IED Industry Enzyme Database

Detail Information for IndEnz0002002009
IED ID IndEnz0002002009
Enzyme Type ID protease002009
Protein Name Hypoxia-inducible factor 1-alpha
HIF-1-alpha
HIF1-alpha
ARNT-interacting protein
Basic-helix-loop-helix-PAS protein MOP1
Class E basic helix-loop-helix protein 78
bHLHe78
Member of PAS protein 1
PAS domain-containing protein 8
Gene Name HIF1A BHLHE78 MOP1 PASD8
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 MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
Enzyme Length 826
Uniprot Accession Number Q16665
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Induced by reactive oxygen species (ROS). {ECO:0000269|PubMed:32697943}.; ACTIVITY REGULATION: (Microbial infection) In monocytes, human coronavirus SARS-CoV-2 increases HIF1A levels and activity which promotes a proinflammatory state. {ECO:0000269|PubMed:32697943}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:9887100, PubMed:30125331). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:9887100, PubMed:30125331). Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (PubMed:22009797). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300 (PubMed:9887100, PubMed:16543236). Activity is enhanced by interaction with NCOA1 and/or NCOA2 (PubMed:10594042). Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP (PubMed:10202154, PubMed:10594042). Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (PubMed:19528298). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:10202154, ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:15465032, ECO:0000269|PubMed:16543236, ECO:0000269|PubMed:16973622, ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:9887100}.; FUNCTION: (Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent proinflammatory state (PubMed:32697943). In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons (PubMed:32697943). Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response (PubMed:32697943). {ECO:0000269|PubMed:32697943}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (3); Beta strand (9); Chain (1); Compositional bias (2); Cross-link (5); Domain (4); Glycosylation (1); Helix (9); Modified residue (12); Motif (1); Mutagenesis (29); Natural variant (3); Region (12); Sequence conflict (1); Turn (3)
Keywords 3D-structure;Acetylation;Activator;Alternative splicing;Cytoplasm;DNA-binding;Direct protein sequencing;Glycoprotein;Hydroxylation;Isopeptide bond;Nucleus;Phosphoprotein;Reference proteome;Repeat;S-nitrosylation;Transcription;Transcription regulation;Ubl conjugation
Interact With P10275; P27540; P49407; Q9C0J9; O00257; Q92793; P35222; Q96CJ1; Q9GZT9; Q96KS0; Q9H6Z9; Q09472; P11474; P09467; P23771; Q9NWT6; Q92831; Q13330; P46531; Q13438; Q8N2W9; P14618-1; P25789; Q9UHD8-1; P84022; P08047; P63165; O94888; P40818; P40337; P17861; Q99PV5; Q5RIX9; Q6S7F2; Q61539; Q8BIF2; P51450-2
Induction INDUCTION: Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B/interleukin-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. Repressed by HIPK2 and LIMD1. {ECO:0000269|PubMed:19046997, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:22286099}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9822602}. Nucleus {ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:9822602}. Nucleus speckle {ECO:0000250|UniProtKB:Q61221}. Note=Colocalizes with HIF3A in the nucleus and speckles (By similarity). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (PubMed:9822602). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:9822602}.
