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Protein

Hypoxia-inducible factor 1-alpha

Gene

HIF1A

Organism
Homo sapiens (Human)
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

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. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP 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 similarity10 Publications

<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, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-1234162 Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-400253 Circadian Clock
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-8849473 PTK6 Expression
R-HSA-8857538 PTK6 promotes HIF1A stabilization
R-HSA-8951664 Neddylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q16665

SIGNOR Signaling Network Open Resource

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SIGNORi
Q16665

<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:
Hypoxia-inducible factor 1-alpha1 Publication
Short name:
HIF-1-alpha1 Publication
Short name:
HIF1-alpha1 Publication
Alternative name(s):
ARNT-interacting protein
Basic-helix-loop-helix-PAS protein MOP11 Publication
Class E basic helix-loop-helix protein 78
Short name:
bHLHe78
Member of PAS protein 11 Publication
PAS domain-containing protein 8
<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:HIF1A1 Publication
Synonyms:BHLHE78, MOP11 Publication, PASD8
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100644.16

Human Gene Nomenclature Database

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HGNCi
HGNC:4910 HIF1A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603348 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q16665

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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>Mutagenesisi247S → A: Constitutive kinase activity. 1 Publication1
Mutagenesisi247S → D: Impaired kinase activity. 1 Publication1
Mutagenesisi377K → R: No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-391; R-477 and R-532. 1 Publication1
Mutagenesisi389K → R: No change in sumoylation. 1 Publication1
Mutagenesisi391K → R: Abolishes 1 sumoylation. Abolishes 1 sumoylation; when associated with R-532. Abolishes 2 sumoylations; when associated with R-477. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-477 and R-532. 2 Publications1
Mutagenesisi392K → R: No change in sumoylation. 1 Publication1
Mutagenesisi394P → A: No change in VHLE3-dependent ubiquitination. 1 Publication1
Mutagenesisi397L → A: Abolishes VHLE3-dependent ubiquitination; when associated with A-400. 1 Publication1
Mutagenesisi400L → A: Abolishes VHLE3-dependent ubiquitination; when associated with A-397. 1 Publication1
Mutagenesisi402P → A: Abolishes in VHLE3-dependent ubiquitination, abolishes oxygen-dependent regulation of VP16, partially reduced VHLE target site ubiquitination and no interaction with VHL. No VHLE target site ubiquitination; when associated with G-564. Increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation; when associated with A-564. 3 Publications1
Mutagenesisi442K → R: No change in sumoylation. 1 Publication1
Mutagenesisi460K → R: No change in sumoylation nor in ARD1-mediated acetylation. 1 Publication1
Mutagenesisi477K → R: Abolishes 1 sumoylation. Abolishes 2 sumoylations; when associated with R-391. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-532. 2 Publications1
Mutagenesisi532K → R: Reduced ubiquitination. No change in sumoylation nor on interaction with ARD1A. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-477. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-538 and K-547. 5 Publications1
Mutagenesisi538K → R: No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-547. 3 Publications1
Mutagenesisi547K → R: No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-538. 3 Publications1
Mutagenesisi551S → G: Constitutive expression under nonhypoxic conditions by decreasing ubiquitination. 1 Publication1
Mutagenesisi552T → A: Constitutive expression under nonhypoxic conditions by decreasing ubiquitination. 1 Publication1
Mutagenesisi564P → A: Increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation; when associated with A-402. 3 Publications1
Mutagenesisi564P → G: No change in VHL-dependent ubiquitination. Partially reduced VHLE target site ubiquitination. No VHLE target site ubiquitination; when associated with A-402. 3 Publications1
Mutagenesisi576S → A: Induces stabilization of the protein. 1 Publication1
Mutagenesisi657S → A: Induces stabilization of the protein. 1 Publication1
Mutagenesisi709K → R: Abolishes SIRT2-mediated deacetylation, increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation. Increases interaction with EGLN1. 1 Publication1
Mutagenesisi719K → T: Dramatic reduction of accumulation in the nucleus in response to hypoxia. 2 Publications1
Mutagenesisi795L → A: Inhibits interaction with EP300 and transactivation activity. 1 Publication1
Mutagenesisi800C → A: Blocks increase in transcriptional activation caused by nitrosylation. 2 Publications1
Mutagenesisi800C → S: Abolishes hypoxia-inducible transcriptional activation of ctaD. 2 Publications1
Mutagenesisi803N → A: Recruits CREBBP. No enhancement of CREBBP by Clioquinol in the presence of FIH1. No change in nuclear location nor on repression of transcriptional activity in the presence of histone deacetylase inhibitor. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
3091

