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{
"count": 876,
"next": "https://mitotox.org/api/targets/list?format=api&page=6",
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"results": [
{
"targ_id": "T220",
"parent_targ_id": "T",
"full_name": "Mitochondrial uncoupling protein",
"abbrev": "UCP",
"protein_names": "",
"related_func_ids": "F021103",
"category": "enzyme family",
"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": []
},
{
"targ_id": "T221",
"parent_targ_id": "T",
"full_name": "Mitochondrial brown fat uncoupling protein 1",
"abbrev": "UCP 1",
"protein_names": "Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin)",
"related_func_ids": "F021103",
"category": "protein",
"subcategories": "Ion channel",
"Uniport_ID": "P25874",
"Uniprot_name": "UCP1_HUMAN",
"EC_numbers": "",
"gene_symbol": "UCP1",
"gene_synonyms": "SLC25A7, UCP",
"gene_synonyms_links": "",
"gene_name": "Uncoupling protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000109424",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "Mitochondrial protein responsible for thermogenicrespiration, a specialized capacity of brown adipose tissue and beigefat that participates in non-shivering adaptive thermogenesis totemperature and diet variations and more generally to the regulation ofenergy balance (By similarity). Functions as a long-chain fattyacid/LCFA and proton symporter, simultaneously transporting one LCFAand one proton through the inner mitochondrial membrane(PubMed:24196960). However, LCFAs remaining associated with thetransporter via their hydrophobic tails, it results in an apparenttransport of protons activated by LCFAs. Thereby, dissipates themitochondrial proton gradient and converts the energy of substrateoxydation into heat instead of ATP. Regulates the production ofreactive oxygen species/ROS by mitochondria (By similarity).{ECO:0000250|UniProtKB:P12242, ECO:0000269|PubMed:24196960}.",
"references": [
"RC03498",
"RC03499"
]
},
{
"targ_id": "T222",
"parent_targ_id": "T",
"full_name": "Mitochondrial uncoupling protein 2",
"abbrev": "UCP 2",
"protein_names": "Mitochondrial uncoupling protein 2 (UCP 2) (Solute carrier family 25 member 8) (UCPH)",
"related_func_ids": "F021103",
"category": "enzyme",
"subcategories": "transporter",
"Uniport_ID": "P55851",
"Uniprot_name": "UCP2_HUMAN",
"EC_numbers": "",
"gene_symbol": "UCP2",
"gene_synonyms": "BMIQ4, SLC25A8",
"gene_synonyms_links": "",
"gene_name": "Uncoupling protein 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000175567",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "UCP are mitochondrial transporter proteins that create protonleaks across the inner mitochondrial membrane, thus uncouplingoxidative phosphorylation from ATP synthesis. As a result, energy isdissipated in the form of heat.",
"references": []
},
{
"targ_id": "T223",
"parent_targ_id": "T",
"full_name": "Mitochondrial uncoupling protein 3",
"abbrev": "UCP 3",
"protein_names": "Mitochondrial uncoupling protein 3 (UCP 3) (Solute carrier family 25 member 9)",
"related_func_ids": "F021103",
"category": "enzyme",
"subcategories": "transporter",
"Uniport_ID": "P55916",
"Uniprot_name": "UCP3_HUMAN",
"EC_numbers": "",
"gene_symbol": "UCP3",
"gene_synonyms": "SLC25A9",
"gene_synonyms_links": "",
"gene_name": "Uncoupling protein 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000175564",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "UCP are mitochondrial transporter proteins that create protonleaks across the inner mitochondrial membrane, thus uncouplingoxidative phosphorylation. As a result, energy is dissipated in theform of heat. May play a role in the modulation of tissue respiratorycontrol. Participates in thermogenesis and energy balance.",
"references": []
},
{
"targ_id": "T224",
"parent_targ_id": "T",
"full_name": "Mitochondrial uncoupling protein 4",
"abbrev": "UCP 4",
"protein_names": "Mitochondrial uncoupling protein 4 (UCP 4) (Solute carrier family 25 member 27)",
"related_func_ids": "F021103",
"category": "enzyme",
"subcategories": "transporter",
"Uniport_ID": "O95847",
"Uniprot_name": "UCP4_HUMAN",
"EC_numbers": "",
"gene_symbol": "SLC25A27",
"gene_synonyms": "FLJ33552, UCP4",
"gene_synonyms_links": "",
"gene_name": "Solute carrier family 25 member 27",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000153291",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "UCP are mitochondrial transporter proteins that create protonleaks across the inner mitochondrial membrane, thus uncouplingoxidative phosphorylation from ATP synthesis. As a result, energy isdissipated in the form of heat. May play a role in thermoregulatoryheat production and metabolism in brain.",
"references": []
},
{
"targ_id": "T225",
"parent_targ_id": "T",
"full_name": "Adenylate cyclase type 10",
"abbrev": "hsAC",
"protein_names": "Adenylate cyclase type 10 (EC 4.6.1.1) (AH-related protein) (Adenylate cyclase homolog) (Germ cell soluble adenylyl cyclase) (hsAC) (sAC) (Testicular soluble adenylyl cyclase)",
"related_func_ids": "F021103",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q96PN6",
"Uniprot_name": "ADCYA_HUMAN",
"EC_numbers": "4.6.1.1",
"gene_symbol": "ADCY10 SAC",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cell membrane; Peripheral membrane protein; Cytoplasmicside; Cytoplasm, cytoskeleton; Cytoplasm,perinuclear region; Nucleus; Cell projection, cilium; Cytoplasm; Mitochondrion",
"reaction": "ATP = 3',5'-cyclic AMP + diphosphate",
"targ_desciption": "Catalyzes the formation of the signaling molecule cAMP(PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695,PubMed:24567411). May function as sensor that mediates responses tochanges in cellular bicarbonate and CO(2) levels (PubMed:15659711,PubMed:17591988). Has a critical role in mammalian spermatogenesis byproducing the cAMP which regulates cAMP-responsive nuclear factorsindispensable for sperm maturation in the epididymis. Inducescapacitation, the maturational process that sperm undergo prior tofertilization (By similarity). Involved in ciliary beat regulation(PubMed:17591988). {ECO:0000250|UniProtKB:Q8C0T9,ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988,ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449,ECO:0000269|PubMed:25040695}.",
"references": []
},
{
"targ_id": "T226",
"parent_targ_id": "T",
"full_name": "Peroxisomal acyl-coenzyme A oxidase 1",
"abbrev": "AOX",
"protein_names": "Peroxisomal acyl-coenzyme A oxidase 1 (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) (Straight-chain acyl-CoA oxidase) (SCOX) [Cleaved into: Peroxisomal acyl-CoA oxidase 1, A chain; Peroxisomal acyl-CoA oxidase 1, B chain; Peroxisomal acyl-CoA oxidase 1, C chain]",
"related_func_ids": "F021103",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q15067",
"Uniprot_name": "ACOX1_HUMAN",
"EC_numbers": "1.3.3.6",
"gene_symbol": "ACOX1 ACOX",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Peroxisome",
"reaction": "a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2; O2 + octanoyl-CoA = (2E)-octenoyl-CoA + H2O2; decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2; O2 + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O2; hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2; O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2; glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2; hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2; O2 + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O2",
"targ_desciption": "Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. {ECO:0000269|PubMed:15060085, ECO:0000269|PubMed:17458872,ECO:0000269|PubMed:17603022}.; [Isoform 1]: Shows highest activity against medium-chainfatty acyl-CoAs and activity decreases with increasing chain length.{ECO:0000269|PubMed:17603022}.; [Isoform 2]: Is active against a much broader range ofsubstrates and shows activity towards very long-chain acyl-CoAs. Istwice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is25% more active against 1,16-hexadecanodioyl-CoA.{ECO:0000269|PubMed:17603022}.",
"references": [
"RC03836"
]
},
{
"targ_id": "T227",
"parent_targ_id": "T",
"full_name": "Thiol compounds",
"abbrev": "",
"protein_names": "",
"related_func_ids": "F0213",
"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": [
"RC00485",
"RC00486"
]
},
{
"targ_id": "T228",
"parent_targ_id": "T",
"full_name": "F-actin cytoskeleton",
"abbrev": "",
"protein_names": "",
"related_func_ids": "F040101",
"category": "protein",
"subcategories": "cytoskeleton",
"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": []
},
{
"targ_id": "T229",
"parent_targ_id": "T",
"full_name": "Tripeptidyl-peptidase 1",
"abbrev": "TPP-1",
"protein_names": "Tripeptidyl-peptidase 1 (TPP-1) (EC 3.4.14.9) (Cell growth-inhibiting gene 1 protein) (Lysosomal pepstatin-insensitive protease) (LPIC) (Tripeptidyl aminopeptidase) (Tripeptidyl-peptidase I) (TPP-I)",
"related_func_ids": "F040101",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "O14773",
"Uniprot_name": "TPP1_HUMAN",
"EC_numbers": "3.4.14.9",
"gene_symbol": "TPP1 CLN2 GIG1 UNQ267/PRO304",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Lysosome; Melanosome",
"reaction": "Release of an N-terminal tripeptide from a polypeptide, butalso has endopeptidase activity.",
"targ_desciption": "Lysosomal serine protease with tripeptidyl-peptidase Iactivity (PubMed:11054422, PubMed:19038966, PubMed:19038967). May actas a non-specific lysosomal peptidase which generates tripeptides fromthe breakdown products produced by lysosomal proteinases(PubMed:11054422, PubMed:19038966, PubMed:19038967). Requiressubstrates with an unsubstituted N-terminus (PubMed:19038966).{ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966,ECO:0000269|PubMed:19038967}.",
"references": []
},
{
"targ_id": "T230",
"parent_targ_id": "T",
"full_name": "Aurora kinase B",
"abbrev": "AIM-1",
"protein_names": "Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)",
"related_func_ids": "F040101",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q96GD4",
"Uniprot_name": "AURKB_HUMAN",
"EC_numbers": "2.7.11.1",
"gene_symbol": "AURKB AIK2 AIM1 AIRK2 ARK2 STK1 STK12 STK5",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus; Chromosome; Chromosome, centromere; Cytoplasm, cytoskeleton, spindle; Midbody",
"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 component of the chromosomalpassenger complex (CPC), a complex that acts as a key regulator ofmitosis. The CPC complex has essential functions at the centromere inensuring correct chromosome alignment and segregation and is requiredfor chromatin-induced microtubule stabilization and spindle assembly.Involved in the bipolar attachment of spindle microtubules tokinetochores and is a key regulator for the onset of cytokinesis duringmitosis. Required for central/midzone spindle assembly and cleavagefurrow formation. Key component of the cytokinesis checkpoint, aprocess required to delay abscission to prevent both prematureresolution of intercellular chromosome bridges and accumulation of DNAdamage: phosphorylates CHMP4C, leading to retain abscission-competentVPS4 (VPS4A and/or VPS4B) at the midbody ring until abscissioncheckpoint signaling is terminated at late cytokinesis(PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPCcomplex subunits BIRC5/survivin, CDCA8/borealin and INCENP.Phosphorylation of INCENP leads to increased AURKB activity. Otherknown AURKB substrates involved in centromeric functions and mitosisare CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1,VIM/vimentin, HASPIN, and histone H3. A positive feedback loopinvolving HASPIN and AURKB contributes to localization of CPC tocentromeres. Phosphorylation of VIM controls vimentin filamentsegregation in cytokinetic process, whereas histone H3 isphosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph andH3S28ph, respectively). A positive feedback between HASPIN and AURKBcontributes to CPC localization. AURKB is also required for kinetochorelocalization of BUB1 and SGO1. Phosphorylation of p53/TP53 negativelyregulates its transcriptional activity. Key regulator of activepromoters in resting B- and T-lymphocytes: acts by mediatingphosphorylation of H3S28ph at active promoters in resting B-cells,inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A andenhancing binding and activity of the USP16 deubiquitinase attranscribed genes. {ECO:0000269|PubMed:11516652,ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863,ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200,ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593,ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875,ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118,ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581,ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734,ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950,ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515}.",
"references": []
},
{
"targ_id": "T231",
"parent_targ_id": "T",
"full_name": "DNA-directed RNA polymerase, mitochondrial",
"abbrev": "MtRPOL",
"protein_names": "DNA-directed RNA polymerase, mitochondrial (MtRPOL) (EC 2.7.7.6)",
"related_func_ids": "F060102",
"category": "enzyme",
"subcategories": "Nucleotidyltransferase, Transferase",
"Uniport_ID": "O00411",
"Uniprot_name": "RPOM_HUMAN",
"EC_numbers": "2.7.7.6",
"gene_symbol": "POLRMT",
"gene_synonyms": "APOLMT, h-mtRPOL, MTRNAP, MTRPOL",
"gene_synonyms_links": "",
"gene_name": "RNA polymerase mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000099821",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +RNA(n+1)",
