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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)

 HIF1A_HUMAN             Reviewed;         826 AA.
Q16665; C0LZJ3; Q53XP6; Q96PT9; Q9UPB1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 209.
RecName: Full=Hypoxia-inducible factor 1-alpha {ECO:0000303|PubMed:7539918};
Short=HIF-1-alpha {ECO:0000303|PubMed:7539918};
Short=HIF1-alpha {ECO:0000303|PubMed:7539918};
AltName: Full=ARNT-interacting protein;
AltName: Full=Basic-helix-loop-helix-PAS protein MOP1 {ECO:0000303|PubMed:9079689};
AltName: Full=Class E basic helix-loop-helix protein 78;
Short=bHLHe78;
AltName: Full=Member of PAS protein 1 {ECO:0000303|PubMed:9079689};
AltName: Full=PAS domain-containing protein 8;
Name=HIF1A {ECO:0000303|PubMed:7539918};
Synonyms=BHLHE78, MOP1 {ECO:0000303|PubMed:9079689}, PASD8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 166-170; 259-289
AND 771-781.
PubMed=7539918; DOI=10.1073/pnas.92.12.5510;
Wang G.L., Jiang B.-H., Rue E.A., Semenza G.L.;
"Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS
heterodimer regulated by cellular O2 tension.";
Proc. Natl. Acad. Sci. U.S.A. 92:5510-5514(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
PubMed=9079689; DOI=10.1074/jbc.272.13.8581;
Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.-Z.,
Pray-Grant M., Perdew G.H., Bradfield C.A.;
"Characterization of a subset of the basic-helix-loop-helix-PAS
superfamily that interacts with components of the dioxin signaling
pathway.";
J. Biol. Chem. 272:8581-8593(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9782081; DOI=10.1006/geno.1998.5416;
Iyer N.V., Leung S.W., Semenza G.L.;
"The human hypoxia-inducible factor 1alpha gene: HIF1A structure and
evolutionary conservation.";
Genomics 52:159-165(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
PubMed=18638657; DOI=10.1016/j.humimm.2008.05.004;
Lukashev D., Sitkovsky M.;
"Preferential expression of the novel alternative isoform I.3 of
hypoxia-inducible factor 1alpha in activated human T lymphocytes.";
Hum. Immunol. 69:421-425(2008).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Rupert J.L., Hochachka P.W.;
"HIF1a sequence in the Quechua, a high altitude population.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Glial tumor;
Sun B., Zhao H.R., Yu R.T., Ni M.S.H.;
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
Tanaka S., Sugimachi K.;
"Hypoxia-inducible factor-1 alpha variant isolated from human liver
tissue.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Choriocarcinoma, and Placenta;
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).
[11]
IDENTIFICATION IN COMPLEX WITH EP300 AND CREBBP, AND INTERACTION WITH
EP300.
PubMed=8917528; DOI=10.1073/pnas.93.23.12969;
Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C.,
Goldberg M.A., Bunn H.F., Livingston D.M.;
"An essential role for p300/CBP in the cellular response to hypoxia.";
Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996).
[12]
TRANSACTIVATION DOMAINS NTAD AND CTAD.
PubMed=9235919; DOI=10.1074/jbc.272.31.19253;
Jiang B.H., Zheng J.Z., Leung S.W., Roe R., Semenza G.L.;
"Transactivation and inhibitory domains of hypoxia-inducible factor
1alpha. Modulation of transcriptional activity by oxygen tension.";
J. Biol. Chem. 272:19253-19260(1997).
[13]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-719.
PubMed=9822602; DOI=10.1093/emboj/17.22.6573;
Kallio P.J., Okamoto K., O'Brien S., Carrero P., Makino Y., Tanaka H.,
Poellinger L.;
"Signal transduction in hypoxic cells: inducible nuclear translocation
and recruitment of the CBP/p300 coactivator by the hypoxia-inducible
factor-1alpha.";
EMBO J. 17:6573-6586(1998).
[14]
OXYGEN-DEPENDENT DEGRADATION DOMAIN.
PubMed=9653127; DOI=10.1073/pnas.95.14.7987;
Huang L.E., Gu J., Schau M., Bunn H.F.;
"Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-
dependent degradation domain via the ubiquitin-proteasome pathway.";
Proc. Natl. Acad. Sci. U.S.A. 95:7987-7992(1998).
[15]
TRANSACTIVATION DOMAINS NTAD AND CTAD, INTERACTION WITH APEX, AND
MUTAGENESIS OF CYS-800.
PubMed=10202154; DOI=10.1093/emboj/18.7.1905;
Ema M., Hirota K., Mimura J., Abe H., Yodoi J., Sogawa K.,
Poellinger L., Fujii-Kuriyama Y.;
"Molecular mechanisms of transcription activation by HLF and HIF1alpha
in response to hypoxia: their stabilization and redox signal-induced
interaction with CBP/p300.";
EMBO J. 18:1905-1914(1999).
[16]
FUNCTION, DNA-BINDING, AND INTERACTION WITH EP300.
PubMed=9887100; DOI=10.1101/gad.13.1.64;
Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L.,
Livingston D.M.;
"Functional role of p35srj, a novel p300/CBP binding protein, during
transactivation by HIF-1.";
Genes Dev. 13:64-75(1999).
[17]
INTERACTION WITH VHL.
PubMed=11006129; DOI=10.1006/bbrc.2000.3451;
Aso T., Yamazaki K., Aigaki T., Kitajima S.;
"Drosophila von Hippel-Lindau tumor suppressor complex possesses E3
ubiquitin ligase activity.";
Biochem. Biophys. Res. Commun. 276:355-361(2000).
[18]
INTERACTION WITH VHL AND ARNT, AND MUTAGENESIS OF LYS-532; LYS-538;
LYS-547 AND LYS-719.
PubMed=10944113; DOI=10.1093/emboj/19.16.4298;
Tanimoto K., Makino Y., Pereira T., Poellinger L.;
"Mechanism of regulation of the hypoxia-inducible factor-1 alpha by
the von Hippel-Lindau tumor suppressor protein.";
EMBO J. 19:4298-4309(2000).
[19]
INTERACTION WITH NCOA1; NCOA2 AND APEX.
PubMed=10594042; DOI=10.1128/MCB.20.1.402-415.2000;
Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H.,
Poellinger L.;
"Redox-regulated recruitment of the transcriptional coactivators CREB-
binding protein and SRC-1 to hypoxia-inducible factor 1alpha.";
Mol. Cell. Biol. 20:402-415(2000).
[20]
MUTAGENESIS OF SER-551 AND THR-552, AND UBIQUITINATION.
PubMed=10758161; DOI=10.1073/pnas.080072497;
Sutter C.H., Laughner E., Semenza G.L.;
"Hypoxia-inducible factor 1alpha protein expression is controlled by
oxygen-regulated ubiquitination that is disrupted by deletions and
missense mutations.";
Proc. Natl. Acad. Sci. U.S.A. 97:4748-4753(2000).
[21]
HYDROXYLATION AT PRO-402 AND PRO-564, UBIQUITINATION, INTERACTION WITH
THE VHLE COMPLEX, FUNCTION, AND MUTAGENESIS OF PRO-394; LEU-397;
LEU-400; PRO-402 AND PRO-564.
PubMed=11566883; DOI=10.1093/emboj/20.18.5197;
Masson N., Willam C., Maxwell P.H., Pugh C.W., Ratcliffe P.J.;
"Independent function of two destruction domains in hypoxia-inducible
factor-alpha chains activated by prolyl hydroxylation.";
EMBO J. 20:5197-5206(2001).
[22]
INTERACTION WITH PSMA7.
PubMed=11389899; DOI=10.1016/S0014-5793(01)02499-1;
Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E.;
"Binding and regulation of HIF-1alpha by a subunit of the proteasome
complex, PSMA7.";
FEBS Lett. 498:62-66(2001).
[23]
UBIQUITINATION, FUNCTION, AND HYDROXYLATION AT PRO-564.
PubMed=11292861; DOI=10.1126/science.1059796;
Jaakkola P., Mole D.R., Tian Y.-M., Wilson M.I., Gielbert J.,
Gaskell S.J., von Kriegsheim A., Hebestreit H.F., Mukherji M.,
Schofield C.J., Maxwell P.H., Pugh C.W., Ratcliffe P.J.;
"Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation
complex by O2-regulated prolyl hydroxylation.";
Science 292:468-472(2001).
[24]
INTERACTION WITH ARD1A, AND ACETYLATION AT LYS-532.
PubMed=12464182; DOI=10.1016/S0092-8674(02)01085-1;
Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H.,
Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W.;
"Regulation and destabilization of HIF-1alpha by ARD1-mediated
acetylation.";
Cell 111:709-720(2002).
[25]
HYDROXYLATION AT ASN-803, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12080085; DOI=10.1101/gad.991402;
Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L.,
Bruick R.K.;
"FIH-1 is an asparaginyl hydroxylase enzyme that regulates the
transcriptional activity of hypoxia-inducible factor.";
Genes Dev. 16:1466-1471(2002).
[26]
HYDROXYLATION AT PRO-564, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12351678; DOI=10.1073/pnas.192342099;
Ivan M., Haberberger T., Gervasi D.C., Michelson K.S., Guenzler V.,
Kondo K., Yang H., Sorokina I., Conaway R.C., Conaway J.W.,
Kaelin W.G. Jr.;
"Biochemical purification and pharmacological inhibition of a
mammalian prolyl hydroxylase acting on hypoxia-inducible factor.";
Proc. Natl. Acad. Sci. U.S.A. 99:13459-13464(2002).
[27]
S-NITROSYLATION AT CYS-800, AND MUTAGENESIS OF CYS-800.
PubMed=12914934; DOI=10.1016/S0014-5793(03)00807-X;
Yasinska I.M., Sumbayev V.V.;
"S-nitrosation of Cys-800 of HIF-1alpha protein activates its
interaction with p300 and stimulates its transcriptional activity.";
FEBS Lett. 549:105-109(2003).
[28]
S-NITROSYLATION.
PubMed=12560087; DOI=10.1016/S0014-5793(02)03887-5;
Sumbayev V.V., Budde A., Zhou J., Bruene B.;
"HIF-1 alpha protein as a target for S-nitrosation.";
FEBS Lett. 535:106-112(2003).
[29]
INTERACTION WITH EP300, AND MUTAGENESIS OF LEU-795.
PubMed=12778114; DOI=10.1038/nsb936;
Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.;
"Structural basis for negative regulation of hypoxia-inducible factor-
1alpha by CITED2.";
Nat. Struct. Biol. 10:504-512(2003).
[30]
SUMOYLATION AT LYS-391 AND LYS-477, FUNCTION, AND MUTAGENESIS OF
LYS-389; LYS-391; LYS-392; LYS-442; LYS-460; LYS-477; LYS-532; LYS-538
AND LYS-547.
PubMed=15465032; DOI=10.1016/j.bbrc.2004.09.068;
Bae S.-H., Jeong J.-W., Park J.A., Kim S.-H., Bae M.-K., Choi S.-J.,
Kim K.-W.;
"Sumoylation increases HIF-1alpha stability and its transcriptional
activity.";
Biochem. Biophys. Res. Commun. 324:394-400(2004).
[31]
INTERACTION WITH VHLL.
PubMed=14757845;
Qi H., Gervais M.L., Li W., DeCaprio J.A., Challis J.R.G., Ohh M.;
"Molecular cloning and characterization of the von Hippel-Lindau-like
protein.";
Mol. Cancer Res. 2:43-52(2004).
[32]
UBIQUITINATION, DEUBIQUITINATION BY USP20, AND INTERACTION WITH USP20.
PubMed=15776016; DOI=10.1038/sj.embor.7400377;
Li Z., Wang D., Messing E.M., Wu G.;
"VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and
stabilizes HIF-1alpha.";
EMBO Rep. 6:373-378(2005).
[33]
INTERACTION WITH ARD1A, AND MUTAGENESIS OF LYS-532.
PubMed=16288748; DOI=10.1016/j.febslet.2005.10.036;
Arnesen T., Kong X., Evjenth R., Gromyko D., Varhaug J.E., Lin Z.,
Sang N., Caro J., Lillehaug J.R.;
"Interaction between HIF-1 alpha (ODD) and hARD1 does not induce
acetylation and destabilization of HIF-1 alpha.";
FEBS Lett. 579:6428-6432(2005).
[34]
FUNCTION, INTERACTION WITH EP300 IN THE HIF1A/EP300/CREBBP COMPLEX,
AND MUTAGENESIS OF ASN-803.
PubMed=16543236; DOI=10.1074/jbc.M600456200;
Fath D.M., Kong X., Liang D., Lin Z., Chou A., Jiang Y., Fang J.,
Caro J., Sang N.;
"Histone deacetylase inhibitors repress the transactivation potential
of hypoxia-inducible factors independently of direct acetylation of
HIF-alpha.";
J. Biol. Chem. 281:13612-13619(2006).
[35]
UBIQUITINATION, HYDROXYLATION, FUNCTION, INTERACTION WITH CBPP,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF ASN-803.
PubMed=16973622; DOI=10.1074/jbc.M603913200;
Choi S.M., Choi K.-O., Park Y.K., Cho H., Yang E.G., Park H.;
"Clioquinol, a Cu(II)/Zn(II) chelator, inhibits both ubiquitination
and asparagine hydroxylation of hypoxia-inducible factor-1alpha,
leading to expression of vascular endothelial growth factor and
erythropoietin in normoxic cells.";
J. Biol. Chem. 281:34056-34063(2006).
[36]
SUMOYLATION AT LYS-391 AND LYS-477, FUNCTION, AND MUTAGENESIS OF
LYS-377; LYS-391; LYS-477 AND LYS-532.
PubMed=17610843; DOI=10.1016/j.bbrc.2007.06.103;
Berta M.A., Mazure N., Hattab M., Pouyssegur J., Brahimi-Horn M.C.;
"SUMOylation of hypoxia-inducible factor-1alpha reduces its
transcriptional activity.";
Biochem. Biophys. Res. Commun. 360:646-652(2007).
[37]
SUMOYLATION, AND INTERACTION WITH RWDD3.
PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
"RSUME, a small RWD-containing protein, enhances SUMO conjugation and
stabilizes HIF-1alpha during hypoxia.";
Cell 131:309-323(2007).
[38]
INTERACTION WITH RACK1.
PubMed=17244529; DOI=10.1016/j.molcel.2007.01.001;
Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L.;
"RACK1 competes with HSP90 for binding to HIF-1alpha and is required
for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-
1alpha.";
Mol. Cell 25:207-217(2007).
[39]
UBIQUITINATION AT LYS-532; LYS-538 AND LYS-547, INTERACTION WITH VHL,
AND MUTAGENESIS OF PRO-402; LYS-532; LYS-538; LYS-547 AND PRO-564.
PubMed=16862177; DOI=10.1038/sj.onc.1209818;
Paltoglou S., Roberts B.J.;
"HIF-1alpha and EPAS ubiquitination mediated by the VHL tumour
suppressor involves flexibility in the ubiquitination mechanism,
similar to other RING E3 ligases.";
Oncogene 26:604-609(2007).
[40]
INTERACTION WITH RORA.
PubMed=18658046; DOI=10.1161/ATVBAHA.108.171546;
Kim E.J., Yoo Y.G., Yang W.K., Lim Y.S., Na T.Y., Lee I.K., Lee M.O.;
"Transcriptional activation of HIF-1 by RORalpha and its role in
hypoxia signaling.";
Arterioscler. Thromb. Vasc. Biol. 28:1796-1802(2008).
[41]
REVIEW ON REGULATION.
PubMed=18809331; DOI=10.1016/j.tibs.2008.08.002;
Yee Koh M., Spivak-Kroizman T.R., Powis G.;
"HIF-1 regulation: not so easy come, easy go.";
Trends Biochem. Sci. 33:526-534(2008).
[42]
INDUCTION BY HIPK2.
PubMed=19046997; DOI=10.1016/j.bbamcr.2008.10.013;
Nardinocchi L., Puca R., Guidolin D., Belloni A.S., Bossi G.,
Michiels C., Sacchi A., Onisto M., D'Orazi G.;
"Transcriptional regulation of hypoxia-inducible factor 1alpha by
HIPK2 suggests a novel mechanism to restrain tumor growth.";
Biochim. Biophys. Acta 1793:368-377(2009).
[43]
FUNCTION IN MITOCHONDRIAL TRANSPORT.
PubMed=19528298; DOI=10.1083/jcb.200811033;
Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
"HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters
mitochondrial distribution and transport.";
J. Cell Biol. 185:1065-1081(2009).
[44]
FUNCTION.
PubMed=20624928; DOI=10.1096/fj.10-159806;
Gimm T., Wiese M., Teschemacher B., Deggerich A., Schodel J.,
Knaup K.X., Hackenbeck T., Hellerbrand C., Amann K., Wiesener M.S.,
Honing S., Eckardt K.U., Warnecke C.;
"Hypoxia-inducible protein 2 is a novel lipid droplet protein and a
specific target gene of hypoxia-inducible factor-1.";
FASEB J. 24:4443-4458(2010).
[45]
PHOSPHORYLATION AT SER-551; THR-555; SER-576; SER-589 AND SER-657, AND
MUTAGENESIS OF SER-576 AND SER-657.
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).
[46]
PHOSPHORYLATION AT SER-247 BY CSNK1D/CK1, MUTAGENESIS OF SER-247, AND
INTERACTION WITH ARNT.
PubMed=20699359; DOI=10.1242/jcs.068122;
Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E.,
Simos G.;
"Casein kinase 1 regulates human hypoxia-inducible factor HIF-1.";
J. Cell Sci. 123:2976-2986(2010).
[47]
UBIQUITINATION.
PubMed=22537386; DOI=10.1186/1741-7007-10-36;
Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G.;
"UBXN7 docks on neddylated cullin complexes using its UIM motif and
causes HIF1alpha accumulation.";
BMC Biol. 10:36-36(2012).
[48]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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).
[49]
INTERACTION WITH USP19.
PubMed=22128162; DOI=10.1074/jbc.M111.305615;
Altun M., Zhao B., Velasco K., Liu H., Hassink G., Paschke J.,
Pereira T., Lindsten K.;
"Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible
factor 1alpha (HIF-1alpha) during hypoxia.";
J. Biol. Chem. 287:1962-1969(2012).
[50]
INDUCTION.
PubMed=22286099; DOI=10.1038/ncb2424;
Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C.,
Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J.,
Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.;
"The LIMD1 protein bridges an association between the prolyl
hydroxylases and VHL to repress HIF-1 activity.";
Nat. Cell Biol. 14:201-208(2012).
[51]
INTERACTION WITH RWDD3.
PubMed=23469069; DOI=10.1371/journal.pone.0057795;
Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G.,
Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.;
"In silico structural and functional characterization of the RSUME
splice variants.";
PLoS ONE 8:E57795-E57795(2013).
[52]
ACETYLATION AT LYS-709, DEACETYLATION AT LYS-709 BY SIRT2,
HYDROXYLATION, INTERACTION WITH SIRT2 AND EGLN1, AND MUTAGENESIS OF
PRO-402; PRO-564 AND LYS-709.
PubMed=24681946; DOI=10.1038/onc.2014.76;
Seo K.S., Park J.H., Heo J.Y., Jing K., Han J., Min K.N., Kim C.,
Koh G.Y., Lim K., Kang G.Y., Uee Lee J., Yim Y.H., Shong M.,
Kwak T.H., Kweon G.R.;
"SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha
hydroxylation.";
Oncogene 34:1354-1362(2015).
[53]
INTERACTION WITH HSP90AA1 AND HSP90AB1.
PubMed=26517842; DOI=10.1371/journal.pone.0141786;
Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K.,
Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T.,
Beebe K., Trepel J.B., Neckers L.;
"Client proteins and small molecule inhibitors display distinct
binding preferences for constitutive and stress-induced HSP90 isoforms
and their conformationally restricted mutants.";
PLoS ONE 10:E0141786-E0141786(2015).
[54]
HYDROXYLATION PRO-564, UBIQUITINATION, AND INTERACTION WITH CBFA2T3
AND EGLN1.
PubMed=25974097; DOI=10.1371/journal.pone.0123725;
Kumar P., Gullberg U., Olsson I., Ajore R.;
"Myeloid translocation gene-16 co-repressor promotes degradation of
hypoxia-inducible factor 1.";
PLoS ONE 10:E0123725-E0123725(2015).
[55]
REGULATION BY IRON ION, AND HYDROXYLATION.
PubMed=28296633; DOI=10.7554/eLife.22693;
Miles A.L., Burr S.P., Grice G.L., Nathan J.A.;
"The vacuolar-ATPase complex and assembly factors, TMEM199 and
CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular
iron levels.";
Elife 6:E22693-E22693(2017).
[56]
3D-STRUCTURE MODELING.
PubMed=11089639; DOI=10.1080/07391102.2000.10506656;
Michel G., Minet E., Ernest I., Roland I., Durant F., Remacle J.,
Michiels C.;
"A model for the complex between the hypoxia-inducible factor-1 (HIF-
1) and its consensus DNA sequence.";
J. Biomol. Struct. Dyn. 18:169-179(2000).
[57]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 775-826 IN COMPLEX WITH
HIF1AN.
PubMed=12446723; DOI=10.1074/jbc.C200644200;
Elkins J.M., Hewitson K.S., McNeill L.A., Seibel J.F.,
Schlemminger I., Pugh C.W., Ratcliffe P.J., Schofield C.J.;
"Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals
mechanism of oxidative modification of HIF-1 alpha.";
J. Biol. Chem. 278:1802-1806(2003).
[58]
STRUCTURE BY NMR OF 786-826 IN COMPLEX WITH 302-418 OF EP300.
PubMed=11959990; DOI=10.1073/pnas.082117899;
Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M.,
Wagner G., Eck M.J.;
"Structural basis for recruitment of CBP/p300 by hypoxia-inducible
factor-1 alpha.";
Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002).
[59]
STRUCTURE BY NMR OF 776-826 IN COMPLEX WITH 345-439 OF CREBBP.
PubMed=11959977; DOI=10.1073/pnas.082121399;
Dames S.A., Martinez-Yamout M., De Guzman R.N., Dyson H.J.,
Wright P.E.;
"Structural basis for Hif-1 alpha /CBP recognition in the cellular
hypoxic response.";
Proc. Natl. Acad. Sci. U.S.A. 99:5271-5276(2002).
[60]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 556-575 IN COMPLEX WITH
ELOB; ELOC AND 54-213 OF VHL.
PubMed=12004076; DOI=10.1126/science.1073440;
Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr.,
Pavletich N.P.;
"Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition
in signaling.";
Science 296:1886-1889(2002).
[61]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 549-582 IN COMPLEX WITH
17-112 OF ELOB; ELOC AND 52-213 OF VHL.
PubMed=12050673; DOI=10.1038/nature00767;
Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J.,
Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.;
"Structural basis for the recognition of hydroxyproline in HIF-1 alpha
by pVHL.";
Nature 417:975-978(2002).
-!- 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. {ECO:0000269|PubMed:11292861,
ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:16543236, ECO:0000269|PubMed:16973622,
ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:19528298,
ECO:0000269|PubMed:20624928, ECO:0000269|PubMed:22009797,
ECO:0000269|PubMed:9887100}.
-!- SUBUNIT: Interacts with the HIF1A beta/ARNT subunit;
heterodimerization is required for DNA binding. Interacts with
COPS5; the interaction increases the transcriptional activity of
HIF1A through increased stability (By similarity). Interacts with
EP300 (via TAZ-type 1 domains); the interaction is stimulated in
response to hypoxia and inhibited by CITED2. Interacts with CREBBP
(via TAZ-type 1 domains). 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 TSGA10 (By
similarity). Interacts with HIF3A (By similarity). 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 (via
N-terminus) with USP19. Interacts with SIRT2. Interacts
(deacetylated form) with EGLN1. Interacts with CBFA2T3. Interacts
with HSP90AA1 and HSP90AB1 (PubMed:26517842).
{ECO:0000250|UniProtKB:Q61221, ECO:0000269|PubMed:10202154,
ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:10944113,
ECO:0000269|PubMed:11006129, ECO:0000269|PubMed:11389899,
ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:11959977,
ECO:0000269|PubMed:11959990, ECO:0000269|PubMed:12004076,
ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:12778114,
ECO:0000269|PubMed:14757845, ECO:0000269|PubMed:15776016,
ECO:0000269|PubMed:16288748, ECO:0000269|PubMed:16543236,
ECO:0000269|PubMed:16862177, ECO:0000269|PubMed:16973622,
ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956732,
ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:20699359,
ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:23469069,
ECO:0000269|PubMed:24681946, ECO:0000269|PubMed:25974097,
ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:8917528,
ECO:0000269|PubMed:9887100}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-447269, EBI-608057;
P27540:ARNT; NbExp=10; IntAct=EBI-447269, EBI-80809;
P49407:ARRB1; NbExp=3; IntAct=EBI-447269, EBI-743313;
Q9C0J9:BHLHE41; NbExp=2; IntAct=EBI-447269, EBI-10988877;
Q99PV5:Bhlhe41 (xeno); NbExp=3; IntAct=EBI-447269, EBI-6143801;
O00257:CBX4; NbExp=15; IntAct=EBI-447269, EBI-722425;
Q92793:CREBBP; NbExp=2; IntAct=EBI-447269, EBI-81215;
Q6S7F2:E2f7 (xeno); NbExp=3; IntAct=EBI-447269, EBI-8030813;
Q5RIX9:e2f7 (xeno); NbExp=2; IntAct=EBI-447269, EBI-8030618;
Q96CJ1:EAF2; NbExp=3; IntAct=EBI-447269, EBI-1245604;
Q9GZT9:EGLN1; NbExp=4; IntAct=EBI-447269, EBI-1174818;
Q96KS0:EGLN2; NbExp=2; IntAct=EBI-447269, EBI-726614;
Q9H6Z9:EGLN3; NbExp=5; IntAct=EBI-447269, EBI-1175354;
Q09472:EP300; NbExp=20; IntAct=EBI-447269, EBI-447295;
P11474:ESRRA; NbExp=3; IntAct=EBI-447269, EBI-372412;
Q61539:Esrrb (xeno); NbExp=2; IntAct=EBI-447269, EBI-2312731;
P09467:FBP1; NbExp=5; IntAct=EBI-447269, EBI-712740;
Q9NWT6:HIF1AN; NbExp=12; IntAct=EBI-447269, EBI-745632;
Q92831:KAT2B; NbExp=2; IntAct=EBI-447269, EBI-477430;
Q13330:MTA1; NbExp=6; IntAct=EBI-447269, EBI-714236;
P46531:NOTCH1; NbExp=2; IntAct=EBI-447269, EBI-636374;
Q13438:OS9; NbExp=9; IntAct=EBI-447269, EBI-725454;
Q8N2W9:PIAS4; NbExp=3; IntAct=EBI-447269, EBI-473160;
P14618-1:PKM; NbExp=7; IntAct=EBI-447269, EBI-4304679;
P25789:PSMA4; NbExp=4; IntAct=EBI-447269, EBI-359310;
Q8BIF2:Rbfox3 (xeno); NbExp=2; IntAct=EBI-447269, EBI-4567146;
P51450-2:Rorc (xeno); NbExp=2; IntAct=EBI-447269, EBI-4422078;
Q9UHD8-1:SEPT9; NbExp=4; IntAct=EBI-447269, EBI-851558;
P08047:SP1; NbExp=3; IntAct=EBI-447269, EBI-298336;
P63165:SUMO1; NbExp=4; IntAct=EBI-447269, EBI-80140;
O94888:UBXN7; NbExp=3; IntAct=EBI-447269, EBI-1993627;
P40818:USP8; NbExp=2; IntAct=EBI-447269, EBI-1050865;
P40337:VHL; NbExp=18; IntAct=EBI-447269, EBI-301246;
P17861:XBP1; NbExp=3; IntAct=EBI-447269, EBI-6942961;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16665-1; Sequence=Displayed;
Name=2;
IsoId=Q16665-2; Sequence=VSP_047335, VSP_007738;
Note=No experimental confirmation available.;
Name=3; Synonyms=I.3;
IsoId=Q16665-3; Sequence=VSP_044942;
Note=Up-regulated in peripheral T-lymphocytes after T-cell
receptor stimulation. Highest expression in peripheral blood
leukocytes and thymus.;
-!- TISSUE SPECIFICITY: Expressed in most tissues with highest levels
in kidney and heart. Overexpressed in the majority of common human
cancers and their metastases, due to the presence of intratumoral
hypoxia and as a result of mutations in genes encoding
oncoproteins and tumor suppressors. A higher level expression seen
in pituitary tumors as compared to the pituitary gland.
{ECO:0000269|PubMed:22009797}.
-!- 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}.
-!- 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).
-!- 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. Phosphorylation by GSK3-beta and PLK3 promote degradation
by the proteasome. {ECO:0000269|PubMed:20699359,
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:15465032, ECO:0000269|PubMed:15776016,
ECO:0000269|PubMed:17610843, ECO:0000269|PubMed:17956732}.
-!- 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.
-!- WEB RESOURCE: Name=Wikipedia; Note=Hypoxia inducible factor entry;
URL="https://en.wikipedia.org/wiki/Hypoxia_inducible_factor";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U22431; AAC50152.1; -; mRNA.
EMBL; U29165; AAC51210.1; -; mRNA.
EMBL; AF050127; AAC68568.1; -; Genomic_DNA.
EMBL; AF050115; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050116; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050117; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050118; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050119; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050120; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050121; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050122; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050123; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050124; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050125; AAC68568.1; JOINED; Genomic_DNA.
EMBL; AF050126; AAC68568.1; JOINED; Genomic_DNA.
EMBL; FJ790247; ACN88547.1; -; mRNA.
EMBL; AF207601; AAF20139.1; -; mRNA.
EMBL; AF207602; AAF20140.1; -; mRNA.
EMBL; AF208487; AAF20149.1; -; Genomic_DNA.
EMBL; AF304431; AAG43026.1; -; mRNA.
EMBL; AB073325; BAB70608.1; -; mRNA.
EMBL; BT009776; AAP88778.1; -; mRNA.
EMBL; AL137129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012527; AAH12527.1; -; mRNA.
CCDS; CCDS58324.1; -. [Q16665-3]
CCDS; CCDS9753.1; -. [Q16665-1]
CCDS; CCDS9754.1; -. [Q16665-2]
PIR; I38972; I38972.
RefSeq; NP_001230013.1; NM_001243084.1. [Q16665-3]
RefSeq; NP_001521.1; NM_001530.3. [Q16665-1]
RefSeq; NP_851397.1; NM_181054.2. [Q16665-2]
UniGene; Hs.597216; -.
UniGene; Hs.719495; -.
PDB; 1D7G; Model; -; D=15-73.
PDB; 1H2K; X-ray; 2.15 A; S=786-826.
PDB; 1H2L; X-ray; 2.25 A; S=786-826.
PDB; 1H2M; X-ray; 2.50 A; S=775-826.
PDB; 1L3E; NMR; -; A=786-826.
PDB; 1L8C; NMR; -; B=776-826.
PDB; 1LM8; X-ray; 1.85 A; H=556-575.
PDB; 1LQB; X-ray; 2.00 A; D=549-582.
PDB; 2ILM; X-ray; 2.30 A; S=786-826.
PDB; 3HQR; X-ray; 2.00 A; S=558-574.
PDB; 3HQU; X-ray; 2.30 A; S=558-574.
PDB; 4AJY; X-ray; 1.73 A; H=559-577.
PDB; 4H6J; X-ray; 1.52 A; A=238-348.
PDB; 5JWP; X-ray; 2.10 A; B=788-806.
PDB; 5L9B; X-ray; 1.95 A; C/D=556-574.
PDB; 5L9V; X-ray; 1.83 A; C/D=395-411.
PDB; 5LA9; X-ray; 2.81 A; C/D=395-411.
PDB; 5LAS; X-ray; 2.10 A; C/D=395-411.
PDBsum; 1D7G; -.
PDBsum; 1H2K; -.
PDBsum; 1H2L; -.
PDBsum; 1H2M; -.
PDBsum; 1L3E; -.
PDBsum; 1L8C; -.
PDBsum; 1LM8; -.
PDBsum; 1LQB; -.
PDBsum; 2ILM; -.
PDBsum; 3HQR; -.
PDBsum; 3HQU; -.
PDBsum; 4AJY; -.
PDBsum; 4H6J; -.
PDBsum; 5JWP; -.
PDBsum; 5L9B; -.
PDBsum; 5L9V; -.
PDBsum; 5LA9; -.
PDBsum; 5LAS; -.
DisProt; DP00262; -.
ProteinModelPortal; Q16665; -.
SMR; Q16665; -.
BioGrid; 109338; 162.
CORUM; Q16665; -.
DIP; DIP-29722N; -.
ELM; Q16665; -.
IntAct; Q16665; 91.
MINT; MINT-133270; -.
STRING; 9606.ENSP00000338018; -.
BindingDB; Q16665; -.
ChEMBL; CHEMBL4261; -.
DrugBank; DB02342; 2-Methoxyestradiol.
DrugBank; DB01136; Carvedilol.
DrugBank; DB08687; N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE.
iPTMnet; Q16665; -.
PhosphoSitePlus; Q16665; -.
BioMuta; HIF-1A; -.
DMDM; 2498017; -.
MaxQB; Q16665; -.
PaxDb; Q16665; -.
PeptideAtlas; Q16665; -.
PRIDE; Q16665; -.
DNASU; 3091; -.
Ensembl; ENST00000323441; ENSP00000323326; ENSG00000100644. [Q16665-2]
Ensembl; ENST00000337138; ENSP00000338018; ENSG00000100644. [Q16665-1]
Ensembl; ENST00000539097; ENSP00000437955; ENSG00000100644. [Q16665-3]
GeneID; 3091; -.
KEGG; hsa:3091; -.
UCSC; uc001xfq.3; human. [Q16665-1]
CTD; 3091; -.
DisGeNET; 3091; -.
EuPathDB; HostDB:ENSG00000100644.16; -.
GeneCards; HIF1A; -.
HGNC; HGNC:4910; HIF1A.
HPA; CAB017442; -.
HPA; HPA000907; -.
HPA; HPA001275; -.
MIM; 603348; gene.
neXtProt; NX_Q16665; -.
OpenTargets; ENSG00000100644; -.
PharmGKB; PA29283; -.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
GeneTree; ENSGT00760000118788; -.
HOGENOM; HOG000234306; -.
HOVERGEN; HBG060456; -.
InParanoid; Q16665; -.
KO; K08268; -.
OMA; YCFDVDS; -.
OrthoDB; EOG091G0486; -.
PhylomeDB; Q16665; -.
TreeFam; TF317772; -.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-1234162; Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8849473; PTK6 Expression.
Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
Reactome; R-HSA-8951664; Neddylation.
SignaLink; Q16665; -.
SIGNOR; Q16665; -.
ChiTaRS; HIF1A; human.
EvolutionaryTrace; Q16665; -.
GeneWiki; HIF1A; -.
GenomeRNAi; 3091; -.
PRO; PR:Q16665; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100644; -.
CleanEx; HS_HIF1A; -.
ExpressionAtlas; Q16665; baseline and differential.
Genevisible; Q16665; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031514; C:motile cilium; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0070888; F:E-box binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
GO; GO:0001922; P:B-1 B cell homeostasis; IEA:Ensembl.
GO; GO:0003208; P:cardiac ventricle morphogenesis; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:BHF-UCL.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0032963; P:collagen metabolic process; ISS:BHF-UCL.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; ISS:BHF-UCL.
GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0071542; P:dopaminergic neuron differentiation; IEA:Ensembl.
GO; GO:0051541; P:elastin metabolic process; ISS:BHF-UCL.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0061030; P:epithelial cell differentiation involved in mammary gland alveolus development; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0042541; P:hemoglobin biosynthetic process; IEA:Ensembl.
GO; GO:0097411; P:hypoxia-inducible factor-1alpha signaling pathway; IEA:Ensembl.
GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
GO; GO:0061072; P:iris morphogenesis; IEA:Ensembl.
GO; GO:0006089; P:lactate metabolic process; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl.
GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl.
GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IEA:Ensembl.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0032007; P:negative regulation of TOR signaling; IEA:Ensembl.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0021502; P:neural fold elevation formation; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0032364; P:oxygen homeostasis; IDA:HGNC.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; TAS:BHF-UCL.
GO; GO:0070101; P:positive regulation of chemokine-mediated signaling pathway; IC:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IC:BHF-UCL.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:BHF-UCL.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IC:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
GO; GO:0045821; P:positive regulation of glycolytic process; IC:BHF-UCL.
GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IDA:BHF-UCL.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; TAS:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IC:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:1903715; P:regulation of aerobic respiration; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; IMP:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0010039; P:response to iron ion; IEP:UniProtKB.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IMP:BHF-UCL.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0010573; P:vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
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; Direct protein sequencing; DNA-binding;
Hydroxylation; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 826 Hypoxia-inducible factor 1-alpha.
/FTId=PRO_0000127220.
DOMAIN 17 70 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 85 158 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:0000250}.
REGION 380 417 N-terminal VHL recognition site.
REGION 401 603 ODD.
REGION 531 575 NTAD.
REGION 556 572 C-terminal VHL recognition site.
REGION 576 785 ID.
REGION 786 826 CTAD.
MOTIF 718 721 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 615 621 Poly-Thr.
MOD_RES 247 247 Phosphoserine; by CK1.
{ECO:0000269|PubMed:20699359}.
MOD_RES 402 402 4-hydroxyproline.
{ECO:0000269|PubMed:11566883}.
MOD_RES 532 532 N6-acetyllysine.
{ECO:0000269|PubMed:24681946}.
MOD_RES 551 551 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:20889502}.
MOD_RES 555 555 Phosphothreonine; by GSK3-beta.
{ECO:0000269|PubMed:20889502}.
MOD_RES 564 564 4-hydroxyproline.
{ECO:0000269|PubMed:11292861,
ECO:0000269|PubMed:11566883,
ECO:0000269|PubMed:12351678,
ECO:0000269|PubMed:25974097}.
MOD_RES 576 576 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:20889502}.
MOD_RES 589 589 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:20889502}.
MOD_RES 657 657 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:20889502}.
MOD_RES 709 709 N6-acetyllysine.
{ECO:0000269|PubMed:24681946}.
MOD_RES 800 800 S-nitrosocysteine.
{ECO:0000305|PubMed:12914934}.
MOD_RES 803 803 (3S)-3-hydroxyasparagine.
{ECO:0000269|PubMed:12080085}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:17610843}.
CROSSLNK 477 477 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:17610843}.
CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:16862177}.
CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:16862177}.
CROSSLNK 547 547 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:16862177}.
VAR_SEQ 1 12 MEGAGGANDKKK -> MSSQCRSLENKFVFLKEGLGNSKPE
ELEEIRIENGR (in isoform 3).
{ECO:0000303|PubMed:18638657}.
/FTId=VSP_044942.
VAR_SEQ 735 735 G -> I (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_047335.
VAR_SEQ 736 826 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_007738.
VARIANT 582 582 P -> S (in dbSNP:rs11549465).
/FTId=VAR_049541.
VARIANT 588 588 A -> T (in dbSNP:rs11549467).
/FTId=VAR_049542.
VARIANT 796 796 T -> A (in dbSNP:rs1802821).
/FTId=VAR_015854.
MUTAGEN 247 247 S->A: Constitutive kinase activity.
{ECO:0000269|PubMed:20699359}.
MUTAGEN 247 247 S->D: Impaired kinase activity.
{ECO:0000269|PubMed:20699359}.
MUTAGEN 377 377 K->R: No change in HIF1A protein turnover
rate but increased transcriptional
activity; when associated with R-391; R-
477 and R-532.
{ECO:0000269|PubMed:17610843}.
MUTAGEN 389 389 K->R: No change in sumoylation.
{ECO:0000269|PubMed:15465032}.
MUTAGEN 391 391 K->R: Abolishes 1 sumoylation. Abolishes
1 sumoylation; when associated with R-
532. Abolishes 2 sumoylations; when
associated with R-477. No change in HIF1A
protein turnover rate but increased
transcriptional activity; when associated
with R-377; R-477 and R-532.
{ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:17610843}.
MUTAGEN 392 392 K->R: No change in sumoylation.
{ECO:0000269|PubMed:15465032}.
MUTAGEN 394 394 P->A: No change in VHLE3-dependent
ubiquitination.
{ECO:0000269|PubMed:11566883}.
MUTAGEN 397 397 L->A: Abolishes VHLE3-dependent
ubiquitination; when associated with A-
400. {ECO:0000269|PubMed:11566883}.
MUTAGEN 400 400 L->A: Abolishes VHLE3-dependent
ubiquitination; when associated with A-
397. {ECO:0000269|PubMed:11566883}.
MUTAGEN 402 402 P->A: Abolishes in VHLE3-dependent
ubiquitination, abolishes oxygen-
dependent regulation of VP16, partially
reduced VHLE target site ubiquitination
and no interaction with VHL. No VHLE
target site ubiquitination; when
associated with G-564. Increases HIF1A
instability and reduces HIF1A-induced
target gene transcriptional activation;
when associated with A-564.
{ECO:0000269|PubMed:11566883,
ECO:0000269|PubMed:16862177,
ECO:0000269|PubMed:24681946}.
MUTAGEN 442 442 K->R: No change in sumoylation.
{ECO:0000269|PubMed:15465032}.
MUTAGEN 460 460 K->R: No change in sumoylation nor in
ARD1-mediated acetylation.
{ECO:0000269|PubMed:15465032}.
MUTAGEN 477 477 K->R: Abolishes 1 sumoylation. Abolishes
2 sumoylations; when associated with R-
391. No change in HIF1A protein turnover
rate but increased transcriptional
activity; when associated with R-377; R-
391 and R-532.
{ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:17610843}.
MUTAGEN 532 532 K->R: Reduced ubiquitination. No change
in sumoylation nor on interaction with
ARD1A. No change in HIF1A protein
turnover rate but increased
transcriptional activity; when associated
with R-377; R-391 and R-477. Complete
loss of ubiquitination, but no change in
VHL binding; when associated with K-538
and K-547. {ECO:0000269|PubMed:10944113,
ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:16288748,
ECO:0000269|PubMed:16862177,
ECO:0000269|PubMed:17610843}.
MUTAGEN 538 538 K->R: No change in sumoylation, but
reduced ubiquitination. Complete loss of
ubiquitination, but no change in VHL
binding; when associated with K-532 and
K-547. {ECO:0000269|PubMed:10944113,
ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:16862177}.
MUTAGEN 547 547 K->R: No change in sumoylation, but
reduced ubiquitination. Complete loss of
ubiquitination, but no change in VHL
binding; when associated with K-532 and
K-538. {ECO:0000269|PubMed:10944113,
ECO:0000269|PubMed:15465032,
ECO:0000269|PubMed:16862177}.
MUTAGEN 551 551 S->G: Constitutive expression under
nonhypoxic conditions by decreasing
ubiquitination.
{ECO:0000269|PubMed:10758161}.
MUTAGEN 552 552 T->A: Constitutive expression under
nonhypoxic conditions by decreasing
ubiquitination.
{ECO:0000269|PubMed:10758161}.
MUTAGEN 564 564 P->A: Increases HIF1A instability and
reduces HIF1A-induced target gene
transcriptional activation; when
associated with A-402.
{ECO:0000269|PubMed:11566883,
ECO:0000269|PubMed:16862177,
ECO:0000269|PubMed:24681946}.
MUTAGEN 564 564 P->G: No change in VHL-dependent
ubiquitination. Partially reduced VHLE
target site ubiquitination. No VHLE
target site ubiquitination; when
associated with A-402.
{ECO:0000269|PubMed:11566883,
ECO:0000269|PubMed:16862177,
ECO:0000269|PubMed:24681946}.
MUTAGEN 576 576 S->A: Induces stabilization of the
protein. {ECO:0000269|PubMed:20889502}.
MUTAGEN 657 657 S->A: Induces stabilization of the
protein. {ECO:0000269|PubMed:20889502}.
MUTAGEN 709 709 K->R: Abolishes SIRT2-mediated
deacetylation, increases HIF1A
instability and reduces HIF1A-induced
target gene transcriptional activation.
Increases interaction with EGLN1.
{ECO:0000269|PubMed:24681946}.
MUTAGEN 719 719 K->T: Dramatic reduction of accumulation
in the nucleus in response to hypoxia.
{ECO:0000269|PubMed:10944113,
ECO:0000269|PubMed:9822602}.
MUTAGEN 795 795 L->A: Inhibits interaction with EP300 and
transactivation activity.
{ECO:0000269|PubMed:12778114}.
MUTAGEN 800 800 C->A: Blocks increase in transcriptional
activation caused by nitrosylation.
{ECO:0000269|PubMed:10202154,
ECO:0000269|PubMed:12914934}.
MUTAGEN 800 800 C->S: Abolishes hypoxia-inducible
transcriptional activation of ctaD.
{ECO:0000269|PubMed:10202154,
ECO:0000269|PubMed:12914934}.
MUTAGEN 803 803 N->A: Recruits CREBBP. No enhancement of
CREBBP by Clioquinol in the presence of
FIH1. No change in nuclear location nor
on repression of transcriptional activity
in the presence of histone deacetylase
inhibitor. {ECO:0000269|PubMed:16543236,
ECO:0000269|PubMed:16973622}.
CONFLICT 572 572 F -> L (in Ref. 3; AAC68568).
{ECO:0000305}.
STRAND 241 246 {ECO:0000244|PDB:4H6J}.
STRAND 251 255 {ECO:0000244|PDB:4H6J}.
HELIX 258 263 {ECO:0000244|PDB:4H6J}.
HELIX 267 270 {ECO:0000244|PDB:4H6J}.
HELIX 275 277 {ECO:0000244|PDB:4H6J}.
TURN 281 283 {ECO:0000244|PDB:4H6J}.
HELIX 284 297 {ECO:0000244|PDB:4H6J}.
STRAND 298 301 {ECO:0000244|PDB:4H6J}.
STRAND 305 308 {ECO:0000244|PDB:4H6J}.
STRAND 310 325 {ECO:0000244|PDB:4H6J}.
TURN 327 329 {ECO:0000244|PDB:4H6J}.
STRAND 332 341 {ECO:0000244|PDB:4H6J}.
HELIX 397 400 {ECO:0000244|PDB:5L9V}.
STRAND 408 410 {ECO:0000244|PDB:5LA9}.
HELIX 559 562 {ECO:0000244|PDB:5L9B}.
TURN 779 783 {ECO:0000244|PDB:1L8C}.
HELIX 784 787 {ECO:0000244|PDB:1L8C}.
STRAND 789 792 {ECO:0000244|PDB:1L8C}.
HELIX 797 803 {ECO:0000244|PDB:1L3E}.
STRAND 807 809 {ECO:0000244|PDB:1L8C}.
HELIX 815 822 {ECO:0000244|PDB:1H2K}.
SEQUENCE 826 AA; 92670 MW; ABD4F7DAA135BE2D CRC64;
MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM
RLTISYLRVR KLLDAGDLDI EDDMKAQMNC FYLKALDGFV MVLTDDGDMI YISDNVNKYM
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGLVKKGKE QNTQRSFFLR MKCTLTSRGR
TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTECV
LKPVESSDMK MTQLFTKVES EDTSSLFDKL KKEPDALTLL APAAGDTIIS LDFGSNDTET
DDQQLEEVPL YNDVMLPSPN EKLQNINLAM SPLPTAETPK PLRSSADPAL NQEVALKLEP
NPESLELSFT MPQIQDQTPS PSDGSTRQSS PEPNSPSEYC FYVDSDMVNE FKLELVEKLF
AEDTEAKNPF STQDTDLDLE MLAPYIPMDD DFQLRSFDQL SPLESSSASP ESASPQSTVT
VFQQTQIQEP TANATTTTAT TDELKTVTKD RMEDIKILIA SPSPTHIHKE TTSATSSPYR
DTQSRTASPN RAGKGVIEQT EKSHPRSPNV LSVALSQRTT VPEEELNPKI LALQNAQRKR
KMEHDGSLFQ AVGIGTLLQQ PDDHAATTSL SWKRVKGCKS SEQNGMEQKT IILIPSDLAC
RLLGQSMDES GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN


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20-272-192234 HIF1 alpha - Mouse monoclonal [OZ12] to HIF1 alpha; HIF-1 alpha; HIF1 alpha; ARNT-interacting protein; Member of PAS protein 1; Basic-helix-loop-helix-PAS protein MOP1 Monoclonal 0.5 ml
U2004h CLIA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alph 96T
E2004h ELISA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF- 96T
U2004h CLIA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2 96T
E2004h ELISA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alp 96T
EIAAB37697 Basic helix-loop-helix transcription factor scleraxis,bHLHa41,BHLHA41,bHLHa48,Class A basic helix-loop-helix protein 41,Class A basic helix-loop-helix protein 48,Homo sapiens,Human,SCX,SCXA
18-272-195931 HIF2 alpha - Rabbit polyclonal to HIF2 alpha; EPAS-1; Member of PAS protein 2; Basic-helix-loop-helix-PAS protein MOP2; Hypoxia-inducible factor 2 alpha; HIF-2 alpha; HIF2 alpha; HIF-1 alpha-like fact 0.2 ml
EIAAB27612 Basic-helix-loop-helix-PAS protein MOP5,bHLHe11,BHLHE11,Class E basic helix-loop-helix protein 11,Homo sapiens,Human,Member of PAS protein 5,MOP5,Neuronal PAS domain-containing protein 1,Neuronal PAS1
EIAAB27615 Basic-helix-loop-helix-PAS protein MOP4,bHLHe9,BHLHE9,Class E basic helix-loop-helix protein 9,Homo sapiens,Human,Member of PAS protein 4,MOP4,Neuronal PAS domain-containing protein 2,Neuronal PAS2,NP
EIAAB27618 Basic-helix-loop-helix-PAS protein MOP6,bHLHe12,BHLHE12,Class E basic helix-loop-helix protein 12,Homo sapiens,Human,Member of PAS protein 6,MOP6,Neuronal PAS domain-containing protein 3,Neuronal PAS3
EIAAB28826 bHLHb1,BHLHB1,bHLHe19,BHLHE19,Class B basic helix-loop-helix protein 1,Class E basic helix-loop-helix protein 19,Homo sapiens,Human,OLIG2,Oligo2,Oligodendrocyte transcription factor 2,PRKCBP2,Protein
U0255h CLIA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA kit ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
EIAAB28821 bHLHb6,BHLHB6,bHLHe21,BHLHE21,Class B basic helix-loop-helix protein 6,Class E basic helix-loop-helix protein 21,Homo sapiens,Human,OLIG1,Oligo1,Oligodendrocyte transcription factor 1
EIAAB28828 bHLHb7,BHLHB7,bHLHe20,BHLHE20,Class B basic helix-loop-helix protein 7,Class E basic helix-loop-helix protein 20,Homo sapiens,Human,OLIG3,Oligo3,Oligodendrocyte transcription factor 3
EIAAB27132 bHLHa6,BHLHA6,Class A basic helix-loop-helix protein 6,Homo sapiens,Human,NeuroD3,NEUROD3,NEUROG1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,NGN,NGN1,NG
EIAAB27130 Ath4c,Helix-loop-helix protein mATH-4C,mATH4C,Mouse,Mus musculus,NeuroD3,Neurod3,Neurog1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,Ngn,Ngn1,NGN-1
LF-PA40832 anti-Basic-helix-loop-helix-PAS Protein, Rabbit polyclonal to Basic-helix-loop-helix-PAS Protein, Isotype IgG, Host Rabbit 50 ug
18-003-42135 Aryl hydrocarbon receptor nuclear translocator-like protein 1 - Brain and muscle ARNT-like 1; Member of PAS protein 3; Basic-helix-loop-helix-PAS orphan MOP3; bHLH-PAS protein JAP3 Polyclonal 0.1 mg Protein A
HIF3A HIF1A Gene hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)


 

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