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Q61221

- HIF1A_MOUSE

UniProt

Q61221 - HIF1A_MOUSE

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
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (03 Jul 2003)
      Previous versions | rss
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    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 binding Source: IntAct
    5. protein heterodimerization activity Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    7. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    8. RNA polymerase II transcription factor binding transcription factor activity Source: MGI
    9. sequence-specific DNA binding Source: MGI
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. signal transducer activity Source: InterPro
    12. transcription regulatory region DNA binding Source: UniProtKB

    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

    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

    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. 13 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.
    GeneTreeiENSGT00730000110711.
    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

    MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV    50
    SSHLDKASVM RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV 100
    MVLTDDGDMV YISDNVNKYM GLTQFELTGH SVFDFTHPCD HEEMREMLTH 150
    RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR TMNIKSATWK VLHCTGHIHV 200
    YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK TFLSRHSLDM 250
    KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV 300
    TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL 350
    IFSLQQTESV LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL 400
    APAAGDTIIS LDFGSDDTET EDQQLEDVPL YNDVMFPSSN EKLNINLAMS 450
    PLPSSETPKP LRSSADPALN QEVALKLESS PESLGLSFTM PQIQDQPASP 500
    SDGSTRQSSP ERLLQENVNT PNFSQPNSPS EYCFDVDSDM VNVFKLELVE 550
    KLFAEDTEAK NPFSTQDTDL DLEMLAPYIP MDDDFQLRSF DQLSPLESNS 600
    PSPPSMSTVT GFQQTQLQKP TITATATTTA TTDESKTETK DNKEDIKILI 650
    ASPSSTQVPQ ETTTAKASAY SGTHSRTASP DRAGKRVIEQ TDKAHPRSLN 700
    LSATLNQRNT VPEEELNPKT IASQNAQRKR KMEHDGSLFQ AAGIGTLLQQ 750
    PGDCAPTMSL SWKRVKGFIS SEQNGTEQKT IILIPSDLAC RLLGQSMDES 800
    GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN 836
    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. 13 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 ENSGT00730000110711.
    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

    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 1, 2014
    This is version 163 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