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Q9Y2N7

- HIF3A_HUMAN

UniProt

Q9Y2N7 - HIF3A_HUMAN

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Protein

Hypoxia-inducible factor 3-alpha

Gene

HIF3A

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (7)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Involved in adaptive response to hypoxia. Suppresses hypoxia-inducible expression of HIF1A and EPAS1. Binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. The complex HIF3A-ARNT activates the transcription of reporter genes driven by HRE. Isoform 4 has a dominant-negative function of inactivating HIF1A-mediated transcription. Isoform 4 attenuates the binding of HIF1A to hypoxia-responsive elements (HRE), thus inhibiting HRE-driven transcription. Hypoxia induces down-regulation of isoform 4, leading to activation of HIF1A in hypoxia. Conversely, upon restoring normoxia, the expression of isoform 4 increases and thereby secure an inhibition of HIF1A activity. Isoform 4 may be a negative regulator of hypoxia-inducible gene expression in the kidney and may be involved in renal tumorigenesis. Functions as an inhibitor of angiogenesis in the cornea (By similarity).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. sequence-specific DNA binding transcription factor activity Source: Ensembl
  3. signal transducer activity Source: InterPro
  4. transcription coactivator activity Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. cellular response to hypoxia Source: Reactome
  2. negative regulation of nucleic acid-templated transcription Source: GOC
  3. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  5. transcription from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_200812. Transcriptional regulation of pluripotent stem cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia-inducible factor 3-alpha
Short name:
HIF-3-alpha
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:HIF3A
Synonyms:BHLHE17, MOP7, PASD7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:15825. HIF3A.

Subcellular locationi

Nucleus. Cytoplasm
Note: In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi467 – 4671K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-570. 1 Publication
Mutagenesisi492 – 4921P → A: Reduced ubiquitination. 1 Publication
Mutagenesisi570 – 5701K → R: No loss of ubiquitination. Reduced ubiquitination; when associated with R-467. 1 Publication

Organism-specific databases

PharmGKBiPA29285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 669669Hypoxia-inducible factor 3-alphaPRO_0000284414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki467 – 467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei492 – 49214-hydroxyproline1 Publication
Cross-linki570 – 570Glycyl 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 PHD. The hydroxylated proline promotes interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation.1 Publication

Keywords - PTMi

Hydroxylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ9Y2N7.
PRIDEiQ9Y2N7.

PTM databases

PhosphoSiteiQ9Y2N7.

Expressioni

Tissue specificityi

Expressed in kidney. Expressed abundantly in lung epithelial cells. Expression is regulated in an oxygen-dependent manner.1 Publication

Inductioni

Strongly induced by hypoxia (1% O2), both at the level of protein and mRNA due to an increase in protein stability and transcriptional activation.1 Publication

Gene expression databases

BgeeiQ9Y2N7.
CleanExiHS_HIF3A.
ExpressionAtlasiQ9Y2N7. baseline and differential.
GenevestigatoriQ9Y2N7.

Organism-specific databases

HPAiHPA041141.

Interactioni

Subunit structurei

Heterodimerizes with ARNT. Interacts via the oxygen-dependent degradation domain (ODD) with the beta domain of VHL.2 Publications

Protein-protein interaction databases

BioGridi122143. 4 interactions.
STRINGi9606.ENSP00000366898.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2N7.
SMRiQ9Y2N7. Positions 16-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 6754bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini82 – 15473PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini227 – 29771PAS 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni452 – 581130ODDAdd
BLAST
Regioni454 – 50653NTADAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4185LRRLL
Motifi490 – 4978LAPYISMD

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

eggNOGiNOG288942.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234306.
HOVERGENiHBG060456.
InParanoidiQ9Y2N7.
KOiK09096.
OMAiAVGQSIH.
OrthoDBiEOG7JDQX8.
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. Align

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-3alpha1

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-3alpha2

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-3alpha4

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-3alpha3

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     627-669: STPLLNLNEP...QPRAGSAQAD → TELTQFLLSV...APSPLGWFAI

Show »
Length:648
Mass (Da):69,967
Checksum:iF41051A16B629167
GO
Isoform 6 (identifier: Q9Y2N7-6) [UniParc]FASTAAdd to Basket

Also known as: HIF-3alpha6

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     87-137: ACYLKALEGF...SIFDFIHPCD → MRPAAGAARR...ATCACTASAP
     234-323: PPLGRGAFLS...LWTQTQATVV → GFVMVLTAEG...FSPHLPPWWP
     324-669: Missing.

Show »
Length:237
Mass (Da):25,710
Checksum:iA78EC74708561F68
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021A → V in BAB55324. (PubMed:14702039)Curated
Sequence conflicti497 – 4971D → G in BAB55324. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti343 – 3431Q → R.1 Publication
Corresponds to variant rs3764609 [ dbSNP | Ensembl ].		VAR_031731
Natural varianti463 – 4631F → L.
Corresponds to variant rs7253301 [ dbSNP | Ensembl ].		VAR_031732

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120MALGL…HLGLS → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 7. 1 PublicationVSP_043429Add
BLAST
Alternative sequencei1 – 8686Missing in isoform 6. CuratedVSP_024518Add
BLAST
Alternative sequencei1 – 5656Missing in isoform 5. 1 PublicationVSP_024519Add
BLAST
Alternative sequencei1 – 88MALGLQRA → MDWQDH in isoform 2. 1 PublicationVSP_024520
Alternative sequencei87 – 13751ACYLK…IHPCD → MRPAAGAARRPRCCTSWLTR CPSPAASAPTWTRPLSCASP SATCACTASAP in isoform 6. CuratedVSP_024521Add
BLAST
Alternative sequencei234 – 32390PPLGR…QATVV → GFVMVLTAEGDMAYLSENVS NHLGLSQLELIGHSIFDFIH PCDQEELQDALTPHLNTSSL LPKPQGTVSFLAPSYPVPRS FSPHLPPWWP in isoform 6. CuratedVSP_024522Add
BLAST
Alternative sequencei293 – 36371LLSKG…HSRRP → CMYPISPGAKPAATWPPADT RTPQLPIPQDALPPHLNTSS LLPKPQGTVSFLAPSYPVPR SFSPHLPPWWP in isoform 4. 1 PublicationVSP_024523Add
BLAST
Alternative sequencei324 – 669346Missing in isoform 6. CuratedVSP_024524Add
BLAST
Alternative sequencei364 – 669306Missing in isoform 4. 1 PublicationVSP_024525Add
BLAST
Alternative sequencei611 – 66959SFLLT…SAQAD → VCWGINGILWPSLPSWLKPT VL in isoform 3. 3 PublicationsVSP_024526Add
BLAST
Alternative sequencei627 – 66943STPLL…SAQAD → TELTQFLLSVLSFPILDPYP LGCAAPGLHASPFSLPTISV PQNPLHSPPQPSRHALTLTL PHMFGAPGAPSPLGWFAI in isoform 5. 1 PublicationVSP_024527Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB054067 mRNA. Translation: BAB69689.1.
AF463492 mRNA. Translation: AAL69947.1.
AB118749 mRNA. Translation: BAD93355.1.
AB295039 mRNA. Translation: BAG07185.1.
AK021653 mRNA. Translation: BAB13865.1.
AK024095 mRNA. Translation: BAB14824.1.
AK027725 mRNA. Translation: BAB55324.1.
AK297828 mRNA. Translation: BAG60164.1.
AC007193 Genomic DNA. Translation: AAD22668.1.
CH471126 Genomic DNA. Translation: EAW57410.1.
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]
XP_005259211.1. XM_005259154.2. [Q9Y2N7-7]
XP_006723388.1. XM_006723325.1. [Q9Y2N7-7]
UniGeneiHs.420830.

Genome annotation databases

EnsembliENST00000244303; ENSP00000244303; ENSG00000124440. [Q9Y2N7-7]
ENST00000300862; ENSP00000300862; ENSG00000124440. [Q9Y2N7-2]
ENST00000377670; ENSP00000366898; ENSG00000124440. [Q9Y2N7-1]
GeneIDi64344.
KEGGihsa:64344.
UCSCiuc002peg.4. human. [Q9Y2N7-3]
uc002peh.3. human. [Q9Y2N7-1]
uc002pel.3. human. [Q9Y2N7-2]
uc010xxy.2. human. [Q9Y2N7-7]

Polymorphism databases

DMDMi145558932.

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 .
AB118749 mRNA. Translation: BAD93355.1 .
AB295039 mRNA. Translation: BAG07185.1 .
AK021653 mRNA. Translation: BAB13865.1 .
AK024095 mRNA. Translation: BAB14824.1 .
AK027725 mRNA. Translation: BAB55324.1 .
AK297828 mRNA. Translation: BAG60164.1 .
AC007193 Genomic DNA. Translation: AAD22668.1 .
CH471126 Genomic DNA. Translation: EAW57410.1 .
BC080551 mRNA. Translation: AAH80551.1 .
CCDSi CCDS12681.2. [Q9Y2N7-1 ]
CCDS12682.1. [Q9Y2N7-2 ]
CCDS42580.2. [Q9Y2N7-7 ]
PIRi JC7771.
RefSeqi NP_071907.4. NM_022462.4. [Q9Y2N7-7 ]
NP_690007.1. NM_152794.3. [Q9Y2N7-2 ]
NP_690008.2. NM_152795.3. [Q9Y2N7-1 ]
XP_005259211.1. XM_005259154.2. [Q9Y2N7-7 ]
XP_006723388.1. XM_006723325.1. [Q9Y2N7-7 ]
UniGenei Hs.420830.

3D structure databases

ProteinModelPortali Q9Y2N7.
SMRi Q9Y2N7. Positions 16-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122143. 4 interactions.
STRINGi 9606.ENSP00000366898.

PTM databases

PhosphoSitei Q9Y2N7.

Polymorphism databases

DMDMi 145558932.

Proteomic databases

PaxDbi Q9Y2N7.
PRIDEi Q9Y2N7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244303 ; ENSP00000244303 ; ENSG00000124440 . [Q9Y2N7-7 ]
ENST00000300862 ; ENSP00000300862 ; ENSG00000124440 . [Q9Y2N7-2 ]
ENST00000377670 ; ENSP00000366898 ; ENSG00000124440 . [Q9Y2N7-1 ]
GeneIDi 64344.
KEGGi hsa:64344.
UCSCi uc002peg.4. human. [Q9Y2N7-3 ]
uc002peh.3. human. [Q9Y2N7-1 ]
uc002pel.3. human. [Q9Y2N7-2 ]
uc010xxy.2. human. [Q9Y2N7-7 ]

Organism-specific databases

CTDi 64344.
GeneCardsi GC19P046800.
HGNCi HGNC:15825. HIF3A.
HPAi HPA041141.
MIMi 609976. gene.
neXtProti NX_Q9Y2N7.
PharmGKBi PA29285.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288942.
GeneTreei ENSGT00760000118788.
HOGENOMi HOG000234306.
HOVERGENi HBG060456.
InParanoidi Q9Y2N7.
KOi K09096.
OMAi AVGQSIH.
OrthoDBi EOG7JDQX8.
PhylomeDBi Q9Y2N7.
TreeFami TF317772.

Enzyme and pathway databases

Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_200812. Transcriptional regulation of pluripotent stem cells.

Miscellaneous databases

GenomeRNAii 64344.
NextBioi 66283.
PROi Q9Y2N7.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2N7.
CleanExi HS_HIF3A.
ExpressionAtlasi Q9Y2N7. baseline and differential.
Genevestigatori Q9Y2N7.

Family and domain databases

InterProi IPR011598. bHLH_dom.
IPR021537. HIF_alpha_subunit.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view ]
Pfami PF11413. HIF-1. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
TIGRFAMsi TIGR00229. sensory_box. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha."
    Hara S., Hamada J., Kobayashi C., Kondo Y., Imura N.
    Biochem. Biophys. Res. Commun. 287:808-813(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Cloning and characterization of human inhibitory PAS domain protein."
    Cheng J.Q.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma."
    Maynard M.A., Evans A.J., Hosomi T., Hara S., Jewett M.A., Ohh M.
    FASEB J. 19:1396-1406(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH HIF1A AND ARNT.
    Tissue: Cerebellum.
  4. "HIF-3alpha2, one of splicing variants of human hypoxia-inducible factor-3alpha, functions as an inhibitor of hypoxia-induced gene expression and tumor growth."
    Hara S., Hosomi T., Mita M., Sakaue M., Kondo Y.
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Kidney.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 7).
    Tissue: Embryo, Heart and Ovary.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-343.
    Tissue: Pancreas.
  9. "Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex."
    Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S., Conaway R.C., Conaway J.W., Ohh M.
    J. Biol. Chem. 278:11032-11040(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, INTERACTION WITH VHL, UBIQUITINATION AT LYS-467 AND LYS-570, HYDROXYLATION AT PRO-492, MUTAGENESIS OF LYS-467; PRO-492 AND LYS-570.
  10. "Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha."
    Li Q.F., Wang X.R., Yang Y.W., Lin H.
    Cell Res. 16:548-558(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
+Additional computationally mapped references.

Entry informationi

Entry nameiHIF3A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2N7
Secondary accession number(s): B0M185
, B4DNA2, Q58A43, Q66K72, Q8WXA1, Q96K34, Q9H7Z9, Q9HAI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: January 7, 2015
This is version 119 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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