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Protein

Hypoxia-inducible factor 3-alpha

Gene

HIF3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422). Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity).By similarity5 Publications
Isoform 2: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Also inhibits hypoxia-inducible ARNT-mediated gene expression.1 Publication
Isoform 3: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.3 Publications
isoform 4: Attenuates the ability of transcription factor HIF1A and EPAS1/HIF2A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation (PubMed:16126907, PubMed:17998805, PubMed:19694616, PubMed:20416395). May act as a tumor suppressor and inhibits malignant cell transformation (PubMed:17998805).4 Publications
Isoform 5: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Angiogenesis, Apoptosis, Stress response, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124440-MONOMER.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia-inducible factor 3-alpha1 Publication
Short name:
HIF-3-alpha1 Publication
Short name:
HIF3-alpha
Alternative name(s):
Basic-helix-loop-helix-PAS protein MOP7
Class E basic helix-loop-helix protein 17
Short name:
bHLHe17
HIF3-alpha-1
Inhibitory PAS domain protein
Short name:
IPAS
Member of PAS protein 7
PAS domain-containing protein 7
Gene namesi
Name:HIF3AImported
Synonyms:BHLHE17, MOP7, PASD7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:15825. HIF3A.

Subcellular locationi

  • Nucleus 2 Publications
  • Cytoplasm 1 Publication
  • Nucleus speckle By similarity
  • Mitochondrion By similarity

  • Note: In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes with BAD in the cytoplasm. Colocalizes with EPAS1 and HIF1A in the nucleus and speckles (By similarity). Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions (PubMed:19694616). Colocalized with HIF1A in kidney tumors (PubMed:19694616).By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi467K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-570. 1 Publication1
Mutagenesisi492P → A: Reduced hydroxylation activity. Reduced ubiquitination. 1 Publication1
Mutagenesisi570K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-467. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi64344.
OpenTargetsiENSG00000124440.
PharmGKBiPA29285.

Polymorphism and mutation databases

BioMutaiHIF3A.
DMDMi145558932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002844141 – 669Hypoxia-inducible factor 3-alphaAdd BLAST669

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei4924-hydroxyproline1 Publication1
Cross-linki570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

In normoxia, hydroxylated on Pro-492 in the oxygen-dependent degradation domain (ODD) by prolyl hydroxylase(s) (PHD). The hydroxylated proline promotes interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation.1 Publication
Ubiquitinated; ubiquitination occurs in a VHL- and oxygen-dependent pathway and subsequently targeted for proteasomal degradation.1 Publication

Keywords - PTMi

Hydroxylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ9Y2N7.
PeptideAtlasiQ9Y2N7.
PRIDEiQ9Y2N7.

PTM databases

iPTMnetiQ9Y2N7.
PhosphoSitePlusiQ9Y2N7.

Expressioni

Tissue specificityi

Expressed in vascular cells (at protein level) (PubMed:21069422). Expressed in kidney (PubMed:11573933, PubMed:19694616). Expressed in lung epithelial cells (PubMed:16775626). Expressed in endothelial cells (venous and arterial cells from umbilical cord and aortic endothelial cells) and in vascular smooth muscle cells (aorta) (PubMed:21069422). Strongly expressed in the heart, placenta, and skeletal muscle, whereas a weak expression profile was found in the lung, liver, and kidney (PubMed:12538644). Expressed weakly in cell renal cell carcinoma (CC-RCC) compared to normal renal cells (PubMed:16126907). Expression is down-regulated in numerous kidney tumor cells compared to non tumor kidney tissues (PubMed:16126907). Isoform 2 is expressed in heart, placenta, lung, liver, skeletal muscle and pancreas and in numerous cancer cell lines (PubMed:20416395). Isoform 3 and isoform 4 are weakly expressed in heart, placenta, lung, liver, skeletal muscle and pancreas (PubMed:20416395). Isoform 4 is expressed in fetal tissues, such as heart, brain, thymus, lung, liver, skeletal kidney and spleen (PubMed:20416395). Isoform 3 is weakly expressed in fetal tissues, such as liver and kidney (PubMed:20416395).7 Publications

Inductioni

Up-regulated by hypoxia (at protein level) (PubMed:16775626). Induced by hypoxia (PubMed:16775626). Isoform 2, isoform 3, isoform 4 and isoform 5 are up-regulated by hypoxia in a HIF1A- and EPAS1/HIF2A-dependent manner (PubMed:19694616, PubMed:20416395, PubMed:21069422). Isoform 4 is down-regulated by hypoxia and up-regulated upon restoring normoxia in embryonic kidney cells (PubMed:16126907).5 Publications

Gene expression databases

BgeeiENSG00000124440.
CleanExiHS_HIF3A.
ExpressionAtlasiQ9Y2N7. baseline and differential.
GenevisibleiQ9Y2N7. HS.

Organism-specific databases

HPAiHPA041141.

Interactioni

Subunit structurei

Isoform 2 interacts (via ODD domain) with VHL (via beta domain) (PubMed:12538644). Isoform 4 interacts with HIF1A; the interaction inhibits the binding of HIF1A to hypoxia-responsive element (HRE) and HIF1A/ARNT-dependent transcriptional activation (PubMed:16126907). Isoform 4 interacts with ARNT; the interaction occurs in a HIF1A- and DNA-binding-independent manner and does not induce HIF1A/ARNT-dependent transcriptional activation (PubMed:16126907). Isoform 4 interacts with EPAS1 (PubMed:17998805). Interacts with BAD, BCL2L2 and MCL1 (By similarity).By similarity3 Publications

Protein-protein interaction databases

BioGridi122143. 2 interactors.
STRINGi9606.ENSP00000366898.

Structurei

Secondary structure

1669
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi241 – 245Combined sources5
Beta strandi250 – 254Combined sources5
Helixi258 – 262Combined sources5
Helixi266 – 269Combined sources4
Helixi274 – 277Combined sources4
Turni280 – 282Combined sources3
Helixi283 – 296Combined sources14
Beta strandi297 – 300Combined sources4
Beta strandi304 – 307Combined sources4
Beta strandi313 – 323Combined sources11
Helixi329 – 331Combined sources3
Beta strandi333 – 342Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WN5X-ray1.15A/B237-347[»]
ProteinModelPortaliQ9Y2N7.
SMRiQ9Y2N7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 67bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini82 – 154PAS 1PROSITE-ProRule annotationAdd BLAST73
Domaini227 – 297PAS 2PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 100Nuclear localization signalBy similarityAdd BLAST24
Regioni230 – 274Nuclear export signalBy similarityAdd BLAST45
Regioni452 – 581ODDAdd BLAST130
Regioni454 – 506NTADAdd BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 418LRRLL5
Motifi490 – 497LAPYISMD8

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3558. Eukaryota.
ENOG410YK57. LUCA.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234306.
HOVERGENiHBG060456.
InParanoidiQ9Y2N7.
KOiK09096.
OMAiPMAGARK.
OrthoDBiEOG091G0486.
PhylomeDBiQ9Y2N7.
TreeFamiTF317772.

Family and domain databases

InterProiIPR011598. bHLH_dom.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF11413. HIF-1. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.2 Publications
Isoform 1 (identifier: Q9Y2N7-1) [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
MALGLQRARS TTELRKEKSR DAARSRRSQE TEVLYQLAHT LPFARGVSAH
60 70 80 90 100
LDKASIMRLT ISYLRMHRLC AAGEWNQVGA GGEPLDACYL KALEGFVMVL
110 120 130 140 150
TAEGDMAYLS ENVSKHLGLS QLELIGHSIF DFIHPCDQEE LQDALTPQQT
160 170 180 190 200
LSRRKVEAPT ERCFSLRMKS TLTSRGRTLN LKAATWKVLN CSGHMRAYKP
210 220 230 240 250
PAQTSPAGSP DSEPPLQCLV LICEAIPHPG SLEPPLGRGA FLSRHSLDMK
260 270 280 290 300
FTYCDDRIAE VAGYSPDDLI GCSAYEYIHA LDSDAVSKSI HTLLSKGQAV
310 320 330 340 350
TGQYRFLARS GGYLWTQTQA TVVSGGRGPQ SESIVCVHFL ISQVEETGVV
360 370 380 390 400
LSLEQTEQHS RRPIQRGAPS QKDTPNPGDS LDTPGPRILA FLHPPSLSEA
410 420 430 440 450
ALAADPRRFC SPDLRRLLGP ILDGASVAAT PSTPLATRHP QSPLSADLPD
460 470 480 490 500
ELPVGTENVH RLFTSGKDTE AVETDLDIAQ DADALDLEML APYISMDDDF
510 520 530 540 550
QLNASEQLPR AYHRPLGAVP RPRARSFHGL SPPALEPSLL PRWGSDPRLS
560 570 580 590 600
CSSPSRGDPS ASSPMAGARK RTLAQSSEDE DEGVELLGVR PPKRSPSPEH
610 620 630 640 650
ENFLLFPLSL SFLLTGGPAP GSLQDPSTPL LNLNEPLGLG PSLLSPYSDE
660
DTTQPGGPFQ PRAGSAQAD
Length:669
Mass (Da):72,433
Last modified:April 17, 2007 - v2
Checksum:i81C4C84517000DE2
GO
Isoform 2 (identifier: Q9Y2N7-2) [UniParc]FASTAAdd to basket
Also known as: HIF-3alpha11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALGLQRA → MDWQDH

Show »
Length:667
Mass (Da):72,405
Checksum:i67B8794FF9DCCF4B
GO
Isoform 3 (identifier: Q9Y2N7-3) [UniParc]FASTAAdd to basket
Also known as: HIF-3alpha21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     611-669: SFLLTGGPAP...QPRAGSAQAD → VCWGINGILWPSLPSWLKPTVL

Show »
Length:632
Mass (Da):68,964
Checksum:i9665B0AF3998F8EF
GO
Isoform 4 (identifier: Q9Y2N7-4) [UniParc]FASTAAdd to basket
Also known as: HIF-3alpha41 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     293-363: LLSKGQAVTG...EQTEQHSRRP → CMYPISPGAK...FSPHLPPWWP
     364-669: Missing.

Show »
Length:363
Mass (Da):39,962
Checksum:i66CE5B85A2C50A15
GO
Isoform 5 (identifier: Q9Y2N7-5) [UniParc]FASTAAdd to basket
Also known as: HIF-3alpha31 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Note: Incomplete sequence. No experimental confirmation available.
Show »
Length:613
Mass (Da):66,142
Checksum:i4F2122D0D17C55A6
GO
Isoform 6 (identifier: Q9Y2N7-6) [UniParc]FASTAAdd to basket
Also known as: HIF-3alpha61 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     87-137: ACYLKALEGF...SIFDFIHPCD → MRPAAGAARR...ATCACTASAP

Note: Incomplete sequence. No experimental confirmation available.
Show »
Length:583
Mass (Da):62,393
Checksum:i04D6B8408073EEB4
GO
Isoform 7 (identifier: Q9Y2N7-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: MALGLQRARS...ENVSKHLGLS → MRPAAGAARR...ATCACTASAP

Note: No experimental confirmation available.
Show »
Length:600
Mass (Da):64,359
Checksum:i822B55E0513AF129
GO

Sequence cautioni

The sequence AAL69947 differs from that shown. Intron retention.Curated
The sequence BAB13865 differs from that shown. Aberrant splicing site.Curated
The sequence BAB14824 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated
The sequence BAB55324 differs from that shown. Intron retention.Curated
The sequence BAD93355 differs from that shown. Intron retention.Curated
The sequence BAG07185 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti202A → V in BAB55324 (PubMed:14702039).Curated1
Sequence conflicti497D → G in BAB55324 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031731343Q → R.1 PublicationCorresponds to variant rs3764609dbSNPEnsembl.1
Natural variantiVAR_031732463F → L.Corresponds to variant rs7253301dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0434291 – 120MALGL…HLGLS → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 7. 1 PublicationAdd BLAST120
Alternative sequenceiVSP_0245181 – 86Missing in isoform 6. CuratedAdd BLAST86
Alternative sequenceiVSP_0245191 – 56Missing in isoform 5. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_0245201 – 8MALGLQRA → MDWQDH in isoform 2. 1 Publication8
Alternative sequenceiVSP_02452187 – 137ACYLK…IHPCD → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 6. CuratedAdd BLAST51
Alternative sequenceiVSP_024523293 – 363LLSKG…HSRRP → CMYPISPGAKPAATWPPADT RTPQLPIPQDALPPHLNTSS LLPKPQGTVSFLAPSYPVPR SFSPHLPPWWP in isoform 4. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_024525364 – 669Missing in isoform 4. 1 PublicationAdd BLAST306
Alternative sequenceiVSP_024526611 – 669SFLLT…SAQAD → VCWGINGILWPSLPSWLKPT VL in isoform 3. 3 PublicationsAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB054067 mRNA. Translation: BAB69689.1.
AF463492 mRNA. Translation: AAL69947.1. Sequence problems.
AB118749 mRNA. Translation: BAD93355.1. Sequence problems.
AB295039 mRNA. Translation: BAG07185.1. Sequence problems.
AK021653 mRNA. Translation: BAB13865.1. Sequence problems.
AK024095 mRNA. Translation: BAB14824.1. Sequence problems.
AK027725 mRNA. Translation: BAB55324.1. Sequence problems.
AK297828 mRNA. Translation: BAG60164.1.
AC007193 Genomic DNA. Translation: AAD22668.1.
CH471126 Genomic DNA. Translation: EAW57410.1.
BC026308 mRNA. Translation: AAH26308.1.
BC080551 mRNA. Translation: AAH80551.1.
CCDSiCCDS12681.2. [Q9Y2N7-1]
CCDS12682.1. [Q9Y2N7-2]
CCDS42580.2. [Q9Y2N7-7]
PIRiJC7771.
RefSeqiNP_071907.4. NM_022462.4. [Q9Y2N7-7]
NP_690007.1. NM_152794.3. [Q9Y2N7-2]
NP_690008.2. NM_152795.3. [Q9Y2N7-1]
UniGeneiHs.420830.

Genome annotation databases

EnsembliENST00000244303; ENSP00000244303; ENSG00000124440. [Q9Y2N7-7]
ENST00000300862; ENSP00000300862; ENSG00000124440. [Q9Y2N7-2]
ENST00000377670; ENSP00000366898; ENSG00000124440. [Q9Y2N7-1]
GeneIDi64344.
KEGGihsa:64344.
UCSCiuc002peh.3. human. [Q9Y2N7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Hypoxia inducible factor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB054067 mRNA. Translation: BAB69689.1.
AF463492 mRNA. Translation: AAL69947.1. Sequence problems.
AB118749 mRNA. Translation: BAD93355.1. Sequence problems.
AB295039 mRNA. Translation: BAG07185.1. Sequence problems.
AK021653 mRNA. Translation: BAB13865.1. Sequence problems.
AK024095 mRNA. Translation: BAB14824.1. Sequence problems.
AK027725 mRNA. Translation: BAB55324.1. Sequence problems.
AK297828 mRNA. Translation: BAG60164.1.
AC007193 Genomic DNA. Translation: AAD22668.1.
CH471126 Genomic DNA. Translation: EAW57410.1.
BC026308 mRNA. Translation: AAH26308.1.
BC080551 mRNA. Translation: AAH80551.1.
CCDSiCCDS12681.2. [Q9Y2N7-1]
CCDS12682.1. [Q9Y2N7-2]
CCDS42580.2. [Q9Y2N7-7]
PIRiJC7771.
RefSeqiNP_071907.4. NM_022462.4. [Q9Y2N7-7]
NP_690007.1. NM_152794.3. [Q9Y2N7-2]
NP_690008.2. NM_152795.3. [Q9Y2N7-1]
UniGeneiHs.420830.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WN5X-ray1.15A/B237-347[»]
ProteinModelPortaliQ9Y2N7.
SMRiQ9Y2N7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122143. 2 interactors.
STRINGi9606.ENSP00000366898.

PTM databases

iPTMnetiQ9Y2N7.
PhosphoSitePlusiQ9Y2N7.

Polymorphism and mutation databases

BioMutaiHIF3A.
DMDMi145558932.

Proteomic databases

PaxDbiQ9Y2N7.
PeptideAtlasiQ9Y2N7.
PRIDEiQ9Y2N7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244303; ENSP00000244303; ENSG00000124440. [Q9Y2N7-7]
ENST00000300862; ENSP00000300862; ENSG00000124440. [Q9Y2N7-2]
ENST00000377670; ENSP00000366898; ENSG00000124440. [Q9Y2N7-1]
GeneIDi64344.
KEGGihsa:64344.
UCSCiuc002peh.3. human. [Q9Y2N7-1]

Organism-specific databases

CTDi64344.
DisGeNETi64344.
GeneCardsiHIF3A.
HGNCiHGNC:15825. HIF3A.
HPAiHPA041141.
MIMi609976. gene.
neXtProtiNX_Q9Y2N7.
OpenTargetsiENSG00000124440.
PharmGKBiPA29285.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3558. Eukaryota.
ENOG410YK57. LUCA.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234306.
HOVERGENiHBG060456.
InParanoidiQ9Y2N7.
KOiK09096.
OMAiPMAGARK.
OrthoDBiEOG091G0486.
PhylomeDBiQ9Y2N7.
TreeFamiTF317772.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124440-MONOMER.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.

Miscellaneous databases

GenomeRNAii64344.
PROiQ9Y2N7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124440.
CleanExiHS_HIF3A.
ExpressionAtlasiQ9Y2N7. baseline and differential.
GenevisibleiQ9Y2N7. HS.

Family and domain databases

InterProiIPR011598. bHLH_dom.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF11413. HIF-1. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIF3A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2N7
Secondary accession number(s): B0M185
, B4DNA2, I6L988, Q58A43, Q66K72, Q8WXA1, Q96K34, Q9H7Z9, Q9HAI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.