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Hypoxia-inducible factor 3-alpha (HIF-3-alpha) (HIF3-alpha) (Basic-helix-loop-helix-PAS protein MOP7) (Class E basic helix-loop-helix protein 17) (bHLHe17) (HIF3-alpha-1) (Inhibitory PAS domain protein) (IPAS) (Member of PAS protein 7) (PAS domain-containing protein 7)

 HIF3A_HUMAN             Reviewed;         669 AA.
Q9Y2N7; B0M185; B4DNA2; I6L988; Q58A43; Q66K72; Q8WXA1; Q96K34;
Q9H7Z9; Q9HAI2;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
12-SEP-2018, entry version 148.
RecName: Full=Hypoxia-inducible factor 3-alpha {ECO:0000303|PubMed:11573933};
Short=HIF-3-alpha {ECO:0000303|PubMed:11573933};
Short=HIF3-alpha;
AltName: Full=Basic-helix-loop-helix-PAS protein MOP7;
AltName: Full=Class E basic helix-loop-helix protein 17;
Short=bHLHe17;
AltName: Full=HIF3-alpha-1;
AltName: Full=Inhibitory PAS domain protein;
Short=IPAS;
AltName: Full=Member of PAS protein 7;
AltName: Full=PAS domain-containing protein 7;
Name=HIF3A {ECO:0000312|HGNC:HGNC:15825};
Synonyms=BHLHE17, MOP7, PASD7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), AND
TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=11573933; DOI=10.1006/bbrc.2001.5659;
Hara S., Hamada J., Kobayashi C., Kondo Y., Imura N.;
"Expression and characterization of hypoxia-inducible factor (HIF)-
3alpha in human kidney: suppression of HIF-mediated gene expression by
HIF-3alpha.";
Biochem. Biophys. Res. Commun. 287:808-813(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Cheng J.Q.;
"Cloning and characterization of human inhibitory PAS domain
protein.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (ISOFORM 4),
INTERACTION WITH HIF1A AND ARNT (ISOFORM 4), INDUCTION (ISOFORM 4),
AND TISSUE SPECIFICITY.
TISSUE=Cerebellum;
PubMed=16126907; DOI=10.1096/fj.05-3788com;
Maynard M.A., Evans A.J., Hosomi T., Hara S., Jewett M.A., Ohh M.;
"Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is
down-regulated in renal cell carcinoma.";
FASEB J. 19:1396-1406(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Kidney;
Hara S., Hosomi T., Mita M., Sakaue M., Kondo Y.;
"HIF-3alpha2, one of splicing variants of human hypoxia-inducible
factor-3alpha, functions as an inhibitor of hypoxia-induced gene
expression and tumor growth.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-626 (ISOFORM 5), NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 1-233 (ISOFORM 6), AND VARIANT ARG-343.
TISSUE=Embryo, Heart, and Ovary;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
ARG-343.
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH VHL (ISOFORM 2), ALTERNATIVE SPLICING, UBIQUITINATION
AT LYS-467 AND LYS-570, HYDROXYLATION AT PRO-492, TISSUE SPECIFICITY,
AND MUTAGENESIS OF LYS-467; PRO-492 AND LYS-570.
PubMed=12538644; DOI=10.1074/jbc.M208681200;
Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S.,
Conaway R.C., Conaway J.W., Ohh M.;
"Multiple splice variants of the human HIF-3 alpha locus are targets
of the von Hippel-Lindau E3 ubiquitin ligase complex.";
J. Biol. Chem. 278:11032-11040(2003).
[10]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16775626; DOI=10.1038/sj.cr.7310072;
Li Q.F., Wang X.R., Yang Y.W., Lin H.;
"Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression
in lung epithelial cells: characterization and comparison with HIF-
1alpha.";
Cell Res. 16:548-558(2006).
[11]
FUNCTION (ISOFORM 4), AND INTERACTION WITH EPAS1 (ISOFORM 4).