Open Targets

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OpenTargetsi
ENSG00000100644

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29283

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4261

Drug and drug target database

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DrugBanki
DB02342 2-Methoxyestradiol
DB01136 Carvedilol
DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HIF-1A

Domain mapping of disease mutations (DMDM)

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DMDMi
2498017

<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_00001272201 – 826Hypoxia-inducible factor 1-alphaAdd BLAST826

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 residuei247Phosphoserine; by CK11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Modified residuei4024-hydroxyproline1 Publication1
Cross-linki477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Modified residuei532N6-acetyllysine1 Publication1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei551Phosphoserine; by GSK3-beta1 Publication1
Modified residuei555Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei5644-hydroxyproline4 Publications1
Modified residuei576Phosphoserine; by PLK31 Publication1
Modified residuei589Phosphoserine; by GSK3-beta1 Publication1
Modified residuei657Phosphoserine; by PLK31 Publication1
Modified residuei709N6-acetyllysine1 Publication1
Modified residuei800S-nitrosocysteine1 Publication1
Modified residuei803(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

S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.2 Publications
Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding. Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome.2 Publications
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.4 Publications
Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation (PubMed:12464182). Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (PubMed:24681946).2 Publications
Polyubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-532 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-803. Ubiquitinated by a CUL2-based E3 ligase.5 Publications
In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). EGLN3/PHD3 has also been shown to hydroxylate Pro-564 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Deubiquitinated by USP20 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation (PubMed:12080085). This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol (PubMed:12080085). Repressed by iron ion, via Fe2+ prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation (PubMed:28296633).7 Publications
The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16665

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16665

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

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PaxDbi
Q16665

PeptideAtlas

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PeptideAtlasi
Q16665

PRoteomics IDEntifications database

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PRIDEi
Q16665

ProteomicsDB human proteome resource

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ProteomicsDBi
61021
61022 [Q16665-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16665

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

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PhosphoSitePlusi
Q16665

<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 kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. A higher level expression seen in pituitary tumors as compared to the pituitary gland.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B/interleukin-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. Repressed by HIPK2 and LIMD1.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000100644 Expressed in 238 organ(s), highest expression level in visceral pleura

CleanEx database of gene expression profiles

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CleanExi
HS_HIF1A

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16665 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16665 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB017442
HPA000907
HPA001275

<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 the ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:10944113, PubMed:20699359). Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability (By similarity). Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domains). 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 TSGA10 (By similarity). Interacts with HIF3A (By similarity). 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 RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation. Interacts (via N-terminus) with USP19. Interacts with SIRT2. Interacts (deacetylated form) with EGLN1. Interacts with CBFA2T3. Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).By similarity30 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109338, 234 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q16665

Database of interacting proteins

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DIPi
DIP-29722N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q16665

Protein interaction database and analysis system

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IntActi
Q16665, 93 interactors

Molecular INTeraction database

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MINTi
Q16665

STRING: functional protein association networks

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STRINGi
9606.ENSP00000338018

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q16665

<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

1826
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00262

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q16665

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

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SMRi
Q16665

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q16665

<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>Domaini17 – 70bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini85 – 158PAS 1PROSITE-ProRule annotationAdd BLAST74
Domaini228 – 298PAS 2PROSITE-ProRule annotationAdd BLAST71
Domaini302 – 345PACAdd 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>Regioni1 – 401Interaction with TSGA10By similarityAdd BLAST401
Regioni21 – 30DNA-bindingBy similarity10
Regioni170 – 191Required for heterodimer formation with ARNTBy similarityAdd BLAST22
Regioni380 – 417N-terminal VHL recognition siteAdd BLAST38
Regioni401 – 603ODDAdd BLAST203
Regioni531 – 575NTADAdd BLAST45
Regioni556 – 572C-terminal VHL recognition siteAdd BLAST17
Regioni576 – 785IDAdd BLAST210
Regioni786 – 826CTADAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi718 – 721Nuclear localization signalSequence analysis4

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 biasi615 – 621Poly-Thr7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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).

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3558 Eukaryota
ENOG410YK57 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156774

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234306

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG060456

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q16665

KEGG Orthology (KO)

More...
KOi
K08268

Identification of Orthologs from Complete Genome Data

More...
OMAi
TSPSEYC

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0486

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q16665

TreeFam database of animal gene trees

More...
TreeFami
TF317772

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00083 HLH, 1 hit
cd00130 PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011598 bHLH_dom
IPR001321 HIF-1_alpha
IPR014887 HIF-1_TAD_C
IPR021537 HIF_alpha_subunit
IPR036638 HLH_DNA-bd_sf
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

More...
PRINTSi
PR01080 HYPOXIAIF1A

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00229 sensory_box, 2 hits

PROSITE; a protein domain and family database

More...
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>Sequences (3+)i

<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.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q16665-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV
60 70 80 90 100
SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMKAQMNC FYLKALDGFV
110 120 130 140 150
MVLTDDGDMI YISDNVNKYM GLTQFELTGH SVFDFTHPCD HEEMREMLTH
160 170 180 190 200
RNGLVKKGKE QNTQRSFFLR MKCTLTSRGR TMNIKSATWK VLHCTGHIHV
210 220 230 240 250
YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK TFLSRHSLDM
260 270 280 290 300
KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
310 320 330 340 350
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL
360 370 380 390 400
IFSLQQTECV LKPVESSDMK MTQLFTKVES EDTSSLFDKL KKEPDALTLL
410 420 430 440 450
APAAGDTIIS LDFGSNDTET DDQQLEEVPL YNDVMLPSPN EKLQNINLAM
460 470 480 490 500
SPLPTAETPK PLRSSADPAL NQEVALKLEP NPESLELSFT MPQIQDQTPS
510 520 530 540 550
PSDGSTRQSS PEPNSPSEYC FYVDSDMVNE FKLELVEKLF AEDTEAKNPF
560 570 580 590 600
STQDTDLDLE MLAPYIPMDD DFQLRSFDQL SPLESSSASP ESASPQSTVT
610 620 630 640 650
VFQQTQIQEP TANATTTTAT TDELKTVTKD RMEDIKILIA SPSPTHIHKE
660 670 680 690 700
TTSATSSPYR DTQSRTASPN RAGKGVIEQT EKSHPRSPNV LSVALSQRTT
710 720 730 740 750
VPEEELNPKI LALQNAQRKR KMEHDGSLFQ AVGIGTLLQQ PDDHAATTSL
760 770 780 790 800
SWKRVKGCKS SEQNGMEQKT IILIPSDLAC RLLGQSMDES GLPQLTSYDC
810 820
EVNAPIQGSR NLLQGEELLR ALDQVN
Length:826
Mass (Da):92,670
Last modified:November 1, 1996 - v1
<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:iABD4F7DAA135BE2D
GO
Isoform 2 (identifier: Q16665-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     735-735: G → I
     736-826: Missing.

Note: No experimental confirmation available.
Show »
Length:735
Mass (Da):82,746
Checksum:i34DD604FB4E4418E
GO
Isoform 3 (identifier: Q16665-3) [UniParc]FASTAAdd to basket
Also known as: I.3

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MEGAGGANDKKK → MSSQCRSLENKFVFLKEGLGNSKPEELEEIRIENGR

Note: Up-regulated in peripheral T-lymphocytes after T-cell receptor stimulation. Highest expression in peripheral blood leukocytes and thymus.
Show »
Length:850
Mass (Da):95,634
Checksum:i272C9EFAFD7A1E48
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MYV6A8MYV6_HUMAN
Hypoxia-inducible factor 1, alpha s...
HIF1A hCG_21199
827Annotation score:

Annotation score:2 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>
F8W9L0F8W9L0_HUMAN
Hypoxia-inducible factor 1-alpha
HIF1A
767Annotation score:

Annotation score:2 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 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 conflicti572F → L in AAC68568 (PubMed:9782081).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_049541582P → S. Corresponds to variant dbSNP:rs11549465Ensembl.1
Natural variantiVAR_049542588A → T. Corresponds to variant dbSNP:rs11549467Ensembl.1
Natural variantiVAR_015854796T → A. Corresponds to variant dbSNP:rs1802821Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0449421 – 12MEGAG…NDKKK → MSSQCRSLENKFVFLKEGLG NSKPEELEEIRIENGR in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_047335735G → I in isoform 2. 1 Publication1
Alternative sequenceiVSP_007738736 – 826Missing in isoform 2. 1 PublicationAdd BLAST91

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U22431 mRNA Translation: AAC50152.1
U29165 mRNA Translation: AAC51210.1
AF050127
, AF050115, AF050116, AF050117, AF050118, AF050119, AF050120, AF050121, AF050122, AF050123, AF050124, AF050125, AF050126 Genomic DNA Translation: AAC68568.1
FJ790247 mRNA Translation: ACN88547.1
AF207601 mRNA Translation: AAF20139.1
AF207602 mRNA Translation: AAF20140.1
AF208487 Genomic DNA Translation: AAF20149.1
AF304431 mRNA Translation: AAG43026.1
AB073325 mRNA Translation: BAB70608.1
BT009776 mRNA Translation: AAP88778.1
AL137129 Genomic DNA No translation available.
BC012527 mRNA Translation: AAH12527.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS58324.1 [Q16665-3]
CCDS9753.1 [Q16665-1]
CCDS9754.1 [Q16665-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
I38972

NCBI Reference Sequences

More...
RefSeqi
NP_001230013.1, NM_001243084.1 [Q16665-3]
NP_001521.1, NM_001530.3 [Q16665-1]
NP_851397.1, NM_181054.2 [Q16665-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.597216
Hs.719495

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000323441; ENSP00000323326; ENSG00000100644 [Q16665-2]
ENST00000337138; ENSP00000338018; ENSG00000100644 [Q16665-1]
ENST00000539097; ENSP00000437955; ENSG00000100644 [Q16665-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3091

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3091

UCSC genome browser

More...
UCSCi
uc001xfq.3 human [Q16665-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Hypoxia inducible factor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22431 mRNA Translation: AAC50152.1
U29165 mRNA Translation: AAC51210.1
AF050127
, AF050115, AF050116, AF050117, AF050118, AF050119, AF050120, AF050121, AF050122, AF050123, AF050124, AF050125, AF050126 Genomic DNA Translation: AAC68568.1
FJ790247 mRNA Translation: ACN88547.1
AF207601 mRNA Translation: AAF20139.1
AF207602 mRNA Translation: AAF20140.1
AF208487 Genomic DNA Translation: AAF20149.1
AF304431 mRNA Translation: AAG43026.1
AB073325 mRNA Translation: BAB70608.1
BT009776 mRNA Translation: AAP88778.1
AL137129 Genomic DNA No translation available.
BC012527 mRNA Translation: AAH12527.1
CCDSiCCDS58324.1 [Q16665-3]
CCDS9753.1 [Q16665-1]
CCDS9754.1 [Q16665-2]
PIRiI38972
RefSeqiNP_001230013.1, NM_001243084.1 [Q16665-3]
NP_001521.1, NM_001530.3 [Q16665-1]
NP_851397.1, NM_181054.2 [Q16665-2]
UniGeneiHs.597216
Hs.719495

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D7Gmodel-D15-73[»]
1H2KX-ray2.15S786-826[»]
1H2LX-ray2.25S786-826[»]
1H2MX-ray2.50S775-826[»]
1L3ENMR-A786-826[»]
1L8CNMR-B776-826[»]
1LM8X-ray1.85H556-575[»]
1LQBX-ray2.00D549-582[»]
2ILMX-ray2.30S786-826[»]
3HQRX-ray2.00S558-574[»]
3HQUX-ray2.30S558-574[»]
4AJYX-ray1.73H559-577[»]
4H6JX-ray1.52A238-348[»]
5JWPX-ray2.10B788-806[»]
5L9BX-ray1.95C/D556-574[»]
5L9VX-ray1.83C/D395-411[»]
5LA9X-ray2.81C/D395-411[»]
5LASX-ray2.10C/D395-411[»]
DisProtiDP00262
ProteinModelPortaliQ16665
SMRiQ16665
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109338, 234 interactors
CORUMiQ16665
DIPiDIP-29722N
ELMiQ16665
IntActiQ16665, 93 interactors
MINTiQ16665
STRINGi9606.ENSP00000338018

Chemistry databases

BindingDBiQ16665
ChEMBLiCHEMBL4261
DrugBankiDB02342 2-Methoxyestradiol
DB01136 Carvedilol
DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE

PTM databases

iPTMnetiQ16665
PhosphoSitePlusiQ16665

Polymorphism and mutation databases

BioMutaiHIF-1A
DMDMi2498017

Proteomic databases

EPDiQ16665
MaxQBiQ16665
PaxDbiQ16665
PeptideAtlasiQ16665
PRIDEiQ16665
ProteomicsDBi61021
61022 [Q16665-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3091
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323441; ENSP00000323326; ENSG00000100644 [Q16665-2]
ENST00000337138; ENSP00000338018; ENSG00000100644 [Q16665-1]
ENST00000539097; ENSP00000437955; ENSG00000100644 [Q16665-3]
GeneIDi3091
KEGGihsa:3091
UCSCiuc001xfq.3 human [Q16665-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3091
DisGeNETi3091
EuPathDBiHostDB:ENSG00000100644.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HIF1A
HGNCiHGNC:4910 HIF1A
HPAiCAB017442
HPA000907
HPA001275
MIMi603348 gene
neXtProtiNX_Q16665
OpenTargetsiENSG00000100644
PharmGKBiPA29283

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3558 Eukaryota
ENOG410YK57 LUCA
GeneTreeiENSGT00940000156774
HOGENOMiHOG000234306
HOVERGENiHBG060456
InParanoidiQ16665
KOiK08268
OMAiTSPSEYC
OrthoDBiEOG091G0486
PhylomeDBiQ16665
TreeFamiTF317772

Enzyme and pathway databases

ReactomeiR-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-1234162 Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-400253 Circadian Clock
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-8849473 PTK6 Expression
R-HSA-8857538 PTK6 promotes HIF1A stabilization
R-HSA-8951664 Neddylation
SignaLinkiQ16665
SIGNORiQ16665

Miscellaneous databases

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

More...
ChiTaRSi
HIF1A human
EvolutionaryTraceiQ16665

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HIF1A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3091

Protein Ontology

More...
PROi
PR:Q16665

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100644 Expressed in 238 organ(s), highest expression level in visceral pleura
CleanExiHS_HIF1A
ExpressionAtlasiQ16665 baseline and differential
GenevisibleiQ16665 HS

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
IPR001321 HIF-1_alpha
IPR014887 HIF-1_TAD_C
IPR021537 HIF_alpha_subunit
IPR036638 HLH_DNA-bd_sf
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
PRINTSiPR01080 HYPOXIAIF1A
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

More...
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 nameiHIF1A_HUMAN
<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: Q16665
Secondary accession number(s): C0LZJ3
, Q53XP6, Q96PT9, Q9UPB1
<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: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 221 of the entry and version 1 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
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.

<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. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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