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Q61221 (HIF1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length836 AA.
Sequence statusComplete.
Protein existenceEvidence 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, 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 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. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia By similarity. Ref.9 Ref.11

Subunit structure

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 GNB2L1/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) By similarity. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability. Interacts with TSGA10. Interacts (via N-terminus) with USP19 By similarity. Ref.8 Ref.10

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia By similarity. Ref.9

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. Deubiquitinated by USP20. 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. 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.

Sumoylated; with 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 bHLH (basic helix-loop-helix) domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMHydroxylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB-1 B cell homeostasis

Inferred from mutant phenotype PubMed 11854513. Source: MGI

angiogenesis

Inferred from mutant phenotype PubMed 14659802PubMed 15073147. Source: MGI

axon transport of mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

blood vessel development

Inferred from mutant phenotype PubMed 9436976. Source: MGI

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 9606183. Source: MGI

cardiac ventricle morphogenesis

Inferred from mutant phenotype PubMed 9436976. Source: MGI

cartilage development

Inferred from mutant phenotype PubMed 11691837. Source: MGI

cell differentiation

Inferred from mutant phenotype PubMed 15073147. Source: MGI

cellular iron ion homeostasis

Inferred from mutant phenotype PubMed 16787915. Source: MGI

cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from mutant phenotype PubMed 12972594. Source: MGI

collagen metabolic process

Inferred from mutant phenotype PubMed 18037992. Source: BHF-UCL

connective tissue replacement involved in inflammatory response wound healing

Inferred from mutant phenotype PubMed 18037992. Source: BHF-UCL

digestive tract morphogenesis

Inferred from mutant phenotype PubMed 20808783. Source: MGI

dopaminergic neuron differentiation

Inferred from mutant phenotype PubMed 17215402. Source: MGI

elastin metabolic process

Inferred from mutant phenotype PubMed 18037992. Source: BHF-UCL

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 16787915. Source: MGI

embryonic placenta development

Inferred from mutant phenotype PubMed 16287860. Source: MGI

epithelial cell differentiation involved in mammary gland alveolus development

Inferred from mutant phenotype PubMed 12620994. Source: MGI

epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 18037992. Source: BHF-UCL

glucose homeostasis

Inferred from mutant phenotype PubMed 15328538PubMed 17437992. Source: MGI

heart looping

Inferred from mutant phenotype PubMed 14659802. Source: MGI

hemoglobin biosynthetic process

Inferred from mutant phenotype PubMed 16787915. Source: MGI

intestinal epithelial cell maturation

Inferred from mutant phenotype PubMed 20808783. Source: MGI

lactate metabolic process

Inferred from mutant phenotype PubMed 15328538. Source: MGI

lactation

Inferred from mutant phenotype PubMed 12620994. Source: MGI

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 15328538. Source: MGI

negative regulation of TOR signaling

Inferred from mutant phenotype PubMed 20808783. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17181398. Source: MGI

negative regulation of bone mineralization

Inferred from mutant phenotype PubMed 17181398. Source: MGI

negative regulation of growth

Inferred from mutant phenotype PubMed 11691837. Source: MGI

negative regulation of mesenchymal cell apoptotic process

Inferred from mutant phenotype PubMed 10328919. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 12972594. Source: MGI

negative regulation of thymocyte apoptotic process

Inferred from mutant phenotype PubMed 15456877. Source: MGI

neural crest cell migration

Inferred from mutant phenotype PubMed 14659802. Source: MGI

neural fold elevation formation

Inferred from mutant phenotype PubMed 10328919. Source: MGI

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 9436976. Source: MGI

oxygen homeostasis

Inferred from mutant phenotype PubMed 9436976. Source: MGI

positive regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 18037992. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred from mutant phenotype PubMed 16787915. Source: MGI

positive regulation of hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 20440072. Source: MGI

positive regulation of neuroblast proliferation

Inferred from genetic interaction PubMed 17215402. Source: MGI

positive regulation of receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

positive regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 11691837. Source: MGI

positive regulation vascular endothelial growth factor production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of catalytic activity

Inferred from mutant phenotype PubMed 15328538. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 17437992. Source: MGI

regulation of glycolytic process

Inferred from genetic interaction PubMed 17437992. Source: MGI

regulation of thymocyte apoptotic process

Inferred from genetic interaction PubMed 15456877. Source: MGI

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from mutant phenotype PubMed 12832481. Source: MGI

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transforming growth factor beta2 production

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

response to muscle activity

Inferred from mutant phenotype PubMed 15328538. Source: MGI

retina vasculature development in camera-type eye

Inferred from mutant phenotype PubMed 21212189. Source: MGI

transcription from RNA polymerase II promoter

Inferred from physical interaction PubMed 20440072. Source: GOC

vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

vasculature development

Inferred from genetic interaction PubMed 18653562. Source: MGI

visual learning

Inferred from mutant phenotype PubMed 12972594. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

motile cilium

Inferred from direct assay PubMed 11818497. Source: MGI

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 18295594. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15456877. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 21856340. Source: MGI