PubMed=17998805; DOI=10.4161/cc.6.22.4947;
Maynard M.A., Evans A.J., Shi W., Kim W.Y., Liu F.F., Ohh M.;
"Dominant-negative HIF-3 alpha 4 suppresses VHL-null renal cell
carcinoma progression.";
Cell Cycle 6:2810-2816(2007).
[12]
FUNCTION (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=19694616; DOI=10.1042/BJ20090120;
Tanaka T., Wiesener M., Bernhardt W., Eckardt K.U., Warnecke C.;
"The human HIF (hypoxia-inducible factor)-3alpha gene is a HIF-1
target gene and may modulate hypoxic gene induction.";
Biochem. J. 424:143-151(2009).
[13]
FUNCTION (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY
(ISOFORMS 2; 3 AND 4), AND INDUCTION.
PubMed=20416395; DOI=10.1016/j.biocel.2010.04.008;
Pasanen A., Heikkila M., Rautavuoma K., Hirsila M., Kivirikko K.I.,
Myllyharju J.;
"Hypoxia-inducible factor (HIF)-3alpha is subject to extensive
alternative splicing in human tissues and cancer cells and is
regulated by HIF-1 but not HIF-2.";
Int. J. Biochem. Cell Biol. 42:1189-1200(2010).
[14]
FUNCTION (ISOFORMS 3 AND 5), TISSUE SPECIFICITY, AND INDUCTION
(ISOFORMS 2; 3 AND 5).
PubMed=21069422; DOI=10.1007/s00018-010-0575-4;
Augstein A., Poitz D.M., Braun-Dullaeus R.C., Strasser R.H.,
Schmeisser A.;
"Cell-specific and hypoxia-dependent regulation of human HIF-3alpha:
inhibition of the expression of HIF target genes in vascular cells.";
Cell. Mol. Life Sci. 68:2627-2642(2011).
-!- FUNCTION: 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).
{ECO:0000250|UniProtKB:Q0VBL6, ECO:0000269|PubMed:11573933,
ECO:0000269|PubMed:16126907, ECO:0000269|PubMed:19694616,
ECO:0000269|PubMed:20416395, ECO:0000269|PubMed:21069422}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11573933}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395,
ECO:0000269|PubMed:21069422}.
-!- FUNCTION: 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).
{ECO:0000269|PubMed:16126907, ECO:0000269|PubMed:17998805,
ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:21069422}.
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:Q0VBL6,
ECO:0000269|PubMed:12538644, ECO:0000269|PubMed:16126907,
ECO:0000269|PubMed:17998805}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16775626,
ECO:0000269|PubMed:19694616}. Cytoplasm
{ECO:0000269|PubMed:19694616}. Nucleus speckle
{ECO:0000250|UniProtKB:Q0VBL6}. Mitochondrion
{ECO:0000250|UniProtKB:Q0VBL6}. 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).
{ECO:0000250|UniProtKB:Q0VBL6, ECO:0000250|UniProtKB:Q9JHS2,
ECO:0000269|PubMed:19694616}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=Additional isoforms seem to exist.
{ECO:0000303|PubMed:12538644, ECO:0000303|PubMed:20416395};
Name=1;
IsoId=Q9Y2N7-1; Sequence=Displayed;
Name=2; Synonyms=HIF-3alpha1 {ECO:0000303|PubMed:12538644};
IsoId=Q9Y2N7-2; Sequence=VSP_024520;
Name=3; Synonyms=HIF-3alpha2 {ECO:0000303|PubMed:12538644};
IsoId=Q9Y2N7-3; Sequence=VSP_024526;
Name=4; Synonyms=HIF-3alpha4 {ECO:0000303|PubMed:12538644};
IsoId=Q9Y2N7-4; Sequence=VSP_024523, VSP_024525;
Name=5; Synonyms=HIF-3alpha3 {ECO:0000303|PubMed:12538644};
IsoId=Q9Y2N7-5; Sequence=VSP_024519;
Note=Incomplete sequence. No experimental confirmation
available.;
Name=6; Synonyms=HIF-3alpha6 {ECO:0000303|PubMed:12538644};
IsoId=Q9Y2N7-6; Sequence=VSP_024518, VSP_024521;
Note=Incomplete sequence. No experimental confirmation
available.;
Name=7;
IsoId=Q9Y2N7-7; Sequence=VSP_043429;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: 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).
{ECO:0000269|PubMed:11573933, ECO:0000269|PubMed:12538644,
ECO:0000269|PubMed:16126907, ECO:0000269|PubMed:16775626,
ECO:0000269|PubMed:19694616, ECO:0000269|PubMed:20416395,
ECO:0000269|PubMed:21069422}.
-!- INDUCTION: 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). {ECO:0000269|PubMed:16126907,
ECO:0000269|PubMed:16775626, ECO:0000269|PubMed:19694616,
ECO:0000269|PubMed:20416395, ECO:0000269|PubMed:21069422}.
-!- PTM: 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.
{ECO:0000269|PubMed:12538644}.
-!- PTM: Ubiquitinated; ubiquitination occurs in a VHL- and oxygen-
dependent pathway and subsequently targeted for proteasomal
degradation. {ECO:0000269|PubMed:12538644}.
-!- SEQUENCE CAUTION:
Sequence=AAL69947.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAB13865.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing site.; Evidence={ECO:0000305};
Sequence=BAB14824.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
Sequence=BAB55324.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAD93355.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAG07185.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Hypoxia inducible factor entry;
URL="https://en.wikipedia.org/wiki/Hypoxia_inducible_factor";
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EMBL; AB054067; BAB69689.1; -; mRNA.
EMBL; AF463492; AAL69947.1; ALT_SEQ; mRNA.
EMBL; AB118749; BAD93355.1; ALT_SEQ; mRNA.
EMBL; AB295039; BAG07185.1; ALT_SEQ; mRNA.
EMBL; AK021653; BAB13865.1; ALT_SEQ; mRNA.
EMBL; AK024095; BAB14824.1; ALT_SEQ; mRNA.
EMBL; AK027725; BAB55324.1; ALT_SEQ; mRNA.
EMBL; AK297828; BAG60164.1; -; mRNA.
EMBL; AC007193; AAD22668.1; -; Genomic_DNA.
EMBL; CH471126; EAW57410.1; -; Genomic_DNA.
EMBL; BC026308; AAH26308.1; -; mRNA.
EMBL; BC080551; AAH80551.1; -; mRNA.
CCDS; CCDS12681.2; -. [Q9Y2N7-1]
CCDS; CCDS12682.1; -. [Q9Y2N7-2]
CCDS; CCDS42580.2; -. [Q9Y2N7-7]
PIR; JC7771; JC7771.
RefSeq; NP_071907.4; NM_022462.4. [Q9Y2N7-7]
RefSeq; NP_690007.1; NM_152794.3. [Q9Y2N7-2]
RefSeq; NP_690008.2; NM_152795.3. [Q9Y2N7-1]
UniGene; Hs.420830; -.
PDB; 4WN5; X-ray; 1.15 A; A/B=237-347.
PDBsum; 4WN5; -.
ProteinModelPortal; Q9Y2N7; -.
SMR; Q9Y2N7; -.
BioGrid; 122143; 3.
ELM; Q9Y2N7; -.
STRING; 9606.ENSP00000366898; -.
iPTMnet; Q9Y2N7; -.
PhosphoSitePlus; Q9Y2N7; -.
BioMuta; HIF3A; -.
DMDM; 145558932; -.
PaxDb; Q9Y2N7; -.
PeptideAtlas; Q9Y2N7; -.
PRIDE; Q9Y2N7; -.
ProteomicsDB; 85845; -.
ProteomicsDB; 85846; -. [Q9Y2N7-2]
ProteomicsDB; 85847; -. [Q9Y2N7-3]
ProteomicsDB; 85848; -. [Q9Y2N7-4]
ProteomicsDB; 85849; -. [Q9Y2N7-5]
ProteomicsDB; 85850; -. [Q9Y2N7-6]
ProteomicsDB; 85851; -. [Q9Y2N7-7]
Ensembl; ENST00000244303; ENSP00000244303; ENSG00000124440. [Q9Y2N7-7]
Ensembl; ENST00000300862; ENSP00000300862; ENSG00000124440. [Q9Y2N7-2]
Ensembl; ENST00000377670; ENSP00000366898; ENSG00000124440. [Q9Y2N7-1]
GeneID; 64344; -.
KEGG; hsa:64344; -.
UCSC; uc002peh.3; human. [Q9Y2N7-1]
CTD; 64344; -.
DisGeNET; 64344; -.
EuPathDB; HostDB:ENSG00000124440.15; -.
GeneCards; HIF3A; -.
HGNC; HGNC:15825; HIF3A.
HPA; HPA041141; -.
MIM; 609976; gene.
neXtProt; NX_Q9Y2N7; -.
OpenTargets; ENSG00000124440; -.
PharmGKB; PA29285; -.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
GeneTree; ENSGT00760000118788; -.
HOGENOM; HOG000234306; -.
HOVERGEN; HBG060456; -.
InParanoid; Q9Y2N7; -.
KO; K09096; -.
OMA; PMAGARK; -.
OrthoDB; EOG091G0486; -.
PhylomeDB; Q9Y2N7; -.
TreeFam; TF317772; -.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-8951664; Neddylation.
GenomeRNAi; 64344; -.
PRO; PR:Q9Y2N7; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000124440; Expressed in 180 organ(s), highest expression level in esophagus.
CleanEx; HS_HIF3A; -.
ExpressionAtlas; Q9Y2N7; baseline and differential.
Genevisible; Q9Y2N7; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR021537; HIF_alpha_subunit.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR013655; PAS_fold_3.
Pfam; PF11413; HIF-1; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08447; PAS_3; 1.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Apoptosis;
Complete proteome; Cytoplasm; Developmental protein; Hydroxylation;
Isopeptide bond; Mitochondrion; Nucleus; Polymorphism;
Reference proteome; Repeat; Repressor; Stress response; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation.
CHAIN 1 669 Hypoxia-inducible factor 3-alpha.
/FTId=PRO_0000284414.
DOMAIN 14 67 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 82 154 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 227 297 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 77 100 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q0VBL6}.
REGION 230 274 Nuclear export signal.
{ECO:0000250|UniProtKB:Q0VBL6}.
REGION 452 581 ODD.
REGION 454 506 NTAD.
MOTIF 414 418 LRRLL.
MOTIF 490 497 LAPYISMD.
MOD_RES 492 492 4-hydroxyproline.
{ECO:0000269|PubMed:12538644}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12538644}.
CROSSLNK 570 570 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12538644}.
VAR_SEQ 1 120 MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTL
PFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGG
EPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLS ->
MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPS
ATCACTASAP (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043429.
VAR_SEQ 1 86 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_024518.
VAR_SEQ 1 56 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024519.
VAR_SEQ 1 8 MALGLQRA -> MDWQDH (in isoform 2).
{ECO:0000303|PubMed:11573933}.
/FTId=VSP_024520.
VAR_SEQ 87 137 ACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGH
SIFDFIHPCD -> MRPAAGAARRPRCCTSWLTRCPSPAAS
APTWTRPLSCASPSATCACTASAP (in isoform 6).
{ECO:0000305}.
/FTId=VSP_024521.
VAR_SEQ 293 363 LLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSES
IVCVHFLISQVEETGVVLSLEQTEQHSRRP -> CMYPISP
GAKPAATWPPADTRTPQLPIPQDALPPHLNTSSLLPKPQGT
VSFLAPSYPVPRSFSPHLPPWWP (in isoform 4).
{ECO:0000303|PubMed:16126907}.
/FTId=VSP_024523.
VAR_SEQ 364 669 Missing (in isoform 4).
{ECO:0000303|PubMed:16126907}.
/FTId=VSP_024525.
VAR_SEQ 611 669 SFLLTGGPAPGSLQDPSTPLLNLNEPLGLGPSLLSPYSDED
TTQPGGPFQPRAGSAQAD -> VCWGINGILWPSLPSWLKP
TVL (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2, ECO:0000303|Ref.4}.
/FTId=VSP_024526.
VARIANT 343 343 Q -> R (in dbSNP:rs3764609).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031731.
VARIANT 463 463 F -> L (in dbSNP:rs7253301).
/FTId=VAR_031732.
MUTAGEN 467 467 K->R: No loss of ubiquitination. Reduced
ubiquitination; when associated with R-
570. {ECO:0000269|PubMed:12538644}.
MUTAGEN 492 492 P->A: Reduced hydroxylation activity.
Reduced ubiquitination.
{ECO:0000269|PubMed:12538644}.
MUTAGEN 570 570 K->R: No loss of ubiquitination. Reduced
ubiquitination; when associated with R-
467. {ECO:0000269|PubMed:12538644}.
CONFLICT 202 202 A -> V (in Ref. 5; BAB55324).
{ECO:0000305}.
CONFLICT 497 497 D -> G (in Ref. 5; BAB55324).
{ECO:0000305}.
STRAND 241 245 {ECO:0000244|PDB:4WN5}.
STRAND 250 254 {ECO:0000244|PDB:4WN5}.
HELIX 258 262 {ECO:0000244|PDB:4WN5}.
HELIX 266 269 {ECO:0000244|PDB:4WN5}.
HELIX 274 277 {ECO:0000244|PDB:4WN5}.
TURN 280 282 {ECO:0000244|PDB:4WN5}.
HELIX 283 296 {ECO:0000244|PDB:4WN5}.
STRAND 297 300 {ECO:0000244|PDB:4WN5}.
STRAND 304 307 {ECO:0000244|PDB:4WN5}.
STRAND 313 323 {ECO:0000244|PDB:4WN5}.
HELIX 329 331 {ECO:0000244|PDB:4WN5}.
STRAND 333 342 {ECO:0000244|PDB:4WN5}.
SEQUENCE 669 AA; 72433 MW; 81C4C84517000DE2 CRC64;
MALGLQRARS TTELRKEKSR DAARSRRSQE TEVLYQLAHT LPFARGVSAH LDKASIMRLT
ISYLRMHRLC AAGEWNQVGA GGEPLDACYL KALEGFVMVL TAEGDMAYLS ENVSKHLGLS
QLELIGHSIF DFIHPCDQEE LQDALTPQQT LSRRKVEAPT ERCFSLRMKS TLTSRGRTLN
LKAATWKVLN CSGHMRAYKP PAQTSPAGSP DSEPPLQCLV LICEAIPHPG SLEPPLGRGA
FLSRHSLDMK FTYCDDRIAE VAGYSPDDLI GCSAYEYIHA LDSDAVSKSI HTLLSKGQAV
TGQYRFLARS GGYLWTQTQA TVVSGGRGPQ SESIVCVHFL ISQVEETGVV LSLEQTEQHS
RRPIQRGAPS QKDTPNPGDS LDTPGPRILA FLHPPSLSEA ALAADPRRFC SPDLRRLLGP
ILDGASVAAT PSTPLATRHP QSPLSADLPD ELPVGTENVH RLFTSGKDTE AVETDLDIAQ
DADALDLEML APYISMDDDF QLNASEQLPR AYHRPLGAVP RPRARSFHGL SPPALEPSLL
PRWGSDPRLS CSSPSRGDPS ASSPMAGARK RTLAQSSEDE DEGVELLGVR PPKRSPSPEH
ENFLLFPLSL SFLLTGGPAP GSLQDPSTPL LNLNEPLGLG PSLLSPYSDE DTTQPGGPFQ
PRAGSAQAD


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