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{
"count": 876,
"next": "https://mitotox.org/api/targets/list?format=api&page=7",
"previous": "https://mitotox.org/api/targets/list?format=api&page=5",
"results": [
{
"targ_id": "T339",
"parent_targ_id": "T",
"full_name": "tRNA pseudouridine synthase A",
"abbrev": "tRNA pseudouridylate synthase I",
"protein_names": "tRNA pseudouridine synthase A (EC 5.4.99.12) (tRNA pseudouridine(38-40) synthase) (tRNA pseudouridylate synthase I) (tRNA-uridine isomerase I)",
"related_func_ids": "F060302; F060303",
"category": "enzyme",
"subcategories": "Isomerase",
"Uniport_ID": "Q9Y606",
"Uniprot_name": "TRUA_HUMAN",
"EC_numbers": "5.4.99.12",
"gene_symbol": "PUS1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Pseudouridylate synthase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000177192",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; [Isoform 2]: Nucleus",
"reaction": "uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA",
"targ_desciption": "Converts specific uridines to PSI in a number of tRNAsubstrates. Acts on positions 27/28 in the anticodon stem and alsopositions 34 and 36 in the anticodon of an intron containing tRNA.Involved in regulation of nuclear receptor activity throughpseudouridylation of SRA1 RNA. {ECO:0000269|PubMed:24722331}.",
"references": []
},
{
"targ_id": "T340",
"parent_targ_id": "T",
"full_name": "Translational activator of cytochrome c oxidase 1",
"abbrev": "Coiled-coil domain-containing protein 44",
"protein_names": "Translational activator of cytochrome c oxidase 1 (Coiled-coil domain-containing protein 44) (Translational activator of mitochondrially-encoded cytochrome c oxidase I)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "Activator",
"Uniport_ID": "Q9BSH4",
"Uniprot_name": "TACO1_HUMAN",
"EC_numbers": "",
"gene_symbol": "TACO1",
"gene_synonyms": "CCDC44",
"gene_synonyms_links": "",
"gene_name": "Translational activator of cytochrome c oxidase I",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000136463",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Acts as a translational activator of mitochondrially-encodedcytochrome c oxidase 1. {ECO:0000269|PubMed:19503089}.",
"references": []
},
{
"targ_id": "T341",
"parent_targ_id": "T",
"full_name": "Mitochondrial tRNA-specific 2-thiouridylase 1",
"abbrev": "MTO2 homolog",
"protein_names": "Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (MTO2 homolog)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "O75648",
"Uniprot_name": "MTU1_HUMAN",
"EC_numbers": "2.8.1.14",
"gene_symbol": "TRMU",
"gene_synonyms": "FLJ10140, MTO2, TRMT",
"gene_synonyms_links": "",
"gene_name": "TRNA 5-methylaminomethyl-2-thiouridylate methyltransferase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000100416",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +AMP + diphosphate + H(+) + L-cysteinyl-[protein]",
"targ_desciption": "Catalyzes the 2-thiolation of uridine at the wobble position(U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required forthe formation of 5-taurinomethyl-2-thiouridine (tm5s2U) ofmitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobbleposition. ATP is required to activate the C2 atom of the wobble base.{ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150,ECO:0000269|PubMed:16826519}.",
"references": []
},
{
"targ_id": "T342",
"parent_targ_id": "T",
"full_name": "Elongation factor Ts, mitochondrial",
"abbrev": "EF-TsMt",
"protein_names": "Elongation factor Ts, mitochondrial (EF-Ts) (EF-TsMt)",
"related_func_ids": "F0604",
"category": "protein",
"subcategories": "Elongation factor",
"Uniport_ID": "P43897",
"Uniprot_name": "EFTS_HUMAN",
"EC_numbers": "",
"gene_symbol": "TSFM",
"gene_synonyms": "EF-TS, EF-Tsmt",
"gene_synonyms_links": "",
"gene_name": "Ts translation elongation factor, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000123297",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Associates with the EF-Tu.GDP complex and induces theexchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.{ECO:0000255|HAMAP-Rule:MF_03135, ECO:0000269|PubMed:27677415}.",
"references": []
},
{
"targ_id": "T343",
"parent_targ_id": "T",
"full_name": "Elongation factor Tu, mitochondrial",
"abbrev": "EF-Tu",
"protein_names": "Elongation factor Tu, mitochondrial (EF-Tu) (P43)",
"related_func_ids": "F0604",
"category": "protein",
"subcategories": "Elongation factor",
"Uniport_ID": "P49411",
"Uniprot_name": "EFTU_HUMAN",
"EC_numbers": "",
"gene_symbol": "TUFM",
"gene_synonyms": "EF-TuMT, EFTu",
"gene_synonyms_links": "",
"gene_name": "Tu translation elongation factor, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000178952",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Promotes the GTP-dependent binding of aminoacyl-tRNA to theA-site of ribosomes during protein biosynthesis. Plays also a role inthe regulation of autophagy and innate immunity. Recruits ATG5-ATG12and NLRX1 at mitochondria and serves as a checkpoint of the RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferonwhile promoting autophagy. {ECO:0000269|PubMed:22749352,ECO:0000269|PubMed:28407488}.",
"references": []
},
{
"targ_id": "T344",
"parent_targ_id": "T",
"full_name": "Peptide deformylase, mitochondrial",
"abbrev": "Polypeptide deformylase",
"protein_names": "Peptide deformylase, mitochondrial (EC 3.5.1.88) (Polypeptide deformylase)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q9HBH1",
"Uniprot_name": "DEFM_HUMAN",
"EC_numbers": "3.5.1.88",
"gene_symbol": "PDF",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Peptide deformylase, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000258429",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]",
"targ_desciption": "Removes the formyl group from the N-terminal Met of newlysynthesized proteins. {ECO:0000250}.",
"references": []
},
{
"targ_id": "T345",
"parent_targ_id": "T",
"full_name": "Acylglycerol kinase, mitochondrial",
"abbrev": "hAGK",
"protein_names": "Acylglycerol kinase, mitochondrial (hAGK) (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (HsMuLK) (MuLK) (Multi-substrate lipid kinase)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "Kinase, Transferase",
"Uniport_ID": "Q53H12",
"Uniprot_name": "AGK_HUMAN",
"EC_numbers": "2.7.1.107; 2.7.1.138; 2.7.1.94",
"gene_symbol": "AGK",
"gene_synonyms": "FLJ10842, MULK",
"gene_synonyms_links": "",
"gene_name": "Acylglycerol kinase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000006530",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Peripheral membrane protein; Mitochondrion intermembrane space",
"reaction": "a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate; a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); an N-acylsphing-4-enine + ATP = ADP + H(+) + N-acylsphing-4-enine 1-phosphate; 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate +ADP + H(+); 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+); 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+)",
"targ_desciption": "Lipid kinase that can phosphorylate both monoacylglycerol anddiacylglycerol to form lysophosphatidic acid (LPA) and phosphatidicacid (PA), respectively (PubMed:15939762). Does not phosphorylatesphingosine (PubMed:15939762). Phosphorylates ceramide (By similarity).Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinaseactivity, acts as a component of the TIM22 complex (PubMed:28712724,PubMed:28712726). The TIM22 complex mediates the import and insertionof multi-pass transmembrane proteins into the mitochondrial innermembrane by forming a twin-pore translocase that uses the membranepotential as the external driving force (PubMed:28712724,PubMed:28712726). In the TIM22 complex, required for the import of asubset of metabolite carriers into mitochondria, such as ANT1/SLC25A4and SLC25A24, while it is not required for the import of TIMM23(PubMed:28712724). Overexpression increases the formation and secretionof LPA, resulting in transactivation of EGFR and activation of thedownstream MAPK signaling pathway, leading to increased cell growth(PubMed:15939762). {ECO:0000250|UniProtKB:Q9ESW4,ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:28712724,ECO:0000269|PubMed:28712726}.",
"references": []
},
{
"targ_id": "T346",
"parent_targ_id": "T",
"full_name": "Choline/ethanolamine kinase",
"abbrev": "CK",
"protein_names": "Choline/ethanolamine kinase (Choline kinase beta) (CK) (CKB) (EC 2.7.1.32) (Choline kinase-like protein) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (Ethanolamine kinase beta) (EKB) (choline/ethanolamine kinase beta) (CKEKB)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q9Y259",
"Uniprot_name": "CHKB_HUMAN",
"EC_numbers": "2.7.1.32; 2.7.1.82",
"gene_symbol": "CHKB CHETK CHKL",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "ATP + choline = ADP + H(+) + phosphocholine; ATP + ethanolamine = ADP + H(+) + phosphoethanolamine",
"targ_desciption": "Has a key role in phospholipid metabolism, and catalyzes thefirst step of phosphatidylethanolamine and phosphatidylcholinebiosynthesis. {ECO:0000269|PubMed:19915674,ECO:0000269|PubMed:21665002}.",
"references": []
},
{
"targ_id": "T347",
"parent_targ_id": "T",
"full_name": "Mitochondrial import inner membrane translocase subunit TIM14",
"abbrev": "DnaJ homolog subfamily C member 19",
"protein_names": "Mitochondrial import inner membrane translocase subunit TIM14 (DnaJ homolog subfamily C member 19)",
"related_func_ids": "F020605",
"category": "protein subunit",
"subcategories": "Chaperone",
"Uniport_ID": "Q96DA6",
"Uniprot_name": "TIM14_HUMAN",
"EC_numbers": "",
"gene_symbol": "DNAJC19",
"gene_synonyms": "Pam18, Tim14, TIMM14",
"gene_synonyms_links": "",
"gene_name": "DnaJ heat shock protein family (Hsp40) member C19",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000205981",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein; Matrix side",
"reaction": "",
"targ_desciption": "Mitochondrial co-chaperone which forms a complex withprohibitins to regulate cardiolipin remodeling (By similarity). May bea component of the PAM complex, a complex required for thetranslocation of transit peptide-containing proteins from the innermembrane into the mitochondrial matrix in an ATP-dependent manner. Mayact as a co-chaperone that stimulate the ATP-dependent activity (Bysimilarity). {ECO:0000250|UniProtKB:Q07914,ECO:0000250|UniProtKB:Q9CQV7}.",
"references": []
},
{
"targ_id": "T348",
"parent_targ_id": "T",
"full_name": "FAD-linked sulfhydryl oxidase ALR",
"abbrev": "hERV1",
"protein_names": "FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) (Augmenter of liver regeneration) (hERV1) (Hepatopoietin)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "Growth factor, Oxidoreductase",
"Uniport_ID": "P55789",
"Uniprot_name": "ALR_HUMAN",
"EC_numbers": "1.8.3.2",
"gene_symbol": "GFER",
"gene_synonyms": "ALR, ERV1, HERV1, HPO1, HPO2, HSS",
"gene_synonyms_links": "",
"gene_name": "Growth factor, augmenter of liver regeneration",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000127554",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion intermembrane space; Mitochondrion; [Isoform 2]: Cytoplasm; Secreted",
"reaction": "O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'",
"targ_desciption": "[Isoform 1]: FAD-dependent sulfhydryl oxidase thatregenerates the redox-active disulfide bonds in CHCHD4/MIA40, achaperone essential for disulfide bond formation and protein folding inthe mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40forms a transient intermolecular disulfide bridge with GFER/ERV1,resulting in regeneration of the essential disulfide bonds inCHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electronsto cytochrome c or molecular oxygen. {ECO:0000269|PubMed:19397338,ECO:0000269|PubMed:20593814, ECO:0000269|PubMed:21383138,ECO:0000269|PubMed:22224850, ECO:0000269|PubMed:23186364,ECO:0000269|PubMed:23676665}.; [Isoform 2]: May act as an autocrine hepatotrophic growthfactor promoting liver regeneration.",
"references": []
},
{
"targ_id": "T349",
"parent_targ_id": "T",
"full_name": "Mitochondrial intermediate peptidase",
"abbrev": "MIP",
"protein_names": "Mitochondrial intermediate peptidase (MIP) (EC 3.4.24.59)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q99797",
"Uniprot_name": "MIPEP_HUMAN",
"EC_numbers": "3.4.24.59",
"gene_symbol": "MIPEP",
"gene_synonyms": "MIP",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial intermediate peptidase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000027001",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "Release of an N-terminal octapeptide as second stage ofprocessing of some proteins imported into the mitochondrion.",
"targ_desciption": "Cleaves proteins, imported into the mitochondrion, to theirmature size.",
"references": []
},
{
"targ_id": "T350",
"parent_targ_id": "T",
"full_name": "Mitochondrial import inner membrane translocase subunit TIM16",
"abbrev": "Mitochondria-associated granulocyte macrophage CSF-signaling molecule",
"protein_names": "Mitochondrial import inner membrane translocase subunit TIM16 (Mitochondria-associated granulocyte macrophage CSF-signaling molecule) (Presequence translocated-associated motor subunit PAM16)",
"related_func_ids": "F020605",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q9Y3D7",
"Uniprot_name": "TIM16_HUMAN",
"EC_numbers": "",
"gene_symbol": "PAM16",
"gene_synonyms": "Magmas, Tim16, TIMM16",
"gene_synonyms_links": "",
"gene_name": "Presequence translocase associated motor 16",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000217930",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
"reaction": "",
"targ_desciption": "Regulates ATP-dependent protein translocation into themitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/MortalinATPase activity. {ECO:0000269|PubMed:20053669}.",
"references": []
},
{
"targ_id": "T351",
"parent_targ_id": "T",
"full_name": "85/88 kDa calcium-independent phospholipase A2",
"abbrev": "CaI-PLA2",
"protein_names": "85/88 kDa calcium-independent phospholipase A2 (CaI-PLA2) (EC 3.1.1.4) (2-lysophosphatidylcholine acylhydrolase) (EC 3.1.1.5) (Group VI phospholipase A2) (GVI PLA2) (Intracellular membrane-associated calcium-independent phospholipase A2 beta) (iPLA2-beta) (Palmitoyl-CoA hydrolase) (EC 3.1.2.2) (Patatin-like phospholipase domain-containing protein 9) (PNPLA9)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "O60733",
"Uniprot_name": "PLPL9_HUMAN",
"EC_numbers": "3.1.1.4; 3.1.1.5; 3.1.2.2",
"gene_symbol": "PLA2G6",
"gene_synonyms": "iPLA2, iPLA2beta, NBIA2, PARK14, PNPLA9",
"gene_synonyms_links": "",
"gene_name": "Phospholipase A2 group VI",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000184381",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Cell membrane; Mitochondrion; Cell projection, pseudopodium",
"reaction": "a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine+ H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-sn-glycero-3-phosphate + H(+) + hexadecanoate; a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +H(+) + sn-glycerol 3-phosphocholine; 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +hexadecanoate + sn-glycerol 3-phosphocholine; 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine+ H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine+ H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; 1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol + H(+); 1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+); 1-octadecanoyl-2-(15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoethanolamine + 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+)",
"targ_desciption": "Calcium-independent phospholipase involved in phospholipidremodeling with implications in cellular membrane homeostasis,mitochondrial integrity and signal transduction. Hydrolyzes the esterbond of the fatty acyl group attached at sn-1 or sn-2 position ofphospholipids (phospholipase A1 and A2 activity respectively),producing lysophospholipids that are used in deacylation-reacylationcycles (PubMed:9417066, PubMed:10092647, PubMed:10336645,PubMed:20886109). Hydrolyzes both saturated and unsaturated long fattyacyl chains in various glycerophospholipid classes such asphosphatidylcholines, phosphatidylethanolamines and phosphatidates,with a preference for hydrolysis at sn-2 position (PubMed:10092647,PubMed:10336645, PubMed:20886109). Can further hydrolyzelysophospholipids carrying saturated fatty acyl chains(lysophospholipase activity) (PubMed:20886109). Upon oxidative stress,contributes to remodeling of mitochondrial phospholipids in pancreaticbeta cells, in a repair mechanism to reduce oxidized lipid content(PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturatedfatty acyl chains from cardiolipins, yielding monolysocardiolipins thatcan be reacylated with unoxidized fatty acyls to regenerate nativecardiolipin species (By similarity). Hydrolyzes oxidizedglycerophosphoethanolamines present in pancreatic islets, releasingoxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates(HETEs) (By similarity). Has thioesterase activity toward fatty-acylCoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle(PubMed:20886109). Plays a role in regulation of membrane dynamics andhomeostasis. Selectively hydrolyzes sn-2 arachidonoyl group inplasmalogen phospholipids, structural components of lipid rafts andmyelin (By similarity). Regulates F-actin polymerization at thepseudopods, which is required for both speed and directionality ofMCP1/CCL2-induced monocyte chemotaxis (PubMed:18208975). Targetsmembrane phospholipids to produce potent lipid signaling messengers.Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), whichacts via G-protein receptors in various cell types (By similarity). Hasphospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role ininactivation of this potent proinflammatory signaling lipid (Bysimilarity). In response to glucose, amplifies calcium influx inpancreatic beta cells to promote INS secretion (By similarity).{ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97570,ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:10092647,ECO:0000269|PubMed:10336645, ECO:0000269|PubMed:18208975,ECO:0000269|PubMed:20886109, ECO:0000269|PubMed:23533611,ECO:0000269|PubMed:9417066}.; [Isoform Ankyrin-iPLA2-1]: Lacks the catalytic domain and mayact as a negative regulator of the catalytically active isoforms.{ECO:0000269|PubMed:9417066}.; [Isoform Ankyrin-iPLA2-2]: Lacks the catalytic domain and mayact as a negative regulator of the catalytically active isoforms.{ECO:0000269|PubMed:9417066}.",
"references": []
},
{
"targ_id": "T352",
"parent_targ_id": "T",
"full_name": "Mitochondrial-processing peptidase subunit alpha",
"abbrev": "P-55",
"protein_names": "Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (P-55)",
"related_func_ids": "F020605",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q10713",
"Uniprot_name": "MPPA_HUMAN",
"EC_numbers": "",
"gene_symbol": "PMPCA",
"gene_synonyms": "Alpha-MPP, INPP5E, KIAA0123",
"gene_synonyms_links": "",
"gene_name": "Peptidase, mitochondrial processing alpha subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000165688",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Mitochondrion inner membrane",
"reaction": "",
"targ_desciption": "Substrate recognition and binding subunit of the essentialmitochondrial processing protease (MPP), which cleaves themitochondrial sequence off newly imported precursors proteins.{ECO:0000269|PubMed:25808372}.",
"references": []
},
{
"targ_id": "T353",
"parent_targ_id": "T",
"full_name": "Protein SERAC1",
"abbrev": "Serine active site-containing protein 1",
"protein_names": "Protein SERAC1 (Serine active site-containing protein 1)",
"related_func_ids": "F020605",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q96JX3",
"Uniprot_name": "SRAC1_HUMAN",
"EC_numbers": "",
"gene_symbol": "SERAC1",
"gene_synonyms": "FLJ14917",
"gene_synonyms_links": "",
"gene_name": "Serine active site containing 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000122335",
"omim_id": "",
"genecard_link": "",
"locs": "Membrane; Single-pass membrane protein; Endoplasmic reticulum; Mitochondrion",
"reaction": "",
"targ_desciption": "Plays an important role in the phosphatidylglycerolremodeling that is essential for both mitochondrial function andintracellular cholesterol trafficking. May catalyze the remodeling ofphosphatidylglycerol and be involved in the transacylation-acylationreaction to produce phosphatidylglycerol-36:1. May be involved inbis(monoacylglycerol)phosphate biosynthetic pathway.{ECO:0000269|PubMed:22683713}.",
"references": []
},
{
"targ_id": "T354",
"parent_targ_id": "T",
"full_name": "Tafazzin",
"abbrev": "Protein G4.5",
"protein_names": "Tafazzin (Protein G4.5)",
"related_func_ids": "F020605",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q16635",
"Uniprot_name": "TAZ_HUMAN",
"EC_numbers": "",
"gene_symbol": "TAZ",
"gene_synonyms": "BTHS, CMD3A, EFE, EFE2, G4.5, TAZ1, XAP-2",
"gene_synonyms_links": "",
"gene_name": "Tafazzin",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000102125",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Membrane; Single-pass membrane protein; [Isoform 2]: Cytoplasm; [Isoform 3]: Membrane; Single-pass membrane protein; [Isoform 4]: Membrane; Single-pass membrane protein; [Isoform 5]: Membrane; Single-pass membrane protein; [Isoform 6]: Cytoplasm; [Isoform 7]: Membrane; Single-pass membrane protein; [Isoform 8]: Cytoplasm; [Isoform 9]: Cytoplasm",
"reaction": "",
"targ_desciption": "Some isoforms may be involved in cardiolipin (CL) metabolism.{ECO:0000269|PubMed:12930833, ECO:0000269|PubMed:19164547}.",
"references": []
},
{
"targ_id": "T355",
"parent_targ_id": "T",
"full_name": "Mitochondrial import inner membrane translocase subunit Tim8 A",
"abbrev": "Deafness dystonia protein 1",
"protein_names": "Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1) (X-linked deafness dystonia protein)",
"related_func_ids": "F020605",
"category": "protein subunit",
"subcategories": "Chaperone",
"Uniport_ID": "O60220",
"Uniprot_name": "TIM8A_HUMAN",
"EC_numbers": "",
"gene_symbol": "TIMM8A",
"gene_synonyms": "DDP, DFN1, MTS",
"gene_synonyms_links": "",
"gene_name": "Translocase of inner mitochondrial membrane 8A",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000126953",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side",
"reaction": "",
"targ_desciption": "Mitochondrial intermembrane chaperone that participates inthe import and insertion of some multi-pass transmembrane proteins intothe mitochondrial inner membrane. Also required for the transfer ofbeta-barrel precursors from the TOM complex to the sorting and assemblymachinery (SAM complex) of the outer membrane. Acts as a chaperone-likeprotein that protects the hydrophobic precursors from aggregation andguide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23,SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins.Probably necessary for normal neurologic development.{ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.",
"references": []
},
{
"targ_id": "T356",
"parent_targ_id": "T",
"full_name": "Mitochondrial import inner membrane translocase subunit TIM50",
"abbrev": "",
"protein_names": "Mitochondrial import inner membrane translocase subunit TIM50",
"related_func_ids": "F020605",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q3ZCQ8",
"Uniprot_name": "TIM50_HUMAN",
"EC_numbers": "",
"gene_symbol": "TIMM50",
"gene_synonyms": "TIM50L",
"gene_synonyms_links": "",
"gene_name": "Translocase of inner mitochondrial membrane 50",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000105197",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein; [Isoform 2]: Nucleus speckle",
"reaction": "",
"targ_desciption": "Essential component of the TIM23 complex, a complex thatmediates the translocation of transit peptide-containing proteinsacross the mitochondrial inner membrane. Has some phosphatase activityin vitro. however such activity may not be relevant in vivo.{ECO:0000269|PubMed:15044455}.; [Isoform 2]: May participate in the release of snRNPs and SMNfrom the Cajal body. {ECO:0000269|PubMed:16008839}.",
"references": []
},
{
"targ_id": "T357",
"parent_targ_id": "T",
"full_name": "Xaa-Pro aminopeptidase 3",
"abbrev": "APP3",
"protein_names": "Xaa-Pro aminopeptidase 3 (X-Pro aminopeptidase 3) (EC 3.4.11.9) (Aminopeptidase P3) (APP3)",
"related_func_ids": "F020605",
"category": "enzyme",
"subcategories": "Aminopeptidase, Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q9NQH7",
"Uniprot_name": "XPP3_HUMAN",
"EC_numbers": "3.4.11.9",
"gene_symbol": "XPNPEP3",
"gene_synonyms": "APP3, ICP55, NPHPL1",
"gene_synonyms_links": "",
"gene_name": "X-prolyl aminopeptidase 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000196236",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; Cytoplasm; [Isoform 2]: Cytoplasm",
"reaction": "Release of any N-terminal amino acid, including proline, thatis linked to proline, even from a dipeptide or tripeptide.",
"targ_desciption": "Catalyzes the removal of a penultimate prolyl residue fromthe N-termini of peptides, such as Leu-Pro-Ala (PubMed:25609706,PubMed:28476889). Also shows low activity towards peptides with Ala orSer at the P1 position (PubMed:28476889). {ECO:0000269|PubMed:25609706,ECO:0000269|PubMed:28476889}.; [Isoform 1]: Promotes TNFRSF1B-mediated phosphorylation ofMAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter proteinfor TNFRSF1B. the effect is independent of XPNPEP3 peptidase activity.May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling.{ECO:0000269|PubMed:25609706}.",
"references": []
},
{
"targ_id": "T358",
"parent_targ_id": "T",
"full_name": "Dynamin-1-like protein",
"abbrev": "Drp1",
"protein_names": "Dynamin-1-like protein (EC 3.6.5.5) (Dnm1p/Vps1p-like protein) (DVLP) (Dynamin family member proline-rich carboxyl-terminal domain less) (Dymple) (Dynamin-like protein) (Dynamin-like protein 4) (Dynamin-like protein IV) (HdynIV) (Dynamin-related protein 1)",
"related_func_ids": "F030803; F030804",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "O00429",
"Uniprot_name": "DNM1L_HUMAN",
"EC_numbers": "3.6.5.5",
"gene_symbol": "DNM1L",
"gene_synonyms": "DRP1, DVLP, DYMPLE, HDYNIV, VPS1",
"gene_synonyms_links": "",
"gene_name": "Dynamin 1 like",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000087470",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm, cytosol; Golgi apparatus; Endomembrane system; Peripheral membrane protein; Mitochondrion outer membrane; Peripheral membrane protein; Peroxisome; Membrane, clathrin-coated pit; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane",
"reaction": "GTP + H2O = GDP + H(+) + phosphate",
"targ_desciption": "Functions in mitochondrial and peroxisomal division. Mediatesmembrane fission through oligomerization into membrane-associatedtubular structures that wrap around the scission site to constrict andsever the mitochondrial membrane through a GTP hydrolysis-dependentmechanism. The specific recruitment at scission sites is mediated bymembrane receptors like MFF, MIEF1 and MIEF2 for mitochondrialmembranes (PubMed:29899447). While the recruitment by the membranereceptors is GTP-dependent, the following hydrolysis of GTP induces thedissociation from the receptors and allows DNM1L filaments to curl intoclosed rings that are probably sufficient to sever a double membrane(PubMed:29899447). Through its function in mitochondrial division,ensures the survival of at least some types of postmitotic neurons,including Purkinje cells, by suppressing oxidative damage. Required fornormal brain development, including that of cerebellum. Facilitatesdevelopmentally regulated apoptosis during neural tube formation.Required for a normal rate of cytochrome c release and caspaseactivation during apoptosis. this requirement may depend upon the celltype and the physiological apoptotic cues. Plays an important role inmitochondrial fission during mitosis (PubMed:26992161, PubMed:27301544,PubMed:27328748). Required for formation of endocytic vesicles.Proposed to regulate synaptic vesicle membrane dynamics throughassociation with BCL2L1 isoform Bcl-X(L) which stimulates its GTPaseactivity in synaptic vesicles. the function may require its recruitmentby MFF to clathrin-containing vesicles (PubMed:23792689). Required forprogrammed necrosis execution. Rhythmic control of its activityfollowing phosphorylation at Ser-637 is essential for the circadiancontrol of mitochondrial ATP production (PubMed:29478834).{ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366,ECO:0000269|PubMed:17015472, ECO:0000269|PubMed:17301055,ECO:0000269|PubMed:17460227, ECO:0000269|PubMed:17553808,ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687,ECO:0000269|PubMed:19342591, ECO:0000269|PubMed:19411255,ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:20688057,ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241,ECO:0000269|PubMed:23584531, ECO:0000269|PubMed:23792689,ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:26992161,ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27301544,ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29478834,ECO:0000269|PubMed:29899447, ECO:0000269|PubMed:9570752,ECO:0000269|PubMed:9786947}.; [Isoform 1]: Inhibits peroxisomal division whenoverexpressed. {ECO:0000269|PubMed:12618434}.; [Isoform 4]: Inhibits peroxisomal division whenoverexpressed. {ECO:0000269|PubMed:12618434}.",
"references": [
"RC03691",
"RC03952",
"RC03978",
"RC03979"
]
},
{
"targ_id": "T359",
"parent_targ_id": "T",
"full_name": "Ganglioside-induced differentiation-associated protein 1",
"abbrev": "GDAP1",
"protein_names": "Ganglioside-induced differentiation-associated protein 1 (GDAP1)",
"related_func_ids": "F0308",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q8TB36",
"Uniprot_name": "GDAP1_HUMAN",
"EC_numbers": "",
"gene_symbol": "GDAP1",
"gene_synonyms": "CMT2K, CMT4, CMT4A",
"gene_synonyms_links": "",
"gene_name": "Ganglioside induced differentiation associated protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000104381",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Multi-pass membrane protein; Cytoplasm",
"reaction": "",
"targ_desciption": "Regulates the mitochondrial network by promotingmitochondrial fission. {ECO:0000269|PubMed:16172208}.",
"references": []
},
{
"targ_id": "T360",
"parent_targ_id": "T",
"full_name": "Mitochondrial fission factor",
"abbrev": "",
"protein_names": "Mitochondrial fission factor",
"related_func_ids": "F0308",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9GZY8",
"Uniprot_name": "MFF_HUMAN",
"EC_numbers": "",
"gene_symbol": "MFF",
"gene_synonyms": "C2orf33, GL004",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial fission factor",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000168958",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Single-passtype IV membrane protein; Peroxisome; Cytoplasmicvesicle, secretory vesicle, synaptic vesicle",
"reaction": "",
"targ_desciption": "Plays a role in mitochondrial and peroxisomal fission.Promotes the recruitment and association of the fission mediatordynamin-related protein 1 (DNM1L) to the mitochondrial surface. May beinvolved in regulation of synaptic vesicle membrane dynamics byrecruitment of DNM1L to clathrin-containing vesicles.{ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23530241}.",
"references": []
},
{
"targ_id": "T361",
"parent_targ_id": "T",
"full_name": "Mitofusin-2",
"abbrev": "Transmembrane GTPase MFN2",
"protein_names": "Mitofusin-2 (EC 3.6.5.-) (Transmembrane GTPase MFN2)",
"related_func_ids": "F0308",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "O95140",
"Uniprot_name": "MFN2_HUMAN",
"EC_numbers": "3.6.5.-",
"gene_symbol": "MFN2",
"gene_synonyms": "CMT2A2, CPRP1, KIAA0214, MARF",
"gene_synonyms_links": "",
"gene_name": "Mitofusin 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000116688",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Multi-pass membrane protein",
"reaction": "GTP + H2O = GDP + H(+) + phosphate",
"targ_desciption": "Mitochondrial outer membrane GTPase that mediatesmitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885,PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamicorganelles, and their morphology is determined by the equilibriumbetween mitochondrial fusion and fission events (PubMed:28114303).Overexpression induces the formation of mitochondrial networks(PubMed:28114303). Membrane clustering requires GTPase activity and mayinvolve a major rearrangement of the coiled coil domains (Probable).Plays a central role in mitochondrial metabolism and may be associatedwith obesity and/or apoptosis processes (By similarity). Plays animportant role in the regulation of vascular smooth muscle cellproliferation (By similarity). Involved in the clearance of damagedmitochondria via selective autophagy (mitophagy) (PubMed:23620051). Isrequired for PRKN recruitment to dysfunctional mitochondria(PubMed:23620051). Involved in the control of unfolded protein response(UPR) upon ER stress including activation of apoptosis and autophagyduring ER stress (By similarity). Acts as an upstream regulator ofEIF2AK3 and suppresses EIF2AK3 activation under basal conditions (Bysimilarity). {ECO:0000250|UniProtKB:Q80U63,ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:11181170,ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:23620051,ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:26214738,ECO:0000269|PubMed:28114303, ECO:0000305}.",
"references": []
},
{
"targ_id": "T362",
"parent_targ_id": "T",
"full_name": "Protein misato homolog 1",
"abbrev": "",
"protein_names": "Protein misato homolog 1",
"related_func_ids": "F0308",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9BUK6",
"Uniprot_name": "MSTO1_HUMAN",
"EC_numbers": "",
"gene_symbol": "MSTO1",
"gene_synonyms": "FLJ10504, LST005, misato, MST",
"gene_synonyms_links": "",
"gene_name": "Misato 1, mitochondrial distribution and morphology regulator",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000125459",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Cytoplasm",
"reaction": "",
"targ_desciption": "Involved in the regulation of mitochondrial distribution andmorphology (PubMed:17349998, PubMed:28554942, PubMed:28544275).Required for mitochondrial fusion and mitochondrial network formation(PubMed:28554942, PubMed:28544275). {ECO:0000269|PubMed:17349998,ECO:0000269|PubMed:28544275, ECO:0000269|PubMed:28554942}.",
"references": []
},
{
"targ_id": "T363",
"parent_targ_id": "T",
"full_name": "Dynamin-like 120 kDa protein, mitochondrial",
"abbrev": "Optic atrophy protein 1",
"protein_names": "Dynamin-like 120 kDa protein, mitochondrial (EC 3.6.5.5) (Optic atrophy protein 1) [Cleaved into: Dynamin-like 120 kDa protein, form S1]",
"related_func_ids": "F0308",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "O60313",
"Uniprot_name": "OPA1_HUMAN",
"EC_numbers": "3.6.5.5",
"gene_symbol": "OPA1",
"gene_synonyms": "FLJ12460, KIAA0567, MGM1, NPG, NTG",
"gene_synonyms_links": "",
"gene_name": "OPA1, mitochondrial dynamin like GTPase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000198836",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein; Mitochondrion intermembrane space; Mitochondrion membrane",
"reaction": "GTP + H2O = GDP + H(+) + phosphate",
"targ_desciption": "Dynamin-related GTPase that is essential for normalmitochondrial morphology by regulating the equilibrium betweenmitochondrial fusion and mitochondrial fission (PubMed:16778770,PubMed:17709429, PubMed:20185555, PubMed:24616225, PubMed:28746876).Coexpression of isoform 1 with shorter alternative products is requiredfor optimal activity in promoting mitochondrial fusion(PubMed:17709429). Binds lipid membranes enriched in negatively chargedphospholipids, such as cardiolipin, and promotes membrane tubulation(PubMed:20185555). The intrinsic GTPase activity is low, and isstrongly increased by interaction with lipid membranes(PubMed:20185555). Plays a role in remodeling cristae and the releaseof cytochrome c during apoptosis (By similarity). Proteolyticprocessing in response to intrinsic apoptotic signals may lead todisassembly of OPA1 oligomers and release of the caspase activatorcytochrome C (CYCS) into the mitochondrial intermembrane space (Bysimilarity). Plays a role in mitochondrial genome maintenance(PubMed:20974897, PubMed:18158317). {ECO:0000250|UniProtKB:P58281,ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429,ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:20185555,ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:24616225,ECO:0000269|PubMed:28746876}.; [Dynamin-like 120 kDa protein, form S1]: Inactive formproduced by cleavage at S1 position by OMA1 following stress conditionsthat induce loss of mitochondrial membrane potential, leading tonegative regulation of mitochondrial fusion.{ECO:0000269|PubMed:20038677}.; Isoforms that contain the alternative exon 4b (present inisoform 4 and isoform 5) are required for mitochondrial genomemaintenance, possibly by anchoring the mitochondrial nucleoids to theinner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.",
"references": [
"RC03915"
]
},
{
"targ_id": "T364",
"parent_targ_id": "T",
"full_name": "Signal transducer and activator of transcription 2",
"abbrev": "p113",
"protein_names": "Signal transducer and activator of transcription 2 (p113)",
"related_func_ids": "F0308",
"category": "enzyme",
"subcategories": "Activator",
"Uniport_ID": "P52630",
"Uniprot_name": "STAT2_HUMAN",
"EC_numbers": "",
"gene_symbol": "STAT2",
"gene_synonyms": "STAT113",
"gene_synonyms_links": "",
"gene_name": "Signal transducer and activator of transcription 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000170581",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus",
"reaction": "",
"targ_desciption": "Signal transducer and activator of transcription thatmediates signaling by type I IFNs (IFN-alpha and IFN-beta). Followingtype I IFN binding to cell surface receptors, Jak kinases (TYK2 andJAK1) are activated, leading to tyrosine phosphorylation of STAT1 andSTAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G toform a complex termed ISGF3 transcription factor, that enters thenucleus. ISGF3 binds to the IFN stimulated response element (ISRE) toactivate the transcription of interferon stimulated genes, which drivethe cell in an antiviral state (PubMed:9020188, PubMed:23391734). Actsas a regulator of mitochondrial fission by modulating thephosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate andinactivate the GTPase activity of DNM1L respectively (PubMed:26122121).{ECO:0000269|PubMed:23391734, ECO:0000269|PubMed:26122121,ECO:0000269|PubMed:9020188}.",
"references": []
},
{
"targ_id": "T365",
"parent_targ_id": "T",
"full_name": "Trafficking kinesin-binding protein 1",
"abbrev": "106 kDa O-GlcNAc transferase-interacting protein",
"protein_names": "Trafficking kinesin-binding protein 1 (106 kDa O-GlcNAc transferase-interacting protein) (Protein Milton)",
"related_func_ids": "F0308",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9UPV9",
"Uniprot_name": "TRAK1_HUMAN",
"EC_numbers": "",
"gene_symbol": "TRAK1 KIAA1042 OIP106",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus; Mitochondrion; Early endosome; Endosome; Mitochondrion membrane; Cytoplasm, cell cortex",
"reaction": "",
"targ_desciption": "Involved in the regulation of endosome-to-lysosometrafficking, including endocytic trafficking of EGF-EGFR complexes andGABA-A receptors (PubMed:18675823). Involved in mitochondrial motility.When O-glycosylated, abolishes mitochondrial motility. Crucial forrecruiting OGT to the mitochondrial surface of neuronal processes(PubMed:24995978). TRAK1 and RHOT form an essential protein complexthat links KIF5 to mitochondria for light chain-independent,anterograde transport of mitochondria (By similarity).{ECO:0000250|UniProtKB:Q960V3, ECO:0000269|PubMed:18675823,ECO:0000269|PubMed:24995978}.",
"references": []
},
{
"targ_id": "T366",
"parent_targ_id": "T",
"full_name": "ATP-dependent zinc metalloprotease YME1L1",
"abbrev": "PAMP",
"protein_names": "ATP-dependent zinc metalloprotease YME1L1 (EC 3.4.24.-) (ATP-dependent metalloprotease FtsH1) (Meg-4) (Presenilin-associated metalloprotease) (PAMP) (YME1-like protein 1)",
"related_func_ids": "F0308",
"category": "enzyme",
"subcategories": "Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q96TA2",
"Uniprot_name": "YMEL1_HUMAN",
"EC_numbers": "3.4.24.-",
"gene_symbol": "YME1L1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "YME1 like 1 ATPase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000136758",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Mitochondrion",
"reaction": "",
"targ_desciption": "ATP-dependent metalloprotease that catalyzes the degradationof folded and unfolded proteins with a suitable degron sequence in themitochondrial intermembrane region (PubMed:26923599, PubMed:27786171).Plays an important role in regulating mitochondrial morphology andfunction by cleaving OPA1 at position S2, giving rise to a form of OPA1that promotes maintenance of normal mitochondrial structure andmitochondrial protein metabolism (PubMed:18076378, PubMed:26923599,PubMed:27495975). Ensures cell proliferation, maintains normal cristaemorphology and complex I respiration activity, promotes antiapoptoticactivity and protects mitochondria from the accumulation of oxidativelydamaged membrane proteins (PubMed:22262461). Required for normal,constitutive degradation of PRELID1 (PubMed:27495975). Catalyzes thedegradation of OMA1 in response to membrane depolarization(PubMed:26923599). Required to control the accumulation of nonassembledrespiratory chain subunits (NDUFB6, OX4 and ND1) (PubMed:22262461).{ECO:0000269|PubMed:18076378, ECO:0000269|PubMed:22262461,ECO:0000269|PubMed:26923599, ECO:0000269|PubMed:27495975,ECO:0000269|PubMed:27786171}.",
"references": []
},
{
"targ_id": "T36701",
"parent_targ_id": "T36",
"full_name": "Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial",
"abbrev": "Protein N27C7-4",
"protein_names": "Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial (Protein N27C7-4)",
"related_func_ids": "F030602",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q8WYQ3",
"Uniprot_name": "CHC10_HUMAN",
"EC_numbers": "",
"gene_symbol": "CHCHD10",
"gene_synonyms": "C22orf16, N27C7-4",
"gene_synonyms_links": "",
"gene_name": "Coiled-coil-helix-coiled-coil-helix domain containing 10",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000250479",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space",
"reaction": "",
"targ_desciption": "May be involved in the maintenance of mitochondrialorganization and mitochondrial cristae structure.{ECO:0000269|PubMed:24934289}.",
"references": []
},
{
"targ_id": "T368",
"parent_targ_id": "T",
"full_name": "Solute carrier family 25 member 46",
"abbrev": "",
"protein_names": "Solute carrier family 25 member 46",
"related_func_ids": "F030602",
"category": "protein",
"subcategories": "Transporter",
"Uniport_ID": "Q96AG3",
"Uniprot_name": "S2546_HUMAN",
"EC_numbers": "",
"gene_symbol": "SLC25A46",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Solute carrier family 25 member 46",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000164209",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "May play a role in mitochondrial dynamics by controllingmitochondrial membrane fission. {ECO:0000269|PubMed:26168012}.",
"references": []
},
{
"targ_id": "T369",
"parent_targ_id": "T",
"full_name": "ER membrane protein complex subunit 1",
"abbrev": "",
"protein_names": "ER membrane protein complex subunit 1",
"related_func_ids": "F0309",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q8N766",
"Uniprot_name": "EMC1_HUMAN",
"EC_numbers": "",
"gene_symbol": "EMC1 KIAA0090 PSEC0263",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Membrane; Single-pass type I membrane protein",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T370",
"parent_targ_id": "T",
"full_name": "AFG3-like protein 2",
"abbrev": "",
"protein_names": "AFG3-like protein 2 (EC 3.4.24.-) (Paraplegin-like protein)",
"related_func_ids": "F0210",
"category": "enzyme",
"subcategories": "Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q9Y4W6",
"Uniprot_name": "AFG32_HUMAN",
"EC_numbers": "3.4.24.-",
"gene_symbol": "AFG3L2",
"gene_synonyms": "SCA28, SPAX5",
"gene_synonyms_links": "",
"gene_name": "AFG3 like matrix AAA peptidase subunit 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000141385",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "ATP-dependent protease which is essential for axonal andneuron development. In neurons, mediates degradation of SMDT1/EMREbefore its assembly with the uniporter complex, limiting theavailability of SMDT1/EMRE for MCU assembly and promoting efficientassembly of gatekeeper subunits with MCU (PubMed:27642048). Requiredfor the maturation of paraplegin (SPG7) after its cleavage bymitochondrial-processing peptidase (MPP), converting it into aproteolytically active mature form (By similarity). Required for thematuration of PINK1 into its 52kDa mature form after its cleavage bymitochondrial-processing peptidase (MPP) (PubMed:22354088).{ECO:0000250|UniProtKB:Q8JZQ2, ECO:0000269|PubMed:22354088,ECO:0000269|PubMed:27642048}.",
"references": []
},
{
"targ_id": "T371",
"parent_targ_id": "T",
"full_name": "ATPase family AAA domain-containing protein 3A",
"abbrev": "",
"protein_names": "ATPase family AAA domain-containing protein 3A",
"related_func_ids": "F0210",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9NVI7",
"Uniprot_name": "ATD3A_HUMAN",
"EC_numbers": "",
"gene_symbol": "ATAD3A",
"gene_synonyms": "FLJ10709",
"gene_synonyms_links": "",
"gene_name": "ATPase family, AAA domain containing 3A",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000197785",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein; Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "",
"targ_desciption": "Essential for mitochondrial network organization,mitochondrial metabolism and cell growth at organism and cellularlevel. May play an important role in mitochondrial protein synthesis.May also participate in mitochondrial DNA replication. May bind tomitochondrial DNA D-loops and contribute to nucleoid stability.Required for enhanced channeling of cholesterol for hormone-dependentsteroidogenesis. Involved in mitochondrial-mediated antiviral innateimmunity (PubMed:31522117). {ECO:0000269|PubMed:17210950,ECO:0000269|PubMed:20154147, ECO:0000269|PubMed:22453275,ECO:0000269|PubMed:31522117}.",
"references": []
},
{
"targ_id": "T372",
"parent_targ_id": "T",
"full_name": "Caseinolytic peptidase B protein homolog",
"abbrev": "",
"protein_names": "Caseinolytic peptidase B protein homolog (EC 3.6.1.-) (Suppressor of potassium transport defect 3)",
"related_func_ids": "F0210",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q9H078",
"Uniprot_name": "CLPB_HUMAN",
"EC_numbers": "3.6.1.-",
"gene_symbol": "CLPB",
"gene_synonyms": "ANKCLB, FLJ13152, HSP78, SKD3",
"gene_synonyms_links": "",
"gene_name": "ClpB homolog, mitochondrial AAA ATPase chaperonin",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000162129",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space",
"reaction": "ATP + H2O = ADP + H(+) + phosphate",
"targ_desciption": "May function as a regulatory ATPase and be related tosecretion/protein trafficking process. Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signaltransduction and production of IFNB1 and proinflammatory cytokine IL6(PubMed:31522117). {ECO:0000269|PubMed:31522117}.",
"references": []
},
{
"targ_id": "T373",
"parent_targ_id": "T",
"full_name": "ATP-dependent Clp protease proteolytic subunit, mitochondrial",
"abbrev": "",
"protein_names": "ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC 3.4.21.92) (Endopeptidase Clp)",
"related_func_ids": "F0210",
"category": "protein subunit",
"subcategories": "Hydrolase, Protease, Serine protease",
"Uniport_ID": "Q16740",
"Uniprot_name": "CLPP_HUMAN",
"EC_numbers": "3.4.21.92",
"gene_symbol": "CLPP",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Caseinolytic mitochondrial matrix peptidase proteolytic subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000125656",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "Hydrolysis of proteins to small peptides in the presence ofATP and magnesium. Alpha-casein is the usual test substrate. In theabsence of ATP, only oligopeptides shorter than five residues arehydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds alsooccurs).",
"targ_desciption": "Protease component of the Clp complex that cleaves peptidesand various proteins in an ATP-dependent process. Has low peptidaseactivity in the absence of CLPX. The Clp complex can degrade CSN1S1,CSN2 and CSN3, as well as synthetic peptides (in vitro) and may beresponsible for a fairly general and central housekeeping functionrather than for the degradation of specific substrates(PubMed:11923310, PubMed:15522782). Cleaves PINK1 in the mitochondrion(PubMed:22354088). {ECO:0000269|PubMed:11923310,ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088}.",
"references": []
},
{
"targ_id": "T374",
"parent_targ_id": "T",
"full_name": "ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial",
"abbrev": "",
"protein_names": "ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial",
"related_func_ids": "F0210",
"category": "protein subunit",
"subcategories": "Chaperone",
"Uniport_ID": "O76031",
"Uniprot_name": "CLPX_HUMAN",
"EC_numbers": "",
"gene_symbol": "CLPX",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Caseinolytic mitochondrial matrix peptidase chaperone subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000166855",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "",
"targ_desciption": "ATP-dependent specificity component of the Clp proteasecomplex. Hydrolyzes ATP (PubMed:28874591). Targets specific substratesfor degradation by the Clp complex (PubMed:11923310, PubMed:22710082).Can perform chaperone functions in the absence of CLPP. Enhances theDNA-binding activity of TFAM and is required for maintaining a normalmitochondrial nucleoid structure (PubMed:22841477). ATP-dependentunfoldase that stimulates the incorporation of the pyridoxal phosphatecofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis(PubMed:28874591). Important for efficient erythropoiesis throughupregulation of heme biosynthesis (PubMed:25957689, PubMed:28874591).{ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082,ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:25957689,ECO:0000269|PubMed:28874591}.",
"references": []
},
{
"targ_id": "T375",
"parent_targ_id": "T",
"full_name": "10 kDa heat shock protein, mitochondrial",
"abbrev": "Hsp10",
"protein_names": "10 kDa heat shock protein, mitochondrial (Hsp10) (10 kDa chaperonin) (Chaperonin 10) (CPN10) (Early-pregnancy factor) (EPF)",
"related_func_ids": "F0210",
"category": "protein",
"subcategories": "Chaperone",
"Uniport_ID": "P61604",
"Uniprot_name": "CH10_HUMAN",
"EC_numbers": "",
"gene_symbol": "HSPE1",
"gene_synonyms": "CPN10, EPF, GroES, HSP10",
"gene_synonyms_links": "",
"gene_name": "Heat shock protein family E (Hsp10) member 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000115541",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "",
"targ_desciption": "Co-chaperonin implicated in mitochondrial protein import andmacromolecular assembly. Together with Hsp60, facilitates the correctfolding of imported proteins. May also prevent misfolding and promotethe refolding and proper assembly of unfolded polypeptides generatedunder stress conditions in the mitochondrial matrix (PubMed:7912672,PubMed:1346131, PubMed:11422376). The functional units of thesechaperonins consist of heptameric rings of the large subunit Hsp60,which function as a back-to-back double ring. In a cyclic reaction,Hsp60 ring complexes bind one unfolded substrate protein per ring,followed by the binding of ATP and association with 2 heptameric ringsof the co-chaperonin Hsp10. This leads to sequestration of thesubstrate protein in the inner cavity of Hsp60 where, for a certainperiod of time, it can fold undisturbed by other cell components.Synchronous hydrolysis of ATP in all Hsp60 subunits results in thedissociation of the chaperonin rings and the release of ADP and thefolded substrate protein (Probable). {ECO:0000269|PubMed:11422376,ECO:0000269|PubMed:1346131, ECO:0000269|PubMed:7912672,ECO:0000305|PubMed:25918392}.",
"references": []
},
{
"targ_id": "T376",
"parent_targ_id": "T",
"full_name": "Lon protease homolog, mitochondrial",
"abbrev": "LONP",
"protein_names": "Lon protease homolog, mitochondrial (EC 3.4.21.53) (LONHs) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15)",
"related_func_ids": "F0210; F060102",
"category": "enzyme",
"subcategories": "Hydrolase, Protease, Serine protease",
"Uniport_ID": "P36776",
"Uniprot_name": "LONM_HUMAN",
"EC_numbers": "3.4.21.53",
"gene_symbol": "LONP1",
"gene_synonyms": "hLON, LonHS, PIM1, PRSS15",
"gene_synonyms_links": "",
"gene_name": "Lon peptidase 1, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000196365",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "Hydrolysis of proteins in presence of ATP.",
"targ_desciption": "ATP-dependent serine protease that mediates the selectivedegradation of misfolded, unassembled or oxidatively damagedpolypeptides as well as certain short-lived regulatory proteins in themitochondrial matrix. May also have a chaperone function in theassembly of inner membrane protein complexes. Participates in theregulation of mitochondrial gene expression and in the maintenance ofthe integrity of the mitochondrial genome. Binds to mitochondrialpromoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or geneexpression using site-specific, single-stranded DNA binding to targetthe degradation of regulatory proteins binding to adjacent sites inmitochondrial promoters (PubMed:12198491, PubMed:15870080,PubMed:17420247, PubMed:8248235). Endogenous substrates includemitochondrial steroidogenic acute regulatory (StAR) protein, helicaseTwinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m isprotected from degradation by LONP1 when it is bound to a nucleic acid(RNA), but TWNK is not (PubMed:17579211, PubMed:28377575).{ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12198491,ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247,ECO:0000269|PubMed:17579211, ECO:0000269|PubMed:28377575,ECO:0000269|PubMed:8248235}.",
"references": []
},
{
"targ_id": "T377",
"parent_targ_id": "T",
"full_name": "Presequence protease, mitochondrial",
"abbrev": "hPreP",
"protein_names": "Presequence protease, mitochondrial (hPreP) (EC 3.4.24.-) (Pitrilysin metalloproteinase 1) (Metalloprotease 1) (hMP1)",
"related_func_ids": "F0210",
"category": "enzyme",
"subcategories": "Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q5JRX3",
"Uniprot_name": "PREP_HUMAN",
"EC_numbers": "3.4.24.-",
"gene_symbol": "PITRM1",
"gene_synonyms": "hMP1, KIAA1104, MP1, PreP",
"gene_synonyms_links": "",
"gene_name": "Pitrilysin metallopeptidase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000107959",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "",
"targ_desciption": "Metalloendopeptidase of the mitochondrial matrix thatfunctions in peptide cleavage and degradation rather than in proteinprocessing (PubMed:10360838, PubMed:16849325, PubMed:19196155,PubMed:24931469). Has an ATP-independent activity (PubMed:16849325).Specifically cleaves peptides in the range of 5 to 65 residues(PubMed:19196155). Shows a preference for cleavage after small polarresidues and before basic residues, but without any positionalpreference (PubMed:10360838, PubMed:19196155, PubMed:24931469).Degrades the transit peptides of mitochondrial proteins after theircleavage (PubMed:19196155). Also degrades other unstructured peptides(PubMed:19196155). It is also able to degrade amyloid-beta protein 40,one of the peptides produced by APP processing, when it accumulates inmitochondrion (PubMed:16849325, PubMed:24931469). It is a highlyefficient protease, at least toward amyloid-beta protein 40(PubMed:24931469). Cleaves that peptide at a specific position and isprobably not processive, releasing digested peptides intermediates thatcan be further cleaved subsequently (PubMed:24931469).{ECO:0000269|PubMed:10360838, ECO:0000269|PubMed:16849325,ECO:0000269|PubMed:19196155, ECO:0000269|PubMed:24931469}.",
"references": []
},
{
"targ_id": "T378",
"parent_targ_id": "T",
"full_name": "Sacsin",
"abbrev": "DNAJC29",
"protein_names": "Sacsin (DnaJ homolog subfamily C member 29) (DNAJC29)",
"related_func_ids": "F0210",
"category": "protein",
"subcategories": "regulator",
"Uniport_ID": "Q9NZJ4",
"Uniprot_name": "SACS_HUMAN",
"EC_numbers": "",
"gene_symbol": "SACS KIAA0730",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm",
"reaction": "",
"targ_desciption": "Co-chaperone which acts as a regulator of the Hsp70 chaperonemachinery and may be involved in the processing of other ataxia-linkedproteins. {ECO:0000269|PubMed:19208651}.",
"references": []
},
{
"targ_id": "T379",
"parent_targ_id": "T",
"full_name": "Paraplegin",
"abbrev": "Cell matrix adhesion regulator",
"protein_names": "Paraplegin (EC 3.4.24.-) (Cell matrix adhesion regulator) (Spastic paraplegia 7 protein)",
"related_func_ids": "F0210",
"category": "enzyme",
"subcategories": "Hydrolase, Metalloprotease, Protease",
"Uniport_ID": "Q9UQ90",
"Uniprot_name": "SPG7_HUMAN",
"EC_numbers": "3.4.24.-",
"gene_symbol": "SPG7",
"gene_synonyms": "CAR, CMAR, SPG5C",
"gene_synonyms_links": "",
"gene_name": "SPG7, paraplegin matrix AAA peptidase subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000197912",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "ATP-dependent zinc metalloprotease. Plays a role in theformation and regulation of the mitochondrial permeability transitionpore (mPTP) and its proteolytic activity is dispensable for thisfunction (PubMed:26387735). {ECO:0000269|PubMed:26387735, ECO:0000305}.",
"references": []
},
{
"targ_id": "T380",
"parent_targ_id": "T",
"full_name": "Heat shock protein 75 kDa, mitochondrial",
"abbrev": "HSP 75",
"protein_names": "Heat shock protein 75 kDa, mitochondrial (HSP 75) (TNFR-associated protein 1) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1)",
"related_func_ids": "F0210",
"category": "protein",
"subcategories": "Chaperone",
"Uniport_ID": "Q12931",
"Uniprot_name": "TRAP1_HUMAN",
"EC_numbers": "",
"gene_symbol": "TRAP1",
"gene_synonyms": "HSP75, HSP90L",
"gene_synonyms_links": "",
"gene_name": "TNF receptor associated protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000126602",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Mitochondrion inner membrane; Mitochondrion matrix",
"reaction": "",
"targ_desciption": "Chaperone that expresses an ATPase activity. Involved inmaintaining mitochondrial function and polarization, downstream ofPINK1 and mitochondrial complex I. Is a negative regulator ofmitochondrial respiration able to modulate the balance betweenoxidative phosphorylation and aerobic glycolysis. The impact of TRAP1on mitochondrial respiration is probably mediated by modulation ofmitochondrial SRC and inhibition of SDHA. {ECO:0000269|PubMed:23525905,ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.",
"references": []
},
{
"targ_id": "T381",
"parent_targ_id": "T",
"full_name": "ATP-dependent Clp protease proteolytic subunit, mitochondrial",
"abbrev": "Endopeptidase Clp",
"protein_names": "ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC 3.4.21.92) (Endopeptidase Clp)",
"related_func_ids": "F0210",
"category": "protein subunit",
"subcategories": "Hydrolase, Protease, Serine protease",
"Uniport_ID": "Q16740",
"Uniprot_name": "CLPP_HUMAN",
"EC_numbers": "3.4.21.92",
"gene_symbol": "CLPP",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Caseinolytic mitochondrial matrix peptidase proteolytic subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000125656",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "Hydrolysis of proteins to small peptides in the presence ofATP and magnesium. Alpha-casein is the usual test substrate. In theabsence of ATP, only oligopeptides shorter than five residues arehydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds alsooccurs).",
"targ_desciption": "Protease component of the Clp complex that cleaves peptidesand various proteins in an ATP-dependent process. Has low peptidaseactivity in the absence of CLPX. The Clp complex can degrade CSN1S1,CSN2 and CSN3, as well as synthetic peptides (in vitro) and may beresponsible for a fairly general and central housekeeping functionrather than for the degradation of specific substrates(PubMed:11923310, PubMed:15522782). Cleaves PINK1 in the mitochondrion(PubMed:22354088). {ECO:0000269|PubMed:11923310,ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088}.",
"references": []
},
{
"targ_id": "T382",
"parent_targ_id": "T",
"full_name": "Mitochondrial peptide methionine sulfoxide reductase",
"abbrev": "PMSR",
"protein_names": "Mitochondrial peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (PMSR)",
"related_func_ids": "F020713",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "Q9UJ68",
"Uniprot_name": "MSRA_HUMAN",
"EC_numbers": "1.8.4.11",
"gene_symbol": "MSRA",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Methionine sulfoxide reductase A",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000175806",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; [Isoform 2]: Cytoplasm; [Isoform 3]: Cytoplasm; Nucleus; [Isoform 5]: Cytoplasm; Membrane; Lipid-anchor",
"reaction": "[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =[thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide",
"targ_desciption": "Has an important function as a repair enzyme for proteinsthat have been inactivated by oxidation. Catalyzes the reversibleoxidation-reduction of methionine sulfoxide in proteins to methionine.",
"references": []
},
{
"targ_id": "T383",
"parent_targ_id": "T",
"full_name": "Persulfide dioxygenase ETHE1, mitochondrial",
"abbrev": "Ethylmalonic encephalopathy protein 1",
"protein_names": "Persulfide dioxygenase ETHE1, mitochondrial (EC 1.13.11.18) (Ethylmalonic encephalopathy protein 1) (Hepatoma subtracted clone one protein) (Sulfur dioxygenase ETHE1)",
"related_func_ids": "F0221",
"category": "enzyme",
"subcategories": "Dioxygenase, Oxidoreductase",
"Uniport_ID": "O95571",
"Uniprot_name": "ETHE1_HUMAN",
"EC_numbers": "1.13.11.18",
"gene_symbol": "ETHE1",
"gene_synonyms": "HSCO, YF13H12",
"gene_synonyms_links": "",
"gene_name": "ETHE1, persulfide dioxygenase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000105755",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus; Mitochondrion matrix",
"reaction": "H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) +sulfite",
"targ_desciption": "Sulfur dioxygenase that plays an essential role in hydrogensulfide catabolism in the mitochondrial matrix. Hydrogen sulfide(H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfideresidues. ETHE1 consumes molecular oxygen to catalyze the oxidation ofthe persulfide, once it has been transferred to a thiophilic acceptor,such as glutathione (R-SSH). Plays an important role in metabolichomeostasis in mitochondria by metabolizing hydrogen sulfide andpreventing the accumulation of supraphysiological H(2)S levels thathave toxic effects, due to the inhibition of cytochrome c oxidase.First described as a protein that can shuttle between the nucleus andthe cytoplasm and suppress p53-induced apoptosis by sequestering thetranscription factor RELA/NFKB3 in the cytoplasm and preventing itsaccumulation in the nucleus (PubMed:12398897).{ECO:0000269|PubMed:12398897, ECO:0000269|PubMed:14732903,ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459}.",
"references": []
},
{
"targ_id": "T384",
"parent_targ_id": "T",
"full_name": "3-hydroxyisobutyryl-CoA hydrolase, mitochondrial",
"abbrev": "HIBYL-CoA-H",
"protein_names": "3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (HIB-CoA hydrolase) (HIBYL-CoA-H)",
"related_func_ids": "F020720",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q6NVY1",
"Uniprot_name": "HIBCH_HUMAN",
"EC_numbers": "3.1.2.4",
"gene_symbol": "HIBCH",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "3-hydroxyisobutyryl-CoA hydrolase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000198130",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+)",
"targ_desciption": "Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a salinecatabolite. Has high activity toward isobutyryl-CoA. Could be anisobutyryl-CoA dehydrogenase that functions in valine catabolism. Alsohydrolyzes 3-hydroxypropanoyl-CoA. {ECO:0000269|PubMed:8824301}.",
"references": []
},
{
"targ_id": "T385",
"parent_targ_id": "T",
"full_name": "NAD(P) transhydrogenase, mitochondrial",
"abbrev": "Nicotinamide nucleotide transhydrogenase",
"protein_names": "NAD(P) transhydrogenase, mitochondrial (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase) (Pyridine nucleotide transhydrogenase)",
"related_func_ids": "F050501",
"category": "enzyme",
"subcategories": "Translocase",
"Uniport_ID": "Q13423",
"Uniprot_name": "NNTM_HUMAN",
"EC_numbers": "7.1.1.1",
"gene_symbol": "NNT",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Nicotinamide nucleotide transhydrogenase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000112992",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side",
"reaction": "H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)",
"targ_desciption": "The transhydrogenation between NADH and NADP is coupled torespiration and ATP hydrolysis and functions as a proton pump acrossthe membrane (By similarity). May play a role in reactive oxygenspecies (ROS) detoxification in the adrenal gland (PubMed:22634753).{ECO:0000250|UniProtKB:P07001, ECO:0000269|PubMed:22634753}.",
"references": []
},
{
"targ_id": "T386",
"parent_targ_id": "T",
"full_name": "Thioredoxin, mitochondrial",
"abbrev": "Mt-Trx",
"protein_names": "Thioredoxin, mitochondrial (MTRX) (Mt-Trx) (Thioredoxin-2)",
"related_func_ids": "F050501",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q99757",
"Uniprot_name": "THIOM_HUMAN",
"EC_numbers": "",
"gene_symbol": "TXN2",
"gene_synonyms": "MT-TRX",
"gene_synonyms_links": "",
"gene_name": "Thioredoxin 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000100348",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Important for the control of mitochondrial reactive oxygenspecies homeostasis, apoptosis regulation and cell viability. Possessesa dithiol-reducing activity. {ECO:0000269|PubMed:12032145,ECO:0000269|PubMed:12080052, ECO:0000269|PubMed:26626369}.",
"references": [
"RC01244"
]
},
{
"targ_id": "T387",
"parent_targ_id": "T",
"full_name": "Reactive oxygen species",
"abbrev": "ROS",
"protein_names": "",
"related_func_ids": "",
"category": "molecule",
"subcategories": "",
"Uniport_ID": "",
"Uniprot_name": "",
"EC_numbers": "",
"gene_symbol": "",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "",
"references": [
"RC00065",
"RC00066",
"RC00067",
"RC00068",
"RC00796",
"RC00797",
"RC00798",
"RC00799",
"RC00800",
"RC00998",
"RC04664",
"RC04735",
"RC04736",
"RC04644",
"RC04645",
"RC04646",
"RC04665",
"RC04666",
"RC04667",
"RC04668",
"RC04669",
"RC04670",
"RC04671",
"RC04672",
"RC04673",
"RC04674",
"RC04675",
"RC04676",
"RC04677",
"RC04701",
"RC04702",
"RC04703",
"RC04704",
"RC04729"
]
},
{
"targ_id": "T387001",
"parent_targ_id": "T387",
"full_name": "superoxide",
"abbrev": "O2s",
"protein_names": "",
"related_func_ids": "",
"category": "molecule",
"subcategories": "",
"Uniport_ID": "",
"Uniprot_name": "",
"EC_numbers": "",
"gene_symbol": "",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "",
"references": [
"RC00690",
"RC00746",
"RC00747",
"RC00748",
"RC00749",
"RC00750",
"RC00751",
"RC00752",
"RC00753",
"RC00754",
"RC00755"
]
},
{
"targ_id": "T387002",
"parent_targ_id": "T387",
"full_name": "hydrogen peroxide",
"abbrev": "H2O2",
"protein_names": "",
"related_func_ids": "",
"category": "molecule",
"subcategories": "",
"Uniport_ID": "",
"Uniprot_name": "",
"EC_numbers": "",
"gene_symbol": "",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "",
"references": [
"RC00691",
"RC00756",
"RC00757"
]
},
{
"targ_id": "T388",
"parent_targ_id": "T",
"full_name": "Catalase",
"abbrev": "",
"protein_names": "Catalase (EC 1.11.1.6)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "Mitogen, Oxidoreductase, Peroxidase",
"Uniport_ID": "P04040",
"Uniprot_name": "CATA_HUMAN",
"EC_numbers": "1.11.1.6",
"gene_symbol": "CAT",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Catalase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000121691",
"omim_id": "",
"genecard_link": "",
"locs": "Peroxisome",
"reaction": "2 H2O2 = 2 H2O + O2",
"targ_desciption": "Occurs in almost all aerobically respiring organisms andserves to protect cells from the toxic effects of hydrogen peroxide.Promotes growth of cells including T-cells, B-cells, myeloid leukemiacells, melanoma cells, mastocytoma cells and normal and transformedfibroblast cells. {ECO:0000269|PubMed:7882369}.",
"references": []
},
{
"targ_id": "T389",
"parent_targ_id": "T",
"full_name": "Glutathione reductase, mitochondrial",
"abbrev": "GRase",
"protein_names": "Glutathione reductase, mitochondrial (GR) (GRase) (EC 1.8.1.7)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "P00390",
"Uniprot_name": "GSHR_HUMAN",
"EC_numbers": "1.8.1.7",
"gene_symbol": "GSR",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Glutathione-disulfide reductase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000104687",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Mitochondrial]: Mitochondrion; [Isoform Cytoplasmic]: Cytoplasm",
"reaction": "2 glutathione + NADP(+) = glutathione disulfide + H(+) +NADPH",
"targ_desciption": "Maintains high levels of reduced glutathione in the cytosol.",
"references": []
},
{
"targ_id": "T390",
"parent_targ_id": "T",
"full_name": "Glutathione synthetase",
"abbrev": "GSH-S",
"protein_names": "Glutathione synthetase (GSH synthetase) (GSH-S) (EC 6.3.2.3) (Glutathione synthase)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "P48637",
"Uniprot_name": "GSHB_HUMAN",
"EC_numbers": "6.3.2.3",
"gene_symbol": "GSS",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +glutathione + H(+) + phosphate",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T391",
"parent_targ_id": "T",
"full_name": "Peroxiredoxin-5, mitochondrial",
"abbrev": "Prx-V",
"protein_names": "Peroxiredoxin-5, mitochondrial (EC 1.11.1.24) (Alu corepressor 1) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 71B) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (TPx type VI) (Thioredoxin peroxidase PMP20) (Thioredoxin-dependent peroxiredoxin 5)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "Antioxidant, Oxidoreductase, Peroxidase",
"Uniport_ID": "P30044",
"Uniprot_name": "PRDX5_HUMAN",
"EC_numbers": "1.11.1.24",
"gene_symbol": "PRDX5",
"gene_synonyms": "ACR1, AOEB166, B166, MGC117264, MGC142283, MGC142285, PLP, PMP20, PRDX6, PRXV, SBBI10",
"gene_synonyms_links": "",
"gene_name": "Peroxiredoxin 5",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000126432",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Mitochondrial]: Mitochondrion; [Isoform Cytoplasmic+peroxisomal]: Cytoplasm; Peroxisome matrix",
"reaction": "[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O",
"targ_desciption": "Thiol-specific peroxidase that catalyzes the reduction ofhydrogen peroxide and organic hydroperoxides to water and alcohols,respectively. Plays a role in cell protection against oxidative stressby detoxifying peroxides and as sensor of hydrogen peroxide-mediatedsignaling events. {ECO:0000269|PubMed:10514471,ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}.",
"references": []
},
{
"targ_id": "T392",
"parent_targ_id": "T",
"full_name": "Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase",
"abbrev": "XD",
"protein_names": "Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)]",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "P47989",
"Uniprot_name": "XDH_HUMAN",
"EC_numbers": "1.17.1.4; 1.17.3.2",
"gene_symbol": "XDH XDHA",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Peroxisome; Secreted",
"reaction": "H2O + NAD(+) + xanthine = H(+) + NADH + urate; H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine; H2O + O2 + xanthine = H2O2 + urate",
"targ_desciption": "Key enzyme in purine degradation. Catalyzes the oxidation ofhypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uricacid. Contributes to the generation of reactive oxygen species. Hasalso low oxidase activity towards aldehydes (in vitro).{ECO:0000269|PubMed:17301077}.",
"references": []
},
{
"targ_id": "T393",
"parent_targ_id": "T",
"full_name": "Myeloperoxidase",
"abbrev": "MPO",
"protein_names": "Myeloperoxidase (MPO) (EC 1.11.2.2) [Cleaved into: Myeloperoxidase; 89 kDa myeloperoxidase; 84 kDa myeloperoxidase; Myeloperoxidase light chain; Myeloperoxidase heavy chain]",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "P05164",
"Uniprot_name": "PERM_HUMAN",
"EC_numbers": "1.11.2.2",
"gene_symbol": "MPO",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Lysosome",
"reaction": "chloride + H(+) + H2O2 = H2O + hypochlorous acid",
"targ_desciption": "Part of the host defense system of polymorphonuclearleukocytes. It is responsible for microbicidal activity against a widerange of organisms. In the stimulated PMN, MPO catalyzes the productionof hypohalous acids, primarily hypochlorous acid in physiologicsituations, and other toxic intermediates that greatly enhance PMNmicrobicidal activity. {ECO:0000269|PubMed:9922160}.",
"references": []
},
{
"targ_id": "T394",
"parent_targ_id": "T",
"full_name": "NADPH oxidase",
"abbrev": "NOX",
"protein_names": "",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "",
"Uniprot_name": "",
"EC_numbers": "",
"gene_symbol": "",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "",
"references": [
"RC00880"
]
},
{
"targ_id": "T395",
"parent_targ_id": "T",
"full_name": "NADPH oxidase 1",
"abbrev": "NOX1",
"protein_names": "NADPH oxidase 1 (NOX-1) (EC 1.-.-.-) (Mitogenic oxidase 1) (MOX-1) (NADH/NADPH mitogenic oxidase subunit P65-MOX) (NOH-1)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q9Y5S8",
"Uniprot_name": "NOX1_HUMAN",
"EC_numbers": "1.-.-.-",
"gene_symbol": "NOX1 MOX1 NOH1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cell projection, invadopodium membrane; Multi-pass membrane protein; Cell membrane",
"reaction": "",
"targ_desciption": "NOH-1S is a voltage-gated proton channel that mediates theH(+) currents of resting phagocytes and other tissues. It participatesin the regulation of cellular pH and is blocked by zinc. NOH-1L is apyridine nucleotide-dependent oxidoreductase that generates superoxideand might conduct H(+) ions as part of its electron transportmechanism, whereas NOH-1S does not contain an electron transport chain.",
"references": []
},
{
"targ_id": "T396",
"parent_targ_id": "T",
"full_name": "NADPH oxidase 4",
"abbrev": "NOX4",
"protein_names": "NADPH oxidase 4 (EC 1.6.3.-) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q9NPH5",
"Uniprot_name": "NOX4_HUMAN",
"EC_numbers": "1.6.3.-",
"gene_symbol": "NOX4 RENOX",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Endoplasmic reticulum membrane; Multi-pass membrane protein; Cell membrane; Multi-pass membrane protein; Cell junction, focal adhesion; [Isoform 4]: Nucleus; Nucleus, nucleolus",
"reaction": "",
"targ_desciption": "Constitutive NADPH oxidase which generates superoxideintracellularly upon formation of a complex with CYBA/p22phox.Regulates signaling cascades probably through phosphatases inhibition.May function as an oxygen sensor regulating the KCNK3/TASK-1 potassiumchannel and HIF1A activity. May regulate insulin signaling cascade. Mayplay a role in apoptosis, bone resorption and lipolysaccharide-mediatedactivation of NFKB. May produce superoxide in the nucleus and play arole in regulating gene expression upon cell stimulation. Isoform 3 isnot functional. Isoform 5 and isoform 6 display reduced activity.; [Isoform 4]: Involved in redox signaling in vascular cells.Constitutively and NADPH-dependently generates reactive oxygen species(ROS). Modulates the nuclear activation of ERK1/2 and the ELK1transcription factor, and is capable of inducing nuclear DNA damage.Displays an increased activity relative to isoform 1.",
"references": []
},
{
"targ_id": "T397",
"parent_targ_id": "T",
"full_name": "Superoxide dismutase [Mn], mitochondrial",
"abbrev": "",
"protein_names": "Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "P04179",
"Uniprot_name": "SODM_HUMAN",
"EC_numbers": "1.15.1.1",
"gene_symbol": "SOD2",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Superoxide dismutase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000285441",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "2 H(+) + 2 superoxide = H2O2 + O2",
"targ_desciption": "Destroys superoxide anion radicals which are normallyproduced within the cells and which are toxic to biological systems.{ECO:0000269|PubMed:10334867}.",
"references": [
"RC03661"
]
},
{
"targ_id": "T398",
"parent_targ_id": "T",
"full_name": "Phospholipid hydroperoxide glutathione peroxidase",
"abbrev": "PHGPx",
"protein_names": "Phospholipid hydroperoxide glutathione peroxidase (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4)",
"related_func_ids": "F0221",
"category": "enzyme",
"subcategories": "Developmental protein, Oxidoreductase, Peroxidase",
"Uniport_ID": "P36969",
"Uniprot_name": "GPX4_HUMAN",
"EC_numbers": "1.11.1.12",
"gene_symbol": "GPX4",
"gene_synonyms": "MCSP, PHGPx",
"gene_synonyms_links": "",
"gene_name": "Glutathione peroxidase 4",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000167468",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Mitochondrial]: Mitochondrion; [Isoform Cytoplasmic]: Cytoplasm",
"reaction": "a hydroperoxy polyunsaturated fatty acid + 2 glutathione = ahydroxy polyunsaturated fatty acid + glutathione disulfide + H2O; (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +glutathione disulfide + H2O; (13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =(13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +H2O",
"targ_desciption": "Essential antioxidant peroxidase that directly reducesphospholipid hydroperoxide even if they are incorporated in membranesand lipoproteins (By similarity). Can also reduce fatty acidhydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (Bysimilarity). Plays a key role in protecting cells from oxidative damageby preventing membrane lipid peroxidation (By similarity). Required toprevent cells from ferroptosis, a non-apoptotic cell death resultingfrom an iron-dependent accumulation of lipid reactive oxygen species(PubMed:24439385). The presence of selenocysteine (Sec) versus Cys atthe active site is essential for life: it provides resistance tooveroxidation and prevents cells against ferroptosis (By similarity).The presence of Sec at the active site is also essential for thesurvival of a specific type of parvalbumin-positive interneurons,thereby preventing against fatal epileptic seizures (By similarity).May be required to protect cells from the toxicity of ingested lipidhydroperoxides (By similarity). Required for normal sperm developmentand male fertility (By similarity). Essential for maturation andsurvival of photoreceptor cells (By similarity). Plays a role in aprimary T-cell response to viral and parasitic infection by protectingT-cells from ferroptosis and by supporting T-cell expansion (Bysimilarity). Plays a role of glutathione peroxidase in platelets in thearachidonic acid metabolism (PubMed:11115402). Reduces hydroperoxyester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity).{ECO:0000250|UniProtKB:O70325, ECO:0000250|UniProtKB:P36968,ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:24439385}.",
"references": []
},
{
"targ_id": "T399",
"parent_targ_id": "T",
"full_name": "Thioredoxin reductase 2, mitochondrial",
"abbrev": "TR-beta",
"protein_names": "Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Selenoprotein Z) (SelZ) (TR-beta) (Thioredoxin reductase TR3)",
"related_func_ids": "F0505",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "Q9NNW7",
"Uniprot_name": "TRXR2_HUMAN",
"EC_numbers": "1.8.1.9",
"gene_symbol": "TXNRD2",
"gene_synonyms": "TR, TR3, TRXR2",
"gene_synonyms_links": "",
"gene_name": "Thioredoxin reductase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000184470",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +H(+) + NADPH",
"targ_desciption": "Involved in the control of reactive oxygen species levels andthe regulation of mitochondrial redox homeostasis (PubMed:24601690).Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling. {ECO:0000269|PubMed:24601690}.",
"references": [
"RC03837",
"RC03838"
]
},
{
"targ_id": "T400",
"parent_targ_id": "T",
"full_name": "oxidized glutathione",
"abbrev": "GSSH",
"protein_names": "",
"related_func_ids": "",
"category": "metabolite",
"subcategories": "",
"Uniport_ID": "",
"Uniprot_name": "",
"EC_numbers": "",
"gene_symbol": "",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "",
"references": [
"RC00806",
"RC00807",
"RC00808",
"RC00809",
"RC00810",
"RC03657"
]
},
{
"targ_id": "T401",
"parent_targ_id": "T",
"full_name": "Glycine N-acyltransferase",
"abbrev": "AAc",
"protein_names": "Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71) (HRP-1(CLP))",
"related_func_ids": "F020708",
"category": "enzyme",
"subcategories": "Acyltransferase, Transferase",
"Uniport_ID": "Q6IB77",
"Uniprot_name": "GLYAT_HUMAN",
"EC_numbers": "2.3.1.13; 2.3.1.71",
"gene_symbol": "GLYAT",
"gene_synonyms": "ACGNAT, GAT",
"gene_synonyms_links": "",
"gene_name": "Glycine-N-acyltransferase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000149124",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "an acyl-CoA + glycine = an N-acylglycine + CoA + H(+); benzoyl-CoA + glycine = CoA + H(+) + N-benzoylglycine",
"targ_desciption": "Mitochondrial acyltransferase which transfers an acyl groupto the N-terminus of glycine and glutamine, although much lessefficiently. Can conjugate numerous substrates to form a variety of N-acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoAas acyl donors. Thereby detoxify xenobiotics, such as benzoic acid orsalicylic acid, and endogenous organic acids, such as isovaleric acid.{ECO:0000269|PubMed:22475485, ECO:0000269|PubMed:7802672}.",
"references": []
},
{
"targ_id": "T403",
"parent_targ_id": "T",
"full_name": "Apoptosis regulator Bcl-2",
"abbrev": "",
"protein_names": "Apoptosis regulator Bcl-2",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "regulator",
"Uniport_ID": "P10415",
"Uniprot_name": "BCL2_HUMAN",
"EC_numbers": "",
"gene_symbol": "BCL2",
"gene_synonyms": "Bcl-2, PPP1R50",
"gene_synonyms_links": "",
"gene_name": "BCL2, apoptosis regulator",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000171791",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Single-pass membrane protein; Nucleus membrane; Single-pass membrane protein; Endoplasmic reticulum membrane; Single-pass membrane protein",
"reaction": "",
"targ_desciption": "Suppresses apoptosis in a variety of cell systems includingfactor-dependent lymphohematopoietic and neural cells. Regulates celldeath by controlling the mitochondrial membrane permeability. Appearsto function in a feedback loop system with caspases. Inhibits caspaseactivity either by preventing the release of cytochrome c from themitochondria and/or by binding to the apoptosis-activating factor(APAF-1). May attenuate inflammation by impairing NLRP1-inflammasomeactivation, hence CASP1 activation and IL1B release (PubMed:17418785).{ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871}.",
"references": [
"RC00456",
"RC00457",
"RC00458",
"RC00459",
"RC00460",
"RC00461",
"RC00468",
"RC03486"
]
},
{
"targ_id": "T404",
"parent_targ_id": "T",
"full_name": "Apoptosis regulator BAX",
"abbrev": "Bcl2-L-4",
"protein_names": "Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "regulator",
"Uniport_ID": "Q07812",
"Uniprot_name": "BAX_HUMAN",
"EC_numbers": "",
"gene_symbol": "BAX",
"gene_synonyms": "BCL2L4",
"gene_synonyms_links": "",
"gene_name": "BCL2 associated X, apoptosis regulator",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000087088",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Alpha]: Mitochondrion outer membrane; Single-pass membrane protein; Cytoplasm; [Isoform Beta]: Cytoplasm; [Isoform Gamma]: Cytoplasm; [Isoform Delta]: Cytoplasm",
"reaction": "",
"targ_desciption": "Plays a role in the mitochondrial apoptotic process. Undernormal conditions, BAX is largely cytosolic via constantretrotranslocation from mitochondria to the cytosol mediated byBCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at themitochondrial outer membrane (MOM) (PubMed:21458670). Under stressconditions, undergoes a conformation change that causes translocationto the mitochondrion membrane, leading to the release of cytochrome cthat then triggers apoptosis. Promotes activation of CASP3, and therebyapoptosis. {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:16113678,ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865,ECO:0000269|PubMed:21458670, ECO:0000269|PubMed:8358790,ECO:0000269|PubMed:8521816}.",
"references": [
"RC00462",
"RC00463",
"RC00464",
"RC00465",
"RC00466",
"RC00467",
"RC00469"
]
},
{
"targ_id": "T405",
"parent_targ_id": "T",
"full_name": "Bcl-2-like protein 2",
"abbrev": "Bcl2-L-2",
"protein_names": "Bcl-2-like protein 2 (Bcl2-L-2) (Apoptosis regulator Bcl-W)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q92843",
"Uniprot_name": "B2CL2_HUMAN",
"EC_numbers": "",
"gene_symbol": "BCL2L2",
"gene_synonyms": "BCL-W, KIAA0271, PPP1R51",
"gene_synonyms_links": "",
"gene_name": "BCL2 like 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000129473",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion membrane; Peripheral membrane protein",
"reaction": "",
"targ_desciption": "Promotes cell survival. Blocks dexamethasone-inducedapoptosis. Mediates survival of postmitotic Sertoli cells bysuppressing death-promoting activity of BAX.{ECO:0000269|PubMed:8761287}.",
"references": []
},
{
"targ_id": "T406",
"parent_targ_id": "T",
"full_name": "Bcl-2-like protein 1",
"abbrev": "Bcl2-L-1",
"protein_names": "Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q07817",
"Uniprot_name": "B2CL1_HUMAN",
"EC_numbers": "",
"gene_symbol": "BCL2L1",
"gene_synonyms": "Bcl-X, bcl-xL, bcl-xS, BCL2L, BCLX, PPP1R52",
"gene_synonyms_links": "",
"gene_name": "BCL2 like 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000171552",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Bcl-X(L)]: Mitochondrion inner membrane; Mitochondrion outer membrane; Mitochondrion matrix; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Cytoplasm, cytosol; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Nucleus membrane; Single-pass membrane protein; Cytoplasmic side",
"reaction": "",
"targ_desciption": "Potent inhibitor of cell death. Inhibits activation ofcaspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing therelease of the caspase activator, CYC1, from the mitochondrialmembrane. Also acts as a regulator of G2 checkpoint and progression tocytokinesis during mitosis.; Isoform Bcl-X(L) also regulates presynaptic plasticity,including neurotransmitter release and recovery, number of axonalmitochondria as well as size and number of synaptic vesicle clusters.During synaptic stimulation, increases ATP availability frommitochondria through regulation of mitochondrial membrane ATP synthaseF(1)F(0) activity and regulates endocytic vesicle retrieval inhippocampal neurons through association with DMN1L and stimulation ofits GTPase activity in synaptic vesicles. May attenuate inflammationimpairing NLRP1-inflammasome activation, hence CASP1 activation andIL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785}.; Isoform Bcl-X(S) promotes apoptosis.",
"references": []
},
{
"targ_id": "T407",
"parent_targ_id": "T",
"full_name": "Bcl2-associated agonist of cell death",
"abbrev": "BAD",
"protein_names": "Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-2-like protein 8) (Bcl2-L-8) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q92934",
"Uniprot_name": "BAD_HUMAN",
"EC_numbers": "",
"gene_symbol": "BAD",
"gene_synonyms": "BBC2, BCL2L8",
"gene_synonyms_links": "",
"gene_name": "BCL2 associated agonist of cell death",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000002330",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane; Cytoplasm",
"reaction": "",
"targ_desciption": "Promotes cell death. Successfully competes for the binding toBcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level ofheterodimerization of these proteins with BAX. Can reverse the deathrepressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity).Appears to act as a link between growth factor receptor signaling andthe apoptotic pathways. {ECO:0000250}.",
"references": []
},
{
"targ_id": "T408",
"parent_targ_id": "T",
"full_name": "Cytochrome c",
"abbrev": "cytc",
"protein_names": "Cytochrome c",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "P99999",
"Uniprot_name": "CYC_HUMAN",
"EC_numbers": "",
"gene_symbol": "CYCS",
"gene_synonyms": "CYC, HCS",
"gene_synonyms_links": "",
"gene_name": "Cytochrome c, somatic",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000172115",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space",
"reaction": "",
"targ_desciption": "Electron carrier protein. The oxidized form of the cytochromec heme group can accept an electron from the heme group of thecytochrome c1 subunit of cytochrome reductase. Cytochrome c thentransfers this electron to the cytochrome oxidase complex, the finalprotein carrier in the mitochondrial electron-transport chain.; Plays a role in apoptosis. Suppression of the anti-apoptoticmembers or activation of the pro-apoptotic members of the Bcl-2 familyleads to altered mitochondrial membrane permeability resulting inrelease of cytochrome c into the cytosol. Binding of cytochrome c toApaf-1 triggers the activation of caspase-9, which then acceleratesapoptosis by activating other caspases.",
"references": [
"RC00424",
"RC00425",
"RC00426",
"RC00427",
"RC00428",
"RC01043",
"RC01178",
"RC04268",
"RC04269",
"RC04270",
"RC04271",
"RC04272",
"RC04273",
"RC04274",
"RC04275",
"RC04276",
"RC04277",
"RC04278",
"RC04279",
"RC04280",
"RC04281",
"RC04282",
"RC04283",
"RC04284",
"RC04285",
"RC04286",
"RC04287",
"RC04288",
"RC04289",
"RC04290",
"RC04291",
"RC04292",
"RC04294",
"RC04297",
"RC04298",
"RC04299",
"RC04300",
"RC04301",
"RC04304",
"RC04307",
"RC04311",
"RC04312",
"RC04313",
"RC04315",
"RC04316",
"RC04318",
"RC04319",
"RC04321",
"RC04322",
"RC04323",
"RC04324",
"RC04325",
"RC04326",
"RC04327",
"RC04328",
"RC04329",
"RC04330",
"RC04331",
"RC04332",
"RC04333",
"RC04335",
"RC04339",
"RC04340",
"RC04345",
"RC04346",
"RC04348",
"RC04349",
"RC04353",
"RC04356",
"RC04357",
"RC04358",
"RC04360",
"RC04362",
"RC04363",
"RC04364",
"RC04365",
"RC04368",
"RC04370",
"RC04371",
"RC04376",
"RC04379",
"RC04383",
"RC04385",
"RC04386",
"RC04388",
"RC04391"
]
},
{
"targ_id": "T409",
"parent_targ_id": "T",
"full_name": "Caspase-3",
"abbrev": "CASP-3",
"protein_names": "Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]",
"related_func_ids": "F0701",
"category": "enzyme",
"subcategories": "Hydrolase, Protease, Thiol protease",
"Uniport_ID": "P42574",
"Uniprot_name": "CASP3_HUMAN",
"EC_numbers": "3.4.22.56",
"gene_symbol": "CASP3",
"gene_synonyms": "apopain, CPP32, CPP32B, Yama",
"gene_synonyms_links": "",
"gene_name": "Caspase 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000164305",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm",
"reaction": "Strict requirement for an Asp residue at positions P1 and P4.It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with ahydrophobic amino-acid residue at P2 and a hydrophilic amino-acidresidue at P3, although Val or Ala are also accepted at thisposition.",
"targ_desciption": "Involved in the activation cascade of caspases responsiblefor apoptosis execution. At the onset of apoptosis it proteolyticallycleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217'bond. Cleaves and activates sterol regulatory element binding proteins(SREBPs) between the basic helix-loop-helix leucine zipper domain andthe membrane attachment domain. Cleaves and activates caspase-6, -7 and-9. Involved in the cleavage of huntingtin. Triggers cell adhesion insympathetic neurons through RET cleavage. {ECO:0000269|PubMed:21357690,ECO:0000269|PubMed:7596430}.",
"references": [
"RC03906",
"RC04753",
"RC04754",
"RC04999"
]
},
{
"targ_id": "T410",
"parent_targ_id": "T",
"full_name": "Serine/threonine-protein kinase PAK 5",
"abbrev": "PAK-5",
"protein_names": "Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7)",
"related_func_ids": "F0701",
"category": "enzyme",
"subcategories": "Kinase",
"Uniport_ID": "Q9P286",
"Uniprot_name": "PAK5_HUMAN",
"EC_numbers": "2.7.11.1",
"gene_symbol": "PAK5 KIAA1264 PAK7",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Cytoplasm; Nucleus",
"reaction": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]",
"targ_desciption": "Serine/threonine protein kinase that plays a role in avariety of different signaling pathways including cytoskeletonregulation, cell migration, proliferation or cell survival. Activationby various effectors including growth factor receptors or active CDC42and RAC1 results in a conformational change and a subsequentautophosphorylation on several serine and/or threonine residues.Phosphorylates the proto-oncogene RAF1 and stimulates its kinaseactivity. Promotes cell survival by phosphorylating the BCL2 antagonistof cell death BAD. Phosphorylates CTNND1, probably to regulatecytoskeletal organization and cell morphology. Keeps microtubulesstable through MARK2 inhibition and destabilizes the F-actin networkleading to the disappearance of stress fibers and focal adhesions.{ECO:0000269|PubMed:12897128, ECO:0000269|PubMed:16014608,ECO:0000269|PubMed:16581795, ECO:0000269|PubMed:18465753,ECO:0000269|PubMed:20564219}.",
"references": []
},
{
"targ_id": "T411",
"parent_targ_id": "T",
"full_name": "Apoptosis-inducing factor 1, mitochondrial",
"abbrev": "Programmed cell death protein 8",
"protein_names": "Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)",
"related_func_ids": "F0701",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "O95831",
"Uniprot_name": "AIFM1_HUMAN",
"EC_numbers": "1.6.99.-",
"gene_symbol": "AIFM1",
"gene_synonyms": "AIF, CMTX4, NAMSD, PDCD8",
"gene_synonyms_links": "",
"gene_name": "Apoptosis inducing factor mitochondria associated 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000156709",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space; Mitochondrion inner membrane; Cytoplasm; Nucleus; Cytoplasm, perinuclear region; [Isoform 3]: Mitochondrion intermembrane space; Mitochondrion inner membrane; [Isoform 4]: Mitochondrion; Cytoplasm, cytosol; [Isoform 5]: Cytoplasm",
"reaction": "A + H(+) + NADH = AH2 + NAD(+); A + H(+) + NADH = AH2 + NAD(+)",
"targ_desciption": "Functions both as NADH oxidoreductase and as regulator ofapoptosis (PubMed:20362274, PubMed:23217327, PubMed:17094969). Inresponse to apoptotic stimuli, it is released from the mitochondrionintermembrane space into the cytosol and to the nucleus, where itfunctions as a proapoptotic factor in a caspase-independent pathway.The soluble form (AIFsol) found in the nucleus induces 'parthanatos'i.e. caspase-independent fragmentation of chromosomal DNA (Bysimilarity). Binds to DNA in a sequence-independent manner(PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3machinery and protein synthesis, and activates caspase-7 to amplifyapoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells(PubMed:19418225). In contrast, participates in normal mitochondrialmetabolism. Plays an important role in the regulation of respiratorychain biogenesis by interacting with CHCHD4 and controlling CHCHD4mitochondrial import (PubMed:26004228). {ECO:0000250|UniProtKB:Q9Z0X1,ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225,ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327,ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:27178839}.; [Isoform 4]: Has NADH oxidoreductase activity. Does notinduce nuclear apoptosis. {ECO:0000269|PubMed:16644725}.; [Isoform 5]: Pro-apoptotic isoform.{ECO:0000269|PubMed:16365034}.",
"references": [
"RC03485"
]
},
{
"targ_id": "T412",
"parent_targ_id": "T",
"full_name": "Cytochrome c oxidase assembly factor 8",
"abbrev": "COA8",
"protein_names": "Cytochrome c oxidase assembly factor 8 (COA8) (Apoptogenic protein 1, mitochondrial) (APOP-1)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q96IL0",
"Uniprot_name": "COA8_HUMAN",
"EC_numbers": "",
"gene_symbol": "APOPT1",
"gene_synonyms": "APOP-1, C14orf153, MGC2562",
"gene_synonyms_links": "",
"gene_name": "Apoptogenic 1, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000256053",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
"reaction": "",
"targ_desciption": "Required for cytochrome c complex (COX) IV assembly andfunction Protects COX assembly from oxidation-induced degradation, COXbeing the terminal component of the mitochondrial respiratory chain.{ECO:0000269|PubMed:25175347, ECO:0000269|PubMed:30552096}.",
"references": []
},
{
"targ_id": "T413",
"parent_targ_id": "T",
"full_name": "Diablo homolog, mitochondrial",
"abbrev": "Smac",
"protein_names": "Diablo homolog, mitochondrial (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspase) (Smac)",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9NR28",
"Uniprot_name": "DBLOH_HUMAN",
"EC_numbers": "",
"gene_symbol": "DIABLO",
"gene_synonyms": "DFNA64, DIABLO-S, FLJ10537, FLJ25049, SMAC",
"gene_synonyms_links": "",
"gene_name": "Diablo IAP-binding mitochondrial protein",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000184047",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Promotes apoptosis by activating caspases in the cytochromec/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity ofinhibitor of apoptosis proteins (IAP). Inhibits the activity ofBIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuatesthe stability and apoptosis-inhibiting activity of XIAP/BIRC4 bypromoting XIAP/BIRC4 ubiquitination and degradation through theubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4interacting with processed caspase-9 and promotes caspase-3 activation.Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4abundance. {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:14523016,ECO:0000269|PubMed:15200957}.",
"references": []
},
{
"targ_id": "T414",
"parent_targ_id": "T",
"full_name": "Serine protease HTRA2, mitochondrial",
"abbrev": "HtrA2",
"protein_names": "Serine protease HTRA2, mitochondrial (EC 3.4.21.108) (High temperature requirement protein A2) (HtrA2) (Omi stress-regulated endoprotease) (Serine protease 25) (Serine proteinase OMI)",
"related_func_ids": "F0701",
"category": "enzyme",
"subcategories": "Hydrolase, Protease, Serine protease",
"Uniport_ID": "O43464",
"Uniprot_name": "HTRA2_HUMAN",
"EC_numbers": "3.4.21.108",
"gene_symbol": "HTRA2",
"gene_synonyms": "OMI, PARK13, PRSS25",
"gene_synonyms_links": "",
"gene_name": "HtrA serine peptidase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000115317",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space; Mitochondrion membrane; Single-pass membrane protein",
"reaction": "Cleavage of non-polar aliphatic amino-acids at the P1position, with a preference for Val, Ile and Met. At the P2 and P3positions, Arg is selected most strongly with a secondary preferencefor other hydrophilic residues.",
"targ_desciption": "Serine protease that shows proteolytic activity against anon-specific substrate beta-casein. Promotes or induces cell deatheither by direct binding to and inhibition of BIRC proteins (alsocalled inhibitor of apoptosis proteins, IAPs), leading to an increasein caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. CleavesTHAP5 and promotes its degradation during apoptosis. Isoform 2 seems tobe proteolytically inactive. {ECO:0000269|PubMed:15200957,ECO:0000269|PubMed:19502560}.",
"references": []
},
{
"targ_id": "T415",
"parent_targ_id": "T",
"full_name": "Peptidyl-tRNA hydrolase 2, mitochondrial",
"abbrev": "PTH 2",
"protein_names": "Peptidyl-tRNA hydrolase 2, mitochondrial (PTH 2) (EC 3.1.1.29) (Bcl-2 inhibitor of transcription 1)",
"related_func_ids": "F0701",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q9Y3E5",
"Uniprot_name": "PTH2_HUMAN",
"EC_numbers": "3.1.1.29",
"gene_symbol": "PTRH2",
"gene_synonyms": "BIT1, CFAP37, CGI-147, PTH2",
"gene_synonyms_links": "",