Modified Residue MOD_RES 247; /note="Phosphoserine; by CK1"; /evidence="ECO:0000269|PubMed:20699359"; MOD_RES 402; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:11566883"; MOD_RES 532; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:24681946"; MOD_RES 551; /note="Phosphoserine; by GSK3-beta"; /evidence="ECO:0000269|PubMed:20889502"; MOD_RES 555; /note="Phosphothreonine; by GSK3-beta"; /evidence="ECO:0000269|PubMed:20889502"; MOD_RES 564; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097"; MOD_RES 576; /note="Phosphoserine; by PLK3"; /evidence="ECO:0000269|PubMed:20889502"; MOD_RES 589; /note="Phosphoserine; by GSK3-beta"; /evidence="ECO:0000269|PubMed:20889502"; MOD_RES 657; /note="Phosphoserine; by PLK3"; /evidence="ECO:0000269|PubMed:20889502"; MOD_RES 709; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:24681946"; MOD_RES 800; /note="S-nitrosocysteine"; /evidence="ECO:0000305|PubMed:12914934"; MOD_RES 803; /note="(3S)-3-hydroxyasparagine"; /evidence="ECO:0000269|PubMed:12080085"
Post Translational Modification PTM: S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex. {ECO:0000269|PubMed:12560087, ECO:0000269|PubMed:12914934}.; PTM: Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding (PubMed:20699359, PubMed:20889502). Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:20889502}.; PTM: Sumoylated; with SUMO1 under hypoxia (PubMed:15465032, PubMed:15776016, PubMed:17610843). Sumoylation is enhanced through interaction with RWDD3 (PubMed:17956732). Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia (PubMed:15465032, PubMed:15776016, PubMed:17610843). Sumoylation can promote either its stabilization or its VHL-dependent degradation by promoting hydroxyproline-independent HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination and proteasomal degradation (PubMed:15465032, PubMed:15776016, PubMed:17610843). Desumoylation by SENP1 increases its stability amd transcriptional activity (By similarity). There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity (Probable). {ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:15465032, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:17956732, ECO:0000305}.; PTM: Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation (PubMed:12464182). Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (PubMed:24681946). {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:24681946}.; PTM: Polyubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-532 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-803. Ubiquitinated by a CUL2-based E3 ligase. {ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:16862177, ECO:0000269|PubMed:22537386, ECO:0000269|PubMed:25974097}.; PTM: In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). EGLN3/PHD3 has also been shown to hydroxylate Pro-564 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Deubiquitinated by USP20 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation (PubMed:12080085). This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol (PubMed:12080085). Repressed by iron ion, via Fe(2+) prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation (PubMed:28296633). {ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:25974097, ECO:0000269|PubMed:28296633}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. {ECO:0000269|PubMed:12080085}.; PTM: (Microbial infection) Glycosylated at Arg-18 by enteropathogenic E.coli protein NleB1: arginine GlcNAcylation enhances transcription factor activity and impairs glucose metabolism. {ECO:0000269|PubMed:30125331}.
Signal Peptide
Structure 3D NMR spectroscopy (2); X-ray crystallography (19)
Cross Reference PDB 1H2K; 1H2L; 1H2M; 1L3E; 1L8C; 1LM8; 1LQB; 2ILM; 3HQR; 3HQU; 4AJY; 4H6J; 5JWP; 5L9B; 5L9V; 5LA9; 5LAS; 6GFX; 6GMR; 6YW3; 7LVS;
Mapped Pubmed ID 10535940; 10823831; 10867011; 10878807; 10973499; 11024059; 11063749; 11120780; 11156414; 11292862; 11358837; 11404481; 11454738; 11504942; 11598268; 11823643; 11852072; 11861398; 11868612; 11886167; 11940656; 11943784; 11971899; 11980639; 11992540; 12016145; 12042299; 12062197; 12084725; 12099689; 12101228; 12123724; 12124396; 12136249; 12149254; 12154057; 12207089; 12209691; 12213597; 12215445; 12228247; 12237125; 12242281; 12296651; 12376345; 12401798; 12411310; 12451989; 12468553; 12482756; 12482858; 12485908; 12485909; 12488445; 12538644; 12586627; 12588875; 12600988; 12606552; 12615973; 12632503; 12651620; 12670503; 12673675; 12682018; 12697836; 12727858; 12743597; 12764143; 12781449; 12788921; 12810083; 12821113; 12821933; 12823854; 12855680; 12858534; 12865501; 12871382; 12876287; 12883692; 12885785; 12912907; 12914933; 12919954; 12937141; 12944107; 12966423; 14512791; 14521712; 14523474; 14559790; 14636255; 14638687; 14645546; 14657004; 14668441; 14671307; 14672622; 14680803; 14680833; 14681237; 14699081; 14701857; 14712484; 14726529; 14729605; 14742449; 14744756; 14744852; 14981919; 15024076; 15024078; 15031145; 15062033; 15064771; 15071503; 15082785; 15084243; 15084514; 15111179; 15135259; 15155569; 15156561; 15160341; 15169887; 15170665; 15175080; 15184875; 15191555; 15199114; 15199132; 15199161; 15217953; 15239670; 15240510; 15240563; 15247232; 15252039; 15261140; 15280364; 15280370; 15312651; 15322093; 15328163; 15331549; 15342390; 15342781; 15350301; 15374877; 15385570; 15388333; 15474027; 15474452; 15475194; 15479785; 15485863; 15489637; 15492789; 15527772; 15538748; 15543236; 15556623; 15561954; 15598682; 15598882; 15611046; 15611064; 15615775; 15623945; 15629713; 15652751; 15656883; 15665520; 15669079; 15674338; 15696961; 15709180; 15718424; 15721254; 15735682; 15750626; 15770733; 15805230; 15805242; 15809750; 15811877; 15814637; 15831177; 15832512; 15838297; 15838334; 15850830; 15862159; 15862307; 15864753; 15878343; 15897903; 15902299; 15913349; 15935515; 15947089; 15950906; 15962286; 15964822; 15967109; 15970466; 15983061; 15987702; 15994306; 16005427; 16007214; 16011198; 16035955; 16046581; 16100168; 16109785; 16110315; 16136272; 16136514; 16139409; 16140212; 16142350; 16144691; 16149050; 16157596; 16161047; 16168127; 16170370; 16189514; 16195397; 16205110; 16208522; 16229017; 16229182; 16242072; 16246222; 16253768; 16256737; 16261165; 16263938; 16278378; 16278385; 16284786; 16288478; 16304044; 16331995; 16337862; 16338068; 16341243; 16396931; 16397018; 16407835; 16408279; 16421254; 16424018; 16438736; 16452478; 16490744; 16506055; 16510571; 16511565; 16515634; 16516166; 16516853; 16533170; 16543242; 16543245; 16552335; 16554418; 16555123; 16579968; 16596228; 16611863; 16612574; 16627691; 16629644; 16631533; 16638120; 16682946; 16721291; 16736613; 16738327; 16756955; 16760477; 16768548; 16769565; 16775626; 16775835; 16777103; 16779673; 16782814; 16815840; 16826425; 16826581; 16828081; 16837101; 16847054; 16849522; 16854377; 16865676; 16871792; 16873253; 16883594; 16890383; 16899596; 16899602; 16901993; 16920734; 16937436; 16951198; 16951228; 16954218; 16969516; 16970912; 16979927; 16998808; 17010341; 17015263; 17015745; 17024177; 17043658; 17045016; 17055760; 17060326; 17060462; 17066447; 17067582; 17075581; 17077301; 17097641; 17102128; 17102633; 17135241; 17143338; 17179985; 17189520; 17236590; 17245699; 17268888; 17289019; 17289897; 17290185; 17292638; 17294729; 17307335; 17310851; 17320759; 17325032; 17335808; 17336340; 17343848; 17353276; 17360382; 17376295; 17382205; 17382325; 17387384; 17400550; 17404022; 17407091; 17418410; 17418790; 17418979; 17426247; 17426252; 17434750; 17437013; 17438103; 17442277; 17442736; 17445471; 17451682; 17452775; 17458899; 17461470; 17473988; 17474992; 17477366; 17487356; 17488873; 17490410; 17495954; 17507435; 17511040; 17519536; 17519789; 17525282; 17532031; 17536453; 17544543; 17545054; 17555795; 17558023; 17562539; 17562866; 17563752; 17568584; 17570486; 17591803; 17592963; 17595907; 17597020; 17606258; 17624927; 17634230; 17637739; 17640715; 17650819; 17653093; 17662481; 17666400; 17674038; 17676480; 17684492; 17713282; 17714861; 17718430; 17721610; 17725546; 17726031; 17785433; 17804822; 17805961; 17822384; 17826745; 17828303; 17848618; 17852557; 17875644; 17889387; 17891484; 17893997; 17898080; 17916562; 17927572; 17932327; 17942596; 17947829; 17965024; 17967865; 17967866; 17967880; 17978497; 17982282; 17984117; 17986458; 17989922; 17990984; 17999410; 18000826; 18006690; 18021370; 18024825; 18025805; 18030615; 18031949; 18035072; 18037992; 18047470; 18050215; 18050252; 18055454; 18060642; 18062281; 18065728; 18081507; 18083891; 18094421; 18097583; 18154573; 18159247; 18160046; 18163427; 18166158; 18172210; 18172309; 18178340; 18184809; 18184961; 18187047; 18199003; 18209490; 18221327; 18222538; 18225753; 18239067; 18240292; 18246800; 18250065; 18256363; 18258605; 18279708; 18290322; 18292935; 18294451; 18295594; 18297062; 18299578; 18307947; 18309031; 18314489; 18315897; 18323857; 18325389; 18337469; 18339685; 18342368; 18347341; 18351386; 18353781; 18354193; 18362831; 18365547; 18370960; 18376310; 18381358; 18384112; 18385176; 18393939; 18398039; 18411415; 18413745; 18418234; 18422279; 18422749; 18424433; 18424783; 18440561; 18447642; 18447926; 18452596; 18459144; 18462799; 18465238; 18473128; 18476562; 18476629; 18476949; 18484090; 18493321; 18506785; 18521687; 18528739; 18533565; 18538669; 18546529; 18551130; 18554951; 18561315; 18563339; 18563715; 18570733; 18574470; 18592007; 18593917; 18595517; 18606657; 18611856; 18617693; 18619649; 18621534; 18630523; 18632605; 18641302; 18644974; 18648372; 18655183; 18687685; 18694926; 18703592; 18704463; 18713068; 18713836; 18718909; 18720385; 18728026; 18762723; 18763582; 18772337; 18775313; 18779379; 18780286; 18784753; 18785001; 18787502; 18790175; 18790176; 18792019; 18799519; 18813785; 18832593; 18834862; 18835464; 18835792; 18838541; 18841476; 18844219; 18922940; 18927085; 18936210; 18936945; 18945681; 18945963; 18949419; 18950958; 18979225; 18980686; 18983642; 18984585; 18985005; 18987249; 18996102; 18996491; 18998488; 19007879; 19016246; 19016766; 19018165; 19018560; 19028277; 19028544; 19028566; 19030186; 19030229; 19048182; 19054610; 19057015; 19061835; 19071119; 19074848; 19077164; 19077391; 19080330; 19091459; 19096126; 19096962; 19097132; 19097995; 19098000; 19105964; 19106642; 19107364; 19109240; 19121088; 19128456; 19130303; 19132225; 19141292; 19142800; 19147752; 19147754; 19151763; 19165496; 19168635; 19172095; 19176596; 19179292; 19179443; 19180921; 19183269; 19184477; 19188659; 19188818; 19204000; 19211554; 19211927; 19212630; 19223463; 19223895; 19235921; 19238077; 19240858; 19244104; 19251694; 19252526; 19254160; 19254710; 19255431; 19265035; 19266161; 19268443; 19279559; 19287200; 19287962; 19293442; 19302703; 19303436; 19304911; 19306159; 19307182; 19321184; 19335985; 19336661; 19347037; 19359588; 19360424; 19362550; 19381167; 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Motif MOTIF 718..721; /note=Nuclear localization signal; /evidence=ECO:0000255
Gene Encoded By
Mass 92,670
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda