CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005119
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock factor protein 
Protein Synonyms/Alias
 HSF; Heat shock transcription factor; HSTF 
Gene Name
 Hsf 
Gene Synonyms/Alias
 CG5748 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
174SKILTDVKVMRGRQDacetylation[1]
518QSTVSSGKFASNFDVacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
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 46 150
 MOD_RES 256 256 Phosphoserine.
 MOD_RES 258 258 Phosphothreonine.
 MOD_RES 260 260 Phosphoserine.
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 580 580 Phosphoserine.  
Keyword
 3D-structure; Activator; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Stress response; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 691 AA 
Protein Sequence
MSRSRSSAKA VQFKHESEEE EEDEEEQLPS RRMHSYGDAA AIGSGVPAFL AKLWRLVDDA 60
DTNRLICWTK DGQSFVIQNQ AQFAKELLPL NYKHNNMASF IRQLNMYGFH KITSIDNGGL 120
RFDRDEIEFS HPFFKRNSPF LLDQIKRKIS NNKNGDDKGV LKPEAMSKIL TDVKVMRGRQ 180
DNLDSRFSAM KQENEVLWRE IASLRQKHAK QQQIVNKLIQ FLITIVQPSR NMSGVKRHVQ 240
LMINNTPEID RARTTSETES ESGGGPVIHE LREELLDEVM NPSPAGYTAA SHYDQESVSP 300
PAVERPRSNM SISSHNVDYS NQSVEDLLLQ GNGTAGGNIL VGGAASPMAQ SVSQSPAQHD 360
VYTVTEAPDS HVQEVPNSPP YYEEQNVLTT PMVREQEQQK RQQLKENNKL RRQAGDVILD 420
AGDILVDSSS PKAQRTSIQH STQPDVMVQP MIIKSEPENS SGLMDLMTPA NDLYSVNFIS 480
EDMPTDIFED ALLPDGVEEA AKLDQQQKFG QSTVSSGKFA SNFDVPTNST LLDANQASTS 540
KAAAKAQASE EEGMAVAKYS GAENGNNRDT NNSQLLRMAS VDELHGHLES MQDELETLKD 600
LLRGDGVAID QNMLMGLFND SDLMDNYGLS FPNDSISSEK KAPSGSELIS YQPMYDLSDI 660
LDTDDGNNDQ EASRRQMQTQ SSVLNTPRHE L 691 
Gene Ontology
 GO:0005634; C:nucleus; IDA:FlyBase.
 GO:0005700; C:polytene chromosome; IDA:FlyBase.
 GO:0003677; F:DNA binding; IDA:FlyBase.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:FlyBase.
 GO:0042742; P:defense response to bacterium; IMP:FlyBase.
 GO:0050832; P:defense response to fungus; IMP:FlyBase.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:FlyBase.
 GO:0022008; P:neurogenesis; IMP:FlyBase.
 GO:0043388; P:positive regulation of DNA binding; IDA:FlyBase.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
 GO:0009408; P:response to heat; IDA:FlyBase.
 GO:0031427; P:response to methotrexate; IEP:FlyBase.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000232; HSF_DNA-bd.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00447; HSF_DNA-bind 
SMART
 SM00415; HSF 
PROSITE
 PS00434; HSF_DOMAIN 
PRINTS
 PR00056; HSFDOMAIN.