HSF2

From Wikipedia, the free encyclopedia

Heat shock transcription factor 2

Identifiers

HSF2; MGC117376; MGC156196; MGC75048

External IDs

OMIM: 140581 MGI: 96239 HomoloGene: 37931

Gene ontology
Molecular Function:	• transcription factor activity • transcription coactivator activity • sequence-specific DNA binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• transcription • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • protein folding • response to unfolded protein • spermatogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004506 (mRNA)
NP_004497 (protein)

NM_008297 (mRNA)
NP_032323 (protein)

Location

Chr 6: 122.76 - 122.8 Mb

Chr 10: 57.17 - 57.2 Mb

Pubmed search

[1]

[2]

Heat shock transcription factor 2, also known as HSF2, is a human gene.^[1]

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.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Heat shock factor

[edit] References

^ ^a ^b Entrez Gene: HSF2 heat shock transcription factor 2.

[edit] 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. 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. PMID 1717345.
Schuetz TJ, Gallo GJ, Sheldon L, et al. (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. PMID 1871106.
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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 16428449.

[edit] External links

MeSH HSF2+protein,+human

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

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD