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Q99814

- EPAS1_HUMAN

UniProt

Q99814 - EPAS1_HUMAN

Protein

Endothelial PAS domain-containing protein 1

Gene

EPAS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (03 Jul 2003)
      Previous versions | rss
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    Functioni

    Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation seems to require recruitment of transcriptional coactivators such as CREBPB and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD.

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood vessel remodeling Source: Ensembl
    3. cell maturation Source: Ensembl
    4. cellular response to hypoxia Source: UniProtKB
    5. embryonic placenta development Source: Ensembl
    6. erythrocyte differentiation Source: Ensembl
    7. lung development Source: Ensembl
    8. mitochondrion organization Source: Ensembl
    9. myoblast fate commitment Source: BHF-UCL
    10. norepinephrine metabolic process Source: Ensembl
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. regulation of heart rate Source: Ensembl
    13. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    14. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
    15. response to hypoxia Source: MGI
    16. signal transduction Source: ProtInc
    17. surfactant homeostasis Source: Ensembl
    18. transcription from RNA polymerase II promoter Source: ProtInc
    19. visual perception Source: Ensembl

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Angiogenesis, Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_121226. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinkiQ99814.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endothelial PAS domain-containing protein 1
    Short name:
    EPAS-1
    Alternative name(s):
    Basic-helix-loop-helix-PAS protein MOP2
    Class E basic helix-loop-helix protein 73
    Short name:
    bHLHe73
    HIF-1-alpha-like factor
    Short name:
    HLF
    Hypoxia-inducible factor 2-alpha
    Short name:
    HIF-2-alpha
    Short name:
    HIF2-alpha
    Member of PAS protein 2
    PAS domain-containing protein 2
    Gene namesi
    Name:EPAS1
    Synonyms:BHLHE73, HIF2A, MOP2, PASD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3374. EPAS1.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Erythrocytosis, familial, 4 (ECYT4) [MIM:611783]: An autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal platelet and leukocyte counts.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti534 – 5341P → L in ECYT4; impairs interaction with EGLN1 and VHL. 1 Publication
    VAR_067358
    Natural varianti535 – 5351M → T in ECYT4. 1 Publication
    VAR_067359
    Natural varianti535 – 5351M → V in ECYT4; impairs interaction with EGLN1. 1 Publication
    VAR_067360
    Natural varianti537 – 5371G → R in ECYT4; impairs interaction with EGLN1 and VHL. 1 Publication
    VAR_067361
    Natural varianti537 – 5371G → W in ECYT4; gain of function; affects hydroxylation. 1 Publication
    VAR_042443
    Natural varianti540 – 5401F → L in ECYT4; affects the interaction with EGLN1 and VHL. 1 Publication
    VAR_067362

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi844 – 8441C → S: Abolishes hypoxia-inducible transcriptional activation of ctaD. 1 Publication

    Keywords - Diseasei

    Congenital erythrocytosis, Disease mutation

    Organism-specific databases

    MIMi611783. phenotype.
    Orphaneti247511. Autosomal dominant secondary polycythemia.
    324299. Multiple paragangliomas associated with polycythemia.
    276624. Sporadic pheochromocytoma.
    276627. Sporadic secreting paraganglioma.
    PharmGKBiPA27809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870Endothelial PAS domain-containing protein 1PRO_0000127419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei405 – 40514-hydroxyprolineBy similarity
    Modified residuei531 – 53114-hydroxyprolineBy similarity
    Modified residuei840 – 8401PhosphothreonineBy similarity
    Modified residuei847 – 8471(3S)-3-hydroxyasparagineBy similarity

    Post-translational modificationi

    In normoxia, is probably hydroxylated on Pro-405 and Pro-531 by EGLN1/PHD1, EGLN2/PHD2 and/or EGLN3/PHD3. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization By similarity.By similarity
    In normoxia, is hydroxylated on Asn-847 by HIF1AN thus probably abrogating interaction with CREBBP and EP300 and preventing transcriptional activation.By similarity
    Phosphorylated on multiple sites in the CTAD.By similarity
    The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.By similarity

    Keywords - PTMi

    Hydroxylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99814.
    PaxDbiQ99814.
    PRIDEiQ99814.

    PTM databases

    PhosphoSiteiQ99814.

    Expressioni

    Tissue specificityi

    Expressed in most tissues, with highest levels in placenta, lung and heart. Selectively expressed in endothelial cells.

    Gene expression databases

    ArrayExpressiQ99814.
    BgeeiQ99814.
    CleanExiHS_EPAS1.
    GenevestigatoriQ99814.

    Organism-specific databases

    HPAiCAB012248.

    Interactioni

    Subunit structurei

    Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerizes with ARNT. Interacts with CREBBP By similarity. Interacts with EGLN1. Interacts with VHL.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BBS4Q96RK42EBI-447470,EBI-1805814
    EGLN1Q9GZT92EBI-447470,EBI-1174818
    EIF3EP6022810EBI-447470,EBI-347740
    MAXP612442EBI-447470,EBI-751711
    SMAD3P840222EBI-447470,EBI-347161
    SP1P080472EBI-447470,EBI-298336
    USP8P408182EBI-447470,EBI-1050865

    Protein-protein interaction databases

    BioGridi108348. 103 interactions.
    DIPiDIP-32857N.
    IntActiQ99814. 29 interactions.
    MINTiMINT-1199606.
    STRINGi9606.ENSP00000263734.

    Structurei

    Secondary structure

    1
    870
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi240 – 2423
    Beta strandi243 – 2486
    Turni250 – 2523
    Beta strandi253 – 2575
    Helixi260 – 2656
    Helixi269 – 2724
    Helixi277 – 2804
    Helixi283 – 2853
    Helixi286 – 29914
    Beta strandi300 – 3034
    Beta strandi307 – 3104
    Beta strandi314 – 32714
    Turni329 – 3313
    Beta strandi334 – 34310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P97NMR-A240-350[»]
    2A24NMR-A242-348[»]
    3F1NX-ray1.48A239-350[»]
    3F1OX-ray1.60A239-350[»]
    3F1PX-ray1.17A239-350[»]
    3H7WX-ray1.65A239-350[»]
    3H82X-ray1.50A239-350[»]
    4GHIX-ray1.50A239-350[»]
    4GS9X-ray1.72A239-350[»]
    ProteinModelPortaliQ99814.
    SMRiQ99814. Positions 16-348, 836-868.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99814.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 6754bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini84 – 15471PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini230 – 30071PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini304 – 34744PACAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni496 – 54247NTADAdd
    BLAST
    Regioni830 – 87041CTADAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi474 – 4807Poly-Ser

    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.
    HOGENOMiHOG000234306.
    HOVERGENiHBG060456.
    InParanoidiQ99814.
    KOiK09095.
    OMAiDPPLHFG.
    OrthoDBiEOG7JDQX8.
    PhylomeDBiQ99814.
    TreeFamiTF317772.

    Family and domain databases

    InterProiIPR011598. bHLH_dom.
    IPR014887. HIF-1_TAD_C.
    IPR021537. HIF_alpha_subunit.
    IPR001067. Nuc_translocat.
    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]
    PRINTSiPR00785. NCTRNSLOCATR.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q99814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTADKEKKRS SSERRKEKSR DAARCRRSKE TEVFYELAHE LPLPHSVSSH    50
    LDKASIMRLA ISFLRTHKLL SSVCSENESE AEADQQMDNL YLKALEGFIA 100
    VVTQDGDMIF LSENISKFMG LTQVELTGHS IFDFTHPCDH EEIRENLSLK 150
    NGSGFGKKSK DMSTERDFFM RMKCTVTNRG RTVNLKSATW KVLHCTGQVK 200
    VYNNCPPHNS LCGYKEPLLS CLIIMCEPIQ HPSHMDIPLD SKTFLSRHSM 250
    DMKFTYCDDR ITELIGYHPE ELLGRSAYEF YHALDSENMT KSHQNLCTKG 300
    QVVSGQYRML AKHGGYVWLE TQGTVIYNPR NLQPQCIMCV NYVLSEIEKN 350
    DVVFSMDQTE SLFKPHLMAM NSIFDSSGKG AVSEKSNFLF TKLKEEPEEL 400
    AQLAPTPGDA IISLDFGNQN FEESSAYGKA ILPPSQPWAT ELRSHSTQSE 450
    AGSLPAFTVP QAAAPGSTTP SATSSSSSCS TPNSPEDYYT SLDNDLKIEV 500
    IEKLFAMDTE AKDQCSTQTD FNELDLETLA PYIPMDGEDF QLSPICPEER 550
    LLAENPQSTP QHCFSAMTNI FQPLAPVAPH SPFLLDKFQQ QLESKKTEPE 600
    HRPMSSIFFD AGSKASLPPC CGQASTPLSS MGGRSNTQWP PDPPLHFGPT 650
    KWAVGDQRTE FLGAAPLGPP VSPPHVSTFK TRSAKGFGAR GPDVLSPAMV 700
    ALSNKLKLKR QLEYEEQAFQ DLSGGDPPGG STSHLMWKRM KNLRGGSCPL 750
    MPDKPLSANV PNDKFTQNPM RGLGHPLRHL PLPQPPSAIS PGENSKSRFP 800
    PQCYATQYQD YSLSSAHKVS GMASRLLGPS FESYLLPELT RYDCEVNVPV 850
    LGSSTLLQGG DLLRALDQAT 870
    Length:870
    Mass (Da):96,459
    Last modified:July 3, 2003 - v3
    Checksum:i4838989598234FC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601A → E in AAB41495. (PubMed:9000051)Curated
    Sequence conflicti539 – 5391D → G in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti601 – 6011H → R in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti693 – 6931D → N in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti716 – 7161E → K in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti722 – 7221L → P in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti765 – 7651F → L in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti769 – 7691P → S in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti844 – 8441C → R in AAC51212. (PubMed:9079689)Curated
    Sequence conflicti847 – 8471N → K in AAC51212. (PubMed:9079689)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti534 – 5341P → L in ECYT4; impairs interaction with EGLN1 and VHL. 1 Publication
    VAR_067358
    Natural varianti535 – 5351M → T in ECYT4. 1 Publication
    VAR_067359
    Natural varianti535 – 5351M → V in ECYT4; impairs interaction with EGLN1. 1 Publication
    VAR_067360
    Natural varianti537 – 5371G → R in ECYT4; impairs interaction with EGLN1 and VHL. 1 Publication
    VAR_067361
    Natural varianti537 – 5371G → W in ECYT4; gain of function; affects hydroxylation. 1 Publication
    VAR_042443
    Natural varianti540 – 5401F → L in ECYT4; affects the interaction with EGLN1 and VHL. 1 Publication
    VAR_067362
    Natural varianti766 – 7661T → P.
    Corresponds to variant rs59901247 [ dbSNP | Ensembl ].
    VAR_061261
    Natural varianti785 – 7851P → T.
    Corresponds to variant rs61518065 [ dbSNP | Ensembl ].
    VAR_061262

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81984 mRNA. Translation: AAB41495.1.
    U51626 mRNA. Translation: AAC51212.1.
    BC051338 mRNA. Translation: AAH51338.1.
    CCDSiCCDS1825.1.
    RefSeqiNP_001421.2. NM_001430.4.
    UniGeneiHs.468410.

    Genome annotation databases

    EnsembliENST00000263734; ENSP00000263734; ENSG00000116016.
    GeneIDi2034.
    KEGGihsa:2034.
    UCSCiuc002ruv.3. human.

    Polymorphism databases

    DMDMi32470617.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81984 mRNA. Translation: AAB41495.1 .
    U51626 mRNA. Translation: AAC51212.1 .
    BC051338 mRNA. Translation: AAH51338.1 .
    CCDSi CCDS1825.1.
    RefSeqi NP_001421.2. NM_001430.4.
    UniGenei Hs.468410.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P97 NMR - A 240-350 [» ]
    2A24 NMR - A 242-348 [» ]
    3F1N X-ray 1.48 A 239-350 [» ]
    3F1O X-ray 1.60 A 239-350 [» ]
    3F1P X-ray 1.17 A 239-350 [» ]
    3H7W X-ray 1.65 A 239-350 [» ]
    3H82 X-ray 1.50 A 239-350 [» ]
    4GHI X-ray 1.50 A 239-350 [» ]
    4GS9 X-ray 1.72 A 239-350 [» ]
    ProteinModelPortali Q99814.
    SMRi Q99814. Positions 16-348, 836-868.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108348. 103 interactions.
    DIPi DIP-32857N.
    IntActi Q99814. 29 interactions.
    MINTi MINT-1199606.
    STRINGi 9606.ENSP00000263734.

    Chemistry

    BindingDBi Q99814.
    ChEMBLi CHEMBL1744522.

    PTM databases

    PhosphoSitei Q99814.

    Polymorphism databases

    DMDMi 32470617.

    Proteomic databases

    MaxQBi Q99814.
    PaxDbi Q99814.
    PRIDEi Q99814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263734 ; ENSP00000263734 ; ENSG00000116016 .
    GeneIDi 2034.
    KEGGi hsa:2034.
    UCSCi uc002ruv.3. human.

    Organism-specific databases

    CTDi 2034.
    GeneCardsi GC02P046436.
    HGNCi HGNC:3374. EPAS1.
    HPAi CAB012248.
    MIMi 603349. gene.
    611783. phenotype.
    neXtProti NX_Q99814.
    Orphaneti 247511. Autosomal dominant secondary polycythemia.
    324299. Multiple paragangliomas associated with polycythemia.
    276624. Sporadic pheochromocytoma.
    276627. Sporadic secreting paraganglioma.
    PharmGKBi PA27809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289264.
    HOGENOMi HOG000234306.
    HOVERGENi HBG060456.
    InParanoidi Q99814.
    KOi K09095.
    OMAi DPPLHFG.
    OrthoDBi EOG7JDQX8.
    PhylomeDBi Q99814.
    TreeFami TF317772.

    Enzyme and pathway databases

    Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_121226. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinki Q99814.

    Miscellaneous databases

    ChiTaRSi EPAS1. human.
    EvolutionaryTracei Q99814.
    GeneWikii EPAS1.
    GenomeRNAii 2034.
    NextBioi 8255.
    PROi Q99814.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99814.
    Bgeei Q99814.
    CleanExi HS_EPAS1.
    Genevestigatori Q99814.

    Family and domain databases

    InterProi IPR011598. bHLH_dom.
    IPR014887. HIF-1_TAD_C.
    IPR021537. HIF_alpha_subunit.
    IPR001067. Nuc_translocat.
    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 PR00785. NCTRNSLOCATR.
    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. "Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells."
      Tian H., McKnight S.L., Russell D.W.
      Genes Dev. 11:72-82(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway."
      Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.-Z., Pray-Grant M., Perdew G.H., Bradfield C.A.
      J. Biol. Chem. 272:8581-8593(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hepatoma.
    3. "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].
      Tissue: Eye.
    4. "Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300."
      Ema M., Hirota K., Mimura J., Abe H., Yodoi J., Sogawa K., Poellinger L., Fujii-Kuriyama Y.
      EMBO J. 18:1905-1914(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSACTIVATION DOMAINS NTAD AND CTAD, INTERACTION WITH APEX, MUTAGENESIS OF CYS-844.
    5. "Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline."
      Furlow P.W., Percy M.J., Sutherland S., Bierl C., McMullin M.F., Master S.R., Lappin T.R., Lee F.S.
      J. Biol. Chem. 284:9050-9058(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGLN1 AND VHL, VARIANT ECYT4 LEU-534, CHARACTERIZATION OF VARIANTS ECYT4 LEU-534; VAL-535 AND ARG-537.
    6. Cited for: VARIANTS ECYT4 VAL-535 AND ARG-537.
    7. "A gain-of-function mutation in the HIF2A gene in familial erythrocytosis."
      Percy M.J., Furlow P.W., Lucas G.S., Li X., Lappin T.R., McMullin M.F., Lee F.S.
      N. Engl. J. Med. 358:162-168(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ECYT4 TRP-537, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF VARIANT ECYT4 TRP-537.
    8. Cited for: VARIANTS ECYT4 THR-535 AND LEU-540, CHARACTERIZATION OF VARIANT ECYT4 LEU-540.

    Entry informationi

    Entry nameiEPAS1_HUMAN
    AccessioniPrimary (citable) accession number: Q99814
    Secondary accession number(s): Q86VA2, Q99630
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 3, 2003
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3