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Entry version 171 (13 Feb 2019)
Sequence version 2 (15 Dec 1998)
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Protein

Endothelial PAS domain-containing protein 1

Gene

Epas1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). 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 requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).By similarity1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding
Biological processAngiogenesis, Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-1234162 Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-8951664 Neddylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Endothelial PAS domain-containing protein 1
Short name:
EPAS-1
Alternative name(s):
HIF-1-alpha-like factor
Short name:
HLF
Short name:
mHLF
HIF-related factor
Short name:
HRF
Hypoxia-inducible factor 2-alpha
Short name:
HIF-2-alpha
Short name:
HIF2-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Epas1
Synonyms:Hif2a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:109169 Epas1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi23A → D: Decreases HRE DNA binding. 1 Publication1
Mutagenesisi27R → A: Decreases HRE DNA binding. 1 Publication1
Mutagenesisi169F → D: Decreases heterodimer formation with ARNT. 1 Publication1
Mutagenesisi171R → A: Markedly decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with D-192. 1 Publication1
Mutagenesisi184N → D: Decreases HRE DNA binding; when associated with D-186. 1 Publication1
Mutagenesisi186K → D: Decreases HRE DNA binding; when associated with D-184. 1 Publication1
Mutagenesisi192V → D: Markedly decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with A-171. 1 Publication1
Mutagenesisi194H → A: Decreases heterodimer formation with ARNT. 1 Publication1
Mutagenesisi530P → A: Confers transcriptional activity at normoxia; when associated with A-851. 1 Publication1
Mutagenesisi844T → A: Decreases interaction with CREBBP. 1 Publication1
Mutagenesisi851N → A: Confers transcriptional activity at normoxia; when associated with A-530. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001274201 – 874Endothelial PAS domain-containing protein 1Add BLAST874

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4054-hydroxyprolineBy similarity1
Modified residuei5304-hydroxyprolineBy similarity1
Modified residuei844Phosphothreonine1 Publication1
Modified residuei851(3S)-3-hydroxyasparagine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

In normoxia, is probably hydroxylated on Pro-405 and Pro-530 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-851 by HIF1AN thus probably abrogating interaction with CREBBP and EP300 and preventing transcriptional activation.1 Publication
Phosphorylated on multiple sites in the CTAD.1 Publication
The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.1 Publication

Keywords - PTMi

Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P97481

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P97481

PRoteomics IDEntifications database

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PRIDEi
P97481

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P97481

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P97481

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in most tissues, with highest levels in lung, followed by heart, kidney, brain and liver. Predominantly expressed in endothelial cells. Also found in smooth muscle cells of the uterus, neurons, and brown adipose tissue. High expression in embryonic choroid plexus and kidney glomeruli.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In day 11 embryo, expression is almost exclusively seen in endothelial cells of the intersegmental blood vessels separating the somites, the atrial and ventricular chambers of the heart, and the dorsal aorta. High expression also occurs in extraembryonic membranes. In the developing brain of day 13 embryo, endothelial cells of the highly vascularized choroid plexus contain high levels of EPAS1.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000024140 Expressed in 302 organ(s), highest expression level in right lung

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P97481 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with HIF3A isoform 2 (PubMed:21546903). Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). Interacts with CREBBP (PubMed:11983697). Interacts with EGLN1. Interacts with VHL (By similarity).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ArntP537625EBI-15704570,EBI-78852

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199458, 7 interactors

Database of interacting proteins

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DIPi
DIP-46109N

Protein interaction database and analysis system

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IntActi
P97481, 4 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000024954

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1874
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZP4X-ray2.35B/D3-361[»]
4ZPHX-ray2.80B/D3-361[»]
4ZPKX-ray3.60B3-361[»]
4ZQDX-ray2.87B/D3-361[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P97481

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P97481

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini14 – 67bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini84 – 154PAS 1PROSITE-ProRule annotationAdd BLAST71
Domaini230 – 300PAS 2PROSITE-ProRule annotationAdd BLAST71
Domaini304 – 347PACAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 53DNA-binding1 PublicationAdd BLAST28
Regioni171 – 192Required for heterodimer formation with ARNT1 PublicationAdd BLAST22
Regioni495 – 541NTADAdd BLAST47
Regioni834 – 874CTADAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi471 – 479Poly-Ser9

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3558 Eukaryota
ENOG410YK57 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155930

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234306

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG060456

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P97481

KEGG Orthology (KO)

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KOi
K09095

Identification of Orthologs from Complete Genome Data

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OMAi
NNCPPHS

Database of Orthologous Groups

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OrthoDBi
547545at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P97481

TreeFam database of animal gene trees

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TreeFami
TF317772

Family and domain databases

Conserved Domains Database

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CDDi
cd00083 HLH, 1 hit
cd00130 PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011598 bHLH_dom
IPR014887 HIF-1_TAD_C
IPR021537 HIF_alpha_subunit
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
IPR013655 PAS_fold_3

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11413 HIF-1, 1 hit
PF08778 HIF-1a_CTAD, 1 hit
PF00989 PAS, 1 hit
PF08447 PAS_3, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00785 NCTRNSLOCATR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00229 sensory_box, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P97481-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTADKEKKRS SSELRKEKSR DAARCRRSKE TEVFYELAHE LPLPHSVSSH
60 70 80 90 100
LDKASIMRLA ISFLRTHKLL SSVCSENESE AEADQQMDNL YLKALEGFIA
110 120 130 140 150
VVTQDGDMIF LSENISKFMG LTQVELTGHS IFDFTHPCDH EEIRENLTLK
160 170 180 190 200
NGSGFGKKSK DVSTERDFFM RMKCTVTNRG RTVNLKSATW KVLHCTGQVR
210 220 230 240 250
VYNNCPPHSS LCGSKEPLLS CLIIMCEPIQ HPSHMDIPLD SKTFLSRHSM
260 270 280 290 300
DMKFTYCDDR ILELIGYHPE ELLGRSAYEF YHALDSENMT KSHQNLCTKG
310 320 330 340 350
QVVSGQYRML AKHGGYVWLE TQGTVIYNPR NLQPQCIMCV NYVLSEIEKN
360 370 380 390 400
DVVFSMDQTE SLFKPHLMAM NSIFDSSDDV AVTEKSNYLF TKLKEEPEEL
410 420 430 440 450
AQLAPTPGDA IISLDFGSQN FDEPSAYGKA ILPPGQPWVS GLRSHSAQSE
460 470 480 490 500
SGSLPAFTVP QADTPGNTTP SASSSSSCST PSSPEDYYSS LENPLKIEVI
510 520 530 540 550
EKLFAMDTEP RDPGSTQTDF SELDLETLAP YIPMDGEDFQ LSPICPEEPL
560 570 580 590 600
MPESPQPTPQ HCFSTMTSIF QPLTPGATHG PFFLDKYPQQ LESRKTESEH
610 620 630 640 650
WPMSSIFFDA GSKGSLSPCC GQASTPLSSM GGRSNTQWPP DPPLHFGPTK
660 670 680 690 700
WPVGDQSAES LGALPVGSSQ LEPPSAPPHV SMFKMRSAKD FGARGPYMMS
710 720 730 740 750
PAMIALSNKL KLKRQLEYEE QAFQDTSGGD PPGTSSSHLM WKRMKSLMGG
760 770 780 790 800
TCPLMPDKTI SANMAPDEFT QKSMRGLGQP LRHLPPPQPP STRSSGENAK
810 820 830 840 850
TGFPPQCYAS QFQDYGPPGA QKVSGVASRL LGPSFEPYLL PELTRYDCEV
860 870
NVPVPGSSTL LQGRDLLRAL DQAT
Length:874
Mass (Da):96,712
Last modified:December 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA6FFA490AE43640C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti25C → S in BAA20130 (PubMed:9113979).Curated1
Sequence conflicti191K → KS in AAB41496 (PubMed:9000051).Curated1
Sequence conflicti439 – 440VS → AA in AAC12871 (PubMed:9178256).Curated2
Sequence conflicti463D → G in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti654G → V in BAA20130 (PubMed:9113979).Curated1
Sequence conflicti663A → P in BAA20130 (PubMed:9113979).Curated1
Sequence conflicti669S → W in AAB41496 (PubMed:9000051).Curated1
Sequence conflicti673P → L in AAB41496 (PubMed:9000051).Curated1
Sequence conflicti678P → L in AAB41496 (PubMed:9000051).Curated1
Sequence conflicti725D → E in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti731P → L in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti762A → G in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti786P → L in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti791S → F in AAC12871 (PubMed:9178256).Curated1
Sequence conflicti794S → N in AAC12871 (PubMed:9178256).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U81983 mRNA Translation: AAB41496.1
D89787 mRNA Translation: BAA20130.1
AF045160 mRNA Translation: AAC12871.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS37713.1

NCBI Reference Sequences

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RefSeqi
NP_034267.3, NM_010137.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.1415

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000024954; ENSMUSP00000024954; ENSMUSG00000024140

Database of genes from NCBI RefSeq genomes

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GeneIDi
13819

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13819

UCSC genome browser

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UCSCi
uc008duj.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81983 mRNA Translation: AAB41496.1
D89787 mRNA Translation: BAA20130.1
AF045160 mRNA Translation: AAC12871.1
CCDSiCCDS37713.1
RefSeqiNP_034267.3, NM_010137.3
UniGeneiMm.1415

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZP4X-ray2.35B/D3-361[»]
4ZPHX-ray2.80B/D3-361[»]
4ZPKX-ray3.60B3-361[»]
4ZQDX-ray2.87B/D3-361[»]
ProteinModelPortaliP97481
SMRiP97481
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199458, 7 interactors
DIPiDIP-46109N
IntActiP97481, 4 interactors
STRINGi10090.ENSMUSP00000024954

PTM databases

iPTMnetiP97481
PhosphoSitePlusiP97481

Proteomic databases

MaxQBiP97481
PaxDbiP97481
PRIDEiP97481

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024954; ENSMUSP00000024954; ENSMUSG00000024140
GeneIDi13819
KEGGimmu:13819
UCSCiuc008duj.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2034
MGIiMGI:109169 Epas1

Phylogenomic databases

eggNOGiKOG3558 Eukaryota
ENOG410YK57 LUCA
GeneTreeiENSGT00940000155930
HOGENOMiHOG000234306
HOVERGENiHBG060456
InParanoidiP97481
KOiK09095
OMAiNNCPPHS
OrthoDBi547545at2759
PhylomeDBiP97481
TreeFamiTF317772

Enzyme and pathway databases

ReactomeiR-MMU-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-1234162 Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-8951664 Neddylation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Epas1 mouse

Protein Ontology

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PROi
PR:P97481

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024140 Expressed in 302 organ(s), highest expression level in right lung
GenevisibleiP97481 MM

Family and domain databases

CDDicd00083 HLH, 1 hit
cd00130 PAS, 2 hits
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR014887 HIF-1_TAD_C
IPR021537 HIF_alpha_subunit
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
IPR013655 PAS_fold_3
PfamiView protein in Pfam
PF11413 HIF-1, 1 hit
PF08778 HIF-1a_CTAD, 1 hit
PF00989 PAS, 1 hit
PF08447 PAS_3, 1 hit
PRINTSiPR00785 NCTRNSLOCATR
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits
SUPFAMiSSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits
TIGRFAMsiTIGR00229 sensory_box, 2 hits
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPAS1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P97481
Secondary accession number(s): O08787, O55046
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: February 13, 2019
This is version 171 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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