+ |
PRKCA | up-regulates activity
phosphorylation
|
HSPB8 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107684 |
Ser14 |
PFSCHYPsRLRRDPF |
Homo sapiens |
|
pmid |
sentence |
11342557 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107688 |
Thr63 |
LSSAWPGtLRSGMVP |
Homo sapiens |
|
pmid |
sentence |
11342557 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
PRKCA | up-regulates
phosphorylation
|
HSPB8 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197940 |
Ser14 |
PFSCHYPsRLRRDPF |
Homo sapiens |
|
pmid |
sentence |
22721717 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197949 |
Thr63 |
LSSAWPGtLRSGMVP |
Homo sapiens |
|
pmid |
sentence |
22721717 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PKA | down-regulates quantity by destabilization
phosphorylation
|
HSPB8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276152 |
Ser24 |
RRDPFRDsPLSSRLL |
in vitro |
|
pmid |
sentence |
18298377 |
Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 susceptibility to chymotrypsinolysis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276151 |
Ser57 |
DWALPRLsSAWPGTL |
in vitro |
|
pmid |
sentence |
18298377 |
Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 susceptibility to chymotrypsinolysis. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
MAPK3 | up-regulates
phosphorylation
|
HSPB8 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197932 |
Ser27 |
PFRDSPLsSRLLDDG |
Homo sapiens |
|
pmid |
sentence |
22721717 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197936 |
Thr87 |
GVPAEGRtPPPFPGE |
Homo sapiens |
|
pmid |
sentence |
22721717 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK3 | up-regulates activity
phosphorylation
|
HSPB8 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107676 |
Ser27 |
PFRDSPLsSRLLDDG |
Homo sapiens |
|
pmid |
sentence |
11342557 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107680 |
Thr87 |
GVPAEGRtPPPFPGE |
Homo sapiens |
|
pmid |
sentence |
11342557 |
Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |