IED Industry Enzyme Database

Detail Information for IndEnz0002006463
IED ID IndEnz0002006463
Enzyme Type ID protease006463
Protein Name Serine/threonine-protein kinase mTOR
EC 2.7.11.1
FK506-binding protein 12-rapamycin complex-associated protein 1
FKBP12-rapamycin complex-associated protein
Mammalian target of rapamycin
mTOR
Mechanistic target of rapamycin
Rapamycin and FKBP12 target 1
Rapamycin target protein 1
Gene Name MTOR FRAP FRAP1 FRAP2 RAFT1 RAPT1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW
Enzyme Length 2549
Uniprot Accession Number P42345
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD (PubMed:18497260, PubMed:20381137, PubMed:25561175, PubMed:25567906). On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway. {ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:17386266, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:22343943, ECO:0000269|PubMed:22576015, ECO:0000269|PubMed:22692423}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21659604};
DNA Binding
EC Number 2.7.11.1
Enzyme Function FUNCTION: Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862, PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (By similarity). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:12150925, PubMed:12087098, PubMed:18925875). This also includes mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3: in the presence of nutrients, mediates phosphorylation of TFEB and TFE3, promoting their cytosolic retention and inactivation (PubMed:22576015, PubMed:22343943, PubMed:22692423). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed:22576015, PubMed:22343943, PubMed:22692423). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed:23429704, PubMed:23429703). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). mTORC1 also negatively regulates autophagy through phosphorylation of ULK1 (By similarity). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed:23524951, PubMed:25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (PubMed:15718470). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity). Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex (By similarity). {ECO:0000250|UniProtKB:P42346, ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:22343943, ECO:0000269|PubMed:22576015, ECO:0000269|PubMed:22692423, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:23524951, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25799227, ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:30704899}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (21); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Frameshift (1); Helix (55); Modified residue (12); Mutagenesis (8); Natural variant (31); Region (7); Repeat (48); Sequence conflict (14); Turn (12)
Keywords 3D-structure;ATP-binding;Acetylation;Biological rhythms;Cytoplasm;Cytoplasmic vesicle;Disease variant;Endoplasmic reticulum;Epilepsy;Golgi apparatus;Kinase;Lysosome;Membrane;Mental retardation;Microsome;Mitochondrion;Mitochondrion outer membrane;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;TPR repeat;Transferase
Interact With P31749; Q07817-1; Q8TB45; Q13541; P62942; Q8WUA4; Q9BVC4; Q9BVC4-1; Q13615; Itself; Q8TCU6; P62820; Q15382; Q6R327; Q8N122; Q96EB6; Q8NHX9; O75385
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14578359}; Peripheral membrane protein {ECO:0000269|PubMed:14578359}; Cytoplasmic side {ECO:0000269|PubMed:14578359}. Golgi apparatus membrane {ECO:0000269|PubMed:14578359}; Peripheral membrane protein {ECO:0000269|PubMed:14578359}; Cytoplasmic side {ECO:0000269|PubMed:14578359}. Mitochondrion outer membrane {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:14578359}; Peripheral membrane protein {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:14578359}; Cytoplasmic side {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:14578359}. Lysosome {ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:29750193}. Cytoplasm {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:18497260}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9JLN9}. Microsome membrane {ECO:0000269|PubMed:9434772}. Lysosome membrane {ECO:0000269|PubMed:30956113}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:27623384}. Note=Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB (PubMed:18497260, PubMed:20381137). Lysosome targeting also depends on interaction with MEAK7. Translocates to the lysosome membrane in the presence of TM4SF5 (PubMed:30956113). {ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:29750193, ECO:0000269|PubMed:30956113}.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 567; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231"; MOD_RES 1162; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES 1218; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 1261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19487463, ECO:0007744|PubMed:23186163"; MOD_RES 2159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21576368"; MOD_RES 2164; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:21576368"; MOD_RES 2173; /note="Phosphothreonine; by PKB/AKT1"; /evidence="ECO:0000269|PubMed:24247430"; MOD_RES 2446; /note="Phosphothreonine; by RPS6KB1"; /evidence="ECO:0000269|PubMed:15905173"; MOD_RES 2448; /note="Phosphoserine; by RPS6KB1"; /evidence="ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:19145465, ECO:0007744|PubMed:24275569"; MOD_RES 2478; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 2481; /note="Phosphoserine; by autocatalysis"; /evidence="ECO:0000269|PubMed:21576368, ECO:0007744|PubMed:18669648"
Post Translational Modification PTM: Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity. {ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:19145465, ECO:0000269|PubMed:19487463, ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:24247430}.
Signal Peptide
Structure 3D NMR spectroscopy (3); Electron microscopy (17); X-ray crystallography (21)
Cross Reference PDB 1AUE; 1FAP; 1NSG; 2FAP; 2GAQ; 2NPU; 2RSE; 3FAP; 3JBZ; 4DRH; 4DRI; 4DRJ; 4FAP; 4JSN; 4JSP; 4JSV; 4JSX; 4JT5; 4JT6; 5FLC; 5GPG; 5H64; 5WBH; 5WBU; 5WBY; 5ZCS; 6BCU; 6BCX; 6M4U; 6M4W; 6SB0; 6SB2; 6ZWM; 6ZWO; 7OWG; 7PE7; 7PE8; 7PE9; 7PEA; 7PEB; 7PEC;
Mapped Pubmed ID 10567225; 10702316; 10910062; 11438723; 11691993; 11729323; 11884412; 12000755; 12080086; 12145207; 12151408; 12167717; 12172553; 12242281; 12271141; 12370290; 12524439; 12558800; 12604610; 12807916; 12813467; 12820960; 12869586; 12906785; 12912989; 12935885; 12937293; 14560963; 14668532; 14729629; 14743216; 14970221; 15001544; 15004009; 15028555; 15056668; 15161933; 15208671; 15218033; 15292249; 15292274; 15317677; 15388509; 15388791; 15452223; 15489897; 15496972; 15522880; 15576463; 15580312; 15584862; 15604215; 15605414; 15623621; 15624760; 15625077; 15632115; 15632201; 15657358; 15659381; 15702344; 15708965; 15723049; 15755954; 15760475; 15802268; 15809305; 15854902; 15878852; 15899889; 15953364; 15963500; 16006564; 16027121; 16049009; 16098202; 16098514; 16099944; 16109716; 16141350; 16183647; 16242075; 16263769; 16282343; 16286006; 16288304; 16322256; 16341243; 16354680; 16407298; 16427044; 16467080; 16543150; 16584539; 16652388; 16786123; 16818690; 16824195; 16847060; 16870609; 16874098; 16884363; 16886599; 16912159; 16912980; 16914728; 16916907; 16920842; 16922504; 16927414; 16929481; 16934436; 16952420; 16954686; 16959214; 16962653; 16963469; 17016437; 17018601; 17028174; 17052453; 17075574; 17102641; 17110454; 17110594; 17114181; 17142137; 17148679; 17162089; 17178807; 17215282; 17253963; 17277771; 17289850; 17318075; 17329620; 17351147; 17363738; 17372934; 17409838; 17461779; 17463046; 17470430; 17482291; 17483438; 17488873; 17517883; 17545512; 17553806; 17562705; 17562865; 17565979; 17595159; 17604271; 17611497; 17616684; 17616691; 17631500; 17640392; 17643959; 17646396; 17656678; 17683115; 17684489; 17698027; 17721511; 17721885; 17724079; 17726467; 17889116; 17911267; 17914450; 17928295; 17935273; 17942603; 17971512; 17976640; 17990907; 17991864; 17993259; 17996122; 18006825; 18033679; 18048359; 18056791; 18160036; 18215133; 18247380; 18250445; 18276609; 18276949; 18292222; 18337562; 18339839; 18339899; 18351386; 18372248; 18395956; 18413763; 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Motif
Gene Encoded By
Mass 288,892
Kinetics
Metal Binding
Rhea ID RHEA:17989; RHEA:46608
Cross Reference Brenda