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Q99814

- EPAS1_HUMAN

UniProt

Q99814 - EPAS1_HUMAN

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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

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 heterodimerization activity Source: BHF-UCL
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  5. signal transducer activity Source: InterPro
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ99814.
CleanExiHS_EPAS1.
ExpressionAtlasiQ99814. baseline and differential.
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. 106 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.
GeneTreeiENSGT00760000118788.
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

        10         20         30         40         50
MTADKEKKRS SSERRKEKSR DAARCRRSKE TEVFYELAHE LPLPHSVSSH
60 70 80 90 100
LDKASIMRLA ISFLRTHKLL SSVCSENESE AEADQQMDNL YLKALEGFIA
110 120 130 140 150
VVTQDGDMIF LSENISKFMG LTQVELTGHS IFDFTHPCDH EEIRENLSLK
160 170 180 190 200
NGSGFGKKSK DMSTERDFFM RMKCTVTNRG RTVNLKSATW KVLHCTGQVK
210 220 230 240 250
VYNNCPPHNS LCGYKEPLLS CLIIMCEPIQ HPSHMDIPLD SKTFLSRHSM
260 270 280 290 300
DMKFTYCDDR ITELIGYHPE ELLGRSAYEF YHALDSENMT KSHQNLCTKG
310 320 330 340 350
QVVSGQYRML AKHGGYVWLE TQGTVIYNPR NLQPQCIMCV NYVLSEIEKN
360 370 380 390 400
DVVFSMDQTE SLFKPHLMAM NSIFDSSGKG AVSEKSNFLF TKLKEEPEEL
410 420 430 440 450
AQLAPTPGDA IISLDFGNQN FEESSAYGKA ILPPSQPWAT ELRSHSTQSE
460 470 480 490 500
AGSLPAFTVP QAAAPGSTTP SATSSSSSCS TPNSPEDYYT SLDNDLKIEV
510 520 530 540 550
IEKLFAMDTE AKDQCSTQTD FNELDLETLA PYIPMDGEDF QLSPICPEER
560 570 580 590 600
LLAENPQSTP QHCFSAMTNI FQPLAPVAPH SPFLLDKFQQ QLESKKTEPE
610 620 630 640 650
HRPMSSIFFD AGSKASLPPC CGQASTPLSS MGGRSNTQWP PDPPLHFGPT
660 670 680 690 700
KWAVGDQRTE FLGAAPLGPP VSPPHVSTFK TRSAKGFGAR GPDVLSPAMV
710 720 730 740 750
ALSNKLKLKR QLEYEEQAFQ DLSGGDPPGG STSHLMWKRM KNLRGGSCPL
760 770 780 790 800
MPDKPLSANV PNDKFTQNPM RGLGHPLRHL PLPQPPSAIS PGENSKSRFP
810 820 830 840 850
PQCYATQYQD YSLSSAHKVS GMASRLLGPS FESYLLPELT RYDCEVNVPV
860 870
LGSSTLLQGG DLLRALDQAT
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. 106 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.
GeneTreei ENSGT00760000118788.
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

Bgeei Q99814.
CleanExi HS_EPAS1.
ExpressionAtlasi Q99814. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 159 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