"gene_name": "Peptidyl-tRNA hydrolase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000141378",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino acid +H(+) + tRNA",
"targ_desciption": "The natural substrate for this enzyme may be peptidyl-tRNAswhich drop off the ribosome during protein synthesis. {ECO:0000250}.; Promotes caspase-independent apoptosis by regulating thefunction of two transcriptional regulators, AES and TLE1.{ECO:0000269|PubMed:15006356}.",
"references": []
},
{
"targ_id": "T416",
"parent_targ_id": "T",
"full_name": "Serine/threonine-protein kinase mTOR",
"abbrev": "mTOR",
"protein_names": "Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin and FKBP12 target 1) (Rapamycin target protein 1)",
"related_func_ids": "F0801; F0808",
"category": "enzyme",
"subcategories": "Kinase, Serine/threonine-protein kinase, Transferase",
"Uniport_ID": "P42345",
"Uniprot_name": "MTOR_HUMAN",
"EC_numbers": "2.7.11.1",
"gene_symbol": "MTOR",
"gene_synonyms": "FLJ44809, FRAP, FRAP1, FRAP2, RAFT1, RAPT1",
"gene_synonyms_links": "",
"gene_name": "Mechanistic target of rapamycin kinase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000198793",
"omim_id": "",
"genecard_link": "",
"locs": "Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side; Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side; Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side; Lysosome; Cytoplasm; Nucleus, PML body; Microsome membrane; Lysosome membrane",
"reaction": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]",
"targ_desciption": "Serine/threonine protein kinase which is a central regulatorof cellular metabolism, growth and survival in response to hormones,growth factors, nutrients, energy and stress signals (PubMed:12087098,PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876,PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625,PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875,PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703,PubMed:23429704, PubMed:25799227, PubMed:26018084). MTOR directly orindirectly regulates the phosphorylation of at least 800 proteins.Functions as part of 2 structurally and functionally distinct signalingcomplexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862,PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213,PubMed:21576368, PubMed:21659604, PubMed:23429704). Activated mTORC1up-regulates protein synthesis by phosphorylating key regulators ofmRNA translation and ribosome synthesis (PubMed:12087098,PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876,PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625,PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875,PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703,PubMed:23429704, PubMed:25799227, PubMed:26018084). This includesphosphorylation of EIF4EBP1 and release of its inhibition toward theelongation initiation factor 4E (eiF4E) (By similarity). Moreover,phosphorylates and activates RPS6KB1 and RPS6KB2 that promote proteinsynthesis by modulating the activity of their downstream targetsincluding ribosomal protein S6, eukaryotic translation initiationfactor EIF4B, and the inhibitor of translation initiation PDCD4(PubMed:12150925, PubMed:12087098, PubMed:18925875). This also includesmTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3:in the presence of nutrients, mediates phosphorylation of TFEB andTFE3, promoting their cytosolic retention and inactivation(PubMed:22576015, PubMed:22343943, PubMed:22692423). Upon starvation orlysosomal stress, inhibition of mTORC1 induces dephosphorylation andnuclear translocation of TFEB and TFE3, promoting their transcriptionfactor activity (PubMed:22576015, PubMed:22343943, PubMed:22692423).Stimulates the pyrimidine biosynthesis pathway, both by acuteregulation through RPS6KB1-mediated phosphorylation of the biosyntheticenzyme CAD, and delayed regulation, through transcriptional enhancementof the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step insynthesis, this function is dependent on the mTORC1 complex(PubMed:23429704, PubMed:23429703). Regulates ribosome synthesis byactivating RNA polymerase III-dependent transcription throughphosphorylation and inhibition of MAF1 an RNA polymerase III-repressor(PubMed:20516213). In parallel to protein synthesis, also regulateslipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity). Tomaintain energy homeostasis mTORC1 may also regulate mitochondrialbiogenesis through regulation of PPARGC1A (By similarity). mTORC1 alsonegatively regulates autophagy through phosphorylation of ULK1 (Bysimilarity). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation ofULK1 (By similarity). Also prevents autophagy through phosphorylationof the autophagy inhibitor DAP (PubMed:20537536). Also preventsautophagy by phosphorylating RUBCNL/Pacer under nutrient-richconditions (PubMed:30704899). mTORC1 exerts a feedback control onupstream growth factor signaling that includes phosphorylation andactivation of GRB10 a INSR-dependent signaling suppressor(PubMed:21659604). Among other potential targets mTORC1 mayphosphorylate CLIP1 and regulate microtubules (PubMed:12231510). Aspart of the mTORC2 complex MTOR may regulate other cellular processesincluding survival and organization of the cytoskeleton(PubMed:15268862, PubMed:15467718). Plays a critical role in thephosphorylation at 'Ser-473' of AKT1, a pro-survival effector ofphosphoinositide 3-kinase, facilitating its activation by PDK1(PubMed:15718470). mTORC2 may regulate the actin cytoskeleton, throughphosphorylation of PRKCA, PXN and activation of the Rho-type guaninenucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862).mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'(PubMed:18925875). Regulates osteoclastogenesis by adjusting theexpression of CEBPB isoforms (By similarity). Plays an importantregulatory role in the circadian clock function. regulates periodlength and rhythm amplitude of the suprachiasmatic nucleus (SCN) andliver clocks (By similarity). Phosphorylates SQSTM1, promotinginteraction between SQSTM1 and KEAP1 and subsequent inactivation of theBCR(KEAP1) complex (By similarity). {ECO:0000250|UniProtKB:P42346,ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098,ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876,ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862,ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625,ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18497260,ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875,ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536,ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:21659604,ECO:0000269|PubMed:22343943, ECO:0000269|PubMed:22576015,ECO:0000269|PubMed:22692423, ECO:0000269|PubMed:23429703,ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:25799227,ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:30704899}.",
"references": [
"RC03484",
"RC03724",
"RC03725",
"RC03755"
]
},
{
"targ_id": "T417",
"parent_targ_id": "T",
"full_name": "5'-AMP-activated protein kinase catalytic subunit alpha-2",
"abbrev": "AMPK subunit alpha-2",
"protein_names": "5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)",
"related_func_ids": "F0801; F0802",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "P54646",
"Uniprot_name": "AAPK2_HUMAN",
"EC_numbers": "2.7.11.1; 2.7.11.27; 2.7.11.31",
"gene_symbol": "PRKAA2 AMPK AMPK2",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus",
"reaction": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; [acetyl-CoA carboxylase]-L-serine + ATP = [acetyl-CoAcarboxylase]-O-phospho-L-serine + ADP + H(+); [3-hydroxy-3-methylglutaryl-coenzyme A reductase]-L-serine +ATP = [3-hydroxy-3-methylglutaryl-coenzyme A reductase]-O-phospho-L-serine + ADP + H(+)",
"targ_desciption": "Catalytic subunit of AMP-activated protein kinase (AMPK), anenergy sensor protein kinase that plays a key role in regulatingcellular energy metabolism. In response to reduction of intracellularATP levels, AMPK activates energy-producing pathways and inhibitsenergy-consuming processes: inhibits protein, carbohydrate and lipidbiosynthesis, as well as cell growth and proliferation. AMPK acts viadirect phosphorylation of metabolic enzymes, and by longer-term effectsvia phosphorylation of transcription regulators. Also acts as aregulator of cellular polarity by remodeling the actin cytoskeleton.probably by indirectly activating myosin. Regulates lipid synthesis byphosphorylating and inactivating lipid metabolic enzymes such as ACACA,ACACB, GYS1, HMGCR and LIPE. regulates fatty acid and cholesterolsynthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB)and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulatesinsulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 andPFKFB3. Involved in insulin receptor/INSR internalization(PubMed:25687571). AMPK stimulates glucose uptake in muscle byincreasing the translocation of the glucose transporter SLC2A4/GLUT4 tothe plasma membrane, possibly by mediating phosphorylation ofTBC1D4/AS160. Regulates transcription and chromatin structure byphosphorylating transcription regulators involved in energy metabolismsuch as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP,EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a keyregulator of glucose homeostasis in liver by phosphorylatingCRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. Inresponse to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph),leading to promote transcription. Acts as a key regulator of cellgrowth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1:in response to nutrient limitation, negatively regulates the mTORC1complex by phosphorylating RPTOR component of the mTORC1 complex and byphosphorylating and activating TSC2. In response to nutrientlimitation, promotes autophagy by phosphorylating and activatingATG1/ULK1. In that process also activates WDR45 (PubMed:28561066). AMPKalso acts as a regulator of circadian rhythm by mediatingphosphorylation of CRY1, leading to destabilize it. May regulate theWnt signaling pathway by phosphorylating CTNNB1, leading to stabilizeit. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays animportant role in the differential regulation of pro-autophagy(composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in responseto glucose starvation. Can inhibit the non-autophagy complex byphosphorylating PIK3C3 and can activate the pro-autophagy complex byphosphorylating BECN1 (By similarity). {ECO:0000250|UniProtKB:Q8BRK8,ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11554766,ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:14651849,ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17486097,ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18184930,ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076,ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:25687571,ECO:0000269|PubMed:28561066, ECO:0000269|PubMed:7959015}.",
"references": [
"RC03690",
"RC03782",
"RC04011"
]
},
{
"targ_id": "T418",
"parent_targ_id": "T",
"full_name": "Hypoxia-inducible factor 1-alpha",
"abbrev": "HIF-1-alpha",
"protein_names": "Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Basic-helix-loop-helix-PAS protein MOP1) (Class E basic helix-loop-helix protein 78) (bHLHe78) (Member of PAS protein 1) (PAS domain-containing protein 8)",
"related_func_ids": "F0803",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q16665",
"Uniprot_name": "HIF1A_HUMAN",
"EC_numbers": "",
"gene_symbol": "HIF1A BHLHE78 MOP1 PASD8",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus; Nucleus speckle",
"reaction": "",
"targ_desciption": "Functions as a master transcriptional regulator of theadaptive response to hypoxia. Under hypoxic conditions, activates thetranscription of over 40 genes, including erythropoietin, glucosetransporters, glycolytic enzymes, vascular endothelial growth factor,HILPDA, and other genes whose protein products increase oxygen deliveryor facilitate metabolic adaptation to hypoxia. Plays an essential rolein embryonic vascularization, tumor angiogenesis and pathophysiology ofischemic disease. Heterodimerizes with ARNT. heterodimer binds to coreDNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) oftarget gene promoters (By similarity). Activation requires recruitmentof transcriptional coactivators such as CREBBP and EP300. Activity isenhanced by interaction with both, NCOA1 or NCOA2. Interaction withredox regulatory protein APEX seems to activate CTAD and potentiatesactivation by NCOA1 and CREBBP. Involved in the axonal distribution andtransport of mitochondria in neurons during hypoxia.{ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:11292861,ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:15465032,ECO:0000269|PubMed:16543236, ECO:0000269|PubMed:16973622,ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:19528298,ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:22009797,ECO:0000269|PubMed:9887100}.",
"references": [
"RC01180"
]
},
{
"targ_id": "T419",
"parent_targ_id": "T",
"full_name": "Peroxisome proliferator-activated receptor gamma coactivator 1-alpha",
"abbrev": "PGC-1-alpha",
"protein_names": "Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1-alpha) (PPAR-gamma coactivator 1-alpha) (PPARGC-1-alpha) (Ligand effect modulator 6)",
"related_func_ids": "F0802; F0805",
"category": "enzyme",
"subcategories": "Activator",
"Uniport_ID": "Q9UBK2",
"Uniprot_name": "PRGC1_HUMAN",
"EC_numbers": "",
"gene_symbol": "PPARGC1A",
"gene_synonyms": "PGC-1alpha, PGC1, PGC1A, PPARGC1",
"gene_synonyms_links": "",
"gene_name": "PPARG coactivator 1 alpha",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000109819",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Nucleus; Nucleus, PML body; [Isoform B4]: Nucleus; [Isoform B4-8a]: Cytoplasm; Nucleus; [Isoform B5]: Nucleus; Nucleus, PML body; [Isoform 9]: Nucleus",
"reaction": "",
"targ_desciption": "Transcriptional coactivator for steroid receptors and nuclearreceptors. Greatly increases the transcriptional activity of PPARG andthyroid hormone receptor on the uncoupling protein promoter. Canregulate key mitochondrial genes that contribute to the program ofadaptive thermogenesis. Plays an essential role in metabolicreprogramming in response to dietary availability through coordinationof the expression of a wide array of genes involved in glucose andfatty acid metabolism. Induces the expression of PERM1 in the skeletalmuscle in an ESRRA-dependent manner. Also involved in the integrationof the circadian rhythms and energy metabolism. Required foroscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1,through the coactivation of RORA and RORC, and metabolic genes, such asPDK4 and PEPCK. {ECO:0000269|PubMed:10713165,ECO:0000269|PubMed:20005308, ECO:0000269|PubMed:21376232,ECO:0000269|PubMed:23836911}.",
"references": [
"RC03753",
"RC03974"
]
},
{
"targ_id": "T420",
"parent_targ_id": "T",
"full_name": "Peroxisome proliferator-activated receptor gamma coactivator 1-beta",
"abbrev": "PGC-1-beta",
"protein_names": "Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PGC-1-beta) (PPAR-gamma coactivator 1-beta) (PPARGC-1-beta) (PGC-1-related estrogen receptor alpha coactivator)",
"related_func_ids": "F060301",
"category": "enzyme",
"subcategories": "Activator",
"Uniport_ID": "Q86YN6",
"Uniprot_name": "PRGC2_HUMAN",
"EC_numbers": "",
"gene_symbol": "PPARGC1B",
"gene_synonyms": "PERC, PGC1B",
"gene_synonyms_links": "",
"gene_name": "PPARG coactivator 1 beta",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000155846",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus",
"reaction": "",
"targ_desciption": "Plays a role of stimulator of transcription factors andnuclear receptors activities. Activates transcriptional activity ofestrogen receptor alpha, nuclear respiratory factor 1 (NRF1) andglucocorticoid receptor in the presence of glucocorticoids. May play arole in constitutive non-adrenergic-mediated mitochondrial biogenesisas suggested by increased basal oxygen consumption and mitochondrialnumber when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energyexpenditure. Induces the expression of PERM1 in the skeletal muscle inan ESRRA-dependent manner. {ECO:0000269|PubMed:11854298,ECO:0000269|PubMed:12678921, ECO:0000269|PubMed:15546003,ECO:0000269|PubMed:23836911}.",
"references": []
},
{
"targ_id": "T421",
"parent_targ_id": "T",
"full_name": "Cyclic AMP-responsive element-binding protein 1",
"abbrev": "CREB-1",
"protein_names": "Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)",
"related_func_ids": "F0808; F0802",
"category": "enzyme",
"subcategories": "Activator",
"Uniport_ID": "P16220",
"Uniprot_name": "CREB1_HUMAN",
"EC_numbers": "",
"gene_symbol": "CREB1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "CAMP responsive element binding protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000118260",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus",
"reaction": "",
"targ_desciption": "Phosphorylation-dependent transcription factor thatstimulates transcription upon binding to the DNA cAMP response element(CRE), a sequence present in many viral and cellular promoters.Transcription activation is enhanced by the TORC coactivators which actindependently of Ser-133 phosphorylation. Involved in differentcellular processes including the synchronization of circadianrhythmicity and the differentiation of adipose cells.",
"references": []
},
{
"targ_id": "T422",
"parent_targ_id": "T",
"full_name": "NAD-dependent protein deacetylase sirtuin-1",
"abbrev": "hSIRT1",
"protein_names": "NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]",
"related_func_ids": "F0805; F0802",
"category": "enzyme",
"subcategories": "Developmental protein, Transferase",
"Uniport_ID": "Q96EB6",
"Uniprot_name": "SIR1_HUMAN",
"EC_numbers": "2.3.1.286; 2.3.1.-",
"gene_symbol": "SIRT1",
"gene_synonyms": "SIR2L1",
"gene_synonyms_links": "",
"gene_name": "Sirtuin 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000096717",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus, PML body; Cytoplasm; Nucleus; [SirtT1 75 kDa fragment]: Cytoplasm; Mitochondrion",
"reaction": "H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide",
"targ_desciption": "NAD-dependent protein deacetylase that links transcriptionalregulation directly to intracellular energetics and participates in thecoordination of several separated cellular functions such as cellcycle, response to DNA damage, metabolism, apoptosis and autophagy(PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222,PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825,PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051,PubMed:16998810, PubMed:17283066, PubMed:17290224, PubMed:17334224,PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707,PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677,PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166,PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304,PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729,PubMed:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201,PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047,PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893,PubMed:21947282, PubMed:22274616, PubMed:24415752, PubMed:24824780).Can modulate chromatin function through deacetylation of histones andcan promote alterations in the methylation of histones and DNA, leadingto transcriptional repression (PubMed:15469825). Deacetylates a broadrange of transcription factors and coregulators, thereby regulatingtarget gene expression positively and negatively (PubMed:15152190,PubMed:14980222, PubMed:14976264). Serves as a sensor of the cytosolicratio of NAD(+)/NADH which is altered by glucose deprivation andmetabolic changes associated with caloric restriction(PubMed:15205477). Is essential in skeletal muscle cell differentiationand in response to low nutrients mediates the inhibitory effect onskeletal myoblast differentiation which also involves 5'-AMP-activatedprotein kinase (AMPK) and nicotinamide phosphoribosyltransferase(NAMPT) (By similarity). Component of the eNoSC (energy-dependentnucleolar silencing) complex, a complex that mediates silencing of rDNAin response to intracellular energy status and acts by recruitinghistone-modifying enzymes (PubMed:18485871). The eNoSC complex is ableto sense the energy status of cell: upon glucose starvation, elevationof NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) bySUV39H1 and the formation of silent chromatin in the rDNA locus(PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1,leading to its activation (PubMed:21504832). Inhibits skeletal muscledifferentiation by deacetylating PCAF and MYOD1 (PubMed:19188449).Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). Deacetylates'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepressionfunction through chromatin remodeling: Recruited to LRH1 target genepromoters by NR0B2/SHP thereby stimulating histone H3 and H4deacetylation leading to transcriptional repression (PubMed:20375098).Proposed to contribute to genomic integrity via positive regulation oftelomere length. however, reports on localization to pericentromericheterochromatin are conflicting (By similarity). Proposed to play arole in constitutive heterochromatin (CH) formation and/or maintenancethrough regulation of the available pool of nuclear SUV39H1(PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stressdecreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitinationby MDM2 (PubMed:18004385, PubMed:21504832). This increase in SUV39H1levels enhances SUV39H1 turnover in CH, which in turn seems toaccelerate renewal of the heterochromatin which correlates with greatergenomic integrity during stress response (PubMed:18004385,PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs itsability to induce transcription-dependent proapoptotic program andmodulate cell senescence (PubMed:11672523, PubMed:12006491).Deacetylates TAF1B and thereby represses rDNA transcription by the RNApolymerase I (By similarity). Deacetylates MYC, promotes theassociation of MYC with MAX and decreases MYC stability leading tocompromised transformational capability (PubMed:19364925,PubMed:21807113). Deacetylates FOXO3 in response to oxidative stressthereby increasing its ability to induce cell cycle arrest andresistance to oxidative stress but inhibiting FOXO3-mediated inductionof apoptosis transcriptional activity. also leading to FOXO3ubiquitination and protesomal degradation (PubMed:14980222,PubMed:14976264, PubMed:21841822). Appears to have a similar effect onMLLT7/FOXO4 in regulation of transcriptional activity and apoptosis(PubMed:15126506). Deacetylates DNMT1. thereby impairs DNMT1methyltransferase-independent transcription repressor activity,modulates DNMT1 cell cycle regulatory function and DNMT1-mediated genesilencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 therebyinhibiting its transactivating potential and augments apoptosis inresponse to TNF-alpha (PubMed:15152190). Deacetylates HIF1A,KAT5/TIP60, RB1 and HIC1 (PubMed:17620057, PubMed:17283066,PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in itsnuclear retention and enhancement of its transcriptional activityleading to increased gluconeogenesis in liver (PubMed:15692560).Inhibits E2F1 transcriptional activity and apoptotic function, possiblyby deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediatedtranscriptional repression (PubMed:12535671). In cooperation with MYCNseems to be involved in transcriptional repression of DUSP6/MAPK3leading to MYCN stabilization by phosphorylation at 'Ser-62'(PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required forantagonist-mediated transcription suppression of AR-dependent geneswhich may be linked to local deacetylation of histone H3(PubMed:17505061). Represses HNF1A-mediated transcription (Bysimilarity). Required for the repression of ESRRG by CREBZF(PubMed:19690166). Deacetylates NR1H3 and NR1H2 and deacetylation ofNR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXRtarget genes, promotes NR1H3 proteosomal degradation and results incholesterol efflux. a promoter clearing mechanism after reach round oftranscription is proposed (PubMed:17936707). Involved in lipidmetabolism (PubMed:20817729). Implicated in regulation of adipogenesisand fat mobilization in white adipocytes by repression of PPARG whichprobably involves association with NCOR1 and SMRT/NCOR2 (Bysimilarity). Deacetylates p300/EP300 and PRMT1 (By similarity).Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation(PubMed:21701047). Involved in liver and muscle metabolism. Throughdeacetylation and activation of PPARGC1A is required to activate fattyacid oxidation in skeletal muscle under low-glucose conditions and isinvolved in glucose homeostasis. Involved in regulation of PPARA andfatty acid beta-oxidation in liver. Involved in positive regulation ofinsulin secretion in pancreatic beta cells in response to glucose. thefunction seems to imply transcriptional repression of UCP2. Proposed todeacetylate IRS2 thereby facilitating its insulin-induced tyrosinephosphorylation. Deacetylates SREBF1 isoform SREBP-1C therebydecreasing its stability and transactivation in lipogenic geneexpression (PubMed:17290224, PubMed:20817729). Involved in DNA damageresponse by repressing genes which are involved in DNA repair, such asXPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment ofadditional factors to sites of damaged DNA, such as SIRT1-deacetylatedNBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPAinteracts with RPA2 (PubMed:15205477, PubMed:17334224, PubMed:16998810,PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved inDNA repair of DNA double-strand breaks by homologous recombination andspecifically single-strand annealing independently of XRCC6/Ku70 andNBN (PubMed:15205477, PubMed:17334224, PubMed:20097625).Transcriptional suppression of XPC probably involves an E2F4:RBL2suppressor complex and protein kinase B (AKT) signaling.Transcriptional suppression of TP73 probably involves E2F4 and PCAF.Deacetylates WRN thereby regulating its helicase and exonucleaseactivities and regulates WRN nuclear translocation in response to DNAdamage (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' andstimulates cellular AP endonuclease activity by promoting theassociation of APEX1 to XRCC1 (PubMed:19934257). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nucleartranslocation of cytoplasmic p53/TP53 and probably redirecting it tomitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542'causing it to sequester BAX away from mitochondria thereby inhibitingstress-induced apoptosis. Is involved in autophagy, presumably bydeacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641).Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 toPIP3 and promotes their activation (PubMed:21775285). Proposed to playrole in regulation of STK11/LBK1-dependent AMPK signaling pathwaysimplicated in cellular senescence which seems to involve the regulationof the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 andthereby increase its activity, cytoplasmic localization and associationwith STRAD. however, the relevance of such activity in normal cells isunclear (PubMed:18687677, PubMed:20203304). In endothelial cells isshown to inhibit STK11/LBK1 activity and to promote its degradation.Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting itsdegradation. Deacetylates CIITA and augments its MHC class IItransactivation and contributes to its stability (PubMed:21890893).Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclearlocalization (PubMed:22274616). During the neurogenic transition,represses selective NOTCH1-target genes through histone deacetylationin a BCL6-dependent manner and leading to neuronal differentiation.Regulates the circadian expression of several core clock genes,including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role inmaintaining a controlled rhythmicity in histone acetylation, therebycontributing to circadian chromatin remodeling (PubMed:18662546).Deacetylates ARNTL/BMAL1 and histones at the circadian gene promotersin order to facilitate repression by inhibitory components of thecircadian oscillator (By similarity). Deacetylates PER2, facilitatingits ubiquitination and degradation by the proteosome (By similarity).Protects cardiomyocytes against palmitate-induced apoptosis (Bysimilarity). Deacetylates XBP1 isoform 2. deacetylation decreasesprotein stability of XBP1 isoform 2 and inhibits its transcriptionalactivity (PubMed:20955178). Deacetylates PCK1 and directs its activitytoward phosphoenolpyruvate production promoting gluconeogenesis(PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49'(PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required forleptin-induced activation of PI3K signaling (By similarity). Inaddition to protein deacetylase activity, also acts as protein-lysinedeacylase: acts as a protein depropionylase by mediatingdepropionylation of Osterix (SP7) (By similarity). Deacetylates SOX9.promoting SOX9 nuclear localization and transactivation activity (Bysimilarity). {ECO:0000250|UniProtKB:Q923E4,ECO:0000269|PubMed:11672523, ECO:0000269|PubMed:12006491,ECO:0000269|PubMed:12535671, ECO:0000269|PubMed:14976264,ECO:0000269|PubMed:14980222, ECO:0000269|PubMed:15126506,ECO:0000269|PubMed:15152190, ECO:0000269|PubMed:15205477,ECO:0000269|PubMed:15469825, ECO:0000269|PubMed:15692560,ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16166628,ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:16998810,ECO:0000269|PubMed:17283066, ECO:0000269|PubMed:17290224,ECO:0000269|PubMed:17334224, ECO:0000269|PubMed:17505061,ECO:0000269|PubMed:17612497, ECO:0000269|PubMed:17620057,ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18203716,ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18485871,ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18687677,ECO:0000269|PubMed:19188449, ECO:0000269|PubMed:19220062,ECO:0000269|PubMed:19364925, ECO:0000269|PubMed:19690166,ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20097625,ECO:0000269|PubMed:20100829, ECO:0000269|PubMed:20203304,ECO:0000269|PubMed:20375098, ECO:0000269|PubMed:20620956,ECO:0000269|PubMed:20670893, ECO:0000269|PubMed:20817729,ECO:0000269|PubMed:20955178, ECO:0000269|PubMed:21149730,ECO:0000269|PubMed:21245319, ECO:0000269|PubMed:21471201,ECO:0000269|PubMed:21504832, ECO:0000269|PubMed:21555002,ECO:0000269|PubMed:21698133, ECO:0000269|PubMed:21701047,ECO:0000269|PubMed:21775285, ECO:0000269|PubMed:21807113,ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21890893,ECO:0000269|PubMed:21947282, ECO:0000269|PubMed:22274616,ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780,ECO:0000269|PubMed:30193097}.; [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however withlower activity than isoform 1. In combination, the two isoforms exertan additive effect. Isoform 2 regulates p53/TP53 expression andcellular stress response and is in turn repressed by p53/TP53presenting a SIRT1 isoform-dependent auto-regulatory loop.{ECO:0000269|PubMed:20975832}.; (Microbial infection) In case of HIV-1 infection, interactswith and deacetylates the viral Tat protein. The viral Tat proteininhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65,thereby potentiates its transcriptional activity and SIRT1 is proposedto contribute to T-cell hyperactivation during infection.{ECO:0000269|PubMed:18329615}.; [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 maybe involved in regulation of apoptosis. May be involved in protectingchondrocytes from apoptotic death by associating with cytochrome C andinterfering with apoptosome assembly. {ECO:0000269|PubMed:21987377}.",
"references": [
"RC03758"
]
},
{
"targ_id": "T423",
"parent_targ_id": "T",
"full_name": "NAD-dependent protein deacetylase sirtuin-3, mitochondrial",
"abbrev": "hSIRT3",
"protein_names": "NAD-dependent protein deacetylase sirtuin-3, mitochondrial (hSIRT3) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 3) (SIR2-like protein 3)",
"related_func_ids": "F0805; F030802",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q9NTG7",
"Uniprot_name": "SIR3_HUMAN",
"EC_numbers": "2.3.1.286",
"gene_symbol": "SIRT3",
"gene_synonyms": "SIR2L3",
"gene_synonyms_links": "",
"gene_name": "Sirtuin 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000142082",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide",
"targ_desciption": "NAD-dependent protein deacetylase (PubMed:12186850,PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531,PubMed:23283301, PubMed:24121500, PubMed:24252090, PubMed:19535340).Activates or deactivates mitochondrial target proteins by deacetylatingkey lysine residues (PubMed:12186850, PubMed:12374852, PubMed:16788062,PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500,PubMed:24252090). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1,LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed:16788062,PubMed:18680753, PubMed:24121500, PubMed:24252090, PubMed:19535340).Contributes to the regulation of the cellular energy metabolism(PubMed:24252090). Important for regulating tissue-specific ATP levels(PubMed:18794531). In response to metabolic stress, deacetylatestranscription factor FOXO3 and recruits FOXO3 and mitochondrial RNApolymerase POLRMT to mtDNA to promote mtDNA transcription(PubMed:23283301). Acts as a regulator of ceramide metabolism bymediating deacetylation of ceramide synthases CERS1, CERS2 and CERS6,thereby increasing their activity and promoting mitochondrial ceramideaccumulation (By similarity). {ECO:0000250|UniProtKB:Q8R104,ECO:0000269|PubMed:12186850, ECO:0000269|PubMed:12374852,ECO:0000269|PubMed:16788062, ECO:0000269|PubMed:18680753,ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:19535340,ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:24121500,ECO:0000269|PubMed:24252090}.",
"references": []
},
{
"targ_id": "T424",
"parent_targ_id": "T",
"full_name": "NAD-dependent protein lipoamidase sirtuin-4, mitochondrial",
"abbrev": "SIRT4",
"protein_names": "NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 2.3.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4)",
"related_func_ids": "F030802; F02060101",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q9Y6E7",
"Uniprot_name": "SIR4_HUMAN",
"EC_numbers": "2.3.1.-; 2.4.2.-; 2.3.1.286",
"gene_symbol": "SIRT4",
"gene_synonyms": "SIR2L4",
"gene_synonyms_links": "",
"gene_name": "Sirtuin 4",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000089163",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-D-ribosyl)-L-cysteinyl-[protein]; H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide",
"targ_desciption": "Acts as NAD-dependent protein lipoamidase, ADP-ribosyltransferase and deacetylase. Catalyzes more efficiently removal oflipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits thepyruvate dehydrogenase complex (PDH) activity via the enzymatichydrolysis of the lipoamide cofactor from the E2 component, DLAT, in aphosphorylation-independent manner (PubMed:25525879). Catalyzes thetransfer of ADP-ribosyl groups onto target proteins, includingmitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as anegative regulator of mitochondrial glutamine metabolism by mediatingmono ADP-ribosylation of GLUD1: expressed in response to DNA damage andnegatively regulates anaplerosis by inhibiting GLUD1, leading to blockmetabolism of glutamine into tricarboxylic acid cycle and promotingcell cycle arrest (PubMed:16959573, PubMed:17715127). In response tomTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis andcell proliferation. Acts as a tumor suppressor (PubMed:23562301,PubMed:23663782). Also acts as a NAD-dependent protein deacetylase:mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity,thereby acting as a regulator of lipid homeostasis (By similarity).Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acidoxidation by inhibiting PPARA transcriptional activation. ImpairsSIRT1:PPARA interaction probably through the regulation of NAD(+)levels (PubMed:24043310). Down-regulates insulin secretion.{ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573,ECO:0000269|PubMed:17715127, ECO:0000269|PubMed:23438705,ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23663782,ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:25525879}.",
"references": []
},
{
"targ_id": "T425",
"parent_targ_id": "T",
"full_name": "NAD-dependent protein deacylase sirtuin-5, mitochondrial",
"abbrev": "SIRT5",
"protein_names": "NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5)",
"related_func_ids": "F0504; F02060201",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q9NXA8",
"Uniprot_name": "SIR5_HUMAN",
"EC_numbers": "2.3.1.-",
"gene_symbol": "SIRT5",
"gene_synonyms": "SIR2L5",
"gene_synonyms_links": "",
"gene_name": "Sirtuin 5",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000124523",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Mitochondrion intermembrane space; Cytoplasm, cytosol; Nucleus; [Isoform 1]: Cytoplasm; Mitochondrion; [Isoform 2]: Mitochondrion",
"reaction": "H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide",
"targ_desciption": "NAD-dependent lysine demalonylase, desuccinylase anddeglutarylase that specifically removes malonyl, succinyl and glutarylgroups on target proteins (PubMed:21908771, PubMed:22076378,PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes tothe regulation of blood ammonia levels during prolonged fasting: actsby mediating desuccinylation and deglutarylation of CPS1, therebyincreasing CPS1 activity in response to elevated NAD levels duringfasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediatingits desuccinylation, leading to reduced reactive oxygen species(PubMed:24140062). Activates SHMT2 by mediating its desuccinylation(PubMed:29180469). Modulates ketogenesis through the desuccinylationand activation of HMGCS2 (By similarity). Has weak NAD-dependentprotein deacetylase activity. however this activity may not bephysiologically relevant in vivo. Can deacetylate cytochrome c (CYCS)and a number of other proteins in vitro such as UOX.{ECO:0000250|UniProtKB:Q8K2C6, ECO:0000269|PubMed:18680753,ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378,ECO:0000269|PubMed:24140062, ECO:0000269|PubMed:24703693,ECO:0000269|PubMed:29180469}.",
"references": []
},
{
"targ_id": "T426",
"parent_targ_id": "T",
"full_name": "Mitogen-activated protein kinase 14",
"abbrev": "MAPK14",
"protein_names": "Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)",
"related_func_ids": "F0804; F070103",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q16539",
"Uniprot_name": "MK14_HUMAN",
"EC_numbers": "2.7.11.24",
"gene_symbol": "MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus",
"reaction": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]",
"targ_desciption": "Serine/threonine kinase which acts as an essential componentof the MAP kinase signal transduction pathway. MAPK14 is one of thefour p38 MAPKs which play an important role in the cascades of cellularresponses evoked by extracellular stimuli such as proinflammatorycytokines or physical stress leading to direct activation oftranscription factors. Accordingly, p38 MAPKs phosphorylate a broadrange of proteins and it has been estimated that they may haveapproximately 200 to 300 substrates each. Some of the targets aredownstream kinases which are activated through phosphorylation andfurther phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2can directly phosphorylate and activate transcription factors such asCREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, butcan also phosphorylate histone H3 and the nucleosomal protein HMGN1.RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapidinduction of immediate-early genes in response to stress or mitogenicstimuli, either by inducing chromatin remodeling or by recruiting thetranscription machinery. On the other hand, two other kinase targets,MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of geneexpression mostly at the post-transcriptional level, by phosphorylatingZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which isimportant for the elongation of mRNA during translation. MKNK1/MNK1 andMKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate proteinsynthesis by phosphorylating the initiation factor EIF4E2. MAPK14interacts also with casein kinase II, leading to its activation throughautophosphorylation and further phosphorylation of TP53/p53. In thecytoplasm, the p38 MAPK pathway is an important regulator of proteinturnover. For example, CFLAR is an inhibitor of TNF-induced apoptosiswhose proteasome-mediated degradation is regulated by p38 MAPKphosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitinligase SIAH2, regulating its activity towards EGLN3. MAPK14 may alsoinhibit the lysosomal degradation pathway of autophagy by interferingwith the intracellular trafficking of the transmembrane protein ATG9.Another function of MAPK14 is to regulate the endocytosis of membranereceptors by different mechanisms that impinge on the small GTPaseRAB5A. In addition, clathrin-mediated EGFR internalization induced byinflammatory cytokines and UV irradiation depends on MAPK14-mediatedphosphorylation of EGFR itself as well as of RAB5A effectors.Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKsas well. In response to inflammatory stimuli, p38 MAPKs phosphorylatethe membrane-associated metalloprotease ADAM17. Such phosphorylation isrequired for ADAM17-mediated ectodomain shedding of TGF-alpha familyligands, which results in the activation of EGFR signaling and cellproliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can betranslocated from the extracellular space into the cytosol and nucleusof target cells, and regulates processes such as rRNA synthesis andcell growth. FGFR1 translocation requires p38 MAPK activation. In thenucleus, many transcription factors are phosphorylated and activated byp38 MAPKs in response to different stimuli. Classical examples includeATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. Thep38 MAPKs are emerging as important modulators of gene expression byregulating chromatin modifiers and remodelers. The promoters of severalgenes involved in the inflammatory response, such as IL6, IL8 andIL12B, display a p38 MAPK-dependent enrichment of histone H3phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells.This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-Brecruitment. Phosphorylates CDC25B and CDC25C which is required forbinding to 14-3-3 proteins and leads to initiation of a G2 delay afterultraviolet radiation. Phosphorylates TIAR following DNA damage,releasing TIAR from GADD45A mRNA and preventing mRNA degradation. Thep38 MAPKs may also have kinase-independent roles, which are thought tobe due to the binding to targets in the absence of phosphorylation.Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14,and, although OGT does not seem to be phosphorylated by MAPK14, theirinteraction increases upon MAPK14 activation induced by glucosedeprivation. This interaction may regulate OGT activity by recruitingit to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth ofembryo-derived blood vessels in the labyrinth layer of the placenta.Also plays an essential role in developmental and stress-inducederythropoiesis, through regulation of EPO gene expression. Isoform MXI2activation is stimulated by mitogens and oxidative stress and onlypoorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role inthe early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'.{ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10747897,ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11154262,ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15905572,ECO:0000269|PubMed:16932740, ECO:0000269|PubMed:17003045,ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:19893488,ECO:0000269|PubMed:20188673, ECO:0000269|PubMed:20932473,ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510,ECO:0000269|PubMed:9792677, ECO:0000269|PubMed:9858528}.; (Microbial infection) Activated by phosphorylation byM.tuberculosis EsxA in T-cells leading to inhibition of IFN-gammaproduction. phosphorylation is apparent within 15 minute and isinhibited by kinase-specific inhibitors SB203580 and siRNA(PubMed:21586573). {ECO:0000269|PubMed:21586573}.",
"references": []
},
{
"targ_id": "T427",
"parent_targ_id": "T",
"full_name": "A-kinase anchor protein 1, mitochondrial",
"abbrev": "AKAP 149",
"protein_names": "A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 149 kDa) (AKAP 149) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84)",
"related_func_ids": "F02110301",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q92667",
"Uniprot_name": "AKAP1_HUMAN",
"EC_numbers": "",
"gene_symbol": "AKAP1",
"gene_synonyms": "AKAP121, AKAP149, AKAP84, D-AKAP1, PPP1R43, PRKA1, S-AKAP84, SAKAP84, TDRD17",
"gene_synonyms_links": "",
"gene_name": "A-kinase anchoring protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000121057",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion outer membrane",
"reaction": "",
"targ_desciption": "Binds to type I and II regulatory subunits of protein kinaseA and anchors them to the cytoplasmic face of the mitochondrial outermembrane. Involved in mitochondrial-mediated antiviral innate immunity(PubMed:31522117). {ECO:0000269|PubMed:31522117}.",
"references": []
},
{
"targ_id": "T428",
"parent_targ_id": "T",
"full_name": "Anoctamin-10",
"abbrev": "Transmembrane protein 16K",
"protein_names": "Anoctamin-10 (Transmembrane protein 16K)",
"related_func_ids": "F021103",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9NW15",
"Uniprot_name": "ANO10_HUMAN",
"EC_numbers": "",
"gene_symbol": "ANO10 TMEM16K",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cell membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "Does not exhibit calcium-activated chloride channel (CaCC)activity. Can inhibit the activity of ANO1.{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.",
"references": []
},
{
"targ_id": "T429",
"parent_targ_id": "T",
"full_name": "MICOS complex subunit MIC13",
"abbrev": "Protein P117",
"protein_names": "MICOS complex subunit MIC13 (Protein P117)",
"related_func_ids": "F02110301; F0309",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q5XKP0",
"Uniprot_name": "MIC13_HUMAN",
"EC_numbers": "",
"gene_symbol": "C19orf70",
"gene_synonyms": "MIC13, P117, QIL1",
"gene_synonyms_links": "",
"gene_name": "Chromosome 19 open reading frame 70",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000174917",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein",
"reaction": "",
"targ_desciption": "Component of the MICOS complex, a large protein complex ofthe mitochondrial inner membrane that plays crucial roles in themaintenance of crista junctions, inner membrane architecture, andformation of contact sites to the outer membrane. Constituent of matureMICOS complex, it is required for the formation of cristae junction(CJ) and maintenance of cristae morphology. Required for theincorporation of MICOS10/MIC10 into the MICOS complex.{ECO:0000269|PubMed:25997101, ECO:0000269|PubMed:27623147}.",
"references": []
},
{
"targ_id": "T430",
"parent_targ_id": "T",
"full_name": "CDGSH iron-sulfur domain-containing protein 2",
"abbrev": "NAF-1",
"protein_names": "CDGSH iron-sulfur domain-containing protein 2 (Endoplasmic reticulum intermembrane small protein) (MitoNEET-related 1 protein) (Miner1) (Nutrient-deprivation autophagy factor-1) (NAF-1)",
"related_func_ids": "F030801",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q8N5K1",
"Uniprot_name": "CISD2_HUMAN",
"EC_numbers": "",
"gene_symbol": "CISD2",
"gene_synonyms": "ERIS, Miner1, NAF-1, WFS2, ZCD2",
"gene_synonyms_links": "",
"gene_name": "CDGSH iron sulfur domain 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000145354",
"omim_id": "",
"genecard_link": "",
"locs": "Endoplasmic reticulum membrane; Single-pass membrane protein; Mitochondrion outer membrane; Single-pass membrane protein",
"reaction": "",
"targ_desciption": "Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participatesin the interaction of BCL2 with BECN1 and is required for BCL2-mediateddepression of endoplasmic reticulum Ca(2+) stores during autophagy.Contributes to BIK-initiated autophagy, while it is not involved inBIK-dependent activation of caspases. Involved in life span control,probably via its function as regulator of autophagy.{ECO:0000269|PubMed:17846994, ECO:0000269|PubMed:20010695}.",
"references": []
},
{
"targ_id": "T431",
"parent_targ_id": "T",
"full_name": "1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial",
"abbrev": "Cytochrome P450 24A1",
"protein_names": "1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1.14.15.16) (Cytochrome P450 24A1) (Cytochrome P450-CC24)",
"related_func_ids": "F02110301",
"category": "enzyme",
"subcategories": "Monooxygenase, Oxidoreductase",
"Uniport_ID": "Q07973",
"Uniprot_name": "CP24A_HUMAN",
"EC_numbers": "1.14.15.16",
"gene_symbol": "CYP24A1",
"gene_synonyms": "CP24, CYP24, P450-CC24",
"gene_synonyms_links": "",
"gene_name": "Cytochrome P450 family 24 subfamily A member 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000019186",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =calcitetrol + H2O + 2 oxidized [adrenodoxin]; calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin]; (1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced[adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2oxidized [adrenodoxin]; (1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2+ 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin]; (1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2+ 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized[adrenodoxin]; calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =1alpha,23S,25-trihydroxycholecalciferol + H2O + 2 oxidized[adrenodoxin]; calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2oxidized [adrenodoxin] + secalciferol; 2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = 25-hydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin]; 25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced[adrenodoxin] = 23S,25-dihydroxy-24-oxocholecalciferol + H2O + 2oxidized [adrenodoxin]; calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (23S)-23,25-dihydroxycalciol + H2O + 2 oxidized [adrenodoxin]; 20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced[adrenodoxin] = 20S,25-dihydroxycholecalciferol + H2O + 2 oxidized[adrenodoxin]; 20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced[adrenodoxin] = 20S,24R-dihydroxycholecalciferol + H2O + 2 oxidized[adrenodoxin]; 20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced[adrenodoxin] = 20S,23,25-trihydroxycholecalciferol + H2O + 2oxidized [adrenodoxin]",
"targ_desciption": "A cytochrome P450 monooxygenase with a key role in vitamin Dcatabolism and calcium homeostasis. Via C24- and C23-oxidationpathways, catalyzes the inactivation of both the vitamin D precursorcalcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol(1-alpha,25-dihydroxyvitamin D(3)) (PubMed:24893882, PubMed:15574355,PubMed:8679605, PubMed:11012668, PubMed:16617161). With initialhydroxylation at C-24 (via C24-oxidation pathway), performs asequential 6-step oxidation of calcitriol leading to the formation ofthe biliary metabolite calcitroic acid (PubMed:24893882,PubMed:15574355). With initial hydroxylation at C-23 (via C23-oxidationpathway), catalyzes sequential oxidation of calcidiol leading to theformation of 25(OH)D3-26,23-lactone as end product (PubMed:11012668,PubMed:8679605). Preferentially hydroxylates at C-25 other vitamin Dactive metabolites, such as CYP11A1-derived secosteroids 20S-hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol(PubMed:25727742). Mechanistically, uses molecular oxygen inserting oneoxygen atom into a substrate, and reducing the second into a watermolecule, with two electrons provided by NADPH via FDXR/adrenodoxinreductase and FDX1/adrenodoxin (PubMed:8679605).{ECO:0000269|PubMed:11012668, ECO:0000269|PubMed:15574355,ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:24893882,ECO:0000269|PubMed:25727742, ECO:0000269|PubMed:8679605}.",
"references": []
},
{
"targ_id": "T432",
"parent_targ_id": "T",
"full_name": "Calcium uptake protein 1, mitochondrial",
"abbrev": "ara CALC",
"protein_names": "Calcium uptake protein 1, mitochondrial (Atopy-related autoantigen CALC) (ara CALC) (Calcium-binding atopy-related autoantigen 1) (allergen Hom s 4)",
"related_func_ids": "F02110301",
"category": "protein",
"subcategories": "Transporter",
"Uniport_ID": "Q9BPX6",
"Uniprot_name": "MICU1_HUMAN",
"EC_numbers": "",
"gene_symbol": "MICU1",
"gene_synonyms": "CALC, CBARA1, EFHA3, FLJ12684",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial calcium uptake 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000107745",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein; Mitochondrion intermembrane space",
"reaction": "",
"targ_desciption": "Key regulator of mitochondrial calcium uniporter (MCU) thatsenses calcium level via its EF-hand domains (PubMed:20693986,PubMed:23101630, PubMed:23747253, PubMed:24313810, PubMed:24332854,PubMed:24503055, PubMed:24560927, PubMed:26341627, PubMed:26903221,PubMed:27099988). MICU1 and MICU2 form a disulfide-linked heterodimerthat stimulates and inhibits MCU activity, depending on theconcentration of calcium. MICU1 acts both as an activator or inhibitorof mitochondrial calcium uptake (PubMed:26903221). Acts as a gatekeeperof MCU at low concentration of calcium, preventing channel opening(PubMed:26903221). Enhances MCU opening at high calcium concentration,allowing a rapid response of mitochondria to calcium signals generatedin the cytoplasm (PubMed:24560927, PubMed:26903221). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulatingmitochondrial calcium uptake (PubMed:22904319). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG(PubMed:16002733). {ECO:0000269|PubMed:16002733,ECO:0000269|PubMed:20693986, ECO:0000269|PubMed:22904319,ECO:0000269|PubMed:23101630, ECO:0000269|PubMed:23747253,ECO:0000269|PubMed:24313810, ECO:0000269|PubMed:24332854,ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927,ECO:0000269|PubMed:26341627, ECO:0000269|PubMed:26903221,ECO:0000269|PubMed:27099988}.",
"references": [
"RC03941",
"RC03942",
"RC03947",
"RC03948"
]
},
{
"targ_id": "T433",
"parent_targ_id": "T",
"full_name": "Calcium uptake protein 2, mitochondrial",
"abbrev": "EF-hand domain-containing family member A1",
"protein_names": "Calcium uptake protein 2, mitochondrial (EF-hand domain-containing family member A1)",
"related_func_ids": "F02110301",
"category": "protein",
"subcategories": "Transporter",
"Uniport_ID": "Q8IYU8",
"Uniprot_name": "MICU2_HUMAN",
"EC_numbers": "",
"gene_symbol": "MICU2",
"gene_synonyms": "EFHA1",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial calcium uptake 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000165487",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space",
"reaction": "",
"targ_desciption": "Key regulator of mitochondrial calcium uniporter (MCU)required to limit calcium uptake by MCU when cytoplasmic calcium is low(PubMed:24503055, PubMed:24560927, PubMed:26903221). MICU1 and MICU2form a disulfide-linked heterodimer that stimulate and inhibit MCUactivity, depending on the concentration of calcium (PubMed:24560927).MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting calcium, avoidingenergy dissipation and cell-death triggering (PubMed:24560927).{ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927,ECO:0000269|PubMed:26387864, ECO:0000269|PubMed:26903221}.",
"references": []
},
{
"targ_id": "T434",
"parent_targ_id": "T",
"full_name": "Wolframin",
"abbrev": "",
"protein_names": "Wolframin",
"related_func_ids": "F02110301",
"category": "protein",
"subcategories": "",
"Uniport_ID": "O76024",
"Uniprot_name": "WFS1_HUMAN",
"EC_numbers": "",
"gene_symbol": "WFS1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Endoplasmic reticulum membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "Participates in the regulation of cellular Ca(2+)homeostasis, at least partly, by modulating the filling state of theendoplasmic reticulum Ca(2+) store. {ECO:0000269|PubMed:16989814}.",
"references": []
},
{
"targ_id": "T435",
"parent_targ_id": "T",
"full_name": "Arginase-2, mitochondrial",
"abbrev": "Arginase II",
"protein_names": "Arginase-2, mitochondrial (EC 3.5.3.1) (Arginase II) (Kidney-type arginase) (Non-hepatic arginase) (Type II arginase)",
"related_func_ids": "F0223",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "P78540",
"Uniprot_name": "ARGI2_HUMAN",
"EC_numbers": "3.5.3.1",
"gene_symbol": "ARG2",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Arginase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000081181",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "H2O + L-arginine = L-ornithine + urea",
"targ_desciption": "May play a role in the regulation of extra-urea cyclearginine metabolism and also in down-regulation of nitric oxidesynthesis. Extrahepatic arginase functions to regulate L-argininebioavailability to nitric oxid synthase (NOS). Arginine metabolism is acritical regulator of innate and adaptive immune responses. Seems to beinvolved in negative regulation of the survival capacity of activatedCD4(+) and CD8(+) T cells (PubMed:27745970). May suppress inflammation-related signaling in asthmatic airway epithelium (PubMed:27214549). Maycontribute to the immune evasion of H.pylori by restricting M1macrophage activation and polyamine metabolism (By similarity). Infetal dendritic cells may play a role in promoting immune suppressionand T cell TNF-alpha production during gestation (PubMed:28614294).Regulates RPS6KB1 signaling, which promotes endothelial cell senescenceand inflammation and implicates NOS3/eNOS dysfunction(PubMed:22928666). Can inhibit endothelial autophagy independently ofits enzymatic activity implicating mTORC2 signaling (PubMed:25484082).Involved in vascular smooth muscle cell senescence and apoptosisindependently of its enzymatic activity (PubMed:23832324). Since NOS isfound in the penile corpus cavernosum smooth muscle, the clitoralcorpus cavernosum and the vagina, arginase-2 plays a role in both maleand female sexual arousal (PubMed:12859189).{ECO:0000250|UniProtKB:O08691, ECO:0000269|PubMed:12859189,ECO:0000269|PubMed:22928666, ECO:0000269|PubMed:23832324,ECO:0000269|PubMed:25484082, ECO:0000269|PubMed:27214549,ECO:0000269|PubMed:27745970}.",
"references": []
},
{
"targ_id": "T436",
"parent_targ_id": "T",
"full_name": "N-acetylglutamate synthase, mitochondrial",
"abbrev": "Amino-acid acetyltransferase",
"protein_names": "N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) (Amino-acid acetyltransferase) [Cleaved into: N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase conserved domain form]",
"related_func_ids": "F0223",
"category": "enzyme",
"subcategories": "Acyltransferase, Transferase",
"Uniport_ID": "Q8N159",
"Uniprot_name": "NAGS_HUMAN",
"EC_numbers": "2.3.1.1",
"gene_symbol": "NAGS",
"gene_synonyms": "AGAS, ARGA, NAT7",
"gene_synonyms_links": "",
"gene_name": "N-acetylglutamate synthase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000161653",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate",
"targ_desciption": "Plays a role in the regulation of ureagenesis by producingthe essential cofactor N-acetylglutamate (NAG), thus modulatingcarbamoylphosphate synthase I (CPS1) activity.{ECO:0000269|PubMed:12459178, ECO:0000269|PubMed:23894642,ECO:0000269|PubMed:7126172}.",
"references": []
},
{
"targ_id": "T437",
"parent_targ_id": "T",
"full_name": "Carbamoyl-phosphate synthase [ammonia], mitochondrial",
"abbrev": "CPSase I",
"protein_names": "Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I)",
"related_func_ids": "F0223",
"category": "enzyme",
"subcategories": "Allosteric enzyme, Ligase",
"Uniport_ID": "P31327",
"Uniprot_name": "CPSM_HUMAN",
"EC_numbers": "6.3.4.16",
"gene_symbol": "CPS1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Carbamoyl-phosphate synthase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000021826",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Nucleus, nucleolus",
"reaction": "2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoylphosphate + 2 H(+) + phosphate",
"targ_desciption": "Involved in the urea cycle of ureotelic animals where theenzyme plays an important role in removing excess ammonia from thecell.",
"references": []
}
]
}