"targ_desciption": "DNA-dependent RNA polymerase catalyzes the transcription ofmitochondrial DNA into RNA using the four ribonucleoside triphosphatesas substrates (PubMed:21278163). Component of the mitochondrialtranscription initiation complex, composed at least of TFB2M, TFAM andPOLRMT that is required for basal transcription of mitochondrial DNA(PubMed:29149603). In this complex, TFAM recruits POLRMT to a specificpromoter whereas TFB2M induces structural changes in POLRMT to enablepromoter opening and trapping of the DNA non-template strand(PubMed:29149603). {ECO:0000269|PubMed:21278163,ECO:0000269|PubMed:29149603}.",
"references": [
"RC03998",
"RC03999",
"RC04000"
]
},
{
"targ_id": "T232",
"parent_targ_id": "T",
"full_name": "mitochondrial topoisomerases",
"abbrev": "",
"protein_names": "",
"related_func_ids": "F060102",
"category": "enzyme family",
"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": []
},
{
"targ_id": "T233",
"parent_targ_id": "T",
"full_name": "Transcription factor A, mitochondrial",
"abbrev": "mtTFA",
"protein_names": "Transcription factor A, mitochondrial (mtTFA) (Mitochondrial transcription factor 1) (MtTF1) (Transcription factor 6) (TCF-6) (Transcription factor 6-like 2)",
"related_func_ids": "F060102",
"category": "protein",
"subcategories": "Activator",
"Uniport_ID": "Q00059",
"Uniprot_name": "TFAM_HUMAN",
"EC_numbers": "",
"gene_symbol": "TFAM",
"gene_synonyms": "TCF6, TCF6L2",
"gene_synonyms_links": "",
"gene_name": "Transcription factor A, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000108064",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "",
"targ_desciption": "Binds to the mitochondrial light strand promoter andfunctions in mitochondrial transcription regulation (PubMed:29445193,PubMed:32183942). Component of the mitochondrial transcriptioninitiation complex, composed at least of TFB2M, TFAM and POLRMT that isrequired for basal transcription of mitochondrial DNA(PubMed:29149603). In this complex, TFAM recruits POLRMT to a specificpromoter whereas TFB2M induces structural changes in POLRMT to enablepromoter opening and trapping of the DNA non-template strand(PubMed:20410300). Required for accurate and efficient promoterrecognition by the mitochondrial RNA polymerase (PubMed:22037172).Promotes transcription initiation from the HSP1 and the light strandpromoter by binding immediately upstream of transcriptional start sites(PubMed:22037172). Is able to unwind DNA (PubMed:22037172). Bends themitochondrial light strand promoter DNA into a U-turn shape via its HMGboxes (PubMed:1737790). Required for maintenance of normal levels ofmitochondrial DNA (PubMed:22841477, PubMed:19304746). May play a rolein organizing and compacting mitochondrial DNA (PubMed:22037171).{ECO:0000269|PubMed:1737790, ECO:0000269|PubMed:19304746,ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:22037171,ECO:0000269|PubMed:22037172, ECO:0000269|PubMed:22841477,ECO:0000269|PubMed:29149603, ECO:0000269|PubMed:29445193,ECO:0000269|PubMed:32183942}.",
"references": []
},
{
"targ_id": "T234",
"parent_targ_id": "T",
"full_name": "DNA polymerase gamma",
"abbrev": "PolG",
"protein_names": "",
"related_func_ids": "F060102",
"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": [
"RC00597",
"RC00598",
"RC00599",
"RC03674",
"RC03675",
"RC03676",
"RC03677",
"RC03678",
"RC03679",
"RC03680",
"RC03681",
"RC03682",
"RC03683"
]
},
{
"targ_id": "T234001",
"parent_targ_id": "T234",
"full_name": "DNA polymerase subunit gamma-1",
"abbrev": "PolG-alpha",
"protein_names": "DNA polymerase subunit gamma-1 (EC 2.7.7.7) (Mitochondrial DNA polymerase catalytic subunit) (PolG-alpha)",
"related_func_ids": "F060102; F060301",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "P54098",
"Uniprot_name": "DPOG1_HUMAN",
"EC_numbers": "2.7.7.7",
"gene_symbol": "POLG",
"gene_synonyms": "POLG1, POLGA",
"gene_synonyms_links": "",
"gene_name": "DNA polymerase gamma, catalytic subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000140521",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =diphosphate + DNA(n+1)",
"targ_desciption": "Involved in the replication of mitochondrial DNA. Associateswith mitochondrial DNA.",
"references": []
},
{
"targ_id": "T234002",
"parent_targ_id": "T234",
"full_name": "DNA polymerase subunit gamma-2, mitochondrial",
"abbrev": "PolG-beta",
"protein_names": "DNA polymerase subunit gamma-2, mitochondrial (DNA polymerase gamma accessory 55 kDa subunit) (p55) (Mitochondrial DNA polymerase accessory subunit) (MtPolB) (PolG-beta)",
"related_func_ids": "F060102",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q9UHN1",
"Uniprot_name": "DPOG2_HUMAN",
"EC_numbers": "",
"gene_symbol": "POLG2",
"gene_synonyms": "HP55, MTPOLB",
"gene_synonyms_links": "",
"gene_name": "DNA polymerase gamma 2, accessory subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000256525",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Mitochondrial polymerase processivity subunit. It regulatesthe polymerase and exonuclease activities promoting processive DNAsynthesis. Binds to ss-DNA. {ECO:0000269|PubMed:30157269}.",
"references": []
},
{
"targ_id": "T235",
"parent_targ_id": "T",
"full_name": "Mitochondrial thymidine kinase 2",
"abbrev": "TK2",
"protein_names": "Thymidine kinase 2, mitochondrial",
"related_func_ids": "F060102",
"category": "enzyme",
"subcategories": "Kinase, Transferase",
"Uniport_ID": "O00142",
"Uniprot_name": "KITM_HUMAN",
"EC_numbers": "2.7.1.21",
"gene_symbol": "TK2",
"gene_synonyms": "SCA31",
"gene_synonyms_links": "",
"gene_name": "Thymidine kinase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000166548",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + thymidine = ADP + dTMP + H(+)",
"targ_desciption": "Phosphorylates thymidine, deoxycytidine, and deoxyuridine inthe mitochondrial matrix. In non-replicating cells, where cytosolicdNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2and DGUOK. Widely used as target of antiviral and chemotherapeuticagents. {ECO:0000269|PubMed:11687801}.",
"references": [
"RC03577"
]
},
{
"targ_id": "T236",
"parent_targ_id": "T",
"full_name": "deoxyguanosine kinase",
"abbrev": "dGK",
"protein_names": "Deoxyguanosine kinase, mitochondrial",
"related_func_ids": "F060102",
"category": "enzyme",
"subcategories": "Kinase, Transferase",
"Uniport_ID": "Q16854",
"Uniprot_name": "DGUOK_HUMAN",
"EC_numbers": "2.7.1.113",
"gene_symbol": "DGUOK",
"gene_synonyms": "dGK",
"gene_synonyms_links": "",
"gene_name": "Deoxyguanosine kinase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000114956",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "2'-deoxyguanosine + ATP = ADP + dGMP + H(+); 2'-deoxyadenosine + ATP = ADP + dAMP + H(+)",
"targ_desciption": "Phosphorylates deoxyguanosine and deoxyadenosine in themitochondrial matrix, with the highest efficiency for deoxyguanosine(PubMed:8692979, PubMed:8706825, PubMed:11687801, PubMed:17073823,PubMed:23043144). In non-replicating cells, where cytosolic dNTPsynthesis is down-regulated, mtDNA synthesis depends solely on DGUOKand TK2. Phosphorylates certain nucleoside analogs (By similarity).Widely used as target of antiviral and chemotherapeutic agents.{ECO:0000250|UniProtKB:Q9QX60, ECO:0000269|PubMed:11687801,ECO:0000269|PubMed:17073823, ECO:0000269|PubMed:23043144,ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825}.",
"references": [
"RC03578"
]
},
{
"targ_id": "T237",
"parent_targ_id": "T",
"full_name": "twinkle mtDNA helicase",
"abbrev": "",
"protein_names": "Twinkle protein, mitochondrial",
"related_func_ids": "F060102; F060301",
"category": "enzyme",
"subcategories": "Helicase, Hydrolase",
"Uniport_ID": "Q96RR1",
"Uniprot_name": "PEO1_HUMAN",
"EC_numbers": "3.6.4.12",
"gene_symbol": "TWNK",
"gene_synonyms": "C10orf2, FLJ21832, IOSCA, PEO, PEO1, TWINKLE, TWINL",
"gene_synonyms_links": "",
"gene_name": "Twinkle mtDNA helicase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000107815",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "ATP + H2O = ADP + H(+) + phosphate",
"targ_desciption": "Involved in mitochondrial DNA (mtDNA) metabolism. Couldfunction as an adenine nucleotide-dependent DNA helicase. Functioninferred to be critical for lifetime maintenance of mtDNA integrity. Invitro, forms in combination with POLG, a processive replicationmachinery, which can use double-stranded DNA (dsDNA) as template tosynthesize single-stranded DNA (ssDNA) molecules. May be a keyregulator of mtDNA copy number in mammals.{ECO:0000269|PubMed:15167897}.",
"references": []
},
{
"targ_id": "T238",
"parent_targ_id": "T",
"full_name": "Single-stranded DNA-binding protein, mitochondrial",
"abbrev": "Mt-SSB",
"protein_names": "Single-stranded DNA-binding protein, mitochondrial (Mt-SSB) (MtSSB) (PWP1-interacting protein 17)",
"related_func_ids": "F060102",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q04837",
"Uniprot_name": "SSBP_HUMAN",
"EC_numbers": "",
"gene_symbol": "SSBP1",
"gene_synonyms": "mtSSB, SSBP",
"gene_synonyms_links": "",
"gene_name": "Single stranded DNA binding protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000106028",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "Binds preferentially and cooperatively to pyrimidine richsingle-stranded DNA (ss-DNA) (PubMed:21953457, PubMed:23290262). Invitro, required to maintain the copy number of mitochondrial DNA(mtDNA) and plays crucial roles during mtDNA replication that stimulateactivity of the replisome components POLG and TWNK at the replicationfork (PubMed:21953457, PubMed:12975372, PubMed:26446790,PubMed:15167897). Promotes the activity of the gamma complex polymerasePOLG, largely by organizing the template DNA and eliminating secondarystructures to favor ss-DNA conformations that facilitate POLG activity(PubMed:26446790, PubMed:21953457). In addition it is able to promotethe 5'-3' unwinding activity of the mtDNA helicase TWNK(PubMed:12975372). May also function in mtDNA repair (PubMed:23290262).{ECO:0000269|PubMed:12975372, ECO:0000269|PubMed:15167897,ECO:0000269|PubMed:21953457, ECO:0000269|PubMed:23290262,ECO:0000269|PubMed:26446790}.",
"references": []
},
{
"targ_id": "T239",
"parent_targ_id": "T",
"full_name": "DNA ligase 3",
"abbrev": "DNA ligase III",
"protein_names": "DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)",
"related_func_ids": "F060102; F0602; F060103",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "P49916",
"Uniprot_name": "DNLI3_HUMAN",
"EC_numbers": "6.5.1.1",
"gene_symbol": "LIG3",
"gene_synonyms": "LIG2",
"gene_synonyms_links": "",
"gene_name": "DNA ligase 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000005156",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; [Isoform 2]: Mitochondrion; [Isoform 3]: Nucleus; [Isoform 4]: Nucleus",
"reaction": "ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +diphosphate.",
"targ_desciption": "Isoform 3 functions as heterodimer with DNA-repair proteinXRCC1 in the nucleus and can correct defective DNA strand-break repairand sister chromatid exchange following treatment with ionizingradiation and alkylating agents. Isoform 1 is targeted to mitochondria,where it functions as DNA ligase in mitochondrial base-excision DNArepair (PubMed:10207110, PubMed:24674627).{ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.",
"references": []
},
{
"targ_id": "T240",
"parent_targ_id": "T",
"full_name": "Aprataxin",
"abbrev": "FHA-HIT",
"protein_names": "Aprataxin (EC 3.6.1.71) (EC 3.6.1.72) (Forkhead-associated domain histidine triad-like protein) (FHA-HIT)",
"related_func_ids": "F060103",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q7Z2E3",
"Uniprot_name": "APTX_HUMAN",
"EC_numbers": "3.6.1.71; 3.6.1.72",
"gene_symbol": "APTX AXA1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus, nucleoplasm; Nucleus,nucleolus",
"reaction": "adenosine-5'-diphospho-5'-(DNA) + H2O = AMP + 2 H(+) +phospho-5'-(DNA); adenosine-5'-diphospho-5'-(ribonucleotide)-(DNA) + H2O = 5'-phospho-(ribonucleotide)-(DNA) + AMP + 2 H(+); (DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate +GMP + 2 H(+)",
"targ_desciption": "DNA-binding protein involved in single-strand DNA breakrepair, double-strand DNA break repair and base excision repair(PubMed:15380105, PubMed:15044383, PubMed:16964241, PubMed:17276982,PubMed:24362567). Resolves abortive DNA ligation intermediates formedeither at base excision sites, or when DNA ligases attempt to repairnon-ligatable breaks induced by reactive oxygen species(PubMed:16964241, PubMed:24362567). Catalyzes the release of adenylategroups covalently linked to 5'-phosphate termini, resulting in theproduction of 5'-phosphate termini that can be efficiently rejoined(PubMed:16964241, PubMed:17276982, PubMed:24362567). Also able tohydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosinetetraphosphate (AppppA), but with lower catalytic activity(PubMed:16547001). Likewise, catalyzes the release of 3'-linkedguanosine (DNAppG) and inosine (DNAppI) from DNA, but has higherspecific activity with 5'-linked adenosine (AppDNA) (By similarity).{ECO:0000250|UniProtKB:O74859, ECO:0000269|PubMed:15044383,ECO:0000269|PubMed:15380105, ECO:0000269|PubMed:16547001,ECO:0000269|PubMed:16964241, ECO:0000269|PubMed:17276982,ECO:0000269|PubMed:24362567}.",
"references": []
},
{
"targ_id": "T241",
"parent_targ_id": "T",
"full_name": "DNA repair protein XRCC4",
"abbrev": "X-ray repair cross-complementing protein 4",
"protein_names": "DNA repair protein XRCC4 (X-ray repair cross-complementing protein 4)",
"related_func_ids": "F060103",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q13426",
"Uniprot_name": "XRCC4_HUMAN",
"EC_numbers": "",
"gene_symbol": "XRCC4",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus",
"reaction": "",
"targ_desciption": "Involved in DNA non-homologous end joining (NHEJ) requiredfor double-strand break repair and V(D)J recombination. Binds to DNAand to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible forthe NHEJ ligation step, and XRCC4 enhances the joining activity ofLIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on theassembly of the DNA-dependent protein kinase complex DNA-PK to theseDNA ends. {ECO:0000269|PubMed:10757784, ECO:0000269|PubMed:10854421,ECO:0000269|PubMed:16412978, ECO:0000269|PubMed:8548796}.",
"references": []
},
{
"targ_id": "T242",
"parent_targ_id": "T",
"full_name": "DNA topoisomerase I, mitochondrial",
"abbrev": "TOP1mt",
"protein_names": "DNA topoisomerase I, mitochondrial (TOP1mt) (EC 5.6.2.1)",
"related_func_ids": "F060102",
"category": "enzyme",
"subcategories": "Isomerase, Topoisomerase",
"Uniport_ID": "Q969P6",
"Uniprot_name": "TOP1M_HUMAN",
"EC_numbers": "5.6.2.1",
"gene_symbol": "TOP1MT",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "DNA topoisomerase I mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000184428",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP-independent breakage of single-stranded DNA, followed bypassage and rejoining.",
"targ_desciption": "Releases the supercoiling and torsional tension of DNAintroduced during duplication of mitochondrial DNA by transientlycleaving and rejoining one strand of the DNA duplex. Introduces asingle-strand break via transesterification at a target site in duplexDNA. The scissile phosphodiester is attacked by the catalytic tyrosineof the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The freeDNA strand then rotates around the intact phosphodiester bond on theopposing strand, thus removing DNA supercoils. Finally, in thereligation step, the DNA 5'-OH attacks the covalent intermediate toexpel the active-site tyrosine and restore the DNA phosphodiesterbackbone (By similarity). {ECO:0000250, ECO:0000269|PubMed:11526219}.",
"references": []
},
{
"targ_id": "T243",
"parent_targ_id": "T",
"full_name": "Uracil-DNA glycosylase",
"abbrev": "UDG",
"protein_names": "Uracil-DNA glycosylase (UDG) (EC 3.2.2.27)",
"related_func_ids": "F060103",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "P13051",
"Uniprot_name": "UNG_HUMAN",
"EC_numbers": "3.2.2.27",
"gene_symbol": "UNG",
"gene_synonyms": "DGU, HIGM4, UDG, UNG1, UNG2",
"gene_synonyms_links": "",
"gene_name": "Uracil DNA glycosylase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000076248",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; [Isoform 2]: Nucleus",
"reaction": "Hydrolyzes single-stranded DNA or mismatched double-strandedDNA and polynucleotides, releasing free uracil.",
"targ_desciption": "Excises uracil residues from the DNA which can arise as aresult of misincorporation of dUMP residues by DNA polymerase or due todeamination of cytosine.",
"references": []
},
{
"targ_id": "T244",
"parent_targ_id": "T",
"full_name": "4-aminobutyrate aminotransferase, mitochondrial",
"abbrev": "GABA-AT",
"protein_names": "4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Aminotransferase, Transferase",
"Uniport_ID": "P80404",
"Uniprot_name": "GABT_HUMAN",
"EC_numbers": "2.6.1.19; 2.6.1.22",
"gene_symbol": "ABAT",
"gene_synonyms": "GABAT",
"gene_synonyms_links": "",
"gene_name": "4-aminobutyrate aminotransferase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000183044",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinatesemialdehyde; (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate",
"targ_desciption": "Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonatesemialdehyde, respectively. Can also convert delta-aminovalerate andbeta-alanine.",
"references": []
},
{
"targ_id": "T245",
"parent_targ_id": "T",
"full_name": "Adenylate kinase 2, mitochondrial",
"abbrev": "AK 2",
"protein_names": "Adenylate kinase 2, mitochondrial (AK 2) (EC 2.7.4.3) (ATP-AMP transphosphorylase 2) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) [Cleaved into: Adenylate kinase 2, mitochondrial, N-terminally processed]",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Kinase, Transferase",
"Uniport_ID": "P54819",
"Uniprot_name": "KAD2_HUMAN",
"EC_numbers": "2.7.4.3",
"gene_symbol": "AK2",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Adenylate kinase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000004455",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion intermembrane space",
"reaction": "AMP + ATP = 2 ADP",
"targ_desciption": "Catalyzes the reversible transfer of the terminal phosphategroup between ATP and AMP. Plays an important role in cellular energyhomeostasis and in adenine nucleotide metabolism. Adenylate kinaseactivity is critical for regulation of the phosphate utilization andthe AMP de novo biosynthesis pathways. Plays a key role inhematopoiesis. {ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:19043416}.",
"references": [
"RC03839"
]
},
{
"targ_id": "T246",
"parent_targ_id": "T",
"full_name": "Ribonucleoside-diphosphate reductase subunit M2 B",
"abbrev": "p53R2",
"protein_names": "Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) (TP53-inducible ribonucleotide reductase M2 B) (p53-inducible ribonucleotide reductase small subunit 2-like protein) (p53R2)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "Q7LG56",
"Uniprot_name": "RIR2B_HUMAN",
"EC_numbers": "1.17.4.1",
"gene_symbol": "RRM2B",
"gene_synonyms": "p53R2",
"gene_synonyms_links": "",
"gene_name": "Ribonucleotide reductase regulatory TP53 inducible subunit M2B",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000048392",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus",
"reaction": "[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate",
"targ_desciption": "Plays a pivotal role in cell survival by repairing damagedDNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides forDNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl freeradical center required for catalysis. Forms an active ribonucleotidereductase (RNR) complex with RRM1 which is expressed both in restingand proliferating cells in response to DNA damage.{ECO:0000269|PubMed:10716435, ECO:0000269|PubMed:11517226,ECO:0000269|PubMed:11719458}.",
"references": []
},
{
"targ_id": "T247",
"parent_targ_id": "T",
"full_name": "Deoxynucleoside triphosphate triphosphohydrolase SAMHD1",
"abbrev": "dNTPase",
"protein_names": "Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Dendritic cell-derived IFNG-induced protein) (DCIP) (Monocyte protein 5) (MOP-5) (SAM domain and HD domain-containing protein 1) (hSAMHD1)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q9Y3Z3",
"Uniprot_name": "SAMH1_HUMAN",
"EC_numbers": "3.1.5.-",
"gene_symbol": "SAMHD1 MOP5",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus; Chromosome",
"reaction": "a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside + H(+) + triphosphate",
"targ_desciption": "Protein that acts both as a host restriction factor involvedin defense response to virus and as a regulator of DNA end resection atstalled replication forks (PubMed:19525956, PubMed:21613998,PubMed:21720370, PubMed:23602554, PubMed:23601106, PubMed:22056990,PubMed:24336198, PubMed:26294762, PubMed:26431200, PubMed:28229507,PubMed:28834754, PubMed:29670289). Has deoxynucleoside triphosphate(dNTPase) activity, which is required to restrict infection by viruses,such as HIV-1: dNTPase activity reduces cellular dNTP levels to levelstoo low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells(PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:23602554,PubMed:23601106, PubMed:23364794, PubMed:25038827, PubMed:26101257,PubMed:22056990, PubMed:24336198, PubMed:28229507, PubMed:26294762,PubMed:26431200). Likewise, suppresses LINE-1 retrotransposon activity(PubMed:24035396, PubMed:29610582, PubMed:24217394). Not able torestrict infection by HIV-2 virus. because restriction activity iscounteracted by HIV-2 viral protein Vpx (PubMed:21613998,PubMed:21720370). In addition to virus restriction, dNTPase activityacts as a regulator of DNA precursor pools by regulating dNTP pools(PubMed:23858451). Phosphorylation at Thr-592 acts as a switch tocontrol dNTPase-dependent and -independent functions: it inhibitsdNTPase activity and ability to restrict infection by viruses, while itpromotes DNA end resection at stalled replication forks(PubMed:23602554, PubMed:23601106, PubMed:29610582, PubMed:29670289).Functions during S phase at stalled DNA replication forks to promotethe resection of gapped or reversed forks: acts by stimulating theexonuclease activity of MRE11, activating the ATR-CHK1 pathway andallowing the forks to restart replication (PubMed:29670289). Itsability to promote degradation of nascent DNA at stalled replicationforks is required to prevent induction of type I interferons, therebypreventing chronic inflammation (PubMed:27477283, PubMed:29670289).Ability to promote DNA end resection at stalled replication forks isindependent of dNTPase activity (PubMed:29670289). Enhancesimmunoglobulin hypermutation in B-lymphocytes by promoting transversionmutation (By similarity). {ECO:0000250|UniProtKB:Q60710,ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:21613998,ECO:0000269|PubMed:21720370, ECO:0000269|PubMed:22056990,ECO:0000269|PubMed:23364794, ECO:0000269|PubMed:23601106,ECO:0000269|PubMed:23602554, ECO:0000269|PubMed:23858451,ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:24217394,ECO:0000269|PubMed:24336198, ECO:0000269|PubMed:25038827,ECO:0000269|PubMed:26101257, ECO:0000269|PubMed:26294762,ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:27477283,ECO:0000269|PubMed:28229507, ECO:0000269|PubMed:28834754,ECO:0000269|PubMed:29610582, ECO:0000269|PubMed:29670289}.",
"references": []
},
{
"targ_id": "T248",
"parent_targ_id": "T",
"full_name": "Thymidine phosphorylase",
"abbrev": "TP",
"protein_names": "Thymidine phosphorylase (TP) (EC 2.4.2.4) (Gliostatin) (Platelet-derived endothelial cell growth factor) (PD-ECGF) (TdRPase)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Developmental protein, Glycosyltransferase, Growth factor, Transferase",
"Uniport_ID": "P19971",
"Uniprot_name": "TYPH_HUMAN",
"EC_numbers": "2.4.2.4",
"gene_symbol": "TYMP",
"gene_synonyms": "ECGF1, MNGIE",
"gene_synonyms_links": "",
"gene_name": "Thymidine phosphorylase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000025708",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +thymine",
"targ_desciption": "May have a role in maintaining the integrity of the bloodvessels. Has growth promoting activity on endothelial cells, angiogenicactivity in vivo and chemotactic activity on endothelial cells invitro. {ECO:0000269|PubMed:1590793}.; Catalyzes the reversible phosphorolysis of thymidine. Theproduced molecules are then utilized as carbon and energy sources or inthe rescue of pyrimidine bases for nucleotide synthesis.{ECO:0000269|PubMed:1590793}.",
"references": []
},
{
"targ_id": "T249",
"parent_targ_id": "T",
"full_name": "5'(3')-deoxyribonucleotidase, mitochondrial",
"abbrev": "KAT/AadAT",
"protein_names": "5'(3')-deoxyribonucleotidase, mitochondrial (5',3'-nucleotidase, mitochondrial) (EC 3.1.3.-) (Deoxy-5'-nucleotidase 2) (dNT-2)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q9NPB1",
"Uniprot_name": "NT5M_HUMAN",
"EC_numbers": "3.1.3.-",
"gene_symbol": "NT5M",
"gene_synonyms": "dNT-2, dNT2, mdN",
"gene_synonyms_links": "",
"gene_name": "5',3'-nucleotidase, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000205309",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Dephosphorylates specifically the 5' and 2'(3')-phosphates ofuracil and thymine deoxyribonucleotides, and so protects mitochondrialDNA replication from excess dTTP. Has only marginal activity towardsdIMP and dGMP. {ECO:0000269|PubMed:10899995}.",
"references": []
},
{
"targ_id": "T250",
"parent_targ_id": "T",
"full_name": "Dihydroorotate dehydrogenase",
"abbrev": "DHOdehase",
"protein_names": "Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase)",
"related_func_ids": "F022001",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q08210",
"Uniprot_name": "PYRD_PLAF7",
"EC_numbers": "1.3.5.2",
"gene_symbol": "PFF0160c",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein",
"reaction": "(S)-dihydroorotate + a quinone = a quinol + orotate",
"targ_desciption": "Catalyzes the conversion of dihydroorotate to orotate withquinone as electron acceptor.",
"references": []
},
{
"targ_id": "T251",
"parent_targ_id": "T",
"full_name": "Dihydroorotate dehydrogenase",
"abbrev": "DHOdehase",
"protein_names": "Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase)",
"related_func_ids": "F022001",
"category": "enzyme",
"subcategories": "Oxidoreductase",
"Uniport_ID": "Q02127",
"Uniprot_name": "PYRD_HUMAN",
"EC_numbers": "1.3.5.2",
"gene_symbol": "DHODH",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Dihydroorotate dehydrogenase (quinone)",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000102967",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Single-pass membrane protein",
"reaction": "(S)-dihydroorotate + a quinone = a quinol + orotate",
"targ_desciption": "Catalyzes the conversion of dihydroorotate to orotate withquinone as electron acceptor.",
"references": [
"RC03911",
"RC03912",
"RC03914"
]
},
{
"targ_id": "T252",
"parent_targ_id": "T",
"full_name": "Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3",
"abbrev": "NMN/NaMN adenylyltransferase 3",
"protein_names": "Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) (EC 2.7.7.18) (Pyridine nucleotide adenylyltransferase 3) (PNAT-3) (EC 2.7.7.1)",
"related_func_ids": "F022002",
"category": "enzyme",
"subcategories": "Nucleotidyltransferase, Transferase",
"Uniport_ID": "Q96T66",
"Uniprot_name": "NMNA3_HUMAN",
"EC_numbers": "2.7.7.18; 2.7.7.1",
"gene_symbol": "NMNAT3",
"gene_synonyms": "PNAT3",
"gene_synonyms_links": "",
"gene_name": "Nicotinamide nucleotide adenylyltransferase 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000163864",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate+ NAD(+); ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)+ diphosphate",
"targ_desciption": "Catalyzes the formation of NAD(+) from nicotinamidemononucleotide (NMN) and ATP. Can also use the deamidated form.nicotinic acid mononucleotide (NaMN) as substrate with the sameefficiency. Can use triazofurin monophosphate (TrMP) as substrate. Canalso use GTP and ITP as nucleotide donors. Also catalyzes the reversereaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For thepyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acidadenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide(NGD) as substrates. Fails to cleave phosphorylated dinucleotidesNADP(+), NADPH and NaADP(+). Protects against axonal degenerationfollowing injury. {ECO:0000269|PubMed:16118205,ECO:0000269|PubMed:17402747}.",
"references": []
},
{
"targ_id": "T253",
"parent_targ_id": "T",
"full_name": "ADP-ribose pyrophosphatase, mitochondrial",
"abbrev": "ADPR-PPase",
"protein_names": "ADP-ribose pyrophosphatase, mitochondrial (EC 3.6.1.13) (ADP-ribose diphosphatase) (ADP-ribose phosphohydrolase) (Adenosine diphosphoribose pyrophosphatase) (ADPR-PPase) (Nucleoside diphosphate-linked moiety X motif 9) (Nudix motif 9)",
"related_func_ids": "F0220",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q9BW91",
"Uniprot_name": "NUDT9_HUMAN",
"EC_numbers": "3.6.1.13",
"gene_symbol": "NUDT9",
"gene_synonyms": "MGC3037",
"gene_synonyms_links": "",
"gene_name": "Nudix hydrolase 9",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000170502",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion",
"reaction": "ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)",
"targ_desciption": "Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.",
"references": []
},
{
"targ_id": "T254",
"parent_targ_id": "T",
"full_name": "DNA replication ATP-dependent helicase/nuclease DNA2",
"abbrev": "hDNA2",
"protein_names": "DNA replication ATP-dependent helicase/nuclease DNA2 (hDNA2) (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)]",
"related_func_ids": "F060102; F0602; F060301",
"category": "enzyme",
"subcategories": "DNA-binding, Endonuclease, Helicase, Hydrolase, Multifunctional enzyme, Nuclease",
"Uniport_ID": "P51530",
"Uniprot_name": "DNA2_HUMAN",
"EC_numbers": "3.1.-.-; 3.6.4.12",
"gene_symbol": "DNA2",
"gene_synonyms": "DNA2L, KIAA0083",
"gene_synonyms_links": "",
"gene_name": "DNA replication helicase/nuclease 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000138346",
"omim_id": "",
"genecard_link": "",
"locs": "Nucleus; Mitochondrion",
"reaction": "ATP + H2O = ADP + H(+) + phosphate",
"targ_desciption": "Key enzyme involved in DNA replication and DNA repair innucleus and mitochondrion. Involved in Okazaki fragments processing bycleaving long flaps that escape FEN1: flaps that are longer than 27nucleotides are coated by replication protein A complex (RPA), leadingto recruit DNA2 which cleaves the flap until it is too short to bindRPA and becomes a substrate for FEN1. Also involved in 5'-end resectionof DNA during double-strand break (DSB) repair: recruited by BLM andmediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage isprevented by the presence of RPA. Also involved in DNA replicationcheckpoint independently of Okazaki fragments processing. Possessesdifferent enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While theATPase and endonuclease activities are well-defined and play a key rolein Okazaki fragments processing and DSB repair, the 5'-3' DNA helicaseactivity is subject to debate. According to various reports, thehelicase activity is weak and its function remains largely unclear.Helicase activity may promote the motion of DNA2 on the flap, helpingthe nuclease function. {ECO:0000269|PubMed:16595799,ECO:0000269|PubMed:16595800, ECO:0000269|PubMed:18995831,ECO:0000269|PubMed:19487465, ECO:0000269|PubMed:21325134,ECO:0000269|PubMed:21572043, ECO:0000269|PubMed:22570407,ECO:0000269|PubMed:22570476}.",
"references": []
},
{
"targ_id": "T255",
"parent_targ_id": "T",
"full_name": "F-box/LRR-repeat protein 4",
"abbrev": "F-box protein FBL4/FBL5",
"protein_names": "F-box/LRR-repeat protein 4 (F-box and leucine-rich repeat protein 4) (F-box protein FBL4/FBL5)",
"related_func_ids": "F060102; F0602; F060301",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9UKA2",
"Uniprot_name": "FBXL4_HUMAN",
"EC_numbers": "",
"gene_symbol": "FBXL4",
"gene_synonyms": "FBL4, FBL5",
"gene_synonyms_links": "",
"gene_name": "F-box and leucine rich repeat protein 4",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000112234",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Nucleus; Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T256",
"parent_targ_id": "T",
"full_name": "Mitochondrial genome maintenance exonuclease 1",
"abbrev": "",
"protein_names": "Mitochondrial genome maintenance exonuclease 1 (EC 3.1.-.-)",
"related_func_ids": "F060102; F0602; F060301",
"category": "enzyme",
"subcategories": "Exonuclease, Hydrolase, Nuclease",
"Uniport_ID": "Q9BQP7",
"Uniprot_name": "MGME1_HUMAN",
"EC_numbers": "3.1.-.-",
"gene_symbol": "MGME1",
"gene_synonyms": "bA504H3.4, C20orf72, DDK1",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial genome maintenance exonuclease 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000125871",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Metal-dependent single-stranded DNA (ssDNA) exonucleaseinvolved in mitochondrial genome maintenance. Has preference for 5'-3'exonuclease activity but is also capable of endoduclease activity onlinear substrates. Necessary for maintenance of proper 7S DNA levels.Probably involved in mitochondrial DNA (mtDNA) repair, possibly via theprocessing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNAflaps during long-patch base excision repair. Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells.{ECO:0000255|HAMAP-Rule:MF_03030, ECO:0000269|PubMed:23313956,ECO:0000269|PubMed:23358826}.",
"references": []
},
{
"targ_id": "T257",
"parent_targ_id": "T",
"full_name": "Protein Mpv17",
"abbrev": "",
"protein_names": "Protein Mpv17",
"related_func_ids": "F060102; F0602; F060301",
"category": "protein",
"subcategories": "",
"Uniport_ID": "P39210",
"Uniprot_name": "MPV17_HUMAN",
"EC_numbers": "",
"gene_symbol": "MPV17",
"gene_synonyms": "SYM1",
"gene_synonyms_links": "",
"gene_name": "MPV17, mitochondrial inner membrane protein",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000115204",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Multi-pass membrane protein",
"reaction": "",
"targ_desciption": "Non-selective channel that modulates the membrane potentialunder normal conditions and oxidative stress, and is involved inmitochondrial homeostasis (PubMed:25861990). Involved in mitochondrialdeoxynucleoside triphosphates (dNTP) pool homeostasis and mitochondrialDNA (mtDNA) maintenance (PubMed:26760297). May be involved in theregulation of reactive oxygen species metabolism and the control ofoxidative phosphorylation (By similarity).{ECO:0000250|UniProtKB:P19258, ECO:0000269|PubMed:25861990,ECO:0000269|PubMed:26760297}.",
"references": []
},
{
"targ_id": "T258",
"parent_targ_id": "T",
"full_name": "DNA polymerase subunit gamma-2, mitochondrial",
"abbrev": "PolG-beta",
"protein_names": "DNA polymerase subunit gamma-2, mitochondrial (DNA polymerase gamma accessory 55 kDa subunit) (p55) (Mitochondrial DNA polymerase accessory subunit) (MtPolB) (PolG-beta)",
"related_func_ids": "F060102; F0602; F060301",
"category": "protein subunit",
"subcategories": "",
"Uniport_ID": "Q9UHN1",
"Uniprot_name": "DPOG2_HUMAN",
"EC_numbers": "",
"gene_symbol": "POLG2",
"gene_synonyms": "HP55, MTPOLB",
"gene_synonyms_links": "",
"gene_name": "DNA polymerase gamma 2, accessory subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000256525",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Mitochondrial polymerase processivity subunit. It regulatesthe polymerase and exonuclease activities promoting processive DNAsynthesis. Binds to ss-DNA. {ECO:0000269|PubMed:30157269}.",
"references": []
},
{
"targ_id": "T259",
"parent_targ_id": "T",
"full_name": "Single-stranded DNA-binding protein, mitochondrial",
"abbrev": "MtSSB",
"protein_names": "Single-stranded DNA-binding protein, mitochondrial (Mt-SSB) (MtSSB) (PWP1-interacting protein 17)",
"related_func_ids": "F060102; F0602; F060301",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q04837",
"Uniprot_name": "SSBP_HUMAN",
"EC_numbers": "",
"gene_symbol": "SSBP1",
"gene_synonyms": "mtSSB, SSBP",
"gene_synonyms_links": "",
"gene_name": "Single stranded DNA binding protein 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000106028",
"omim_id": "",
"genecard_link": "",
"locs": "",
"reaction": "",
"targ_desciption": "Binds preferentially and cooperatively to pyrimidine richsingle-stranded DNA (ss-DNA) (PubMed:21953457, PubMed:23290262). Invitro, required to maintain the copy number of mitochondrial DNA(mtDNA) and plays crucial roles during mtDNA replication that stimulateactivity of the replisome components POLG and TWNK at the replicationfork (PubMed:21953457, PubMed:12975372, PubMed:26446790,PubMed:15167897). Promotes the activity of the gamma complex polymerasePOLG, largely by organizing the template DNA and eliminating secondarystructures to favor ss-DNA conformations that facilitate POLG activity(PubMed:26446790, PubMed:21953457). In addition it is able to promotethe 5'-3' unwinding activity of the mtDNA helicase TWNK(PubMed:12975372). May also function in mtDNA repair (PubMed:23290262).{ECO:0000269|PubMed:12975372, ECO:0000269|PubMed:15167897,ECO:0000269|PubMed:21953457, ECO:0000269|PubMed:23290262,ECO:0000269|PubMed:26446790}.",
"references": []
},
{
"targ_id": "T260",
"parent_targ_id": "T",
"full_name": "Prohibitin-2",
"abbrev": "D-prohibitin",
"protein_names": "Prohibitin-2 (B-cell receptor-associated protein BAP37) (D-prohibitin) (Repressor of estrogen receptor activity)",
"related_func_ids": "F0701; F0807",
"category": "enzyme",
"subcategories": "Receptor, Repressor",
"Uniport_ID": "Q99623",
"Uniprot_name": "PHB2_HUMAN",
"EC_numbers": "",
"gene_symbol": "PHB2",
"gene_synonyms": "Bap37, BCAP37, p22, REA",
"gene_synonyms_links": "",
"gene_name": "Prohibitin 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000215021",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Cytoplasm; Nucleus; Cell membrane; [Isoform 1]: Mitochondrion inner membrane; [Isoform 2]: Mitochondrion inner membrane",
"reaction": "",
"targ_desciption": "Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasmamembrane-associated cell signaling functions, mitochondrial chaperone,and transcriptional co-regulator of transcription factors and sexsteroid hormones in the nucleus. {ECO:0000269|PubMed:10359819,ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,ECO:0000269|PubMed:24003225, ECO:0000269|PubMed:28017329,ECO:0000269|PubMed:31522117}.; In the mitochondria, together with PHB, forms large ringcomplexes (prohibitin complexes) in the inner mitochondrial membrane(IMM) and functions as chaperone protein that stabilizes mitochondrialrespiratory enzymes and maintains mitochondrial integrity in the IMM,which is required for mitochondrial morphogenesis, neuronal survival,and normal lifespan (Probable). The prohibitin complex, with DNAJC19,regulates cardiolipin remodeling and the protein turnover of OMA1 in acardiolipin-binding manner (By similarity). Also regulates cytochrome-coxidase assembly (COX) and mitochondrial respiration (PubMed:20959514,PubMed:11302691). Binding to sphingoid 1-phosphate (SPP) modulates itsregulator activity (PubMed:20959514, PubMed:11302691). Has a key roleof mitophagy receptor involved in targeting mitochondria for autophagicdegradation (PubMed:28017329). Involved in mitochondrial-mediatedantiviral innate immunity, activates DDX58/RIG-I-mediated signaltransduction and production of IFNB1 and proinflammatory cytokine IL6(PubMed:31522117). {ECO:0000250|UniProtKB:O35129,ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117,ECO:0000305|PubMed:25904163}.; In the nucleus, serves as transcriptional co-regulator(Probable). Acts as a mediator of transcriptional repression by nuclearhormone receptors via recruitment of histone deacetylases. Functions asan estrogen receptor (ER)-selective coregulator that potentiates theinhibitory activities of antiestrogens and represses the activity ofestrogens. Competes with NCOA1 for modulation of ER transcriptionalactivity (By similarity). {ECO:0000250|UniProtKB:O35129,ECO:0000305|PubMed:25904163}.; In the plasma membrane, is involved in IGFBP6-induced cellmigration (PubMed:24003225). Cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 producedthrough the activation of distal signaling intermediates. Upon CD40engagement, required to activate NF-kappa-B signaling pathway viaphospholipase C and protein kinase C activation (By similarity).{ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:24003225}.; (Microbial infection) Involved in human enterovirus 71/EV-71infection by enhancing the autophagy mechanism during the infection.{ECO:0000269|PubMed:32276428}.",
"references": [
"RC03875"
]
},
{
"targ_id": "T261",
"parent_targ_id": "T",
"full_name": "Thiosulfate sulfurtransferase",
"abbrev": "Rhodanese",
"protein_names": "Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese)",
"related_func_ids": "F060103",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q16762",
"Uniprot_name": "THTR_HUMAN",
"EC_numbers": "2.8.1.1",
"gene_symbol": "TST",
"gene_synonyms": "RDS",
"gene_synonyms_links": "",
"gene_name": "Thiosulfate sulfurtransferase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000128311",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +thiocyanate",
