CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011135
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock factor protein 2 
Protein Synonyms/Alias
 HSF 2; Heat shock transcription factor 2; HSTF 2 
Gene Name
 HSF2 
Gene Synonyms/Alias
 HSTF2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51FAKEILPKYFKHNNMubiquitination[1, 2]
54EILPKYFKHNNMASFubiquitination[1, 2]
82HIDSGIVKQERDGPVsumoylation[3, 4, 5]
108DDLLENIKRKVSSSKubiquitination[6]
135KIISSAQKVQIKQETubiquitination[6]
139SAQKVQIKQETIESRsumoylation[5, 7]
139SAQKVQIKQETIESRubiquitination[6, 8]
151ESRLSELKSENESLWubiquitination[6, 9]
210NTNGAQKKNLFQHIVubiquitination[1, 2]
420NKGLETTKNNVVQPVubiquitination[9]
Reference
 [1] 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]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor.
 Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD.
 J Biol Chem. 2001 May 25;276(21):18513-8. [PMID: 11278381]
 [4] Intracellular trafficking of heat shock factor 2.
 Le Goff P, Le Dréan Y, Le Péron C, Le Jossic-Corcos C, Ainouche A, Michel D.
 Exp Cell Res. 2004 Apr 1;294(2):480-93. [PMID: 15023536]
 [5] 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]
 [6] 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]
 [7] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
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. 
Sequence Annotation
 DNA_BIND 7 112 By similarity.
 REGION 119 192 Hydrophobic repeat HR-A/B.
 REGION 360 385 Hydrophobic repeat HR-C.
 MOTIF 108 122 Nuclear localization signal (Potential).
 MOTIF 195 210 Nuclear localization signal (Potential).  
Keyword
 Activator; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Reference proteome; Stress response; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 536 AA 
Protein Sequence
MKQSSNVPAF LSKLWTLVEE THTNEFITWS QNGQSFLVLD EQRFAKEILP KYFKHNNMAS 60
FVRQLNMYGF RKVVHIDSGI VKQERDGPVE FQHPYFKQGQ DDLLENIKRK VSSSKPEENK 120
IRQEDLTKII SSAQKVQIKQ ETIESRLSEL KSENESLWKE VSELRAKHAQ QQQVIRKIVQ 180
FIVTLVQNNQ LVSLKRKRPL LLNTNGAQKK NLFQHIVKEP TDNHHHKVPH SRTEGLKPRE 240
RISDDIIIYD VTDDNADEEN IPVIPETNED VISDPSNCSQ YPDIVIVEDD NEDEYAPVIQ 300
SGEQNEPARE SLSSGSDGSS PLMSSAVQLN GSSSLTSEDP VTMMDSILND NINLLGKVEL 360
LDYLDSIDCS LEDFQAMLSG RQFSIDPDLL VDLFTSSVQM NPTDYINNTK SENKGLETTK 420
NNVVQPVSEE GRKSKSKPDK QLIQYTAFPL LAFLDGNPAS SVEQASTTAS SEVLSSVDKP 480
IEVDELLDSS LDPEPTQSKL VRLEPLTEAE ASEATLFYLC ELAPAPLDSD MPLLDS 536 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 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:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR000232; HSF_DNA-bd.
 IPR010542; Vert_HS_TF.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00447; HSF_DNA-bind
 PF06546; Vert_HS_TF 
SMART
 SM00415; HSF 
PROSITE
 PS00434; HSF_DOMAIN 
PRINTS
 PR00056; HSFDOMAIN.