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription factor binding transcription factor activity

Inferred from physical interaction PubMed 20440072. Source: MGI

histone acetyltransferase binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 19071119. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 20609350PubMed 21871655Ref.10. Source: IntAct

protein heterodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.2. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15456877. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 836836Hypoxia-inducible factor 1-alpha
PRO_0000127221

Regions

Domain17 – 7054bHLH
Domain80 – 15576PAS 1
Domain228 – 29871PAS 2
Domain302 – 34544PAC
Region1 – 401401Interaction with TSGA10
Region380 – 41738N-terminal VHL recognition site By similarity
Region401 – 613213ODD
Region544 – 58845NTAD
Region569 – 58517C-terminal VHL recognition site By similarity
Region589 – 795207ID
Region796 – 83641CTAD
Motif728 – 7314Nuclear localization signal Potential

Amino acid modifications

Modified residue2471Phosphoserine; by CK1 By similarity
Modified residue40214-hydroxyproline By similarity
Modified residue5641Phosphoserine; by GSK3-beta By similarity
Modified residue5681Phosphothreonine; by GSK3-beta By similarity
Modified residue57714-hydroxyproline By similarity
Modified residue5891Phosphoserine; by PLK3 By similarity
Modified residue6021Phosphoserine; by GSK3-beta By similarity
Modified residue6681Phosphoserine; by PLK3 By similarity
Modified residue8131(3S)-3-hydroxyasparagine By similarity
Cross-link391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
Cross-link551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
Cross-link560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Natural variations

Alternative sequence512 – 52514Missing in isoform 2.
VSP_007739

Experimental info

Sequence conflict121K → NR in BAC28578. Ref.4
Sequence conflict311S → T in AAC52730. Ref.1
Sequence conflict1281T → A Ref.1
Sequence conflict1281T → A Ref.6
Sequence conflict3511I → L in AAC52730. Ref.1
Sequence conflict3691M → K in AAH26139. Ref.5
Sequence conflict3821D → A in AAH26139. Ref.5
Sequence conflict3971L → H in BAC28578. Ref.4
Sequence conflict5691D → G in BAC28578. Ref.4
Sequence conflict6601Q → K in BAC28305. Ref.4
Sequence conflict7001N → K Ref.1
Sequence conflict7001N → K Ref.2
Sequence conflict7991E → V Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 3, 2003. Version 3.
Checksum: 84D64ECAC2CC753B

FASTA83693,516
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8DC6E7C1772AF1BF
Show »

FASTA82291,874

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DESUMOYLATION, FUNCTION.
[12]"Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1alpha."
Xu D., Yao Y., Lu L., Costa M., Dai W.
J. Biol. Chem. 285:38944-38950(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PLK3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
CCDSCCDS25977.1. [Q61221-1]
PIRJC4837.
RefSeqNP_034561.2. NM_010431.2. [Q61221-1]
UniGeneMm.3879.
Mm.446610.

3D structure databases

ProteinModelPortalQ61221.
SMRQ61221. Positions 19-393, 786-836.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200304. 13 interactions.
IntActQ61221. 14 interactions.
MINTMINT-1179248.

Chemistry

BindingDBQ61221.
ChEMBLCHEMBL6046.

PTM databases

PhosphoSiteQ61221.

Proteomic databases

PRIDEQ61221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021530; ENSMUSP00000021530; ENSMUSG00000021109. [Q61221-1]
ENSMUST00000110461; ENSMUSP00000106088; ENSMUSG00000021109.
ENSMUST00000110464; ENSMUSP00000106091; ENSMUSG00000021109.
GeneID15251.
KEGGmmu:15251.
UCSCuc007nwo.2. mouse. [Q61221-2]
uc007nwq.2. mouse. [Q61221-1]

Organism-specific databases

CTD3091.
MGIMGI:106918. Hif1a.

Phylogenomic databases

eggNOGNOG289264.
GeneTreeENSGT00730000110711.
HOVERGENHBG060456.
InParanoidQ61221.
KOK08268.
OMAQNAQRKR.
OrthoDBEOG7JDQX8.
PhylomeDBQ61221.
TreeFamTF317772.

Gene expression databases

BgeeQ61221.
CleanExMM_HIF1A.
GenevestigatorQ61221.

Family and domain databases

InterProIPR011598. bHLH_dom.
IPR001321. HIF-1_alpha.
IPR014887. HIF-1_TAD_C.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamPF11413. HIF-1. 1 hit.
PF08778. HIF-1a_CTAD. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSPR01080. HYPOXIAIF1A.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsTIGR00229. sensory_box. 2 hits.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHIF1A. mouse.
NextBio287865.
PROQ61221.
SOURCESearch...

Entry information

Entry nameHIF1A_MOUSE
AccessionPrimary (citable) accession number: Q61221
Secondary accession number(s): O08741 expand/collapse secondary AC list , 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: July 9, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot