HSF2

Heat shock transcription factor 2
Identifiers
Symbols	HSF2; HSF 2; HSTF 2
External IDs	OMIM: 140581 MGI: 96239 HomoloGene: 37931 GeneCards: HSF2 Gene
Gene Ontology Molecular function • RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding • sequence-specific DNA binding transcription factor activity • transcription coactivator activity • protein homodimerization activity Cellular component • nucleus • nucleolus • cytoplasm Biological process • transcription from RNA polymerase II promoter • response to stress • spermatogenesis • positive regulation of transcription from RNA polymerase II promoter Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3298	15500
Ensembl	ENSG00000025156	ENSMUSG00000019878
UniProt	Q03933	P38533
RefSeq (mRNA)	NM_001135564	NM_008297
RefSeq (protein)	NP_001129036	NP_032323
Location (UCSC)	Chr 6: 122.72 – 122.75 Mb	Chr 10: 57.49 – 57.51 Mb
PubMed search	[1]	[2]

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

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

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. PMID 9118008. 
• Sarge KD, Zimarino V, Holm K, et al. (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, 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. 
• 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, et al. (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, et al. (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. PMC 434421. PMID 11795475. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• He H, Soncin F, Grammatikakis N, et al. (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, et al. (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. 
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404. 
• Roccisana JL, Kawanabe N, Kajiya H, et al. (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. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. 
• Xing H, Wilkerson DC, Mayhew CN, et al. (2005). "Mechanism of hsp70i gene bookmarking.". Science 307 (5708): 421–3. doi:10.1126/science.1106478. PMID 15662014. 
• Anckar J, Hietakangas V, Denessiouk K, et al. (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 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.