CPLM-010776

Genbank Nucleotide ID

Heat shock factor protein 1

Protein Synonyms/Alias

HSF 1; Heat shock transcription factor 1; HSTF 1

Homo sapiens (Human)

Position	Peptide	Type	References
54	FDQGQFAKEVLPKYF	ubiquitination	[1]
62	EVLPKYFKHNNMASF	ubiquitination	[1, 2, 3]
80	LNMYGFRKVVHIEQG	acetylation	[4]
116	EQLLENIKRKVTSVS	acetylation	[4]
116	EQLLENIKRKVTSVS	ubiquitination	[1]
118	LLENIKRKVTSVSTL	acetylation	[4]
126	VTSVSTLKSEDIKIR	acetylation	[4]
148	LTDVQLMKGKQECMD	acetylation	[4]
148	LTDVQLMKGKQECMD	ubiquitination	[1]
157	KQECMDSKLLAMKHE	acetylation	[4]
208	RILGVKRKIPLMLND	acetylation	[4]
208	RILGVKRKIPLMLND	ubiquitination	[1]
224	GSAHSMPKYSRQFSL	acetylation	[4]
298	SSPLVRVKEEPPSPP	acetylation	[4]
298	SSPLVRVKEEPPSPP	sumoylation	[5, 6, 7, 8, 9]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1.
Westerheide SD, Anckar J, Stevens SM Jr, Sistonen L, Morimoto RI.
Science. 2009 Feb 20;323(5917):1063-6. [PMID: 19229036]
[5] Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification.
Hong Y, Rogers R, Matunis MJ, Mayhew CN, Goodson ML, Park-Sarge OK, Sarge KD.
J Biol Chem. 2001 Oct 26;276(43):40263-7. [PMID: 11514557]
[6] Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification.
Hilgarth RS, Hong Y, Park-Sarge OK, Sarge KD.
Biochem Biophys Res Commun. 2003 Mar 28;303(1):196-200. [PMID: 12646186]
[7] Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1.
Hietakangas V, Ahlskog JK, Jakobsson AM, Hellesuo M, Sahlberg NM, Holmberg CI, Mikhailov A, Palvimo JJ, Pirkkala L, Sistonen L.
Mol Cell Biol. 2003 Apr;23(8):2953-68. [PMID: 12665592]
[8] Molecular basis for SUMOylation-dependent regulation of DNA binding activity of heat shock factor 2.
Tateishi Y, Ariyoshi M, Igarashi R, Hara H, Mizuguchi K, Seto A, Nakai A, Kokubo T, Tochio H, Shirakawa M.
J Biol Chem. 2009 Jan 23;284(4):2435-47. [PMID: 19017645]
[9] Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity.
Brunet Simioni M, De Thonel A, Hammann A, Joly AL, Bossis G, Fourmaux E, Bouchot A, Landry J, Piechaczyk M, Garrido C.
Oncogene. 2009 Sep 17;28(37):3332-44. [PMID: 19597476]

Functional Description

DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.

DNA_BIND 15 120 By similarity.
REGION 130 203 Hydrophobic repeat HR-A/B.
REGION 221 310 Regulatory domain.
REGION 371 529 Transactivation domain.
REGION 384 409 Hydrophobic repeat HR-C.
MOTIF 412 420 9aaTAD.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 121 121 Phosphoserine; by MAPKAPK2.
MOD_RES 142 142 Phosphothreonine; by CK2.
MOD_RES 230 230 Phosphoserine.
MOD_RES 292 292 Phosphoserine.
MOD_RES 303 303 Phosphoserine.
MOD_RES 307 307 Phosphoserine.
MOD_RES 314 314 Phosphoserine.
MOD_RES 323 323 Phosphothreonine.
MOD_RES 326 326 Phosphoserine.
MOD_RES 344 344 Phosphoserine.
MOD_RES 363 363 Phosphoserine.
MOD_RES 419 419 Phosphoserine.
MOD_RES 444 444 Phosphoserine.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Activator; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Stress response; Transcription; Transcription regulation; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IDA:HPA.
GO:0045120; C:pronucleus; IEA:Compara.
GO:0043234; C:protein complex; IEA:Compara.
GO:0003682; F:chromatin binding; IEA:Compara.
GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO:0001892; P:embryonic placenta development; IEA:Compara.
GO:0060136; P:embryonic process involved in female pregnancy; IEA:Compara.
GO:0007143; P:female meiosis; IEA:Compara.
GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Compara.
GO:0040018; P:positive regulation of multicellular organism growth; IEA:Compara.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO:0006468; P:protein phosphorylation; IEA:Compara.
GO:0090231; P:regulation of spindle checkpoint; IEA:Compara.
GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
GO:0007283; P:spermatogenesis; IEA:Compara.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR027072; HSF1.
IPR000232; HSF_DNA-bd.
IPR010542; Vert_HS_TF.
IPR011991; WHTH_DNA-bd_dom.

PF00447; HSF_DNA-bind
PF06546; Vert_HS_TF