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Protein Page:
HSF1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
HSF1 a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; DNA binding protein
Cellular Component: protein complex; pronucleus; cytoplasm; nucleolus; nucleus
Molecular Function: protein binding; chromatin binding; transcription factor activity
Biological Process: negative regulation of cell proliferation; embryonic placenta development; transcription, DNA-dependent; embryonic process involved in female pregnancy; female meiosis; spermatogenesis; positive regulation of transcription from RNA polymerase II promoter; defense response; response to lipopolysaccharide; negative regulation of tumor necrosis factor production; positive regulation of multicellular organism growth; protein amino acid phosphorylation
Reference #:  Q00613 (UniProtKB)
Alt. Names/Synonyms: Heat shock factor protein 1; Heat shock transcription factor 1; HSF 1; HSF1; HSTF 1; HSTF1
Gene Symbols: HSF1
Molecular weight: 57,260 Da
Basal Isoelectric point: 5.02  Predict pI for various phosphorylation states
CST Pathways:  SAPK/JNK Signaling Cascades
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HSF1

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S216‑p
transcription, altered: T142‑p, S303‑p, S326‑p
transcription, induced: S307‑p, S320‑p, S326‑p
transcription, inhibited: K298‑s, S303‑p, S307‑p
activity, induced: T142‑p, S320‑p, S326‑p
activity, inhibited: S121‑p, S303‑p, S307‑p
intracellular localization: S216‑p, S303‑p, S307‑p, S320‑p
molecular association, regulation: S121‑p, T142‑p, S216‑p, S303‑p, S307‑p
protein degradation: S216‑p, S307‑p
protein processing: S303‑p
sumoylation: S307‑p
ubiquitination: S216‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 0 K80-a LNMYGFRkVVHIEQG
1 0 K118-a LLENIKRkVTsVSTL
2 2 S121-p NIKRkVTsVSTLKsE
0 1 S127-p TsVSTLKsEDIKIRQ
2 0 T142-p DSVTKLLtDVQLMKG
1 0 K208-a RILGVKRkIPLMLND
2 1 S216-p IPLMLNDsGsAHSMP
0 1 S218-p LMLNDsGsAHSMPKY
7 1 S230-p PKYSRQFsLEHVHGS
1 0 S275-p ITELAPAsPMASPGG
2 3 S292-p DERPLSSsPLVRVkE
1 0 K298-a SsPLVRVkEEPPsPP
4 0 K298-s SsPLVRVkEEPPsPP
12 28 S303-p RVkEEPPsPPQsPRV
11 24 S307-p EPPsPPQsPRVEEAs
2 23 S314-p sPRVEEAsPGRPssV
1 5 S319-p EAsPGRPssVDtLLs
3 2 S320-p AsPGRPssVDtLLsP
0 6 T323-p GRPssVDtLLsPTAL
6 21 S326-p ssVDtLLsPTALIDs
0 2 T328 VDtLLsPTALIDsIL
1 1 S333-p sPTALIDsILRESEP
1 3 S344-p ESEPAPAsVTALTDA
0 3 T357-p DARGHTDtEGRPPsP
1 48 S363-p DtEGRPPsPPPtstP
0 12 T367-p RPPsPPPtstPEKCL
0 9 S368-p PPsPPPtstPEKCLS
0 37 T369-p PsPPPtstPEKCLSV
2 1 S419-p SALLDLFsPSVTVPD
1 1 S444-p ASIQELLsPQEPPRP
0 3 S501-p LGEGSYFsEGDGFAE
1 0 K524-a GSEPPKAkDPTVS__
  mouse

