Reviewed, UniProtKB/Swiss-Prot Q61221 (HIF1A_MOUSE)

Names and origin

Protein names

Recommended name:
    Hypoxia-inducible factor 1 alpha
      Short name=HIF-1 alpha
      Short name=HIF1 alpha
Alternative name(s):
    ARNT-interacting protein

Gene names

Name:

Hif1a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	836 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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, 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 CREBPB 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 By similarity.
Subunit structure	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 CREBBP and EP300 (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 RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability By similarity. Interacts with TSGA10.
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia By similarity.
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.
Post-translational modification	In normoxia, is hydroxylated on Pro-402 and Pro-577 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD1 and EGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-577. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization By similarity. 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. S-nitrosylation of Cys-810 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex By similarity. Requires phosphorylation for DNA-binding By similarity. Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transCriptional activity. Ref.9 Ref.11 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. The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains By similarity.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Hydroxylation Isopeptide bond Phosphoprotein S-nitrosylation Ubl conjugation
Gene Ontology (GO)
Biological process	angiogenesis Inferred from mutant phenotype. Source: MGI cartilage development Inferred from mutant phenotype. Source: MGI cellular iron ion homeostasis Inferred from mutant phenotype. Source: MGI collagen metabolic process Inferred from mutant phenotype. Source: UniProtKB connective tissue replacement during inflammatory response Inferred from mutant phenotype. Source: UniProtKB elastin metabolic process Inferred from mutant phenotype. Source: UniProtKB embryonic hemopoiesis Inferred from mutant phenotype. Source: MGI embryonic placenta development Inferred from genetic interaction. Source: MGI epithelial to mesenchymal transition Inferred from mutant phenotype. Source: UniProtKB glucose homeostasis Inferred from mutant phenotype. Source: MGI heart looping Inferred from mutant phenotype. Source: MGI hemoglobin biosynthetic process Inferred from mutant phenotype. Source: MGI lactate metabolic process Inferred from mutant phenotype. Source: MGI muscle homeostasis Inferred from mutant phenotype. Source: MGI negative regulation of growth Inferred from mutant phenotype. Source: MGI neural crest cell migration Inferred from mutant phenotype. Source: MGI positive regulation of epithelial cell migration Inferred from mutant phenotype. Source: UniProtKB positive regulation of erythrocyte differentiation Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: MGI positive regulation of vascular endothelial growth factor receptor signaling pathway Inferred from mutant phenotype. Source: MGI regulation of apoptosis Inferred from mutant phenotype. Source: MGI regulation of catalytic activity Inferred from mutant phenotype. Source: MGI regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from mutant phenotype. Source: MGI response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB response to muscle activity Inferred from mutant phenotype. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule-based flagellum Inferred from direct assay. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	histone acetyltransferase binding Inferred from sequence or structural similarity. Source: UniProtKB histone deacetylase binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sumo1	P63166	2	EBI-298954,EBI-80152

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61221-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q61221-2)

The sequence of this isoform differs from the canonical sequence as follows:
     512-525: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 836	836	Hypoxia-inducible factor 1 alpha		PRO_0000127221
Regions
	Domain	31 – 71	41	Helix-loop-helix motif
	Domain	80 – 155	76	PAS 1
	Domain	228 – 298	71	PAS 2
	Domain	302 – 345	44	PAC
	DNA binding	17 – 30	14	Basic motif
	Region	1 – 401	401	Interaction with TSGA10
	Region	380 – 417	38	N-terminal VHL recognition site By similarity
	Region	401 – 613	213	ODD
	Region	544 – 588	45	NTAD
	Region	569 – 585	17	C-terminal VHL recognition site By similarity
	Region	589 – 795	207	ID
	Region	796 – 836	41	CTAD
	Motif	728 – 731	4	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	402	1	4-hydroxyproline By similarity
	Modified residue	577	1	4-hydroxyproline By similarity
	Modified residue	810	1	S-nitrosocysteine By similarity
	Modified residue	813	1	(3S)-3-hydroxyasparagine By similarity
	Cross-link	391		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	476		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	545		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
	Cross-link	551		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
	Cross-link	560		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
Natural variations
	Alternative sequence	512 – 525	14	Missing in isoform 2.		VSP_007739
Experimental info
	Sequence conflict	12	1	K → NR in BAC28578. Ref.4
	Sequence conflict	31	1	S → T in AAC52730. Ref.1
	Sequence conflict	128	1	T → A Ref.1
	Sequence conflict	128	1	T → A Ref.6
	Sequence conflict	351	1	I → L in AAC52730. Ref.1
	Sequence conflict	369	1	M → K in AAH26139. Ref.5
	Sequence conflict	382	1	D → A in AAH26139. Ref.5
	Sequence conflict	397	1	L → H in BAC28578. Ref.4
	Sequence conflict	569	1	D → G in BAC28578. Ref.4
	Sequence conflict	660	1	Q → K in BAC28305. Ref.4
	Sequence conflict	700	1	N → K Ref.1
	Sequence conflict	700	1	N → K Ref.2
	Sequence conflict	799	1	E → V Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 3, 2003. Version 3. Checksum: 84D64ECAC2CC753B	FASTA	836	93,516
	10 20 30 40 50 60 MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM 70 80 90 100 110 120 RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV MVLTDDGDMV YISDNVNKYM 130 140 150 160 170 180 GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR 190 200 210 220 230 240 TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK 250 260 270 280 290 300 TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV 310 320 330 340 350 360 TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTESV 370 380 390 400 410 420 LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL APAAGDTIIS LDFGSDDTET 430 440 450 460 470 480 EDQQLEDVPL YNDVMFPSSN EKLNINLAMS PLPSSETPKP LRSSADPALN QEVALKLESS 490 500 510 520 530 540 PESLGLSFTM PQIQDQPASP SDGSTRQSSP ERLLQENVNT PNFSQPNSPS EYCFDVDSDM 550 560 570 580 590 600 VNVFKLELVE KLFAEDTEAK NPFSTQDTDL DLEMLAPYIP MDDDFQLRSF DQLSPLESNS 610 620 630 640 650 660 PSPPSMSTVT GFQQTQLQKP TITATATTTA TTDESKTETK DNKEDIKILI ASPSSTQVPQ 670 680 690 700 710 720 ETTTAKASAY SGTHSRTASP DRAGKRVIEQ TDKAHPRSLN LSATLNQRNT VPEEELNPKT 730 740 750 760 770 780 IASQNAQRKR KMEHDGSLFQ AAGIGTLLQQ PGDCAPTMSL SWKRVKGFIS SEQNGTEQKT 790 800 810 820 830 IILIPSDLAC RLLGQSMDES GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN
	Isoform 2. Checksum: 8DC6E7C1772AF1BF	FASTA	822	91,874
	10 20 30 40 50 60 MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM 70 80 90 100 110 120 RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV MVLTDDGDMV YISDNVNKYM 130 140 150 160 170 180 GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR 190 200 210 220 230 240 TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK 250 260 270 280 290 300 TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV 310 320 330 340 350 360 TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTESV 370 380 390 400 410 420 LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL APAAGDTIIS LDFGSDDTET 430 440 450 460 470 480 EDQQLEDVPL YNDVMFPSSN EKLNINLAMS PLPSSETPKP LRSSADPALN QEVALKLESS 490 500 510 520 530 540 PESLGLSFTM PQIQDQPASP SDGSTRQSSP EPNSPSEYCF DVDSDMVNVF KLELVEKLFA 550 560 570 580 590 600 EDTEAKNPFS TQDTDLDLEM LAPYIPMDDD FQLRSFDQLS PLESNSPSPP SMSTVTGFQQ 610 620 630 640 650 660 TQLQKPTITA TATTTATTDE SKTETKDNKE DIKILIASPS STQVPQETTT AKASAYSGTH 670 680 690 700 710 720 SRTASPDRAG KRVIEQTDKA HPRSLNLSAT LNQRNTVPEE ELNPKTIASQ NAQRKRKMEH 730 740 750 760 770 780 DGSLFQAAGI GTLLQQPGDC APTMSLSWKR VKGFISSEQN GTEQKTIILI PSDLACRLLG 790 800 810 820 QSMDESGLPQ LTSYDCEVNA PIQGSRNLLQ GEELLRALDQ VN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Induction of phosphoglycerate kinase 1 gene expression by hypoxia. Roles of Arnt and HIF1alpha." Li H., Ko H.P., Whitlock J.P. Jr. J. Biol. Chem. 271:21262-21267(1996) [PubMed: 8702901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Hepatocyte.
[2]	"Molecular characterization of the murine Hif-1 alpha locus." Luo G., Gu Y.-Z., Jain S., Chan W.K., Carr K.M., Hogenesch J.B., Bradfield C.A. Gene Expr. 6:287-299(1997) [PubMed: 9368100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Strain: 129/SvJ.
[3]	"The mouse gene for hypoxia-inducible factor-1alpha. Genomic organization, expression and characterization of an alternative first exon and 5' flanking sequence." Wenger R.H., Rolfs A., Kvietikova I., Spielmann P., Zimmermann D.R., Gassmann M. Eur. J. Biochem. 246:155-165(1997) [PubMed: 9210478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). Strain: 129/Sv.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Colon, Diencephalon, Embryo and Skin.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary tumor.
[6]	"Nucleotide sequence, chromosomal assignment and mRNA expression of mouse hypoxia-inducible factor-1 alpha." Wenger R.H., Rolfs A., Marti H.H., Guenet J.-L., Gassmann M. Biochem. Biophys. Res. Commun. 223:54-59(1996) [PubMed: 8660378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-822 (ISOFORM 2). Tissue: Hepatocyte.
[7]	O'Rourke J.F. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 22-85. Tissue: Hepatocyte.
[8]	"Jab1 interacts directly with HIF-1alpha and regulates its stability." 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. J. Biol. Chem. 277:9-12(2002) [PubMed: 11707426] [Abstract] Cited for: INTERACTION WITH COPS5.
[9]	"Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1alpha in adult mouse brain and heart in vivo." Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X., Sjoeland H., Billig H. FEBS Lett. 569:293-300(2004) [PubMed: 15225651] [Abstract] Cited for: SUMOYLATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
[10]	"TSGA10 prevents nuclear localization of the hypoxia-inducible factor (HIF)-1alpha." Haegele S., Behnam B., Borter E., Wolfe J., Paasch U., Lukashev D., Sitkovsky M., Wenger R.H., Katschinski D.M. FEBS Lett. 580:3731-3738(2006) [PubMed: 16777103] [Abstract] Cited for: INTERACTION WITH TSGA10.
[11]	"SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia." Cheng J., Kang X., Zhang S., Yeh E.T.H. Cell 131:584-595(2007) [PubMed: 17981124] [Abstract] Cited for: DESUMOYLATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U59496 Genomic DNA. Translation: AAC52730.1. AF003695 mRNA. Translation: AAC53455.1. Y09085, Y13656 Genomic DNA. Translation: CAA70306.1. Y09085 Genomic DNA. Translation: CAA70305.1. AF004155 , AF004141, AF004142, AF004143, AF004144, AF004145, AF004146, AF004147, AF004148, AF004149, AF004150, AF004151, AF004152, AF004153, AF004154 Genomic DNA. Translation: AAC53461.1. AK034087 mRNA. Translation: BAC28578.1. AK076395 mRNA. Translation: BAC36320.1. AK033471 mRNA. Translation: BAC28305.1. AK017853 mRNA. Translation: BAB30975.1. BC026139 mRNA. Translation: AAH26139.1. X95580 mRNA. Translation: CAA64833.1. X95002 mRNA. Translation: CAA64458.1.
IPI	IPI00336700. IPI00406683.
PIR	JC4837.
RefSeq	NP_034561.2.
UniGene	Mm.3879 Mm.446610
3D structure databases
SMR	Q61221. Positions 237-345, 786-836.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61221. 4 interactions.
STRING	Q61221.
PTM databases
PhosphoSite	Q61221.
Genome annotation databases
Ensembl	ENSMUST00000021530; ENSMUSP00000021530; ENSMUSG00000021109; Mus musculus. [Genome view]
GeneID	15251.
KEGG	mmu:15251.
UCSC	uc007nwo.1. mouse. uc007nwq.1. mouse.
Organism-specific databases
CTD	15251.
MGI	MGI:106918. Hif1a.
Phylogenomic databases
HOVERGEN	Q61221.
OMA	MLTHRNG
Gene expression databases
ArrayExpress	Q61221.
Bgee	Q61221.
CleanEx	MM_HIF1A.
Genevestigator	Q61221.
GermOnline	ENSMUSG00000021109. Mus musculus.
Family and domain databases
InterPro	IPR014887. HIF-1_TAD_C. IPR001092. HLH_basic. IPR011598. HLH_DNA_bd. IPR001321. HypoxindF1A_PAS. IPR001610. PAC. IPR000014. PAS. IPR013767. PAS_fold. IPR013655. PAS_fold_3. [Graphical view]
Pfam	PF08778. HIF-1a_CTAD. 1 hit. PF00989. PAS. 1 hit. PF08447. PAS_3. 1 hit. [Graphical view]
PRINTS	PR01080. HYPOXIAIF1A.
SMART	SM00353. HLH. 1 hit. SM00086. PAC. 1 hit. SM00091. PAS. 2 hits. [Graphical view]
PROSITE	PS50888. HLH. 1 hit. PS50113. PAC. False negative. PS50112. PAS. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	287865.
SOURCE	Search...

Entry information

Entry name

HIF1A_MOUSE

Accession

Primary (citable) accession number: Q61221
Secondary accession number(s): O08741 , O08993, Q61664, Q61665, Q8C681, Q8CC19, Q8CCB6, Q8R385, Q9CYA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 3, 2003
Last modified:	November 24, 2009
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)