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Q61221

- HIF1A_MOUSE

UniProt

Q61221 - HIF1A_MOUSE

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Protein

Hypoxia-inducible factor 1-alpha

Gene

Hif1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. histone acetyltransferase binding Source: UniProtKB
  3. histone deacetylase binding Source: BHF-UCL
  4. protein heterodimerization activity Source: UniProtKB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
  7. RNA polymerase II transcription factor binding transcription factor activity Source: MGI
  8. sequence-specific DNA binding Source: MGI
  9. sequence-specific DNA binding transcription factor activity Source: MGI
  10. signal transducer activity Source: InterPro
  11. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. angiogenesis Source: MGI
  2. axon transport of mitochondrion Source: UniProtKB
  3. B-1 B cell homeostasis Source: MGI
  4. blood vessel development Source: MGI
  5. blood vessel morphogenesis Source: MGI
  6. cardiac ventricle morphogenesis Source: MGI
  7. cartilage development Source: MGI
  8. cell differentiation Source: MGI
  9. cellular iron ion homeostasis Source: MGI
  10. cellular response to hypoxia Source: UniProtKB
  11. cellular response to interleukin-1 Source: Ensembl
  12. cerebral cortex development Source: MGI
  13. collagen metabolic process Source: BHF-UCL
  14. connective tissue replacement involved in inflammatory response wound healing Source: BHF-UCL
  15. digestive tract morphogenesis Source: MGI
  16. dopaminergic neuron differentiation Source: MGI
  17. elastin metabolic process Source: BHF-UCL
  18. embryonic hemopoiesis Source: MGI
  19. embryonic placenta development Source: MGI
  20. epithelial cell differentiation involved in mammary gland alveolus development Source: MGI
  21. epithelial to mesenchymal transition Source: BHF-UCL
  22. glucose homeostasis Source: MGI
  23. heart looping Source: MGI
  24. hemoglobin biosynthetic process Source: MGI
  25. intestinal epithelial cell maturation Source: MGI
  26. lactate metabolic process Source: MGI
  27. lactation Source: MGI
  28. muscle cell cellular homeostasis Source: MGI
  29. negative regulation of apoptotic process Source: MGI
  30. negative regulation of bone mineralization Source: MGI
  31. negative regulation of growth Source: MGI
  32. negative regulation of mesenchymal cell apoptotic process Source: MGI
  33. negative regulation of neuron apoptotic process Source: MGI
  34. negative regulation of thymocyte apoptotic process Source: MGI
  35. negative regulation of TOR signaling Source: MGI
  36. neural crest cell migration Source: MGI
  37. neural fold elevation formation Source: MGI
  38. outflow tract morphogenesis Source: MGI
  39. oxygen homeostasis Source: MGI
  40. positive regulation of epithelial cell migration Source: BHF-UCL
  41. positive regulation of erythrocyte differentiation Source: MGI
  42. positive regulation of hormone biosynthetic process Source: Ensembl
  43. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
  44. positive regulation of neuroblast proliferation Source: MGI
  45. positive regulation of receptor biosynthetic process Source: Ensembl
  46. positive regulation of transcription, DNA-templated Source: UniProtKB
  47. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  48. positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  49. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: MGI
  50. positive regulation vascular endothelial growth factor production Source: UniProtKB
  51. regulation of catalytic activity Source: MGI
  52. regulation of cell proliferation Source: MGI
  53. regulation of glycolytic process Source: MGI
  54. regulation of thymocyte apoptotic process Source: MGI
  55. regulation of transcription, DNA-templated Source: UniProtKB
  56. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: MGI
  57. regulation of transforming growth factor beta2 production Source: Ensembl
  58. response to hypoxia Source: UniProtKB
  59. response to muscle activity Source: MGI
  60. retina vasculature development in camera-type eye Source: MGI
  61. transcription from RNA polymerase II promoter Source: GOC
  62. vascular endothelial growth factor production Source: Ensembl
  63. vasculature development Source: MGI
  64. visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_199104. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_199107. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia-inducible factor 1-alpha
Short name:
HIF-1-alpha
Short name:
HIF1-alpha
Alternative name(s):
ARNT-interacting protein
Gene namesi
Name:Hif1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:106918. Hif1a.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. motile cilium Source: MGI
  3. nucleolus Source: Ensembl
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 836836Hypoxia-inducible factor 1-alphaPRO_0000127221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471Phosphoserine; by CK1By similarity
Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei402 – 40214-hydroxyprolineBy similarity
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei545 – 5451N6-acetyllysineBy similarity
Cross-linki545 – 545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Curated
Cross-linki551 – 551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Curated
Cross-linki560 – 560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Curated
Modified residuei564 – 5641Phosphoserine; by GSK3-betaBy similarity
Modified residuei568 – 5681Phosphothreonine; by GSK3-betaBy similarity
Modified residuei577 – 57714-hydroxyprolineBy similarity
Modified residuei589 – 5891Phosphoserine; by PLK3By similarity
Modified residuei602 – 6021Phosphoserine; by GSK3-betaBy similarity
Modified residuei668 – 6681Phosphoserine; by PLK3By similarity
Modified residuei719 – 7191N6-acetyllysineBy similarity
Modified residuei813 – 8131(3S)-3-hydroxyasparagineBy similarity

Post-translational modificationi

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).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).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.By similarity1 Publication
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.2 Publications
Acetylation of Lys-545 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation. Deacetylation of Lys-719 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (By similarity).By similarity
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).By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ61221.

PTM databases

PhosphoSiteiQ61221.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ61221.
CleanExiMM_HIF1A.
GenevestigatoriQ61221.

Interactioni

Subunit structurei

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). Interacts with SIRT2. Interacts (deacetylated form) with EGLN1 (By similarity). Interacts with TSGA10. Interacts (via N-terminus) with USP19. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q094722EBI-298954,EBI-447295From a different organism.
Foxa2P355835EBI-298954,EBI-2893341
Rbfox3Q8BIF22EBI-298954,EBI-4567146
RorcP51450-22EBI-298954,EBI-4422078
Tsga10Q6NY152EBI-8549331,EBI-8549230
VHLP403372EBI-298954,EBI-301246From a different organism.

Protein-protein interaction databases

BioGridi200304. 14 interactions.
IntActiQ61221. 15 interactions.
MINTiMINT-1179248.

Structurei

3D structure databases

ProteinModelPortaliQ61221.
SMRiQ61221. Positions 19-393, 786-836.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 7054bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini80 – 15576PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini228 – 29871PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini302 – 34544PACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 401401Interaction with TSGA10Add
BLAST
Regioni380 – 41738N-terminal VHL recognition siteBy similarityAdd
BLAST
Regioni401 – 613213ODDAdd
BLAST
Regioni544 – 58845NTADAdd
BLAST
Regioni569 – 58517C-terminal VHL recognition siteBy similarityAdd
BLAST
Regioni589 – 795207IDAdd
BLAST
Regioni796 – 83641CTADAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi728 – 7314Nuclear localization signalSequence Analysis

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG289264.
GeneTreeiENSGT00760000118788.
HOVERGENiHBG060456.
InParanoidiQ61221.
KOiK08268.
OMAiQNAQRKR.
OrthoDBiEOG7JDQX8.
PhylomeDBiQ61221.
TreeFamiTF317772.

Family and domain databases

InterProiIPR011598. bHLH_dom.
IPR001321. HIF-1_alpha.
IPR014887. HIF-1_TAD_C.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF11413. HIF-1. 1 hit.
PF08778. HIF-1a_CTAD. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSiPR01080. HYPOXIAIF1A.
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 2 hits.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q61221-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV
60 70 80 90 100
SSHLDKASVM RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV
110 120 130 140 150
MVLTDDGDMV YISDNVNKYM GLTQFELTGH SVFDFTHPCD HEEMREMLTH
160 170 180 190 200
RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR TMNIKSATWK VLHCTGHIHV
210 220 230 240 250
YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK TFLSRHSLDM
260 270 280 290 300
KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
310 320 330 340 350
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL
360 370 380 390 400
IFSLQQTESV LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL
410 420 430 440 450
APAAGDTIIS LDFGSDDTET EDQQLEDVPL YNDVMFPSSN EKLNINLAMS
460 470 480 490 500
PLPSSETPKP LRSSADPALN QEVALKLESS PESLGLSFTM PQIQDQPASP
510 520 530 540 550
SDGSTRQSSP ERLLQENVNT PNFSQPNSPS EYCFDVDSDM VNVFKLELVE
560 570 580 590 600
KLFAEDTEAK NPFSTQDTDL DLEMLAPYIP MDDDFQLRSF DQLSPLESNS
610 620 630 640 650
PSPPSMSTVT GFQQTQLQKP TITATATTTA TTDESKTETK DNKEDIKILI
660 670 680 690 700
ASPSSTQVPQ ETTTAKASAY SGTHSRTASP DRAGKRVIEQ TDKAHPRSLN
710 720 730 740 750
LSATLNQRNT VPEEELNPKT IASQNAQRKR KMEHDGSLFQ AAGIGTLLQQ
760 770 780 790 800
PGDCAPTMSL SWKRVKGFIS SEQNGTEQKT IILIPSDLAC RLLGQSMDES
810 820 830
GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN
Length:836
Mass (Da):93,516
Last modified:July 3, 2003 - v3
Checksum:i84D64ECAC2CC753B
GO
Isoform 2 (identifier: Q61221-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:822
Mass (Da):91,874
Checksum:i8DC6E7C1772AF1BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121K → NR in BAC28578. (PubMed:16141072)Curated
Sequence conflicti31 – 311S → T in AAC52730. (PubMed:8702901)Curated
Sequence conflicti128 – 1281T → A in AAC52730. (PubMed:8702901)Curated
Sequence conflicti128 – 1281T → A in CAA64833. (PubMed:8660378)Curated
Sequence conflicti351 – 3511I → L in AAC52730. (PubMed:8702901)Curated
Sequence conflicti369 – 3691M → K in AAH26139. (PubMed:15489334)Curated
Sequence conflicti382 – 3821D → A in AAH26139. (PubMed:15489334)Curated
Sequence conflicti397 – 3971L → H in BAC28578. (PubMed:16141072)Curated
Sequence conflicti569 – 5691D → G in BAC28578. (PubMed:16141072)Curated
Sequence conflicti660 – 6601Q → K in BAC28305. (PubMed:16141072)Curated
Sequence conflicti700 – 7001N → K in AAC52730. (PubMed:8702901)Curated
Sequence conflicti700 – 7001N → K in AAC53455. (PubMed:9368100)Curated
Sequence conflicti700 – 7001N → K in AAC53461. (PubMed:9368100)Curated
Sequence conflicti799 – 7991E → V in CAA64833. (PubMed:8660378)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei512 – 52514Missing in isoform 2. 1 PublicationVSP_007739Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59496 Genomic DNA. Translation: AAC52730.1.
AF003695 mRNA. Translation: AAC53455.1.
AF004155
, AF004141, AF004142, AF004143, AF004144, AF004145, AF004146, AF004147, AF004148, AF004149, AF004150, AF004151, AF004152, AF004153, AF004154 Genomic DNA. Translation: AAC53461.1.
Y09085 Genomic DNA. Translation: CAA70305.1.
Y09085, Y13656 Genomic DNA. Translation: CAA70306.1.
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.
CCDSiCCDS25977.1. [Q61221-1]
PIRiJC4837.
RefSeqiNP_034561.2. NM_010431.2. [Q61221-1]
UniGeneiMm.3879.
Mm.446610.

Genome annotation databases

EnsembliENSMUST00000021530; ENSMUSP00000021530; ENSMUSG00000021109. [Q61221-1]
ENSMUST00000110461; ENSMUSP00000106088; ENSMUSG00000021109.
ENSMUST00000110464; ENSMUSP00000106091; ENSMUSG00000021109.
GeneIDi15251.
KEGGimmu:15251.
UCSCiuc007nwo.2. mouse. [Q61221-2]
uc007nwq.2. mouse. [Q61221-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59496 Genomic DNA. Translation: AAC52730.1 .
AF003695 mRNA. Translation: AAC53455.1 .
AF004155
, AF004141 , AF004142 , AF004143 , AF004144 , AF004145 , AF004146 , AF004147 , AF004148 , AF004149 , AF004150 , AF004151 , AF004152 , AF004153 , AF004154 Genomic DNA. Translation: AAC53461.1 .
Y09085 Genomic DNA. Translation: CAA70305.1 .
Y09085 , Y13656 Genomic DNA. Translation: CAA70306.1 .
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 .
CCDSi CCDS25977.1. [Q61221-1 ]
PIRi JC4837.
RefSeqi NP_034561.2. NM_010431.2. [Q61221-1 ]
UniGenei Mm.3879.
Mm.446610.

3D structure databases

ProteinModelPortali Q61221.
SMRi Q61221. Positions 19-393, 786-836.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200304. 14 interactions.
IntActi Q61221. 15 interactions.
MINTi MINT-1179248.

Chemistry

BindingDBi Q61221.
ChEMBLi CHEMBL6046.

PTM databases

PhosphoSitei Q61221.

Proteomic databases

PRIDEi Q61221.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021530 ; ENSMUSP00000021530 ; ENSMUSG00000021109 . [Q61221-1 ]
ENSMUST00000110461 ; ENSMUSP00000106088 ; ENSMUSG00000021109 .
ENSMUST00000110464 ; ENSMUSP00000106091 ; ENSMUSG00000021109 .
GeneIDi 15251.
KEGGi mmu:15251.
UCSCi uc007nwo.2. mouse. [Q61221-2 ]
uc007nwq.2. mouse. [Q61221-1 ]

Organism-specific databases

CTDi 3091.
MGIi MGI:106918. Hif1a.

Phylogenomic databases

eggNOGi NOG289264.
GeneTreei ENSGT00760000118788.
HOVERGENi HBG060456.
InParanoidi Q61221.
KOi K08268.
OMAi QNAQRKR.
OrthoDBi EOG7JDQX8.
PhylomeDBi Q61221.
TreeFami TF317772.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_199104. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_199107. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

Miscellaneous databases

ChiTaRSi HIF1A. mouse.
NextBioi 287865.
PROi Q61221.
SOURCEi Search...

Gene expression databases

Bgeei Q61221.
CleanExi MM_HIF1A.
Genevestigatori Q61221.

Family and domain databases

InterProi IPR011598. bHLH_dom.
IPR001321. HIF-1_alpha.
IPR014887. HIF-1_TAD_C.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view ]
Pfami PF11413. HIF-1. 1 hit.
PF08778. HIF-1a_CTAD. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view ]
PRINTSi PR01080. HYPOXIAIF1A.
SMARTi SM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsi TIGR00229. sensory_box. 2 hits.
PROSITEi PS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 [MRNA] 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.
  13. "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour cells."
    Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M., Losa M., Stalla G.K., Arzt E., Renner U.
    Endocr. Relat. Cancer 19:13-27(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHIF1A_MOUSE
AccessioniPrimary (citable) accession number: Q61221
Secondary accession number(s): O08741
, O08993, Q61664, Q61665, Q8C681, Q8CC19, Q8CCB6, Q8R385, Q9CYA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 3, 2003
Last modified: October 29, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3