HSF4: Difference between revisions

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Latest revision as of 14:05, 31 August 2017

Heat shock factor protein 4 is a protein that in humans is encoded by the HSF4 gene.^[1]^[2]^[3]^[4]

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.^[4]

References

↑ 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. PMC 231772. PMID 8972228.
↑ 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.
↑ 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.
↑ ^4.0 ^4.1 "Entrez Gene: HSF4 heat shock transcription factor 4".

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. 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.
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.
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.
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.

This article on a gene on human chromosome 16 is a stub. You can help Wikipedia by expanding it.

[pmid8972228-1] 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. PMC 231772. PMID 8972228.

[pmid10488131-2] 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.

[pmid12089525-3] 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.

[entrez-4] 4.0 ^4.1 "Entrez Gene: HSF4 heat shock transcription factor 4".

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
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+'''Heat shock factor protein 4''' is a [[protein]] that in humans is encoded by the ''HSF4'' [[gene]].<ref name="pmid8972228">{{cite journal |vauthors=Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto RI, Nagata K | title = HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator | journal = Mol Cell Biol | volume = 17 | issue = 1 | pages = 469–81 |date=Jan 1997 | pmid = 8972228 | pmc = 231772 | doi =  }}</ref><ref name="pmid10488131">{{cite journal |vauthors=Tanabe M, Sasai N, Nagata K, Liu XD, Liu PC, Thiele DJ, Nakai A | title = The mammalian HSF4 gene generates both an activator and a repressor of heat shock genes by alternative splicing | journal = J Biol Chem | volume = 274 | issue = 39 | pages = 27845–56 |date=Nov 1999 | pmid = 10488131 | pmc =  | doi =10.1074/jbc.274.39.27845  }}</ref><ref name="pmid12089525">{{cite journal |vauthors=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 | title = Mutant DNA-binding domain of HSF4 is associated with autosomal dominant lamellar and Marner cataract | journal = Nat Genet | volume = 31 | issue = 3 | pages = 276–8 |date=Jun 2002 | pmid = 12089525 | pmc =  | doi = 10.1038/ng921 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSF4 heat shock transcription factor 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3299| accessdate = }}</ref>
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-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Heat shock transcription factor 4
- | HGNCid = 5227
- | Symbol = HSF4
- | AltSymbols =; CTM
- | OMIM = 602438
- | ECnumber =
- | Homologene = 31042
- | MGIid = 1347058
- | GeneAtlas_image1 = PBB_GE_HSF4_210977_s_at_tn.png
-  | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
-  | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0045597 |text = positive regulation of cell differentiation}} {{GNF_GO|id=GO:0048468 |text = cell development}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 3299
-    | Hs_Ensembl = ENSG00000102878
-    | Hs_RefseqProtein = NP_001035757
-    | Hs_RefseqmRNA = NM_001040667
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 16
-    | Hs_GenLoc_start = 65756216
-    | Hs_GenLoc_end = 65761225
-    | Hs_Uniprot = Q9ULV5
-    | Mm_EntrezGene = 26386
-    | Mm_Ensembl =
-    | Mm_RefseqmRNA = NM_011939
-    | Mm_RefseqProtein = NP_036069
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr =
-    | Mm_GenLoc_start =
-    | Mm_GenLoc_end =
-    | Mm_Uniprot =
-  }}
-}}
-'''Heat shock transcription factor 4''', also known as '''HSF4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSF4 heat shock transcription factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3299| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: HSF4 heat shock transcription factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3299| accessdate = }}</ref>
+| summary_text = 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.<ref name="entrez" />
 }}
@@ Line 58: / Line 12: @@
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
@@ Line 64: / Line 18: @@
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
+*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
-*{{cite journal  | author=Nakai A, Tanabe M, Kawazoe Y, ''et al.'' |title=HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator. |journal=Mol. Cell. Biol. |volume=17 |issue= 1 |pages= 469-81 |year= 1997 |pmid= 8972228 |doi=  }}
+*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
+*{{cite journal   |vauthors=Dias Neto E, Correa RG, Verjovski-Almeida S, etal |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=10.1073/pnas.97.7.3491  | pmc=16267  }}
-*{{cite journal  | author=Tanabe M, Sasai N, Nagata K, ''et al.'' |title=The mammalian HSF4 gene generates both an activator and a repressor of heat shock genes by alternative splicing. |journal=J. Biol. Chem. |volume=274 |issue= 39 |pages= 27845-56 |year= 1999 |pmid= 10488131 |doi=  }}
+*{{cite journal   |vauthors=Smaoui N, Beltaief O, BenHamed S, etal |title=A homozygous splice mutation in the HSF4 gene is associated with an autosomal recessive congenital cataract. |journal=Invest. Ophthalmol. Vis. Sci. |volume=45 |issue= 8 |pages= 2716–21 |year= 2004 |pmid= 15277496 |doi= 10.1167/iovs.03-1370 }}
-*{{cite journal  | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
+*{{cite journal  |vauthors=Somasundaram T, Bhat SP |title=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. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44497–503 |year= 2004 |pmid= 15308659 |doi= 10.1074/jbc.M405813200 }}
-*{{cite journal  | author=Bu L, Jin Y, Shi Y, ''et al.'' |title=Mutant DNA-binding domain of HSF4 is associated with autosomal dominant lamellar and Marner cataract. |journal=Nat. Genet. |volume=31 |issue= 3 |pages= 276-8 |year= 2002 |pmid= 12089525 |doi= 10.1038/ng921 }}
+*{{cite journal   |vauthors=Forshew T, Johnson CA, Khaliq S, etal |title=Locus heterogeneity in autosomal recessive congenital cataracts: linkage to 9q and germline HSF4 mutations. |journal=Hum. Genet. |volume=117 |issue= 5 |pages= 452–9 |year= 2005 |pmid= 15959809 |doi= 10.1007/s00439-005-1309-9 }}
-*{{cite journal  | author=Smaoui N, Beltaief O, BenHamed S, ''et al.'' |title=A homozygous splice mutation in the HSF4 gene is associated with an autosomal recessive congenital cataract. |journal=Invest. Ophthalmol. Vis. Sci. |volume=45 |issue= 8 |pages= 2716-21 |year= 2004 |pmid= 15277496 |doi= 10.1167/iovs.03-1370 }}
+*{{cite journal   |vauthors=Oh JH, Yang JO, Hahn Y, etal |title=Transcriptome analysis of human gastric cancer. |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942–54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 }}
-*{{cite journal  | author=Somasundaram T, Bhat SP |title=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. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44497-503 |year= 2004 |pmid= 15308659 |doi= 10.1074/jbc.M405813200 }}
+*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |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  | pmc=1356129 }}
-*{{cite journal  | author=Forshew T, Johnson CA, Khaliq S, ''et al.'' |title=Locus heterogeneity in autosomal recessive congenital cataracts: linkage to 9q and germline HSF4 mutations. |journal=Hum. Genet. |volume=117 |issue= 5 |pages= 452-9 |year= 2005 |pmid= 15959809 |doi= 10.1007/s00439-005-1309-9 }}
+*{{cite journal  |vauthors=Tu N, Hu Y, Mivechi NF |title=Heat shock transcription factor (Hsf)-4b recruits Brg1 during the G1 phase of the cell cycle and regulates the expression of heat shock proteins. |journal=J. Cell. Biochem. |volume=98 |issue= 6 |pages= 1528–42 |year= 2006 |pmid= 16552721 |doi= 10.1002/jcb.20865 }}
-*{{cite journal  | author=Oh JH, Yang JO, Hahn Y, ''et al.'' |title=Transcriptome analysis of human gastric cancer. |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942-54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 }}
+*{{cite journal   |vauthors=Ke T, Wang QK, Ji B, etal |title=Novel HSF4 mutation causes congenital total white cataract in a Chinese family. |journal=Am. J. Ophthalmol. |volume=142 |issue= 2 |pages= 298–303 |year= 2006 |pmid= 16876512 |doi= 10.1016/j.ajo.2006.03.056 }}
-*{{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=Tu N, Hu Y, Mivechi NF |title=Heat shock transcription factor (Hsf)-4b recruits Brg1 during the G1 phase of the cell cycle and regulates the expression of heat shock proteins. |journal=J. Cell. Biochem. |volume=98 |issue= 6 |pages= 1528-42 |year= 2006 |pmid= 16552721 |doi= 10.1002/jcb.20865 }}
-*{{cite journal  | author=Ke T, Wang QK, Ji B, ''et al.'' |title=Novel HSF4 mutation causes congenital total white cataract in a Chinese family. |journal=Am. J. Ophthalmol. |volume=142 |issue= 2 |pages= 298-303 |year= 2006 |pmid= 16876512 |doi= 10.1016/j.ajo.2006.03.056 }}
 }}
 {{refend}}
@@ Line 83: / Line 34: @@
 * {{MeshName|HSF4+protein,+human}}
+{{NLM content}}
+{{Transcription factors|g3}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
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+| update_protein_box = yes
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-{{protein-stub}}
-{{NLM content}}
-{{Transcription factors}}
 [[Category:Transcription factors]]
-{{WikiDoc Sources}}
+{{gene-16-stub}}

HSF4: Difference between revisions

Latest revision as of 14:05, 31 August 2017

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References

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