is distantly evolutionarily related to the Death domain family of protein domains.[1][2][3]Proteins containing a pyrin domain are frequently involved in biological processes called inflammation and apoptosis.[4][5] Proteins that possess a pyrin domain include intracellular microbial sensors called NOD-like receptors, and proteins associated with their function, such as PYCARD and certain fish caspases.			so:0005855	
995	Pyrin and HIN domain family		PYHIN		hgnc.genegroup:994	
996	Deubiquinating enzymes				so:0005855	
997	MJD deubiquinating enzymes				hgnc.genegroup:996	
998	Ubiquitin C-terminal hydrolases		UCHL		hgnc.genegroup:996	
999	JAMM/MPN+ metallopeptidase family				hgnc.genegroup:996