HIF3A: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Hypoxia-inducible factor 3 alpha''' is a [[protein]] that in humans is encoded by the ''HIF3A'' [[gene]].<ref name="pmid11573933">{{cite journal |vauthors=Hara S, Hamada J, Kobayashi C, Kondo Y, Imura N | title = Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha | journal = Biochem Biophys Res Commun | volume = 287 | issue = 4 | pages = 808–13 | date = Sep 2001 | pmid = 11573933 | pmc =  | doi = 10.1006/bbrc.2001.5659 }}</ref><ref name="pmid11734856">{{cite journal |vauthors=Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, Cao Y, Berkenstam A, Poellinger L | title = Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression | journal = Nature | volume = 414 | issue = 6863 | pages = 550–4 | date = Dec 2001 | pmid = 11734856 | pmc = | doi = 10.1038/35107085 }}</ref><ref name="entrez" />
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Hypoxia inducible factor 3, alpha subunit
| HGNCid = 15825
| Symbol = HIF3A
| AltSymbols =; HIF-3A; HIF-3A4; IPAS; MOP7; PASD7
| OMIM = 609976
| ECnumber = 
| Homologene = 9646
| MGIid = 1859778
| GeneAtlas_image1 = PBB_GE_HIF3A_222123_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HIF3A_219319_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64344
    | Hs_Ensembl = ENSG00000124440
    | Hs_RefseqProtein = NP_071907
    | Hs_RefseqmRNA = NM_022462
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 51492154
    | Hs_GenLoc_end = 51538106
    | Hs_Uniprot = 
    | Mm_EntrezGene = 53417
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_989804
    | Mm_RefseqProtein = XP_994898
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Hypoxia inducible factor 3, alpha subunit''', also known as '''HIF3A''', is a human [[gene]].<ref name="entrez" />


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit [[heterodimer]]ic [[transcription factor]]s that regulate many adaptive responses to low oxygen tension ([[Hypoxia (medical)|hypoxia]]). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HIF3A hypoxia inducible factor 3, alpha subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64344| accessdate = }}</ref>
{{PBB_Summary
 
| section_title =
In rats, it plays a negative role in the adaptation to hypoxia, because the inhibition of HIF-3α expression leads to an increase in physical endurance.<ref name="pmid22884965">{{cite journal | vauthors = Drevytska T, Gavenauskas B, Drozdovska S, Nosar V, Dosenko V, Mankovska I | title = HIF-3α mRNA expression changes in different tissues and their role in adaptation to intermittent hypoxia and physical exercise | journal = Pathophysiology | volume = 19 | issue = 3 | pages = 205–14 | year = 2012 | pmid = 22884965 | doi = 10.1016/j.pathophys.2012.06.002  }}</ref>
| summary_text = The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HIF3A hypoxia inducible factor 3, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64344| accessdate = }}</ref>
 
}}
== Clinical significance ==
 
[[DNA methylation]] in the [[intron]]s of HIF3A is associated with [[body mass index|BMI]] an adiposity.<ref>{{cite journal |vauthors=Dick KJ, Nelson CP, Tsaprouni L, Sandling JK, Aïssi D, Wahl S, Meduri E, Morange PE, Gagnon F, Grallert H, Waldenberger M, Peters A, Erdmann J, Hengstenberg C, Cambien F, Goodall AH, Ouwehand WH, Schunkert H, Thompson JR, Spector TD, Gieger C, Trégouët DA, Deloukas P, Samani NJ | title = DNA methylation and body-mass index: a genome-wide analysis. | journal = Lancet | volume = 383 | issue = 9933 | pages = 1990–1998 | year = 2014 | pmid = 24630777 | doi = 10.1016/S0140-6736(13)62674-4 }}</ref>


==See also==
==See also==
Line 59: Line 16:


==References==
==References==
{{reflist|2}}
{{reflist|35em}}
{{Clear}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin|35em}}
*{{cite journal | author=Gu YZ, Moran SM, Hogenesch JB, Wartman L, Bradfield CA. |title=Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha. |journal=Gene Expr. |volume=7 |issue= 3 |pages= 205-13 |year= 1998 |pmid= 9840812}}
*{{cite journal |vauthors=Gu YZ, Moran SM, Hogenesch JB, Wartman L, Bradfield CA | title = Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha. | journal = Gene Expr. | volume = 7 | issue = 3 | pages = 205–13 | year = 1998 | pmid = 9840812 }}
{{PBB_Further_reading
*{{cite journal |vauthors=Makino Y, Kanopka A, Wilson WJ, Tanaka H, Poellinger L | title = Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. | journal = J. Biol. Chem. | volume = 277 | issue = 36 | pages = 32405–8 | year = 2002 | pmid = 12119283 | doi = 10.1074/jbc.C200328200 }}
| citations =
*{{cite journal |vauthors=Maynard MA, Qi H, Chung J, Lee EH, Kondo Y, Hara S, Conaway RC, Conaway JW, Ohh M | title = Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. | journal = J. Biol. Chem. | volume = 278 | issue = 13 | pages = 11032–40 | year = 2003 | pmid = 12538644 | doi = 10.1074/jbc.M208681200 }}
*{{cite journal  | author=Hara S, Hamada J, Kobayashi C, ''et al.'' |title=Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha. |journal=Biochem. Biophys. Res. Commun. |volume=287 |issue= 4 |pages= 808-13 |year= 2001 |pmid= 11573933 |doi= 10.1006/bbrc.2001.5659 }}
*{{cite journal |vauthors=Maynard MA, Evans AJ, Hosomi T, Hara S, Jewett MA, Ohh M | title = Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma. | journal = FASEB J. | volume = 19 | issue = 11 | pages = 1396–406 | year = 2006 | pmid = 16126907 | doi = 10.1096/fj.05-3788com }}
*{{cite journal | author=Makino Y, Cao R, Svensson K, ''et al.'' |title=Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. |journal=Nature |volume=414 |issue= 6863 |pages= 550-4 |year= 2002 |pmid= 11734856 |doi= 10.1038/35107085 }}
*{{cite journal |vauthors=Jang MS, Park JE, Lee JA, Park SG, Myung PK, Lee DH, Park BC, Cho S | title = Binding and regulation of hypoxia-inducible factor-1 by the inhibitory PAS proteins. | journal = Biochem. Biophys. Res. Commun. | volume = 337 | issue = 1 | pages = 209–15 | year = 2005 | pmid = 16182248 | doi = 10.1016/j.bbrc.2005.09.038 }}
*{{cite journal  | author=Makino Y, Kanopka A, Wilson WJ, ''et al.'' |title=Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32405-8 |year= 2002 |pmid= 12119283 |doi= 10.1074/jbc.C200328200 }}
*{{cite journal |vauthors=Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. | journal = Genome Res. | volume = 16 | issue = 1 | pages = 55–65 | year = 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal |vauthors=Li QF, Wang XR, Yang YW, Lin H | title = Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha. | journal = Cell Res. | volume = 16 | issue = 6 | pages = 548–58 | year = 2006 | pmid = 16775626 | doi = 10.1038/sj.cr.7310072 }}
*{{cite journal  | author=Maynard MA, Qi H, Chung J, ''et al.'' |title=Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex. |journal=J. Biol. Chem. |volume=278 |issue= 13 |pages= 11032-40 |year= 2003 |pmid= 12538644 |doi= 10.1074/jbc.M208681200 }}
*{{cite journal |vauthors=Kollers S, Musilova P, Rubes J, Rocha D | title = Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13. | journal = Anim. Genet. | volume = 37 | issue = 6 | pages = 595–6 | year = 2007 | pmid = 17121608 | doi = 10.1111/j.1365-2052.2006.01516.x }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Maynard MA, Evans AJ, Hosomi T, ''et al.'' |title=Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma. |journal=FASEB J. |volume=19 |issue= 11 |pages= 1396-406 |year= 2006 |pmid= 16126907 |doi= 10.1096/fj.05-3788com }}
*{{cite journal | author=Jang MS, Park JE, Lee JA, ''et al.'' |title=Binding and regulation of hypoxia-inducible factor-1 by the inhibitory PAS proteins. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 1 |pages= 209-15 |year= 2005 |pmid= 16182248 |doi= 10.1016/j.bbrc.2005.09.038 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal | author=Li QF, Wang XR, Yang YW, Lin H |title=Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha. |journal=Cell Res. |volume=16 |issue= 6 |pages= 548-58 |year= 2006 |pmid= 16775626 |doi= 10.1038/sj.cr.7310072 }}
*{{cite journal | author=Kollers S, Musilova P, Rubes J, Rocha D |title=Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13. |journal=Anim. Genet. |volume=37 |issue= 6 |pages= 595-6 |year= 2007 |pmid= 17121608 |doi= 10.1111/j.1365-2052.2006.01516.x }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Transcription factors|g1}}
{{Transcription factors}}
 
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}
[[Category:PAS-domain-containing proteins]]
 
 
{{gene-19-stub}}

Latest revision as of 13:36, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Hypoxia-inducible factor 3 alpha is a protein that in humans is encoded by the HIF3A gene.[1][2][3]

Function

The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene.[3]

In rats, it plays a negative role in the adaptation to hypoxia, because the inhibition of HIF-3α expression leads to an increase in physical endurance.[4]

Clinical significance

DNA methylation in the introns of HIF3A is associated with BMI an adiposity.[5]

See also

References

  1. ↑ Hara S, Hamada J, Kobayashi C, Kondo Y, Imura N (Sep 2001). "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 (4): 808–13. doi:10.1006/bbrc.2001.5659. PMID 11573933.
  2. ↑ Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, Cao Y, Berkenstam A, Poellinger L (Dec 2001). "Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression". Nature. 414 (6863): 550–4. doi:10.1038/35107085. PMID 11734856.
  3. ↑ 3.0 3.1 "Entrez Gene: HIF3A hypoxia inducible factor 3, alpha subunit".
  4. ↑ Drevytska T, Gavenauskas B, Drozdovska S, Nosar V, Dosenko V, Mankovska I (2012). "HIF-3α mRNA expression changes in different tissues and their role in adaptation to intermittent hypoxia and physical exercise". Pathophysiology. 19 (3): 205–14. doi:10.1016/j.pathophys.2012.06.002. PMID 22884965.
  5. ↑ Dick KJ, Nelson CP, Tsaprouni L, Sandling JK, Aïssi D, Wahl S, Meduri E, Morange PE, Gagnon F, Grallert H, Waldenberger M, Peters A, Erdmann J, Hengstenberg C, Cambien F, Goodall AH, Ouwehand WH, Schunkert H, Thompson JR, Spector TD, Gieger C, Trégouët DA, Deloukas P, Samani NJ (2014). "DNA methylation and body-mass index: a genome-wide analysis". Lancet. 383 (9933): 1990–1998. doi:10.1016/S0140-6736(13)62674-4. PMID 24630777.

Further reading

  • Gu YZ, Moran SM, Hogenesch JB, Wartman L, Bradfield CA (1998). "Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha". Gene Expr. 7 (3): 205–13. PMID 9840812.
  • Makino Y, Kanopka A, Wilson WJ, Tanaka H, Poellinger L (2002). "Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus". J. Biol. Chem. 277 (36): 32405–8. doi:10.1074/jbc.C200328200. PMID 12119283.
  • Maynard MA, Qi H, Chung J, Lee EH, Kondo Y, Hara S, Conaway RC, Conaway JW, Ohh M (2003). "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 (13): 11032–40. doi:10.1074/jbc.M208681200. PMID 12538644.
  • Maynard MA, Evans AJ, Hosomi T, Hara S, Jewett MA, Ohh M (2006). "Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma". FASEB J. 19 (11): 1396–406. doi:10.1096/fj.05-3788com. PMID 16126907.
  • Jang MS, Park JE, Lee JA, Park SG, Myung PK, Lee DH, Park BC, Cho S (2005). "Binding and regulation of hypoxia-inducible factor-1 by the inhibitory PAS proteins". Biochem. Biophys. Res. Commun. 337 (1): 209–15. doi:10.1016/j.bbrc.2005.09.038. PMID 16182248.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Li QF, Wang XR, Yang YW, Lin H (2006). "Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha". Cell Res. 16 (6): 548–58. doi:10.1038/sj.cr.7310072. PMID 16775626.
  • Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13". Anim. Genet. 37 (6): 595–6. doi:10.1111/j.1365-2052.2006.01516.x. PMID 17121608.


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