► Hide Isoforms
 
K80 LNMYGFRKVVHIEQG
K118 LLENIKRKVTSVSTL
S121 NIKRKVTSVSTLKSE
S127 TSVSTLKSEDIKIRQ
T142-p DSVTRLLtDVQLMKG
K208 RILGVKRKIPLMLSD
S216 IPLMLSDSNSAHSVP
S218 LMLSDSNSAHSVPKY
S230-p PKYGRQYsLEHVHGP
S275 ITELAPTSPLASPGR
S292 DERPLSSSTLVRVKQ
K298 SSTLVRVKQEPPsPP
K298 SSTLVRVKQEPPsPP
S303-p RVKQEPPsPPHsPRV
S307-p EPPsPPHsPRVLEAs
S314-p sPRVLEAsPGRPssM
S319-p EAsPGRPssMDtPLs
S320-p AsPGRPssMDtPLsP
T323-p GRPssMDtPLsPtAF
S326-p ssMDtPLsPtAFIDs
T328-p MDtPLsPtAFIDsIL
S333-p sPtAFIDsILRESEP
S345 SEPTPAASNTAPMDT
- gap
A359 TTGAQAPALPTPStP
P363 QAPALPTPStPEKCL
S364 APALPTPStPEKCLS
T365-p PALPTPStPEKCLSV
S415-p SALLDLFsPSVTMPD
S440 ASIQELLSPQEPPRP
S497 LGESSYFSEGDDYTD
K520 GTEPHKAKDPTVS__
  HSF1 iso2  
K80 LNMYGFRKVVHIEQG
K118 LLENIKRKVTSVSTL
S121 NIKRKVTSVSTLKSE
S127 TSVSTLKSEDIKIRQ
T142 DSVTRLLTDVQLMKG
K208 RILGVKRKIPLMLSD
S216 IPLMLSDSNSAHSVP
S218 LMLSDSNSAHSVPKY
S230 PKYGRQYSLEHVHGP
S275 ITELAPTSPLASPGR
S292 DERPLSSSTLVRVKQ
K298 SSTLVRVKQEPPSPP
K298 SSTLVRVKQEPPSPP
S303 RVKQEPPSPPHSPRV
S307 EPPSPPHSPRVLEAS
S314 SPRVLEASPGRPSSM
S319 EASPGRPSSMDTPLS
S320 ASPGRPSSMDTPLSP
T323 GRPSSMDTPLSPTAF
S326 SSMDTPLSPTAFIDS
T328 MDTPLSPTAFIDSIL
S333 SPTAFIDSILRESEP
S345 SEPTPAASNTAPMDT
- gap
A359 TTGAQAPALPTPSTP
P363 QAPALPTPSTPEKCL
S364 APALPTPSTPEKCLS
T365 PALPTPSTPEKCLSV
- gap
S418 LDIQELLSPQEPPRP
S475 LGESSYFSEGDDYTD
K498 GTEPHKAKDPTVS__
  rat

 
K80 LNMYGFRKVVHIEQG
K118 LLENIKRKVTSVSTL
S121 NIKRKVTSVSTLKSE
S127 TSVSTLKSEDIKIRQ
T142 DSVTRLLTDVQLMKG
K208 RILGVKRKIPLMLSD
S216 IPLMLSDSSSAHSVP
S218 LMLSDSSSAHSVPKY
S230-p PKYGRQYsLEHVHGP
S275 ITELAPTSPLASPGR
S292 DERPLSSSTLVRVKE
K298 SSTLVRVKEEPPsPP
K298 SSTLVRVKEEPPsPP
S303-p RVKEEPPsPPHsPRV
S307-p EPPsPPHsPRVLEAS
S314 sPRVLEASPGRPASM
A319 EASPGRPASMDTPLS
S320 ASPGRPASMDTPLSP
T323 GRPASMDTPLSPTAF
S326 ASMDTPLSPTAFIDS
T328 MDTPLSPTAFIDSIL
S333 SPTAFIDSILRESEP
S345 SEPTPAASNTAPMDT
- gap
A359 TTGAQAPAPPAPSTP
P363 QAPAPPAPSTPEKCL
S364 APAPPAPSTPEKCLS
T365 PAPPAPSTPEKCLSV
S415 SALLDLFSPSVTMPD
S440 ASIQELLSPQEPPRP
S497 LGESSYFSEGDDYTD
K520 GTEPHKAKDPTVS__
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