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Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein)

 HIF1A_MOUSE             Reviewed;         836 AA.
Q61221; O08741; O08993; Q61664; Q61665; Q8C681; Q8CC19; Q8CCB6;
Q8R385; Q9CYA8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
03-JUL-2003, sequence version 3.
30-AUG-2017, entry version 195.
RecName: Full=Hypoxia-inducible factor 1-alpha;
Short=HIF-1-alpha;
Short=HIF1-alpha;
AltName: Full=ARNT-interacting protein;
Name=Hif1a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Hepatocyte;
PubMed=8702901; DOI=10.1074/jbc.271.35.21262;
Li H., Ko H.P., Whitlock J.P. Jr.;
"Induction of phosphoglycerate kinase 1 gene expression by hypoxia.
Roles of Arnt and HIF1alpha.";
J. Biol. Chem. 271:21262-21267(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
STRAIN=129/SvJ;
PubMed=9368100;
Luo G., Gu Y.-Z., Jain S., Chan W.K., Carr K.M., Hogenesch J.B.,
Bradfield C.A.;
"Molecular characterization of the murine Hif-1 alpha locus.";
Gene Expr. 6:287-299(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
STRAIN=129/Sv;
PubMed=9210478; DOI=10.1111/j.1432-1033.1997.t01-1-00155.x;
Wenger R.H., Rolfs A., Kvietikova I., Spielmann P., Zimmermann D.R.,
Gassmann M.;
"The mouse gene for hypoxia-inducible factor-1alpha. Genomic
organization, expression and characterization of an alternative first
exon and 5' flanking sequence.";
Eur. J. Biochem. 246:155-165(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Colon, Diencephalon, Embryo, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-822 (ISOFORM 2).
TISSUE=Hepatocyte;
PubMed=8660378; DOI=10.1006/bbrc.1996.0845;
Wenger R.H., Rolfs A., Marti H.H., Guenet J.-L., Gassmann M.;
"Nucleotide sequence, chromosomal assignment and mRNA expression of
mouse hypoxia-inducible factor-1 alpha.";
Biochem. Biophys. Res. Commun. 223:54-59(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-85.
TISSUE=Hepatocyte;
O'Rourke J.F.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH COPS5.
PubMed=11707426; DOI=10.1074/jbc.C100442200;
Bae M.-K., Ahn M.-Y., Jeong J.-W., Bae M.-H., Lee Y.M., Bae S.-K.,
Park J.-W., Kim K.-R., Kim K.-W.;
"Jab1 interacts directly with HIF-1alpha and regulates its
stability.";
J. Biol. Chem. 277:9-12(2002).
[9]
SUMOYLATION, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
PubMed=15225651; DOI=10.1016/j.febslet.2004.05.079;
Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X.,
Sjoeland H., Billig H.;
"Increase of SUMO-1 expression in response to hypoxia: direct
interaction with HIF-1alpha in adult mouse brain and heart in vivo.";
FEBS Lett. 569:293-300(2004).
[10]
INTERACTION WITH TSGA10.
PubMed=16777103; DOI=10.1016/j.febslet.2006.05.058;
Haegele S., Behnam B., Borter E., Wolfe J., Paasch U., Lukashev D.,
Sitkovsky M., Wenger R.H., Katschinski D.M.;
"TSGA10 prevents nuclear localization of the hypoxia-inducible factor
(HIF)-1alpha.";
FEBS Lett. 580:3731-3738(2006).
[11]
DESUMOYLATION, AND FUNCTION.
PubMed=17981124; DOI=10.1016/j.cell.2007.08.045;
Cheng J., Kang X., Zhang S., Yeh E.T.H.;
"SUMO-specific protease 1 is essential for stabilization of HIF1alpha
during hypoxia.";
Cell 131:584-595(2007).
[12]
PHOSPHORYLATION BY PLK3.
PubMed=20889502; DOI=10.1074/jbc.M110.160325;
Xu D., Yao Y., Lu L., Costa M., Dai W.;
"Plk3 functions as an essential component of the hypoxia regulatory
pathway by direct phosphorylation of HIF-1alpha.";
J. Biol. Chem. 285:38944-38950(2010).
[13]
INTERACTION WITH HIF3A, AND SUBCELLULAR LOCATION.
PubMed=21546903; DOI=10.1038/cdd.2011.47;
Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
Fukumura H., Sogawa K.;
"Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a
negative regulator of HIF-1, through binding to pro-survival Bcl-2
family proteins.";
Cell Death Differ. 18:1711-1725(2011).
[14]
FUNCTION.
PubMed=22009797; DOI=10.1530/ERC-11-0211;
Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M.,
Buchfelder M., Losa M., Stalla G.K., Arzt E., Renner U.;
"RSUME is implicated in HIF-1-induced VEGF-A production in pituitary
tumour cells.";
Endocr. Relat. Cancer 19:13-27(2012).
-!- FUNCTION: Functions as a master transcriptional regulator of the
adaptive response to hypoxia. 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. Plays an essential role in embryonic vascularization,
tumor angiogenesis and pathophysiology of ischemic disease. Binds
to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response
element (HRE) of target gene promoters. Activation requires
recruitment of transcriptional coactivators such as CREBBP and
EP300. Activity is enhanced by interaction with both, NCOA1 or
NCOA2. Interaction with redox regulatory protein APEX seems to
activate CTAD and potentiates activation by NCOA1 and CREBBP.
Involved in the axonal distribution and transport of mitochondria
in neurons during hypoxia (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:17981124,
ECO:0000269|PubMed:22009797}.
-!- SUBUNIT: Interacts with HIF3A isoform 2 (PubMed:21546903).
Interacts with the HIF1A beta/ARNT subunit; heterodimerization is
required for DNA binding. Interacts with Interacts with NCOA1,
NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD
domain) with VHLL (via beta domain); the interaction, leads to
polyubiquitination and subsequent HIF1A proteasomal degradation.
During hypoxia, sumoylated HIF1A also binds VHL; the interaction
promotes the ubiquitination of HIF1A. Interacts with SENP1; the
interaction desumoylates HIF1A resulting in stabilization and
activation of transcription. Interacts (Via the ODD domain) with
ARD1A; the interaction appears not to acetylate HIF1A nor have any
affect on protein stability, during hypoxia. Interacts with RWDD3;
the interaction enhances HIF1A sumoylation. Interacts with RORA
(via the DNA binding domain); the interaction enhances HIF1A
transcription under hypoxia through increasing protein stability.
Interaction with PSMA7 inhibits the transactivation activity of
HIF1A under both normoxic and hypoxia-mimicking conditions.
Interacts with USP20. Interacts with RACK1; promotes HIF1A
ubiquitination and proteasome-mediated degradation. Interacts with
EP300 (via TAZ-type 1 domain); the interaction is stimulated in
response to hypoxia and inhibited by CITED2. Interacts with CREBBP
(via TAZ-type 1 domain). Interacts with SIRT2. Interacts
(deacetylated form) with EGLN1 (By similarity). Interacts with
TSGA10. Interacts (via N-terminus) with USP19. Interacts with
COPS5; the interaction increases the transcriptional activity of
HIF1A through increased stability. Interacts with CBFA2T3.
Interacts with HSP90AA1 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:Q16665, ECO:0000269|PubMed:11707426,
ECO:0000269|PubMed:16777103, ECO:0000269|PubMed:21546903}.
-!- INTERACTION:
Q09472:EP300 (xeno); NbExp=2; IntAct=EBI-298954, EBI-447295;
P35583:Foxa2; NbExp=5; IntAct=EBI-298954, EBI-2893341;
Q8BIF2:Rbfox3; NbExp=2; IntAct=EBI-298954, EBI-4567146;
P51450-2:Rorc; NbExp=2; IntAct=EBI-298954, EBI-4422078;
Q6NY15:Tsga10; NbExp=2; IntAct=EBI-8549331, EBI-8549230;
P40337:VHL (xeno); NbExp=2; IntAct=EBI-298954, EBI-301246;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15225651}.
Nucleus {ECO:0000269|PubMed:15225651,
ECO:0000269|PubMed:21546903}. Nucleus speckle
{ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform
2 in the nucleus and speckles (PubMed:21546903). Cytoplasmic in
normoxia, nuclear translocation in response to hypoxia (By
similarity). {ECO:0000250|UniProtKB:Q16665,
ECO:0000269|PubMed:21546903}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q61221-1; Sequence=Displayed;
Name=2;
IsoId=Q61221-2; Sequence=VSP_007739;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: Contains two independent C-terminal transactivation
domains, NTAD and CTAD, which function synergistically. Their
transcriptional activity is repressed by an intervening inhibitory
domain (ID) (By similarity). {ECO:0000250}.
-!- PTM: In normoxia, is hydroxylated on Pro-402 and Pro-577 in the
oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and
EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-577.
The hydroxylated prolines promote interaction with VHL, initiating
rapid ubiquitination and subsequent proteasomal degradation.
Deubiquitinated by USP20. Under hypoxia, proline hydroxylation is
impaired and ubiquitination is attenuated, resulting in
stabilization (By similarity). {ECO:0000250|UniProtKB:Q16665}.
-!- PTM: In normoxia, is hydroxylated on Asn-813 by HIF1AN, thus
abrogating interaction with CREBBP and EP300 and preventing
transcriptional activation. This hydroxylation is inhibited by the
Cu/Zn-chelator, Clioquinol (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation of Cys-810 may be responsible for increased
recruitment of p300 coactivator necessary for transcriptional
activity of HIF-1 complex. {ECO:0000250}.
-!- PTM: Requires phosphorylation for DNA-binding. Phosphorylation at
Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT
binding (By similarity). Phosphorylation by GSK3-beta and PLK3
promote degradation by the proteasome. {ECO:0000250,
ECO:0000269|PubMed:20889502}.
-!- PTM: Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced
through interaction with RWDD3. Both sumoylation and desumoylation
seem to be involved in the regulation of its stability during
hypoxia. 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. Desumoylation by SENP1 increases its
stability amd transcriptional activity. There is a disaccord
between various publications on the effect of sumoylation and
desumoylation on its stability and transcriptional activity.
{ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:17981124}.
-!- PTM: Acetylation of Lys-545 by ARD1 increases interaction with VHL
and stimulates subsequent proteasomal degradation. Deacetylation
of Lys-719 by SIRT2 increases its interaction with and
hydroxylation by EGLN1 thereby inactivating HIF1A activity by
inducing its proteasomal degradation (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated; in normoxia, following hydroxylation and
interaction with VHL. Lys-545 appears to be the principal site of
ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits
ubiquitination through preventing hydroxylation at Asn-813 (By
similarity). {ECO:0000250|UniProtKB:Q16665}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
asparagine is (S) stereospecific within HIF CTAD domains.
{ECO:0000250}.
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EMBL; U59496; AAC52730.1; -; Genomic_DNA.
EMBL; AF003695; AAC53455.1; -; mRNA.
EMBL; AF004155; AAC53461.1; -; Genomic_DNA.
EMBL; AF004141; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004142; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004143; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004144; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004145; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004146; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004147; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004148; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004149; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004150; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004151; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004152; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004153; AAC53461.1; JOINED; Genomic_DNA.
EMBL; AF004154; AAC53461.1; JOINED; Genomic_DNA.
EMBL; Y09085; CAA70305.1; -; Genomic_DNA.
EMBL; Y09085; CAA70306.1; -; Genomic_DNA.
EMBL; Y13656; CAA70306.1; JOINED; Genomic_DNA.
EMBL; AK034087; BAC28578.1; -; mRNA.
EMBL; AK076395; BAC36320.1; -; mRNA.
EMBL; AK033471; BAC28305.1; -; mRNA.
EMBL; AK017853; BAB30975.1; -; mRNA.
EMBL; BC026139; AAH26139.1; -; mRNA.
EMBL; X95580; CAA64833.1; -; mRNA.
EMBL; X95002; CAA64458.1; -; mRNA.
CCDS; CCDS25977.1; -. [Q61221-1]
PIR; JC4837; JC4837.
RefSeq; NP_001300848.1; NM_001313919.1.
RefSeq; NP_001300849.1; NM_001313920.1.
RefSeq; NP_034561.2; NM_010431.2. [Q61221-1]
RefSeq; XP_017170450.1; XM_017314961.1. [Q61221-2]
UniGene; Mm.3879; -.
UniGene; Mm.446610; -.
PDB; 4ZPR; X-ray; 3.90 A; B=13-357.
PDBsum; 4ZPR; -.
ProteinModelPortal; Q61221; -.
SMR; Q61221; -.
BioGrid; 200304; 18.
DIP; DIP-31083N; -.
IntAct; Q61221; 15.
MINT; MINT-1179248; -.
STRING; 10090.ENSMUSP00000021530; -.
BindingDB; Q61221; -.
ChEMBL; CHEMBL6046; -.
iPTMnet; Q61221; -.
PhosphoSitePlus; Q61221; -.
PaxDb; Q61221; -.
PRIDE; Q61221; -.
Ensembl; ENSMUST00000021530; ENSMUSP00000021530; ENSMUSG00000021109. [Q61221-1]
GeneID; 15251; -.
KEGG; mmu:15251; -.
UCSC; uc007nwo.2; mouse. [Q61221-2]
UCSC; uc007nwq.2; mouse. [Q61221-1]
CTD; 3091; -.
MGI; MGI:106918; Hif1a.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
GeneTree; ENSGT00760000118788; -.
HOVERGEN; HBG060456; -.
InParanoid; Q61221; -.
KO; K08268; -.
OMA; YCFDVDS; -.
OrthoDB; EOG091G0486; -.
PhylomeDB; Q61221; -.
TreeFam; TF317772; -.
Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-MMU-1234162; Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
Reactome; R-MMU-8951664; Neddylation.
ChiTaRS; Hif1a; mouse.
PRO; PR:Q61221; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021109; -.
CleanEx; MM_HIF1A; -.
ExpressionAtlas; Q61221; baseline and differential.
Genevisible; Q61221; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031514; C:motile cilium; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0070888; F:E-box binding; IMP:BHF-UCL.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IPI:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0001922; P:B-1 B cell homeostasis; IMP:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0048593; P:camera-type eye morphogenesis; IGI:MGI.
GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IGI:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0032963; P:collagen metabolic process; IMP:BHF-UCL.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; IMP:BHF-UCL.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
GO; GO:0051541; P:elastin metabolic process; IMP:BHF-UCL.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
GO; GO:0061030; P:epithelial cell differentiation involved in mammary gland alveolus development; IMP:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:MGI.
GO; GO:0042541; P:hemoglobin biosynthetic process; IMP:MGI.
GO; GO:0097411; P:hypoxia-inducible factor-1alpha signaling pathway; IDA:MGI.
GO; GO:0060574; P:intestinal epithelial cell maturation; IMP:MGI.
GO; GO:0061072; P:iris morphogenesis; IGI:MGI.
GO; GO:0006089; P:lactate metabolic process; IMP:MGI.
GO; GO:0007595; P:lactation; IMP:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI.
GO; GO:0045926; P:negative regulation of growth; IMP:MGI.
GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:CACAO.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:MGI.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:MGI.
GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
GO; GO:0021502; P:neural fold elevation formation; IMP:MGI.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
GO; GO:0032364; P:oxygen homeostasis; IMP:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:BHF-UCL.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISO:MGI.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:MGI.
GO; GO:1903599; P:positive regulation of mitophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IMP:MGI.
GO; GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL.
GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0006110; P:regulation of glycolytic process; IGI:MGI.
GO; GO:0070243; P:regulation of thymocyte apoptotic process; IGI:MGI.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IDA:MGI.
GO; GO:0014850; P:response to muscle activity; IMP:MGI.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0010573; P:vascular endothelial growth factor production; ISO:MGI.
GO; GO:0001944; P:vasculature development; IGI:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR001321; HIF-1_alpha.
InterPro; IPR014887; HIF-1_TAD_C.
InterPro; IPR021537; HIF_alpha_subunit.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR013767; PAS_fold.
InterPro; IPR013655; PAS_fold_3.
Pfam; PF11413; HIF-1; 1.
Pfam; PF08778; HIF-1a_CTAD; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08447; PAS_3; 1.
PRINTS; PR01080; HYPOXIAIF1A.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
TIGRFAMs; TIGR00229; sensory_box; 2.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; DNA-binding; Hydroxylation;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 836 Hypoxia-inducible factor 1-alpha.
/FTId=PRO_0000127221.
DOMAIN 17 70 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 80 155 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 228 298 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 302 345 PAC.
REGION 1 401 Interaction with TSGA10.
{ECO:0000269|PubMed:16777103}.
REGION 380 417 N-terminal VHL recognition site.
{ECO:0000250}.
REGION 401 613 ODD.
REGION 544 588 NTAD.
REGION 569 585 C-terminal VHL recognition site.
{ECO:0000250}.
REGION 589 795 ID.
REGION 796 836 CTAD.
MOTIF 728 731 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 247 247 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 402 402 4-hydroxyproline. {ECO:0000250}.
MOD_RES 545 545 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 564 564 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 568 568 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 577 577 4-hydroxyproline.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 589 589 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 602 602 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 668 668 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 719 719 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 813 813 (3S)-3-hydroxyasparagine. {ECO:0000250}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 545 545 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000305}.
CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305}.
CROSSLNK 560 560 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305}.
VAR_SEQ 512 525 Missing (in isoform 2).
{ECO:0000303|PubMed:8660378}.
/FTId=VSP_007739.
CONFLICT 12 12 K -> NR (in Ref. 4; BAC28578).
{ECO:0000305}.
CONFLICT 31 31 S -> T (in Ref. 1; AAC52730).
{ECO:0000305}.
CONFLICT 128 128 T -> A (in Ref. 1; AAC52730 and 6;
CAA64833). {ECO:0000305}.
CONFLICT 351 351 I -> L (in Ref. 1; AAC52730).
{ECO:0000305}.
CONFLICT 369 369 M -> K (in Ref. 5; AAH26139).
{ECO:0000305}.
CONFLICT 382 382 D -> A (in Ref. 5; AAH26139).
{ECO:0000305}.
CONFLICT 397 397 L -> H (in Ref. 4; BAC28578).
{ECO:0000305}.
CONFLICT 569 569 D -> G (in Ref. 4; BAC28578).
{ECO:0000305}.
CONFLICT 660 660 Q -> K (in Ref. 4; BAC28305).
{ECO:0000305}.
CONFLICT 700 700 N -> K (in Ref. 1; AAC52730 and 2;
AAC53455/AAC53461). {ECO:0000305}.
CONFLICT 799 799 E -> V (in Ref. 6; CAA64833).
{ECO:0000305}.
SEQUENCE 836 AA; 93516 MW; 84D64ECAC2CC753B CRC64;
MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM
RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV MVLTDDGDMV YISDNVNKYM
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR
TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTESV
LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL APAAGDTIIS LDFGSDDTET
EDQQLEDVPL YNDVMFPSSN EKLNINLAMS PLPSSETPKP LRSSADPALN QEVALKLESS
PESLGLSFTM PQIQDQPASP SDGSTRQSSP ERLLQENVNT PNFSQPNSPS EYCFDVDSDM
VNVFKLELVE KLFAEDTEAK NPFSTQDTDL DLEMLAPYIP MDDDFQLRSF DQLSPLESNS
PSPPSMSTVT GFQQTQLQKP TITATATTTA TTDESKTETK DNKEDIKILI ASPSSTQVPQ
ETTTAKASAY SGTHSRTASP DRAGKRVIEQ TDKAHPRSLN LSATLNQRNT VPEEELNPKT
IASQNAQRKR KMEHDGSLFQ AAGIGTLLQQ PGDCAPTMSL SWKRVKGFIS SEQNGTEQKT
IILIPSDLAC RLLGQSMDES GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN


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