"targ_desciption": "Formation of iron-sulfur complexes, cyanide detoxification ormodification of sulfur-containing enzymes. Other thiol compounds,besides cyanide, can act as sulfur ion acceptors. Also has weakmercaptopyruvate sulfurtransferase (MST) activity (By similarity).Together with MRPL18, acts as a mitochondrial import factor for thecytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is ableto bind to the 5S rRNA. {ECO:0000250, ECO:0000269|PubMed:20663881,ECO:0000269|PubMed:21685364}.",
"references": []
},
{
"targ_id": "T283",
"parent_targ_id": "T",
"full_name": "Alanine--tRNA ligase, mitochondrial",
"abbrev": "AlaRS",
"protein_names": "Alanine--tRNA ligase, mitochondrial (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q5JTZ9",
"Uniprot_name": "SYAM_HUMAN",
"EC_numbers": "6.1.1.7",
"gene_symbol": "AARS2",
"gene_synonyms": "AARSL, bA444E17.1, KIAA1270",
"gene_synonyms_links": "",
"gene_name": "Alanyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000124608",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)",
"targ_desciption": "Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP andthen transferred to the acceptor end of tRNA(Ala). Also editsincorrectly charged tRNA(Ala) via its editing domain.{ECO:0000255|HAMAP-Rule:MF_03133}.",
"references": []
},
{
"targ_id": "T284",
"parent_targ_id": "T",
"full_name": "Probable cysteine--tRNA ligase, mitochondrial",
"abbrev": "CysRS",
"protein_names": "Probable cysteine--tRNA ligase, mitochondrial (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9HA77",
"Uniprot_name": "SYCM_HUMAN",
"EC_numbers": "6.1.1.16",
"gene_symbol": "CARS2",
"gene_synonyms": "FLJ12118",
"gene_synonyms_links": "",
"gene_name": "Cysteinyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000134905",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T285",
"parent_targ_id": "T",
"full_name": "Aspartate--tRNA ligase, cytoplasmic",
"abbrev": "AspRS",
"protein_names": "Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Cell proliferation-inducing gene 40 protein)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "P14868",
"Uniprot_name": "SYDC_HUMAN",
"EC_numbers": "6.1.1.12",
"gene_symbol": "DARS1 DARS PIG40",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm, cytosol",
"reaction": "ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)",
"targ_desciption": "Catalyzes the specific attachment of an amino acid to itscognate tRNA in a 2 step reaction: the amino acid (AA) is firstactivated by ATP to form AA-AMP and then transferred to the acceptorend of the tRNA. {ECO:0000250|UniProtKB:P15178}.",
"references": []
},
{
"targ_id": "T286",
"parent_targ_id": "T",
"full_name": "Aspartate--tRNA ligase, mitochondrial",
"abbrev": "AspRS",
"protein_names": "Aspartate--tRNA ligase, mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q6PI48",
"Uniprot_name": "SYDM_HUMAN",
"EC_numbers": "6.1.1.12",
"gene_symbol": "DARS2",
"gene_synonyms": "FLJ10514",
"gene_synonyms_links": "",
"gene_name": "Aspartyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000117593",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T287",
"parent_targ_id": "T",
"full_name": "Probable glutamate--tRNA ligase, mitochondrial",
"abbrev": "GluRS",
"protein_names": "Probable glutamate--tRNA ligase, mitochondrial (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q5JPH6",
"Uniprot_name": "SYEM_HUMAN",
"EC_numbers": "6.1.1.17",
"gene_symbol": "EARS2",
"gene_synonyms": "KIAA1970, MSE1",
"gene_synonyms_links": "",
"gene_name": "Glutamyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000103356",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)",
"targ_desciption": "Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP andthen transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.",
"references": []
},
{
"targ_id": "T288",
"parent_targ_id": "T",
"full_name": "Phenylalanine--tRNA ligase, mitochondrial",
"abbrev": "PheRS",
"protein_names": "Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "O95363",
"Uniprot_name": "SYFM_HUMAN",
"EC_numbers": "6.1.1.20",
"gene_symbol": "FARS2",
"gene_synonyms": "dJ236A3.1, FARS1",
"gene_synonyms_links": "",
"gene_name": "Phenylalanyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000145982",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Mitochondrion",
"reaction": "ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +L-phenylalanyl-tRNA(Phe)",
"targ_desciption": "Is responsible for the charging of tRNA(Phe) withphenylalanine in mitochondrial translation. To a lesser extent, alsocatalyzes direct attachment of m-Tyr (an oxidized version of Phe) totRNA(Phe), thereby opening the way for delivery of the misacylated tRNAto the ribosome and incorporation of ROS-damaged amino acid intoproteins. {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}.",
"references": []
},
{
"targ_id": "T289",
"parent_targ_id": "T",
"full_name": "Glycine--tRNA ligase",
"abbrev": "GlyRS",
"protein_names": "Glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase) (GlyRS) (Glycyl-tRNA synthetase 1)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Hydrolase, Ligase, Transferase",
"Uniport_ID": "P41250",
"Uniprot_name": "GARS_HUMAN",
"EC_numbers": "6.1.1.14; 2.7.7.-",
"gene_symbol": "GARS",
"gene_synonyms": "CMT2D, DSMAV, GlyRS, SMAD1",
"gene_synonyms_links": "",
"gene_name": "Glycyl-tRNA synthetase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000106105",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Mitochondrion; Cell projection, axon; Secreted; Secreted, extracellular exosome",
"reaction": "ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly); 2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl)tetraphosphate",
"targ_desciption": "Catalyzes the ATP-dependent ligation of glycine to the 3'-endof its cognate tRNA, via the formation of an aminoacyl-adenylateintermediate (Gly-AMP) (PubMed:17544401, PubMed:28675565,PubMed:24898252). Also produces diadenosine tetraphosphate (Ap4A), auniversal pleiotropic signaling molecule needed for cell regulationpathways, by direct condensation of 2 ATPs. Thereby, may play a specialrole in Ap4A homeostasis (PubMed:19710017).{ECO:0000269|PubMed:17544401, ECO:0000269|PubMed:19710017,ECO:0000269|PubMed:24898252, ECO:0000269|PubMed:28675565}.",
"references": []
},
{
"targ_id": "T290",
"parent_targ_id": "T",
"full_name": "Histidine--tRNA ligase, mitochondrial",
"abbrev": "HisRS",
"protein_names": "Histidine--tRNA ligase, mitochondrial (EC 6.1.1.21) (Histidine--tRNA ligase-like) (Histidyl-tRNA synthetase) (HisRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "P49590",
"Uniprot_name": "SYHM_HUMAN",
"EC_numbers": "6.1.1.21",
"gene_symbol": "HARS2",
"gene_synonyms": "HARSL, HARSR, HO3",
"gene_synonyms_links": "",
"gene_name": "Histidyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000112855",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)",
"targ_desciption": "Mitochondrial aminoacyl-tRNA synthetase that catalyzes theATP-dependent ligation of histidine to the 3'-end of its cognate tRNA,via the formation of an aminoacyl-adenylate intermediate (His-AMP).{ECO:0000269|PubMed:21464306}.",
"references": []
},
{
"targ_id": "T291",
"parent_targ_id": "T",
"full_name": "Isoleucine--tRNA ligase, cytoplasmic",
"abbrev": "IleRS",
"protein_names": "Isoleucine--tRNA ligase, cytoplasmic (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IRS) (IleRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "P41252",
"Uniprot_name": "SYIC_HUMAN",
"EC_numbers": "6.1.1.5",
"gene_symbol": "IARS1 IARS",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Cytoplasm, cytosol",
"reaction": "ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)",
"targ_desciption": "Catalyzes the specific attachment of an amino acid to itscognate tRNA in a 2 step reaction: the amino acid (AA) is firstactivated by ATP to form AA-AMP and then transferred to the acceptorend of the tRNA. {ECO:0000269|PubMed:8052601}.",
"references": []
},
{
"targ_id": "T292",
"parent_targ_id": "T",
"full_name": "Isoleucine--tRNA ligase, mitochondrial",
"abbrev": "IleRS",
"protein_names": "Isoleucine--tRNA ligase, mitochondrial (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9NSE4",
"Uniprot_name": "SYIM_HUMAN",
"EC_numbers": "6.1.1.5",
"gene_symbol": "IARS2",
"gene_synonyms": "FLJ10326",
"gene_synonyms_links": "",
"gene_name": "Isoleucyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000067704",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T293",
"parent_targ_id": "T",
"full_name": "Lysine--tRNA ligase",
"abbrev": "LysRS",
"protein_names": "Lysine--tRNA ligase (EC 2.7.7.-) (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase, Transferase",
"Uniport_ID": "Q15046",
"Uniprot_name": "SYK_HUMAN",
"EC_numbers": "2.7.7.-; 6.1.1.6",
"gene_symbol": "KARS",
"gene_synonyms": "DFNB89, KARS1, KARS2",
"gene_synonyms_links": "",
"gene_name": "Lysyl-tRNA synthetase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000065427",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform Cytoplasmic]: Cytoplasm, cytosol; Cytoplasm; Nucleus; Cell membrane; Peripheral membrane protein; Secreted",
"reaction": "ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)",
"targ_desciption": "Catalyzes the specific attachment of an amino acid to itscognate tRNA in a 2 step reaction: the amino acid (AA) is firstactivated by ATP to form AA-AMP and then transferred to the acceptorend of the tRNA (PubMed:9278442, PubMed:18029264, PubMed:18272479).When secreted, acts as a signaling molecule that induces immuneresponse through the activation of monocyte/macrophages(PubMed:15851690). Catalyzes the synthesis of the signaling moleculediadenosine tetraphosphate (Ap4A), and thereby mediates disruption ofthe complex between HINT1 and MITF and the concomitant activation ofMITF transcriptional activity (PubMed:5338216, PubMed:14975237,PubMed:19524539, PubMed:23159739). {ECO:0000269|PubMed:14975237,ECO:0000269|PubMed:15851690, ECO:0000269|PubMed:18029264,ECO:0000269|PubMed:19524539, ECO:0000269|PubMed:28887846,ECO:0000269|PubMed:5338216, ECO:0000269|PubMed:9278442}.; (Microbial infection) Interacts with HIV-1 virus GAG protein,facilitating the selective packaging of tRNA(3)(Lys), the primer forreverse transcription initiation. {ECO:0000269|PubMed:15220430}.",
"references": []
},
{
"targ_id": "T294",
"parent_targ_id": "T",
"full_name": "Leucine--tRNA ligase, cytoplasmic",
"abbrev": "LeuRS",
"protein_names": "Leucine--tRNA ligase, cytoplasmic (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "Q9P2J5",
"Uniprot_name": "SYLC_HUMAN",
"EC_numbers": "6.1.1.4",
"gene_symbol": "LARS1 KIAA1352 LARS",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm",
"reaction": "ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)",
"targ_desciption": "Catalyzes the specific attachment of an amino acid to itscognate tRNA in a two step reaction: the amino acid (AA) is firstactivated by ATP to form AA-AMP and then transferred to the acceptorend of the tRNA. Exhibits a post-transfer editing activity to hydrolyzemischarged tRNAs. {ECO:0000269|PubMed:19426743}.",
"references": []
},
{
"targ_id": "T295",
"parent_targ_id": "T",
"full_name": "Probable leucine--tRNA ligase, mitochondrial",
"abbrev": "LeuRS",
"protein_names": "Probable leucine--tRNA ligase, mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q15031",
"Uniprot_name": "SYLM_HUMAN",
"EC_numbers": "6.1.1.4",
"gene_symbol": "LARS2",
"gene_synonyms": "KIAA0028, LEURS, MGC26121, mtLeuRS",
"gene_synonyms_links": "",
"gene_name": "Leucyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000011376",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T296",
"parent_targ_id": "T",
"full_name": "Methionine--tRNA ligase, mitochondrial",
"abbrev": "MtMetRS",
"protein_names": "Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Methionyl-tRNA synthetase 2) (Mitochondrial methionyl-tRNA synthetase) (MtMetRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q96GW9",
"Uniprot_name": "SYMM_HUMAN",
"EC_numbers": "6.1.1.10",
"gene_symbol": "MARS2",
"gene_synonyms": "mtMetRS, SPAX3",
"gene_synonyms_links": "",
"gene_name": "Methionyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000247626",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T297",
"parent_targ_id": "T",
"full_name": "Probable asparagine--tRNA ligase, mitochondrial",
"abbrev": "AsnRS",
"protein_names": "Probable asparagine--tRNA ligase, mitochondrial (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q96I59",
"Uniprot_name": "SYNM_HUMAN",
"EC_numbers": "6.1.1.22",
"gene_symbol": "NARS2",
"gene_synonyms": "DFNB94, FLJ23441, SLM5",
"gene_synonyms_links": "",
"gene_name": "Asparaginyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000137513",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Mitochondrion",
"reaction": "ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T298",
"parent_targ_id": "T",
"full_name": "Probable proline--tRNA ligase, mitochondrial",
"abbrev": "ProRS",
"protein_names": "Probable proline--tRNA ligase, mitochondrial (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q7L3T8",
"Uniprot_name": "SYPM_HUMAN",
"EC_numbers": "6.1.1.15",
"gene_symbol": "PARS2",
"gene_synonyms": "DKFZp727A071",
"gene_synonyms_links": "",
"gene_name": "Prolyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000162396",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T299",
"parent_targ_id": "T",
"full_name": "Glutamine--tRNA ligase",
"abbrev": "GlnRS",
"protein_names": "Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "P47897",
"Uniprot_name": "SYQ_HUMAN",
"EC_numbers": "6.1.1.18",
"gene_symbol": "QARS",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Glutaminyl-tRNA synthetase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000172053",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm, cytosol; Cytoplasm",
"reaction": "ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)",
"targ_desciption": "Glutamine--tRNA ligase (PubMed:26869582). Plays a criticalrole in brain development (PubMed:24656866).{ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:26869582}.",
"references": []
},
{
"targ_id": "T300",
"parent_targ_id": "T",
"full_name": "Probable arginine--tRNA ligase, mitochondrial",
"abbrev": "ArgRS",
"protein_names": "Probable arginine--tRNA ligase, mitochondrial (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q5T160",
"Uniprot_name": "SYRM_HUMAN",
"EC_numbers": "6.1.1.19",
"gene_symbol": "RARS2",
"gene_synonyms": "DALRD2, dJ382I10.6, MGC14993, MGC23778, PRO1992, RARSL",
"gene_synonyms_links": "",
"gene_name": "Arginyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000146282",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T301",
"parent_targ_id": "T",
"full_name": "Serine--tRNA ligase, mitochondrial",
"abbrev": "SerRS",
"protein_names": "Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9NP81",
"Uniprot_name": "SYSM_HUMAN",
"EC_numbers": "6.1.1.11",
"gene_symbol": "SARS2",
"gene_synonyms": "FLJ20450, mtSerRS, SARS, SARSM, SerRSmt, SERS, SYS",
"gene_synonyms_links": "",
"gene_name": "Seryl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000104835",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec)",
"targ_desciption": "Catalyzes the attachment of serine to tRNA(Ser). Is alsoprobably able to aminoacylate tRNA(Sec) with serine, to form themisacylated tRNA L-seryl-tRNA(Sec), which will be further convertedinto selenocysteinyl-tRNA(Sec). {ECO:0000250|UniProtKB:Q9N0F3}.",
"references": []
},
{
"targ_id": "T302",
"parent_targ_id": "T",
"full_name": "Threonine--tRNA ligase, mitochondrial",
"abbrev": "ThrRS",
"protein_names": "Threonine--tRNA ligase, mitochondrial (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase-like 1)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9BW92",
"Uniprot_name": "SYTM_HUMAN",
"EC_numbers": "6.1.1.3",
"gene_symbol": "TARS2",
"gene_synonyms": "FLJ12528, TARSL1",
"gene_synonyms_links": "",
"gene_name": "Threonyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000143374",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)",
"targ_desciption": "Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP andthen transferred to the acceptor end of tRNA(Thr). Also editsincorrectly charged tRNA(Thr) via its editing domain.{ECO:0000269|PubMed:26811336}.",
"references": []
},
{
"targ_id": "T303",
"parent_targ_id": "T",
"full_name": "Valine--tRNA ligase, mitochondrial",
"abbrev": "ValRS",
"protein_names": "Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (Valyl-tRNA synthetase-like)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q5ST30",
"Uniprot_name": "SYVM_HUMAN",
"EC_numbers": "6.1.1.9",
"gene_symbol": "VARS2",
"gene_synonyms": "DKFZP434L1435, G7a, KIAA1885, VARS2L, VARSL",
"gene_synonyms_links": "",
"gene_name": "Valyl-tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000137411",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T304",
"parent_targ_id": "T",
"full_name": "Tryptophan--tRNA ligase, mitochondrial",
"abbrev": "TrpRS",
"protein_names": "Tryptophan--tRNA ligase, mitochondrial (EC 6.1.1.2) ((Mt)TrpRS) (Tryptophanyl-tRNA synthetase) (TrpRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9UGM6",
"Uniprot_name": "SYWM_HUMAN",
"EC_numbers": "6.1.1.2",
"gene_symbol": "WARS2",
"gene_synonyms": "TrpRS",
"gene_synonyms_links": "",
"gene_name": "Tryptophanyl tRNA synthetase 2, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000116874",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)",
"targ_desciption": "Mitochondrial aminoacyl-tRNA synthetase that activate andtransfer the amino acids to their corresponding tRNAs during thetranslation of mitochondrial genes and protein synthesis.{ECO:0000305|PubMed:28650581}.",
"references": []
},
{
"targ_id": "T305",
"parent_targ_id": "T",
"full_name": "Tyrosine--tRNA ligase, mitochondrial",
"abbrev": "TyrRS",
"protein_names": "Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Aminoacyl-tRNA synthetase, Ligase",
"Uniport_ID": "Q9Y2Z4",
"Uniprot_name": "SYYM_HUMAN",
"EC_numbers": "6.1.1.1",
"gene_symbol": "YARS2",
"gene_synonyms": "CGI-04, FLJ13995, mt-TyrRS",
"gene_synonyms_links": "",
"gene_name": "Tyrosyl-tRNA synthetase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000139131",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)",
"targ_desciption": "Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP andthen transferred to the acceptor end of tRNA(Tyr).{ECO:0000269|PubMed:15779907, ECO:0000269|PubMed:17997975}.",
"references": []
},
{
"targ_id": "T306",
"parent_targ_id": "T",
"full_name": "Zinc phosphodiesterase ELAC protein 2",
"abbrev": "tRNase Z 2",
"protein_names": "Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Heredity prostate cancer protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Endonuclease, Hydrolase, Nuclease",
"Uniport_ID": "Q9BQ52",
"Uniprot_name": "RNZ2_HUMAN",
"EC_numbers": "3.1.26.11",
"gene_symbol": "ELAC2",
"gene_synonyms": "FLJ10530, HPC2",
"gene_synonyms_links": "",
"gene_name": "ElaC ribonuclease Z 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000006744",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Nucleus",
"reaction": "Endonucleolytic cleavage of RNA, removing extra 3' nucleotidesfrom tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxygroup is left at the tRNA terminus and a 5'-phosphoryl group is leftat the trailer molecule.",
"targ_desciption": "Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, byremoving a 3'-trailer from precursor tRNA.{ECO:0000269|PubMed:21593607}.",
"references": []
},
{
"targ_id": "T307",
"parent_targ_id": "T",
"full_name": "Methionyl-tRNA formyltransferase, mitochondrial",
"abbrev": "MtFMT",
"protein_names": "Methionyl-tRNA formyltransferase, mitochondrial (MtFMT) (EC 2.1.2.9)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q96DP5",
"Uniprot_name": "FMT_HUMAN",
"EC_numbers": "2.1.2.9",
"gene_symbol": "MTFMT",
"gene_synonyms": "FMT1",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial methionyl-tRNA formyltransferase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000103707",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =(6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)",
"targ_desciption": "Formylates methionyl-tRNA in mitochondria. A single tRNA(Met)gene gives rise to both an initiator and an elongator species via anunknown mechanism (By similarity). {ECO:0000250}.",
"references": []
},
{
"targ_id": "T308",
"parent_targ_id": "T",
"full_name": "tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial",
"abbrev": "NOL1",
"protein_names": "tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 3)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Methyltransferase, Transferase",
"Uniport_ID": "Q9H649",
"Uniprot_name": "NSUN3_HUMAN",
"EC_numbers": "2.1.1.-",
"gene_symbol": "NSUN3",
"gene_synonyms": "FLJ22609",
"gene_synonyms_links": "",
"gene_name": "NOP2/Sun RNA methyltransferase family member 3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000178694",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "cytidine(34) in mitochondrial tRNA + S-adenosyl-L-methionine =5-methylcytidine(34) in mitochondrial tRNA + H(+) + S-adenosyl-L-homocysteine",
"targ_desciption": "Mitochondrial tRNA methyltransferase that mediatesmethylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-tRNA(Met) (PubMed:27497299, PubMed:27214402, PubMed:27356879). mt-tRNA(Met) methylation at cytosine(34) takes place at the wobbleposition of the anticodon and initiates the formation of 5-formylcytosine (f(5)c) at this position (PubMed:27497299,PubMed:27214402, PubMed:27356879). mt-tRNA(Met) containing the f(5)cmodification at the wobble position enables recognition of the AUAcodon in addition to the AUG codon, expanding codon recognition inmitochondrial translation (PubMed:27497299, PubMed:27356879).{ECO:0000269|PubMed:27214402, ECO:0000269|PubMed:27356879,ECO:0000269|PubMed:27497299}.",
"references": []
},
{
"targ_id": "T309",
"parent_targ_id": "T",
"full_name": "2',5'-phosphodiesterase 12",
"abbrev": "2-PDE",
"protein_names": "2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Exonuclease, Hydrolase, Nuclease",
"Uniport_ID": "Q6L8Q7",
"Uniprot_name": "PDE12_HUMAN",
"EC_numbers": "3.1.4.-; 3.1.13.4",
"gene_symbol": "PDE12",
"gene_synonyms": "2'-PDE, 3635, DKFZp667B1218",
"gene_synonyms_links": "",
"gene_name": "Phosphodiesterase 12",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000174840",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix",
"reaction": "Exonucleolytic cleavage of poly(A) to 5'-AMP.",
"targ_desciption": "Enzyme that cleaves 2',5'-phosphodiester bond linkingadenosines of the 5'-triphosphorylated oligoadenylates,triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5Asystem. Degrades triphosphorylated 2-5A to produce AMP and ATP(PubMed:26055709). Also cleaves 3',5'-phosphodiester bond ofoligoadenylates (PubMed:21666256, PubMed:30389976, PubMed:26055709).Plays a role as a negative regulator of the 2-5A system that is one ofthe major pathways for antiviral and antitumor functions induced byinterferons (IFNs). Suppression of this enzyme increases cellular 2-5Alevels and decreases viral replication in cultured small-airwayepithelial cells and Hela cells (PubMed:26055709).{ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038,ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541,ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976}.",
"references": []
},
{
"targ_id": "T310",
"parent_targ_id": "T",
"full_name": "Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial",
"abbrev": "Gln",
"protein_names": "Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Glu-AdT subunit A) (EC 6.3.5.7) (Glutaminyl-tRNA synthase-like protein 1)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "Q9H0R6",
"Uniprot_name": "GATA_HUMAN",
"EC_numbers": "6.3.5.7",
"gene_symbol": "QRSL1",
"gene_synonyms": "DKFZP564C1278, FLJ10989, FLJ12189, FLJ13447, GatA",
"gene_synonyms_links": "",
"gene_name": "Glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000130348",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate",
"targ_desciption": "Allows the formation of correctly charged Gln-tRNA(Gln)through the transamidation of misacylated Glu-tRNA(Gln) in themitochondria. The reaction takes place in the presence of glutamine andATP through an activated gamma-phospho-Glu-tRNA(Gln).{ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:19805282}.",
"references": []
},
{
"targ_id": "T311",
"parent_targ_id": "T",
"full_name": "tRNA dimethylallyltransferase",
"abbrev": "hGRO1",
"protein_names": "tRNA dimethylallyltransferase (EC 2.5.1.75) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (hGRO1) (tRNA isopentenyltransferase 1) (IPTase)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Transferase",
"Uniport_ID": "Q9H3H1",
"Uniprot_name": "MOD5_HUMAN",
"EC_numbers": "2.5.1.75",
"gene_symbol": "TRIT1",
"gene_synonyms": "FLJ20061, IPT",
"gene_synonyms_links": "",
"gene_name": "TRNA isopentenyltransferase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000043514",
"omim_id": "",
"genecard_link": "",
"locs": "[Isoform 1]: Mitochondrion; [Isoform 4]: Mitochondrion; [Isoform 2]: Cytoplasm; [Isoform 3]: Cytoplasm; [Isoform 5]: Cytoplasm",
"reaction": "adenosine(37) in tRNA + dimethylallyl diphosphate =diphosphate + N(6)-dimethylallyladenosine(37) in tRNA",
"targ_desciption": "Catalyzes the transfer of a dimethylallyl group onto theadenine at position 37 of both cytosolic and mitochondrial tRNAs,leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).{ECO:0000269|PubMed:11111046, ECO:0000269|PubMed:24901367}.",
"references": []
},
{
"targ_id": "T312",
"parent_targ_id": "T",
"full_name": "tRNA (guanine(37)-N1)-methyltransferase",
"abbrev": "tRNA [GM37] methyltransferase",
"protein_names": "tRNA (guanine(37)-N1)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5 homolog)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Methyltransferase, Transferase",
"Uniport_ID": "Q32P41",
"Uniprot_name": "TRM5_HUMAN",
"EC_numbers": "2.1.1.228",
"gene_symbol": "TRMT5",
"gene_synonyms": "KIAA1393, TRM5",
"gene_synonyms_links": "",
"gene_name": "TRNA methyltransferase 5",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000126814",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Nucleus; Cytoplasm",
"reaction": "guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine",
"targ_desciption": "Involved in mitochondrial tRNA methylation (PubMed:26189817).Specifically methylates the N1 position of guanosine-37 in varioustRNAs. Methylation is not dependent on the nature of the nucleoside 5'of the target nucleoside. This is the first step in the biosynthesis ofwybutosine (yW), a modified base adjacent to the anticodon of tRNAs andrequired for accurate decoding. {ECO:0000269|PubMed:26189817}.",
"references": []
},
{
"targ_id": "T313",
"parent_targ_id": "T",
"full_name": "tRNA methyltransferase 10 homolog C",
"abbrev": "Mitochondrial ribonuclease P protein 1",
"protein_names": "tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Methyltransferase, Transferase",
"Uniport_ID": "Q7L0Y3",
"Uniprot_name": "TM10C_HUMAN",
"EC_numbers": "2.1.1.-; 2.1.1.218; 2.1.1.221",
"gene_symbol": "TRMT10C",
"gene_synonyms": "FLJ20432, MRPP1, RG9MTD1",
"gene_synonyms_links": "",
"gene_name": "TRNA methyltransferase 10C, mitochondrial RNase P subunit",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000174173",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix, mitochondrion nucleoid",
"reaction": "adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine; guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine; adenosine in mRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine in mRNA + S-adenosyl-L-homocysteine",
"targ_desciption": "Mitochondrial tRNA N(1)-methyltransferase involved inmitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607,PubMed:23042678, PubMed:27132592). Component of mitochondrialribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 andPRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends(PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex ofthe mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, whichdisplays functions that are independent of the ribonuclease P activity(PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplexcatalyzes the formation of N(1)-methylguanine and N(1)-methyladenine atposition 9 (m1G9 and m1A9, respectively) in tRNAs. TRMT10C/MRPP1 actingas the catalytic N(1)-methyltransferase subunit (PubMed:23042678). TheMRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform:following 5'-end cleavage by the mitochondrial ribonuclease P complex,the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processingcatalyzed by ELAC2, retains the tRNA product after ELAC2 processing andpresents the nascent tRNA to the mitochondrial CCA tRNAnucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition totRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNAN(1)-methyltransferase by mediating methylation of adenosine residuesat the N(1) position of MT-ND5 mRNA (PubMed:29072297).{ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:21593607,ECO:0000269|PubMed:23042678, ECO:0000269|PubMed:27132592,ECO:0000269|PubMed:29040705, ECO:0000269|PubMed:29072297}.",
"references": []
},
{
"targ_id": "T314",
"parent_targ_id": "T",
"full_name": "CCA tRNA nucleotidyltransferase 1, mitochondrial",
"abbrev": "mt CCA-adding enzyme",
"protein_names": "CCA tRNA nucleotidyltransferase 1, mitochondrial (EC 2.7.7.72) (Mitochondrial tRNA nucleotidyl transferase, CCA-adding) (mt CCA-adding enzyme) (mt tRNA CCA-diphosphorylase) (mt tRNA CCA-pyrophosphorylase) (mt tRNA adenylyltransferase)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "Nucleotidyltransferase, Transferase",
"Uniport_ID": "Q96Q11",
"Uniprot_name": "TRNT1_HUMAN",
"EC_numbers": "2.7.7.72",
"gene_symbol": "TRNT1",
"gene_synonyms": "CCA1, CGI-47, MtCCA",
"gene_synonyms_links": "",
"gene_name": "TRNA nucleotidyl transferase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000072756",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3diphosphate",
"targ_desciption": "[Isoform 1]: Adds and repairs the conserved 3'-CCA sequencenecessary for the attachment of amino acids to the 3' terminus of tRNAmolecules, using CTP and ATP as substrates.{ECO:0000269|PubMed:11504732}.; [Isoform 2]: Adds 2 C residues (CC-) to the 3' terminus oftRNA molecules instead of a complete CCA end as isoform 1 does (invitro). {ECO:0000269|PubMed:17204286}.",
"references": []
},
{
"targ_id": "T315",
"parent_targ_id": "T",
"full_name": "Mitochondrial-derived peptide MOTS-c",
"abbrev": "Mitochondrial open reading frame of the 12S rRNA-c",
"protein_names": "Mitochondrial-derived peptide MOTS-c (Mitochondrial open reading frame of the 12S rRNA-c)",
"related_func_ids": "F060103",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "A0A0C5B5G6",
"Uniprot_name": "MOTSC_HUMAN",
"EC_numbers": "",
"gene_symbol": "MT-RNR1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Secreted",
"reaction": "",
"targ_desciption": "Regulates insulin sensitivity and metabolic homeostasis.Inhibits the folate cycle, thereby reducing de novo purine biosynthesiswhich leads to the accumulation of the de novo purine synthesisintermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activationof the metabolic regulator 5'-AMP-activated protein kinase (AMPK).Protects against age-dependent and diet-induced insulin resistance aswell as diet-induced obesity. {ECO:0000269|PubMed:25738459}.",
"references": []
},
{
"targ_id": "T316",
"parent_targ_id": "T",
"full_name": "Humanin",
"abbrev": "HNM",
"protein_names": "Humanin (Humanin mitochondrial) (HNM)",
"related_func_ids": "F060103",
"category": "protein subunit",
"subcategories": "micropeptide",
"Uniport_ID": "Q8IVG9",
"Uniprot_name": "HUNIN_HUMAN",
"EC_numbers": "",
"gene_symbol": "MT-RNR2",
"gene_synonyms": "HN",
"gene_synonyms_links": "",
"gene_name": "",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "",
"omim_id": "",
"genecard_link": "",
"locs": "Secreted; Cytoplasm",
"reaction": "",
"targ_desciption": "Plays a role as a neuroprotective factor. Protects againstdeath induced by multiple different familial Alzheimer disease genesand amyloid-beta proteins in Alzheimer disease. Suppresses apoptosis bybinding to BAX and preventing the translocation of BAX from the cytosolto mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-inducedcell death Induces chemotaxis of mononuclear phagocytes via FPR2.Reduces the aggregation and fibrillary formation by suppressing theeffect of APP on mononuclear phagocytes and acts by competitivelyinhibiting the access of FPRL1 to APP. {ECO:0000269|PubMed:11371646,ECO:0000269|PubMed:11717357, ECO:0000269|PubMed:12732850,ECO:0000269|PubMed:14561895, ECO:0000269|PubMed:15153530}.",
"references": []
},
{
"targ_id": "T317",
"parent_targ_id": "T",
"full_name": "Polyribonucleotide nucleotidyltransferase 1, mitochondrial",
"abbrev": "PNPase 1",
"protein_names": "Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC 2.7.7.8) (3'-5' RNA exonuclease OLD35) (PNPase old-35) (Polynucleotide phosphorylase 1) (PNPase 1) (Polynucleotide phosphorylase-like protein)",
"related_func_ids": "F060103",
"category": "enzyme",
"subcategories": "Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, RNA-binding, Transferase",
"Uniport_ID": "Q8TCS8",
"Uniprot_name": "PNPT1_HUMAN",
"EC_numbers": "2.7.7.8",
"gene_symbol": "PNPT1",
"gene_synonyms": "DFNB70, old-35, OLD35, PNPase",
"gene_synonyms_links": "",
"gene_name": "Polyribonucleotide nucleotidyltransferase 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000138035",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Mitochondrion matrix; Mitochondrion intermembrane space; Peripheral membrane protein",
"reaction": "phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +RNA(n)",
"targ_desciption": "RNA-binding protein implicated in numerous RNA metabolicprocesses. Catalyzes the phosphorolysis of single-strandedpolyribonucleotides processively in the 3'-to-5' direction.Mitochondrial intermembrane factor with RNA-processing exoribonuleaseactivity. Component of the mitochondrial degradosome (mtEXO) complex,that degrades 3' overhang double-stranded RNA with a 3'-to-5'directionality in an ATP-dependent manner. Involved in the degradationof non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-likemolecules (PubMed:29967381). Required for correct processing andpolyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmicRNA import factor that mediates the translocation of small RNAcomponents, like the 5S RNA, the RNA subunit of ribonuclease P and themitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.Plays a role in mitochondrial morphogenesis and respiration. regulatesthe expression of the electron transport chain (ETC) components at themRNA and protein levels. In the cytoplasm, shows a 3'-to-5'exoribonuclease mediating mRNA degradation activity. degrades c-mycmRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrestin melanoma cells. Regulates the stability of specific mature miRNAs inmelanoma cells. specifically and selectively degrades miR-221,preferentially. Plays also a role in RNA cell surveillance by cleaningup oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNAand miR-221 microRNA. {ECO:0000269|PubMed:12473748,ECO:0000269|PubMed:12721301, ECO:0000269|PubMed:12798676,ECO:0000269|PubMed:16055741, ECO:0000269|PubMed:16410805,ECO:0000269|PubMed:16934922, ECO:0000269|PubMed:18083836,ECO:0000269|PubMed:18083837, ECO:0000269|PubMed:18501193,ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:20547861,ECO:0000269|PubMed:20691904, ECO:0000269|PubMed:29967381}.",
"references": []
},
{
"targ_id": "T318",
"parent_targ_id": "T",
"full_name": "Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial",
"abbrev": "Gln",
"protein_names": "Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial (Glu-AdT subunit B) (EC 6.3.5.-) (Cytochrome c oxidase assembly factor PET112 homolog)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "Ligase",
"Uniport_ID": "O75879",
"Uniprot_name": "GATB_HUMAN",
"EC_numbers": "6.3.5.-",
"gene_symbol": "GATB",
"gene_synonyms": "PET112, PET112L",
"gene_synonyms_links": "",
"gene_name": "Glutamyl-tRNA amidotransferase subunit B",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000059691",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate",
"targ_desciption": "Allows the formation of correctly charged Gln-tRNA(Gln)through the transamidation of misacylated Glu-tRNA(Gln) in themitochondria. The reaction takes place in the presence of glutamine andATP through an activated gamma-phospho-Glu-tRNA(Gln).{ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:19805282}.",
"references": []
},
{
"targ_id": "T319",
"parent_targ_id": "T",
"full_name": "GTPase Era, mitochondrial",
"abbrev": "hERA",
"protein_names": "GTPase Era, mitochondrial (H-ERA) (hERA) (Conserved ERA-like GTPase) (CEGA) (ERA-W) (ERA-like protein 1)",
"related_func_ids": "F060401",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "O75616",
"Uniprot_name": "ERAL1_HUMAN",
"EC_numbers": "",
"gene_symbol": "ERAL1",
"gene_synonyms": "HERA-B",
"gene_synonyms_links": "",
"gene_name": "Era like 12S mitochondrial rRNA chaperone 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000132591",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion matrix; Mitochondrion inner membrane; Peripheral membrane protein",
"reaction": "",
"targ_desciption": "Probable GTPase that plays a role in the mitochondrialribosomal small subunit assembly. Specifically binds the 12Smitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineatingthe 3' terminal stem-loop region. May act as a chaperone that protectsthe 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal smallsubunit assembly. {ECO:0000269|PubMed:20430825,ECO:0000269|PubMed:20604745, ECO:0000269|PubMed:28449065}.",
"references": []
},
{
"targ_id": "T320",
"parent_targ_id": "T",
"full_name": "39S ribosomal protein L3, mitochondrial",
"abbrev": "MRP-L3",
"protein_names": "39S ribosomal protein L3, mitochondrial (L3mt) (MRP-L3) (Mitochondrial large ribosomal subunit protein uL3m)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "P09001",
"Uniprot_name": "RM03_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPL3",
"gene_synonyms": "MRL3, RPML3",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein L3",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000114686",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": [
"RC03829"
]
},
{
"targ_id": "T321",
"parent_targ_id": "T",
"full_name": "39S ribosomal protein L12, mitochondrial",
"abbrev": "MRP-L12",
"protein_names": "39S ribosomal protein L12, mitochondrial (L12mt) (MRP-L12) (5c5-2) (Mitochondrial large ribosomal subunit protein bL12m)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "P52815",
"Uniprot_name": "RM12_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPL12",
"gene_synonyms": "MRPL7, MRPL7/L12, RPML12",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein L12",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000262814",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Associates with mitochondrial RNA polymerase to activatetranscription. {ECO:0000269|PubMed:22003127}.",
"references": []
},
{
"targ_id": "T322",
"parent_targ_id": "T",
"full_name": "39S ribosomal protein L44, mitochondrial",
"abbrev": "MRP-L44",
"protein_names": "39S ribosomal protein L44, mitochondrial (L44mt) (MRP-L44) (EC 3.1.26.-) (Mitochondrial large ribosomal subunit protein mL44)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "Q9H9J2",
"Uniprot_name": "RM44_HUMAN",
"EC_numbers": "3.1.26.-",
"gene_symbol": "MRPL44",
"gene_synonyms": "FLJ12701, FLJ13990",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein L44",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000135900",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Component of the 39S subunit of mitochondrial ribosome. Mayhave a function in the assembly/stability of nascent mitochondrialpolypeptides exiting the ribosome. {ECO:0000269|PubMed:23315540}.",
"references": []
},
{
"targ_id": "T323",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S2, mitochondrial",
"abbrev": "MRP-S2",
"protein_names": "28S ribosomal protein S2, mitochondrial (MRP-S2) (S2mt) (Mitochondrial small ribosomal subunit protein uS2m)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "Q9Y399",
"Uniprot_name": "RT02_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS2",
"gene_synonyms": "CGI-91",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000122140",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Required for mitoribosome formation and stability, andmitochondrial translation. {ECO:0000269|PubMed:29576219}.",
"references": []
},
{
"targ_id": "T324",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S7, mitochondrial",
"abbrev": "MRP-S7",
"protein_names": "28S ribosomal protein S7, mitochondrial (MRP-S7) (S7mt) (Mitochondrial small ribosomal subunit protein uS7m) (bMRP-27a) (bMRP27a)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "Q9Y2R9",
"Uniprot_name": "RT07_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS7",
"gene_synonyms": "MRP-S, RP-S7, RPMS7",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S7",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000125445",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T325",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S16, mitochondrial",
"abbrev": "MRP-S16",
"protein_names": "28S ribosomal protein S16, mitochondrial (MRP-S16) (S16mt) (Mitochondrial small ribosomal subunit protein bS16m)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "Q9Y3D3",
"Uniprot_name": "RT16_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS16",
"gene_synonyms": "CGI-132",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S16",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000182180",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T326",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S22, mitochondrial",
"abbrev": "MRP-S22",
"protein_names": "28S ribosomal protein S22, mitochondrial (MRP-S22) (S22mt) (Mitochondrial small ribosomal subunit protein mS22)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "P82650",
"Uniprot_name": "RT22_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS22",
"gene_synonyms": "C3orf5, GIBT, GK002, MRP-S22",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S22",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000175110",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T327",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S23, mitochondrial",
"abbrev": "MRP-S23",
"protein_names": "28S ribosomal protein S23, mitochondrial (MRP-S23) (S23mt) (Mitochondrial small ribosomal subunit protein mS23)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "Q9Y3D9",
"Uniprot_name": "RT23_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS23",
"gene_synonyms": "CGI-138, HSPC329, MRP-S23",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S23",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000181610",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "",
"references": []
},
{
"targ_id": "T328",
"parent_targ_id": "T",
"full_name": "28S ribosomal protein S34, mitochondrial",
"abbrev": "MRP-S34",
"protein_names": "28S ribosomal protein S34, mitochondrial (MRP-S34) (S34mt) (Mitochondrial small ribosomal subunit protein mS34)",
"related_func_ids": "F060401",
"category": "protein",
"subcategories": "Ribonucleoprotein, Ribosomal protein",
"Uniport_ID": "P82930",
"Uniprot_name": "RT34_HUMAN",
"EC_numbers": "",
"gene_symbol": "MRPS34",
"gene_synonyms": "MGC2616, MRP-S12",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial ribosomal protein S34",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000074071",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Required for mitochondrial translation, plays a role inmaintaining the stability of the small ribosomal subunit and the 12SrRNA that are required for mitoribosome formation.{ECO:0000269|PubMed:28777931}.",
"references": []
},
{
"targ_id": "T329",
"parent_targ_id": "T",
"full_name": "rRNA methyltransferase 2, mitochondrial",
"abbrev": "16S rRNA (uridine(1369",
"protein_names": "rRNA methyltransferase 2, mitochondrial (EC 2.1.1.-) (16S rRNA (uridine(1369)-2'-O)-methyltransferase) (16S rRNA [Um1369] 2'-O-methyltransferase) (Protein ftsJ homolog 2)",
"related_func_ids": "F060401",
"category": "enzyme",
"subcategories": "Methyltransferase, Transferase",
"Uniport_ID": "Q9UI43",
"Uniprot_name": "MRM2_HUMAN",
"EC_numbers": "2.1.1.-",
"gene_symbol": "MRM2",
"gene_synonyms": "FJH1, FTSJ2, RRMJ2",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial rRNA methyltransferase 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000122687",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "S-adenosyl-L-methionine + uridine(1369) in 16S rRNA = 2'-O-methyluridine(1369) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine",
"targ_desciption": "S-adenosyl-L-methionine-dependent 2'-O-ribosemethyltransferase that catalyzes the formation of 2'-O-methyluridine atposition 1369 (Um1369) in the 16S mitochondrial large subunit ribosomalRNA (mtLSU rRNA), a universally conserved modification in the peptidyltransferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:25009282,ECO:0000269|PubMed:25074936}.",
"references": []
},
{
"targ_id": "T330",
"parent_targ_id": "T",
"full_name": "Required for meiotic nuclear division protein 1 homolog",
"abbrev": "",
"protein_names": "Required for meiotic nuclear division protein 1 homolog",
"related_func_ids": "F060401",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q9NWS8",
"Uniprot_name": "RMND1_HUMAN",
"EC_numbers": "",
"gene_symbol": "RMND1",
"gene_synonyms": "bA351K16.3, C6orf96, FLJ20627, RMD1",
"gene_synonyms_links": "",
"gene_name": "Required for meiotic nuclear division 1 homolog",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000155906",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Required for mitochondrial translation, possibly bycoordinating the assembly or maintenance of the mitochondrial ribosome(PubMed:23022098, PubMed:25604853). {ECO:0000269|PubMed:23022098,ECO:0000269|PubMed:25604853}.",
"references": []
},
{
"targ_id": "T331",
"parent_targ_id": "T",
"full_name": "Probable peptide chain release factor C12orf65, mitochondrial",
"abbrev": "",
"protein_names": "Probable peptide chain release factor C12orf65, mitochondrial",
"related_func_ids": "F0701",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9H3J6",
"Uniprot_name": "CL065_HUMAN",
"EC_numbers": "",
"gene_symbol": "C12orf65",
"gene_synonyms": "FLJ38663, SPG55",
"gene_synonyms_links": "",
"gene_name": "Chromosome 12 open reading frame 65",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000130921",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "May act as a codon-independent translation release factorthat has lost all stop codon specificity and directs the termination oftranslation in mitochondrion. May help rescuing stalled mitoribosomesduring translation (By similarity). {ECO:0000250}.",
"references": []
},
{
"targ_id": "T332",
"parent_targ_id": "T",
"full_name": "Elongation factor G, mitochondrial",
"abbrev": "mEF-G 1",
"protein_names": "Elongation factor G, mitochondrial (EF-Gmt) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (hEFG1)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "Elongation factor",
"Uniport_ID": "Q96RP9",
"Uniprot_name": "EFGM_HUMAN",
"EC_numbers": "",
"gene_symbol": "GFM1",
"gene_synonyms": "EFGM, EGF1, GFM",
"gene_synonyms_links": "",
"gene_name": "G elongation factor mitochondrial 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000168827",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Mitochondrial GTPase that catalyzes the GTP-dependentribosomal translocation step during translation elongation. During thisstep, the ribosome changes from the pre-translocational (PRE) to thepost-translocational (POST) state as the newly formed A-site-boundpeptidyl-tRNA and P-site-bound deacylated tRNA move to the P and Esites, respectively. Catalyzes the coordinated movement of the two tRNAmolecules, the mRNA and conformational changes in the ribosome. Doesnot mediate the disassembly of ribosomes from messenger RNA at thetermination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:19716793}.",
"references": []
},
{
"targ_id": "T333",
"parent_targ_id": "T",
"full_name": "Ribosome-releasing factor 2, mitochondrial",
"abbrev": "mEF-G 2",
"protein_names": "Ribosome-releasing factor 2, mitochondrial (RRF2mt) (Elongation factor G 2, mitochondrial) (EF-G2mt) (mEF-G 2) (Elongation factor G2) (hEFG2)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q969S9",
"Uniprot_name": "RRF2M_HUMAN",
"EC_numbers": "",
"gene_symbol": "GFM2",
"gene_synonyms": "EFG2, FLJ21661",
"gene_synonyms_links": "",
"gene_name": "G elongation factor mitochondrial 2",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000164347",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Mitochondrial GTPase that mediates the disassembly ofribosomes from messenger RNA at the termination of mitochondrialprotein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysisfollows the ribosome disassembly and probably occurs on the ribosomelarge subunit. Not involved in the GTP-dependent ribosomaltranslocation step during translation elongation. {ECO:0000255|HAMAP-Rule:MF_03059, ECO:0000269|PubMed:19716793}.",
"references": []
},
{
"targ_id": "T334",
"parent_targ_id": "T",
"full_name": "tRNA modification GTPase GTPBP3, mitochondrial",
"abbrev": "GTP-binding protein 3",
"protein_names": "tRNA modification GTPase GTPBP3, mitochondrial (GTP-binding protein 3) (Mitochondrial GTP-binding protein 1)",
"related_func_ids": "F060303",
"category": "enzyme",
"subcategories": "",
"Uniport_ID": "Q969Y2",
"Uniprot_name": "GTPB3_HUMAN",
"EC_numbers": "",
"gene_symbol": "GTPBP3",
"gene_synonyms": "FLJ14700, GTPBG3, MSS1, MTGP1, THDF1",
"gene_synonyms_links": "",
"gene_name": "GTP binding protein 3, mitochondrial",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000130299",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "GTPase involved in the 5-carboxymethylaminomethylmodification (mnm(5)s(2)U34) of the wobble uridine base inmitochondrial tRNAs. {ECO:0000305}.",
"references": []
},
{
"targ_id": "T335",
"parent_targ_id": "T",
"full_name": "Translation factor GUF1, mitochondrial",
"abbrev": "EF-4",
"protein_names": "Translation factor GUF1, mitochondrial (EC 3.6.5.-) (Elongation factor 4 homolog) (EF-4) (GTPase GUF1) (Ribosomal back-translocase)",
"related_func_ids": "F0604",
"category": "enzyme",
"subcategories": "Hydrolase",
"Uniport_ID": "Q8N442",
"Uniprot_name": "GUF1_HUMAN",
"EC_numbers": "3.6.5.-",
"gene_symbol": "GUF1",
"gene_synonyms": "FLJ13220",
"gene_synonyms_links": "",
"gene_name": "GUF1 homolog, GTPase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000151806",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side",
"reaction": "GTP + H2O = GDP + H(+) + phosphate",
"targ_desciption": "Promotes mitochondrial protein synthesis. May act as afidelity factor of the translation reaction, by catalyzing a one-codonbackward translocation of tRNAs on improperly translocated ribosomes.Binds to mitochondrial ribosomes in a GTP-dependent manner.{ECO:0000255|HAMAP-Rule:MF_03137}.",
"references": []
},
{
"targ_id": "T336",
"parent_targ_id": "T",
"full_name": "Leucine-rich PPR motif-containing protein, mitochondrial",
"abbrev": "LRP 130",
"protein_names": "Leucine-rich PPR motif-containing protein, mitochondrial (130 kDa leucine-rich protein) (LRP 130) (GP130)",
"related_func_ids": "F0604; F0401",
"category": "protein",
"subcategories": "",
"Uniport_ID": "P42704",
"Uniprot_name": "LPPRC_HUMAN",
"EC_numbers": "",
"gene_symbol": "LRPPRC",
"gene_synonyms": "GP130, LRP130, LSFC",
"gene_synonyms_links": "",
"gene_name": "Leucine rich pentatricopeptide repeat containing",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000138095",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion; Nucleus, nucleoplasm; Nucleus inner membrane; Nucleus outer membrane",
"reaction": "",
"targ_desciption": "May play a role in RNA metabolism in both nuclei andmitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAsand is part of nmRNP complexes at late stages of mRNA maturation whichare possibly associated with nuclear mRNA export. May bind mature mRNAin the nucleus outer membrane. In mitochondria binds to poly(A) mRNA.Plays a role in translation or stability of mitochondrially encodedcytochrome c oxidase (COX) subunits. May be involved in transcriptionregulation. Cooperates with PPARGC1A to regulate certainmitochondrially encoded genes and gluconeogenic genes and may regulatedocking of PPARGC1A to transcription factors. Seems to be involved inthe transcription regulation of the multidrug-related genes MDR1 andMVP. Part of a nuclear factor that binds to the invMED1 element of MDR1and MVP gene promoters. Binds single-stranded DNA (By similarity).{ECO:0000250, ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:12832482,ECO:0000269|PubMed:15081402, ECO:0000269|PubMed:15139850,ECO:0000269|PubMed:15272088, ECO:0000269|PubMed:17050673}.",
"references": []
},
{
"targ_id": "T337",
"parent_targ_id": "T",
"full_name": "Protein MTO1 homolog, mitochondrial",
"abbrev": "",
"protein_names": "Protein MTO1 homolog, mitochondrial",
"related_func_ids": "F060303",
"category": "protein",
"subcategories": "",
"Uniport_ID": "Q9Y2Z2",
"Uniprot_name": "MTO1_HUMAN",
"EC_numbers": "",
"gene_symbol": "MTO1",
"gene_synonyms": "",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial tRNA translation optimization 1",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000135297",
"omim_id": "",
"genecard_link": "",
"locs": "Mitochondrion",
"reaction": "",
"targ_desciption": "Involved in the 5-carboxymethylaminomethyl modification(mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.{ECO:0000269|PubMed:12011058}.",
"references": []
},
{
"targ_id": "T338",
"parent_targ_id": "T",
"full_name": "Poly(A) RNA polymerase, mitochondrial",
"abbrev": "mtPAP",
"protein_names": "Poly(A) RNA polymerase, mitochondrial (PAP) (EC 2.7.7.19) (PAP-associated domain-containing protein 1) (Polynucleotide adenylyltransferase) (Terminal uridylyltransferase 1) (TUTase 1) (mtPAP)",
"related_func_ids": "F060302",
"category": "enzyme",
"subcategories": "Nucleotidyltransferase, RNA-binding, Transferase",
"Uniport_ID": "Q9NVV4",
"Uniprot_name": "PAPD1_HUMAN",
"EC_numbers": "2.7.7.19",
"gene_symbol": "MTPAP",
"gene_synonyms": "FLJ10486, mtPAP, PAPD1, SPAX4",
"gene_synonyms_links": "",
"gene_name": "Mitochondrial poly(A) polymerase",
"hgnc_id": "",
"entrez_id": "",
"ensembl_id": "ENSG00000107951",
"omim_id": "",
"genecard_link": "",
"locs": "Cytoplasm; Mitochondrion",
"reaction": "ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide",
"targ_desciption": "Polymerase that creates the 3' poly(A) tail of mitochondrialtranscripts. Can use all four nucleotides, but has higher activity withATP and UTP (in vitro). Plays a role in replication-dependent histonemRNA degradation. May be involved in the terminal uridylation of maturehistone mRNAs before their degradation is initiated. Might beresponsible for the creation of some UAA stop codons which are notencoded in mtDNA. {ECO:0000269|PubMed:15547249,ECO:0000269|PubMed:15769737, ECO:0000269|PubMed:18172165,ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}.",
"references": []
}
]
}
