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Entry version 188 (25 May 2022)
Sequence version 1 (01 Jan 1998)
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Protein

Hypoxia-inducible factor 1-alpha

Gene

Hif1a

Organism
Rattus norvegicus (Rat)
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 transcript 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 (By similarity).

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 NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Induced by reactive oxygen species (ROS).By similarity

<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

More...
Reactomei
R-RNO-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-RNO-1234174, Cellular response to hypoxia
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-5689880, Ub-specific processing proteases
R-RNO-8857538, PTK6 promotes HIF1A stabilization
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">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-alpha
Short name:
HIF-1-alpha
Short name:
HIF1-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Hif1a
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
61928, Hif1a

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001272221 – 825Hypoxia-inducible factor 1-alphaAdd BLAST825

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 CK1By similarity1
Modified residuei4024-hydroxyprolineBy similarity1
Modified residuei531N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki537Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei550Phosphoserine; by GSK3-betaBy similarity1
Modified residuei554Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei5634-hydroxyprolineBy similarity1
Modified residuei575Phosphoserine; by PLK3By similarity1
Modified residuei588Phosphoserine; by GSK3-betaBy similarity1
Modified residuei657Phosphoserine; by PLK3By similarity1
Modified residuei799S-nitrosocysteineBy similarity1
Modified residuei802(3S)-3-hydroxyasparagineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-799 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.By similarity
Acetylation of Lys-531 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation. Deacetylated by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (By similarity).By similarity
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 (By similarity).By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.By similarity
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 (By similarity).By similarity
In normoxia, is hydroxylated on Pro-402 and Pro-563 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-563. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Deubiquitinated by USP20. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (By similarity). In normoxia, is hydroxylated on Asn-802 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. Repressed by iron ion, via Fe2+ prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation.By similarity

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
O35800

PRoteomics IDEntifications database

More...
PRIDEi
O35800

PTM databases

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

More...
PhosphoSitePlusi
O35800

<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 the kidney, higher expression is seen in the renal medulla than in the cortex. Expressed also in the perivenous zone of the liver.

<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%5Fsection">'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%5Fsection">'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 (By similarity).

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, APEX1 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 (By similarity).

Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription (By similarity).

Interacts (via the ODD domain) with NAA10; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia.

Interacts with RWDD3; the interaction enhances HIF1A sumoylation (By similarity).

Interacts with TSGA10.

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.

Interacts with DCUN1D1; this interaction increases the interaction between VHL and DCUN1D1.

Interacts with HIF1AN (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
248194, 10 interactors

Protein interaction database and analysis system

More...
IntActi
O35800, 1 interactor

Molecular INTeraction database

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MINTi
O35800

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000042230

<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

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
O35800

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

More...
SMRi
O35800

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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
Regioni1 – 30DisorderedSequence analysisAdd BLAST30
Regioni21 – 30DNA-bindingBy similarity10
Regioni170 – 191Required for heterodimer formation with ARNTBy similarityAdd BLAST22
Regioni401 – 602ODDAdd BLAST202
Regioni492 – 520DisorderedSequence analysisAdd BLAST29
Regioni530 – 574NTADAdd BLAST45
Regioni575 – 784IDAdd BLAST210
Regioni579 – 602DisorderedSequence analysisAdd BLAST24
Regioni654 – 674DisorderedSequence analysisAdd BLAST21
Regioni785 – 825CTADAdd 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>Motifi717 – 721Nuclear localization signalSequence analysis5

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi492 – 515Polar residuesSequence analysisAdd BLAST24

<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) (By similarity).By similarity

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3558, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O35800

Database of Orthologous Groups

More...
OrthoDBi
547545at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
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
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
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
PF08447, PAS_3, 1 hit
PF13426, PAS_9, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01080, HYPOXIAIF1A

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O35800-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV
60 70 80 90 100
SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDEMKAQMNC FYLKAPDGFV
110 120 130 140 150
MVLTDDGDMI YISDNVNKYM GLTQFELTGH SVFDFTHPCD HEEMREMLTH
160 170 180 190 200
RNGPVRKGKE QNTQRSFFLR MKCTLTSRGR TMNIKSATWK VLHCTGHIHV
210 220 230 240 250
YDTSSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK TFLSRHSLDM
260 270 280 290 300
KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
310 320 330 340 350
TTGQYRMLAK RGGYVWVETQ ATVIYNTKDS QPQCIVCVNY VVSGIIQHDL
360 370 380 390 400
IFSLQQTESV LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL
410 420 430 440 450
APAAGDTIIS LDFGSDDTET EDQQLEDVPL YNDVMFPSSN EKLNINLAMS
460 470 480 490 500
PLPASETPKP LRSSADPALN QEVALKLESS PESLGLSFTM PQIQDQPASP
510 520 530 540 550
SDGSTRQSSP EPNSPSEYCF DVDSDMVNVF KLELVEKLFA EDTEAKNPFS
560 570 580 590 600
AQDTDLDLEM LAPYIPMDDD FQLRSFDQLS PLESNSPSPP SVSTVTGFQQ
610 620 630 640 650
TQLQKPTITV TAATATTATT TDESKAVTKD NIEDIKILIA SPPSTQVPQE
660 670 680 690 700
MTTAKASAYS GTHSRTASPD RAGKRVIEKT DKAHPRSLNL SVTLNQRNTV
710 720 730 740 750
PEEELNPRTI ALQNAQRKRK MEHDGSLFQA AGIGTLLQQP GDRAPTMSLS
760 770 780 790 800
WKRVKGYISS EQDGMEQKTI FLIPSDLACR LLGQSMDESG LPQLTSYDCE
810 820
VNAPIQGSRN LLQGEELLRA LDQVN
Length:825
Mass (Da):92,319
Last modified:January 1, 1998 - 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:iC4109A57F38667E9
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D4A8P8D4A8P8_RAT
Hypoxia-inducible factor 1-alpha
Hif1a rCG_62077
826Annotation 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 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 conflicti12K → NR in AAD24413 (PubMed:11526200).Curated1
Sequence conflicti74D → G in AAD24413 (PubMed:11526200).Curated1
Sequence conflicti96P → L in AAD24413 (PubMed:11526200).Curated1
Sequence conflicti329D → N in AAD24413 (PubMed:11526200).Curated1
Sequence conflicti613 – 619ATATTAT → TATA in AAD24413 (PubMed:11526200).Curated7
Sequence conflicti708R → K in AAD24413 (PubMed:11526200).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
Y09507 mRNA Translation: CAA70701.1
AF057308 mRNA Translation: AAD24413.1

Protein sequence database of the Protein Information Resource

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PIRi
JC5809

NCBI Reference Sequences

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RefSeqi
NP_077335.1, NM_024359.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
29560

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:29560

UCSC genome browser

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UCSCi
RGD:61928, rat

<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
Y09507 mRNA Translation: CAA70701.1
AF057308 mRNA Translation: AAD24413.1
PIRiJC5809
RefSeqiNP_077335.1, NM_024359.1

3D structure databases

AlphaFoldDBiO35800
SMRiO35800
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi248194, 10 interactors
IntActiO35800, 1 interactor
MINTiO35800
STRINGi10116.ENSRNOP00000042230

PTM databases

PhosphoSitePlusiO35800

Proteomic databases

PaxDbiO35800
PRIDEiO35800

Genome annotation databases

GeneIDi29560
KEGGirno:29560
UCSCiRGD:61928, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3091
RGDi61928, Hif1a

Phylogenomic databases

eggNOGiKOG3558, Eukaryota
InParanoidiO35800
OrthoDBi547545at2759

Enzyme and pathway databases

ReactomeiR-RNO-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-RNO-1234174, Cellular response to hypoxia
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-5689880, Ub-specific processing proteases
R-RNO-8857538, PTK6 promotes HIF1A stabilization
R-RNO-8951664, Neddylation

Miscellaneous databases

Protein Ontology

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PROi
PR:O35800

Family and domain databases

CDDicd00130, 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
IPR013655, PAS_fold_3
PfamiView protein in Pfam
PF11413, HIF-1, 1 hit
PF08778, HIF-1a_CTAD, 1 hit
PF08447, PAS_3, 1 hit
PF13426, PAS_9, 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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_RAT
<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: O35800
Secondary accession number(s): Q9WTU9
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: January 1, 1998
Last modified: May 25, 2022
This is version 188 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

<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

Reference proteome
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