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HSF1 (human)

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; sequence-specific DNA binding; transcription factor activity Biological Process: negative regulation of cell proliferation; embryonic placenta development; transcription, DNA-dependent; response to heat; embryonic process involved in female pregnancy; spermatogenesis; 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®

Select Structure to View Below HSF1 2LDU - A=10-123 (human)

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	Sites Implicated In
cell cycle regulation: S216‑p transcription, altered: T142‑p, K298‑s, S303‑p, S307‑p, S320‑p, S326‑p transcription, induced: S307‑p activation: T142‑p, S320‑p, S326‑p inhibition: 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

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
1	0		K80-a	LNMYGFRkVVHIEQG
2	2		S121-p	NIKRKVTsVSTLKsE
0	1		S127-p	TsVSTLKsEDIKIRQ
1	0		T142-p	DSVTKLLtDVQLMKG
2	0		S216-p	IPLMLNDsGSAHSMP
5	1		S230-p	PKYSRQFsLEHVHGS
1	0		S275-p	ITELAPAsPMAsPGG
0	1		S279-p	APAsPMAsPGGsIDE
0	1		S283-p	PMAsPGGsIDERPLS
1	3		S292-p	DERPLSSsPLVRVkE
4	0		K298-s	SsPLVRVkEEPPsPP
11	23		S303-p	RVkEEPPsPPQsPRV
11	20		S307-p	EPPsPPQsPRVEEAs
1	22		S314-p	sPRVEEAsPGRPssV
1	5		S319-p	EAsPGRPssVDtLLs
3	2		S320-p	AsPGRPssVDtLLsP
0	6		T323-p	GRPssVDtLLsPTAL
3	21		S326-p	ssVDtLLsPTALIDS
0	2		T328	VDtLLsPTALIDSIL
1	1		S333	sPTALIDSILRESEP
1	2		S344-p	ESEPAPAsVTALTDA
0	1		T355-p	LTDARGHtDtEGRPP
0	3		T357-p	DARGHtDtEGRPPsP
1	46		S363-p	DtEGRPPsPPPtstP
0	11		T367-p	RPPsPPPtstPEKCL
0	9		S368-p	PPsPPPtstPEKCLS
0	36		T369-p	PsPPPtstPEKCLSV
0	1		S403	DNLQTMLSSHGFSVD
0	1		S404	NLQTMLSSHGFSVDT
2	1		S419-p	SALLDLFsPSVTVPD
1	1		S444-p	ASIQELLsPQEPPRP
0	3		S501-p	LGEGSYFsEGDGFAE

	mouse ► Hide Isoforms
K80	LNMYGFRKVVHIEQG
S121	NIKRKVTSVSTLKSE
S127	TSVSTLKSEDIKIRQ
T142	DSVTRLLTDVQLMKG
S216	IPLMLSDSNSAHSVP
S230-p	PKYGRQYsLEHVHGP
S275	ITELAPTSPLASPGR
S279	APTSPLASPGRSIDE
S283	PLASPGRSIDERPLS
S292	DERPLSSSTLVRVKQ
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
-	gap
-	gap
-	gap
S364	APALPTPStPEKCLS
T365-p	PALPTPStPEKCLSV
T399	DNLQTMLTSHGFSVD
S400	NLQTMLTSHGFSVDT
S415-p	SALLDLFsPSVTMPD
S440	ASIQELLSPQEPPRP
S497	LGESSYFSEGDDYTD

	HSF1 iso2
K80	LNMYGFRKVVHIEQG
S121	NIKRKVTSVSTLKSE
S127	TSVSTLKSEDIKIRQ
T142	DSVTRLLTDVQLMKG
S216	IPLMLSDSNSAHSVP
S230	PKYGRQYSLEHVHGP
S275	ITELAPTSPLASPGR
S279	APTSPLASPGRSIDE
S283	PLASPGRSIDERPLS
S292	DERPLSSSTLVRVKQ
K298	SSTLVRVKQEPPSPP
S303	RVKQEPPSPPHSPRV
S307	EPPSPPHSPRVLEAS
S314	SPRVLEASPGRPSSM
S319	EASPGRPSSMDTPLS
S320	ASPGRPSSMDTPLSP
T323	GRPSSMDTPLSPTAF
S326	SSMDTPLSPTAFIDS
T328	MDTPLSPTAFIDSIL
S333	SPTAFIDSILRESEP
S345	SEPTPAASNTAPMDT
-	gap
-	gap
-	gap
-	gap
S364	APALPTPSTPEKCLS
T365	PALPTPSTPEKCLSV
T399-p	DNLQTMLtsHGFSVD
S400-p	NLQTMLtsHGFSVDT
-	gap
S418	LDIQELLSPQEPPRP
S475	LGESSYFSEGDDYTD

	rat
K80	LNMYGFRKVVHIEQG
S121	NIKRKVTSVSTLKSE
S127	TSVSTLKSEDIKIRQ
T142	DSVTRLLTDVQLMKG
S216	IPLMLSDSSSAHSVP
S230-p	PKYGRQYsLEHVHGP
S275	ITELAPTSPLASPGR
S279	APTSPLASPGRSIDE
S283	PLASPGRSIDERPLS
S292	DERPLSSSTLVRVKE
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
-	gap
-	gap
-	gap
S364	APAPPAPSTPEKCLS
T365	PAPPAPSTPEKCLSV
T399	DNLQTMLTSHGFSVD
S400	NLQTMLTSHGFSVDT
S415	SALLDLFSPSVTMPD
S440	ASIQELLSPQEPPRP
S497	LGESSYFSEGDDYTD

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