| + |
MAPKAPK2 | down-regulates 
phosphorylation
|
HSPB1 |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166629 |
Ser15 |
FSLLRGPsWDPFRDW |
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
Notably mk2 is well known to play an important role in actin filament remodellng by phosphorylating hsp27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94021 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12367505 |
Notably mk2 is well known to play an important role in actin filament remodellng by phosphorylating hsp27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166633 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
Notably mk2 is well known to play an important role in actin filament remodellng by phosphorylating hsp27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94025 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12367505 |
Notably mk2 is well known to play an important role in actin filament remodellng by phosphorylating hsp27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166637 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
Notably mk2 is well known to play an important role in actin filament remodellng by phosphorylating hsp27. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
RPS6KB1 | down-regulates
phosphorylation
|
HSPB1 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186951 |
Ser15 |
FSLLRGPsWDPFRDW |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Ser-15, ser-78, and ser-82 in hsp27 (ser-15 and ser-86 in hsp25) are part of the rxxs motif, a known recognition site for p70rsk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186955 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Ser-15, ser-78, and ser-82 in hsp27 (ser-15 and ser-86 in hsp25) are part of the rxxs motif, a known recognition site for p70rsk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186959 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Ser-15, ser-78, and ser-82 in hsp27 (ser-15 and ser-86 in hsp25) are part of the rxxs motif, a known recognition site for p70rsk. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK3 |
phosphorylation
|
HSPB1 |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250159 |
Ser15 |
FSLLRGPsWDPFRDW |
in vitro |
|
| pmid |
sentence |
| 8774846 |
MAPKAP kinase-3 and MAPKAP kinase-2 phosphorylated peptide substrates with similar kinetic constants and phosphorylated the same serine residues in HSP27 at the same relative rates.The three serine residues in HSP27 phosphorylated by MAPKAPK2 were also phosphorylated at the same relative rates by MAPKAP-K3 (Ser-82>>Ser-78 >Ser-15) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250160 |
Ser78 |
PAYSRALsRQLSSGV |
in vitro |
|
| pmid |
sentence |
| 8774846 |
MAPKAP kinase-3 and MAPKAP kinase-2 phosphorylated peptide substrates with similar kinetic constants and phosphorylated the same serine residues in HSP27 at the same relative rates.The three serine residues in HSP27 phosphorylated by MAPKAPK2 were also phosphorylated at the same relative rates by MAPKAP-K3 (Ser-82>>Ser-78 >Ser-15) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250161 |
Ser82 |
RALSRQLsSGVSEIR |
in vitro |
|
| pmid |
sentence |
| 8774846 |
MAPKAP kinase-3 and MAPKAP kinase-2 phosphorylated peptide substrates with similar kinetic constants and phosphorylated the same serine residues in HSP27 at the same relative rates.The three serine residues in HSP27 phosphorylated by MAPKAPK2 were also phosphorylated at the same relative rates by MAPKAP-K3 (Ser-82>>Ser-78 >Ser-15) |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCD | down-regulates activity
phosphorylation
|
HSPB1 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278424 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 22974980 |
Radioactive kinase assays confirmed that PKC\u03b4 phosphorylated Hsp27 at Ser78 and Ser82 ( Fig. 3 B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278425 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 22974980 |
Radioactive kinase assays confirmed that PKC\u03b4 phosphorylated Hsp27 at Ser78 and Ser82 ( Fig. 3 B). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates
phosphorylation
|
HSPB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186796 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186943 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186947 |
Thr143 |
RCFTRKYtLPPGVDP |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates
phosphorylation
|
HSPB1 |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186784 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186788 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186792 |
Thr143 |
RCFTRKYtLPPGVDP |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT | down-regulates
phosphorylation
|
HSPB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186772 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
HSPB1 |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186776 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | down-regulates
phosphorylation
|
HSPB1 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186780 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates
phosphorylation
|
HSPB1 |
0.665 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252526 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cells resulted in hsp27 phosphorylation at the same residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPB1 | up-regulates quantity by stabilization 
binding
|
GCH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252222 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18241680 |
GTP cyclohydrolase I (GCH), an oligomeric protein composed of 10 identical subunits, is required for the synthesis of neurotransmitters; mutations in GCH are associated with dopa-responsive dystonia (DRD) and hyperphenylalaninemia. Mutated GCH proteins are unstable and prone to dominant-negative effect. We show herein that expression of the GCH mutant GCH-201E or the splicing variant GCH-II caused intracellular inclusion bodies. When Hsp27 was expressed together with the GCH mutants, Hsp27 expression decreased the formation of inclusion bodies by GCH (as assessed by immunofluorescence) and decreased the amount of insoluble GCH mutant proteins (as assessed by Western blot). we demonstrated that Hsp27 increases the expression of the wild-type GCH protein, causes the appearance of the soluble GCH-II protein, and decreases the quantities of insoluble mutated GCH protein. Therefore, it is likely that Hsp27 improves the folding of mutated GCH proteins, so they can stay in free cytosolic compartment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPB1 | down-regulates 
|
CASP3 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71869 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10544189 |
Hsp27 overexpression delays poly(adp-ribose)polymerase cleavage and procaspase-3 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPB1 | down-regulates
|
DIABLO |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103539 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12855565 |
These data demonstrate that hsp27 inhibits the release of smac |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
HSPB1
- 
- 