HSF4

HSF4
Identifiers
Aliases	HSF4 , CTM, CTRCT5, heat shock transcription factor 4
External IDs	OMIM: 602438 MGI: 1347058 HomoloGene: 100128 GeneCards: HSF4
Gene location (Human) Chr. Chromosome 16 (human) [1] Band 16q22.1 Start 67,164,681 bp [1] End 67,169,945 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 D3 Start 105,269,801 bp [2] End 105,275,845 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • sequence-specific DNA binding • DNA binding • GO:0001106 transcription corepressor activity • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • protein phosphatase binding • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding Cellular component • nucleus • nuclear speck Biological process • eye development • regulation of transcription, DNA-templated • cell development • histone H3-K9 demethylation • negative regulation of transcription by RNA polymerase II • transcription, DNA-templated • protein homotrimerization • positive regulation of cell differentiation • positive regulation of cell population proliferation • camera-type eye development • negative regulation of transcription, DNA-templated • protein homooligomerization • positive regulation of transcription by RNA polymerase II • visual perception • cellular response to heat • positive regulation of transcription from RNA polymerase II promoter in response to heat stress Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3299	26386
Ensembl	ENSG00000102878	ENSMUSG00000033249
UniProt	Q9ULV5	Q9R0L1
RefSeq (mRNA)	NM_001538 NM_001040667 NM_001374674 NM_001374675	NM_001256042 NM_001256044 NM_011939
RefSeq (protein)	NP_001035757 NP_001529 NP_001361603 NP_001361604	NP_001242971 NP_001242973 NP_036069
Location (UCSC)	Chr 16: 67.16 – 67.17 Mb	Chr 8: 105.27 – 105.28 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Heat shock factor protein 4 is a protein that in humans is encoded by the HSF4 gene. ^{[5] [6] [7] [8]}

Heat-shock transcription factors (HSFs) activate heat-shock response genes under conditions of heat or other stresses. HSF4 lacks the carboxyl-terminal hydrophobic repeat which is shared among all vertebrate HSFs and has been suggested to be involved in the negative regulation of DNA binding activity. Two alternatively spliced transcripts encoding distinct isoforms and possessing different transcriptional activity have been described. ^[8]

See also

• Heat shock factor

References

1. GRCh38: Ensembl release 89: ENSG00000102878 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033249 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto RI, Nagata K (Jan 1997). "HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator". Mol Cell Biol. 17 (1): 469–81. doi:10.1128/mcb.17.1.469. PMC   231772 . PMID   8972228.
6. Tanabe M, Sasai N, Nagata K, Liu XD, Liu PC, Thiele DJ, Nakai A (Nov 1999). "The mammalian HSF4 gene generates both an activator and a repressor of heat shock genes by alternative splicing". J Biol Chem. 274 (39): 27845–56. doi: 10.1074/jbc.274.39.27845 . PMID   10488131.
7. Bu L, Jin Y, Shi Y, Chu R, Ban A, Eiberg H, Andres L, Jiang H, Zheng G, Qian M, Cui B, Xia Y, Liu J, Hu L, Zhao G, Hayden MR, Kong X (Jun 2002). "Mutant DNA-binding domain of HSF4 is associated with autosomal dominant lamellar and Marner cataract". Nat Genet. 31 (3): 276–8. doi:10.1038/ng921. PMID   12089525. S2CID   27368940.
8. "Entrez Gene: HSF4 heat shock transcription factor 4".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi: 10.1073/pnas.97.7.3491 . PMC   16267 . PMID   10737800.
• Smaoui N, Beltaief O, BenHamed S, et al. (2004). "A homozygous splice mutation in the HSF4 gene is associated with an autosomal recessive congenital cataract". Invest. Ophthalmol. Vis. Sci. 45 (8): 2716–21. doi: 10.1167/iovs.03-1370 . PMID   15277496.
• Somasundaram T, Bhat SP (2004). "Developmentally dictated expression of heat shock factors: exclusive expression of HSF4 in the postnatal lens and its specific interaction with alphaB-crystallin heat shock promoter". J. Biol. Chem. 279 (43): 44497–503. doi: 10.1074/jbc.M405813200 . PMID   15308659.
• Forshew T, Johnson CA, Khaliq S, et al. (2005). "Locus heterogeneity in autosomal recessive congenital cataracts: linkage to 9q and germline HSF4 mutations". Hum. Genet. 117 (5): 452–9. doi:10.1007/s00439-005-1309-9. PMID   15959809. S2CID   21135251.
• Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID   16341674. S2CID   69278.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (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.
• Tu N, Hu Y, Mivechi NF (2006). "Heat shock transcription factor (Hsf)-4b recruits Brg1 during the G1 phase of the cell cycle and regulates the expression of heat shock proteins". J. Cell. Biochem. 98 (6): 1528–42. doi:10.1002/jcb.20865. PMID   16552721. S2CID   36553127.
• Ke T, Wang QK, Ji B, et al. (2006). "Novel HSF4 mutation causes congenital total white cataract in a Chinese family". Am. J. Ophthalmol. 142 (2): 298–303. doi:10.1016/j.ajo.2006.03.056. PMID   16876512.

External links

• HSF4+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.