+ |
PLK1 | down-regulates
phosphorylation
|
HSF1 |
0.455 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-180915 |
Ser216 |
IPLMLNDsGSAHSMP |
Homo sapiens |
|
pmid |
sentence |
18794143 |
Hsf1 was phosphorylated by plk1 at ser(216) of the dsgxxs motif during the timing of mitosis and a phospho-defective mutant form of hsf1 inhibited mitotic progression. Phosphorylated hsf1 during spindle pole localization underwent ubiquitin degradation through the scf(beta-trcp) pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates activity
phosphorylation
|
HSF1 |
0.416 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277580 |
Ser230 |
PKYSRQFsLEHVHGS |
in vitro |
|
pmid |
sentence |
35080342 |
Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277581 |
Ser326 |
SSVDTLLsPTALIDS |
in vitro |
|
pmid |
sentence |
35080342 |
Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277579 |
Thr142 |
DSVTKLLtDVQLMKG |
in vitro |
|
pmid |
sentence |
35080342 |
Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277578 |
Thr527 |
PPKAKDPtVS |
in vitro |
|
pmid |
sentence |
35080342 |
Mass spectrometry showed that AKT1 also phosphorylated HSF1 at T142, S230 and T527 in addition to S326, whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326 and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9. |
|
Publications: |
4 |
Organism: |
In Vitro |
+ |
CAMK2A | up-regulates activity
phosphorylation
|
HSF1 |
0.49 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250631 |
Ser230 |
PKYSRQFsLEHVHGS |
|
K-562 Cell |
pmid |
sentence |
11447121 |
Ser230 is located in the regulatory domain of HSF1, and promotes the magnitude of the inducible transcriptional activity. Ser230 lies within a consensus site for calcium/calmodulin-dependent protein kinase II (CaMKII), and CaMKII overexpression enhances both the level of in vivo Ser230 phosphorylation and transactivation of HSF1. The importance of Ser230 was further established by the S230A HSF1 mutant showing markedly reduced activity relative to wild-type HSF1 when expressed in hsf1(-/-) cells. |
|
Publications: |
1 |
+ |
GSK3B | down-regulates
phosphorylation
|
HSF1 |
0.539 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-44995 |
Ser303 |
RVKEEPPsPPQSPRV |
Homo sapiens |
|
pmid |
sentence |
8940068 |
Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3B | down-regulates activity
phosphorylation
|
HSF1 |
0.539 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251216 |
Ser303 |
RVKEEPPsPPQSPRV |
in vitro |
|
pmid |
sentence |
8940068 |
Ser-303 is phosphorylated by glycogen synthase kinase 3 (GSK3) through a mechanism dependent on primary phosphorylation of Ser-307 by MAPK. Secondary phosphorylation of Ser-303 by GSK3 may thus repress the activity of HSF-1, and its requirement for priming by MAPK phosphorylation of Ser-307 provides a potential link between the MAPK cascade and HSF-1. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPK3 | down-regulates
phosphorylation
|
HSF1 |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-44999 |
Ser307 |
EPPSPPQsPRVEEAS |
Homo sapiens |
|
pmid |
sentence |
8940068 |
Sequential phosphorylation of hsf1 by mitogen-activated protein kinase and glycogen synthase kinase 3 at ser-303 and ser-307 represses transcriptional activation by heat shock factor-1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | up-regulates
phosphorylation
|
HSF1 |
0.32 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-169853 |
Ser320 |
ASPGRPSsVDTLLSP |
Homo sapiens |
|
pmid |
sentence |
21085490 |
Protein kinase a binds and activates heat shock factor 1hsf1 binds avidly to the catalytic subunit of pka, (pkac_) and becomes phosphorylated on a novel serine phosphorylation site within its central regulatory domain (serine 320 or s320), both in vitro and in vivo. Intracellular pkac_ levels and phosphorylation of hsf1 at s320 were both required for hsf1 to be localized to the nucleus, bind to response elements in the promoter of an hsf1 target gene |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8 | down-regulates activity
phosphorylation
|
HSF1 |
0.512 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250119 |
Ser363 |
DTEGRPPsPPPTSTP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10747973 |
JNK is activated by heat shock and phosphorylates HSF-1 on serine 363. JNK Phosphorylation of HSF-1 Leads to Reduction in Its Transcriptional Activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK2A2 | up-regulates
phosphorylation
|
HSF1 |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-99606 |
Thr142 |
DSVTKLLtDVQLMKG |
Homo sapiens |
|
pmid |
sentence |
12659875 |
Transcriptional activity and dna binding of heat shock factor-1 involve phosphorylation on threonine 142 by ck2.As hsf1 is activated by heat shock simultaneously with the nuclear translocation of the protein kinase ck2, we have investigated the role of ck2 in hsf1 activatio |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 | up-regulates activity
phosphorylation
|
HSF1 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250898 |
Thr142 |
DSVTKLLtDVQLMKG |
in vitro |
|
pmid |
sentence |
12659875 |
Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
HSF1 | up-regulates quantity by expression
transcriptional regulation
|
HSPA6 |
0.44 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254477 |
|
|
Homo sapiens |
|
pmid |
sentence |
12813038 |
These experiments suggest that HSF2 is involved in the stress response, but unlike the ubiquitous HSF1 operates in a cell-line specific manner through differential expression of alternatively spliced isoforms. Curiously, HSF2A could not be activated by heat shock in cells deficient in functional HSF1 and required the expression of HSF1 for heat induction of the hsp70B gene in cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCQ | up-regulates
phosphorylation
|
HSF1 |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200576 |
|
|
Homo sapiens |
|
pmid |
sentence |
23352416 |
At the same time, ea causes pkc?-Mediated phosphorylation and activation of the transcription factor heat shock factor 1, an inducer of glucose dependence. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSBP1 | down-regulates activity
binding
|
HSF1 |
0.686 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261181 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9649501 |
HSBP1 is nuclear-localized and interacts in vivo with the active trimeric state of HSF1 that appears during heat shock. During attenuation of HSF1 to the inert monomer, HSBP1 associates with Hsp70. HSBP1 negatively affects HSF1 DNA-binding activity, and overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1. HSF1 interacts with HSBP1 in vivo and is a nuclear localized protein. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |