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HSF2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5D8K, 5D8L
Identifiers
Aliases	HSF2, HSF 2, HSTF 2, heat shock transcription factor 2
External IDs	OMIM: 140581; MGI: 96239; HomoloGene: 37931; GeneCards: HSF2; OMA:HSF2 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6q22.31 Start 122,399,551 bp End 122,433,119 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 B4 Start 57,362,481 bp End 57,389,231 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle Skeletal muscle tissue of biceps brachii muscle of leg gastrocnemius muscle muscle of thigh ganglionic eminence gonad Skeletal muscle tissue of rectus abdominis Achilles tendon bronchial epithelial cell Top expressed in spermatid genital tubercle tail of embryo ventricular zone muscle of thigh neural layer of retina morula spermatocyte embryo superior frontal gyrus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding DNA-binding transcription factor activity RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding DNA binding sequence-specific DNA binding protein homodimerization activity DNA-binding transcription activator activity, RNA polymerase II-specific transcription coactivator activity RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component nucleus cytoplasm nucleoplasm Biological process regulation of transcription, DNA-templated positive regulation of transcription by RNA polymerase II transcription by RNA polymerase II spermatogenesis regulation of transcription by RNA polymerase II transcription, DNA-templated 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 3298 15500 Ensembl ENSG00000025156 ENSMUSG00000019878 UniProt Q03933 Q9BS48 P38533 RefSeq (mRNA) NM_004506 NM_001135564 NM_001243094 NM_008297 RefSeq (protein) NP_001129036 NP_001230023 NP_004497 NP_001230023.1 NP_032323 Location (UCSC) Chr 6: 122.4 – 122.43 Mb Chr 10: 57.36 – 57.39 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Heat shock factor protein 2 is a protein that in humans is encoded by the HSF2 gene.

Function

HSF2, as well as the related gene HSF1, encodes a protein that binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stresses. Although the names HSF1 and HSF2 were chosen for historical reasons, these peptides should be referred to as heat-shock transcription factors.

Interactions

HSF2 has been shown to interact with Nucleoporin 62 and HSF1.

See also

• Heat shock factor

References

1. ^ GRCh38: Ensembl release 89: ENSG00000025156 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000019878 – 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. Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (Sep 1991). "Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans". Proc Natl Acad Sci U S A. 88 (16): 6911–5. Bibcode:1991PNAS...88.6911S. doi:10.1073/pnas.88.16.6911. PMC 52203. PMID 1871106.
6. ^ "Entrez Gene: HSF2 heat shock transcription factor 2".
7. Yoshima T, Yura T, Yanagi H (Nov 1997). "The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62". Biochem. Biophys. Res. Commun. 240 (1): 228–33. doi:10.1006/bbrc.1997.7662. PMID 9367915.
8. He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, Brown SA, Kingston RE, Calderwood SK (Sep 2003). "Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress". J. Biol. Chem. 278 (37): 35465–75. doi:10.1074/jbc.M304663200. PMID 12813038.

Further reading

• Walsh D, Li Z, Wu Y, Nagata K (1997). "Heat shock and the role of the HSPs during neural plate induction in early mammalian CNS and brain development". Cell. Mol. Life Sci. 53 (2): 198–211. doi:10.1007/PL00000592. PMC 11147247. PMID 9118008. S2CID 32425345.
• Sarge KD, Zimarino V, Holm K, Wu C, Morimoto RI (1991). "Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability". Genes Dev. 5 (10): 1902–11. doi:10.1101/gad.5.10.1902. PMID 1717345.
• 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.
• Sheldon LA, Kingston RE (1993). "Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2". Genes Dev. 7 (8): 1549–58. doi:10.1101/gad.7.8.1549. PMID 8339932.
• Yoshima T, Yura T, Yanagi H (1997). "The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62". Biochem. Biophys. Res. Commun. 240 (1): 228–33. doi:10.1006/bbrc.1997.7662. PMID 9367915.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (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.
• Yoshima T, Yura T, Yanagi H (1998). "Novel testis-specific protein that interacts with heat shock factor 2". Gene. 214 (1–2): 139–46. doi:10.1016/S0378-1119(98)00208-X. PMID 9651507.
• Hong Y, Sarge KD (1999). "Regulation of protein phosphatase 2A activity by heat shock transcription factor 2". J. Biol. Chem. 274 (19): 12967–70. doi:10.1074/jbc.274.19.12967. PMID 10224043.
• Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD (2001). "Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor". J. Biol. Chem. 276 (21): 18513–8. doi:10.1074/jbc.M008066200. PMID 11278381.
• Nykänen P, Alastalo TP, Ahlskog J, Horelli-Kuitunen N, Pirkkala L, Sistonen L (2002). "Genomic organization and promoter analysis of the human heat shock factor 2 gene". Cell Stress & Chaperones. 6 (4): 377–85. doi:10.1379/1466-1268(2001)006<0377:goapao>2.0.co;2 (inactive 2024-11-02). PMC 434421. PMID 11795475.{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link)
• He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, Brown SA, Kingston RE, Calderwood SK (2003). "Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress". J. Biol. Chem. 278 (37): 35465–75. doi:10.1074/jbc.M304663200. PMID 12813038.
• Alastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L (2004). "Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70". J. Cell Sci. 116 (Pt 17): 3557–70. doi:10.1242/jcs.00671. PMID 12865437.
• Roccisana JL, Kawanabe N, Kajiya H, Koide M, Roodman GD, Reddy SV (2004). "Functional role for heat shock factors in the transcriptional regulation of human RANK ligand gene expression in stromal/osteoblast cells". J. Biol. Chem. 279 (11): 10500–7. doi:10.1074/jbc.M303727200. PMID 14699143.
• Xing H, Wilkerson DC, Mayhew CN, Lubert EJ, Skaggs HS, Goodson ML, Hong Y, Park-Sarge OK, Sarge KD (2005). "Mechanism of hsp70i gene bookmarking". Science. 307 (5708): 421–3. Bibcode:2005Sci...307..421X. doi:10.1126/science.1106478. PMID 15662014. S2CID 37132180.
• Anckar J, Hietakangas V, Denessiouk K, Thiele DJ, Johnson MS, Sistonen L (2006). "Inhibition of DNA binding by differential sumoylation of heat shock factors". Mol. Cell. Biol. 26 (3): 955–64. doi:10.1128/MCB.26.3.955-964.2006. PMC 1347039. PMID 16428449.

External links

• HSF2+protein,+human at the U.S. 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.

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