+ |
MAPKAPK3 |
phosphorylation
|
HSPB1 |
0.672 |
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 |
+ |
MAPKAPK3 | down-regulates activity
phosphorylation
|
RCSD1 |
0.496 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263081 |
Ser179 |
RRFRRSQsDCGELGD |
in vitro |
|
pmid |
sentence |
15850461 |
Human CapZIP was phosphorylated at Ser-179 and Ser-244 by MAPKAP-K2 (mitogen-activated protein kinase-activated protein kinase 2) or MAPKAP-K3 in vitro. In the present paper we have identified CapZIP as a protein that is phosphorylated exceptionally rapidly by several SAPKs in vitro (Figure 4), and which is expressed in muscles and immune cells. Both MAPKAP-K2 and MAPKAP-K3 phosphorylated CapZIP at Ser-179 in vitro. An important clue to the function of CapZIP and its phosphorylation came from the finding that it binds to the actin-capping protein CapZ (Figure 7A), and that cellular stresses trigger the dissociation of these two proteins (Figure 7B).Such an effect is presumably lost when CapZIP is phosphorylated and dissociates from CapZ. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263082 |
Ser244 |
PPLRRSPsRTEKQEE |
in vitro |
|
pmid |
sentence |
15850461 |
Human CapZIP was phosphorylated at Ser-179 and Ser-244 by MAPKAP-K2 (mitogen-activated protein kinase-activated protein kinase 2) or MAPKAP-K3 in vitro. In the present paper we have identified CapZIP as a protein that is phosphorylated exceptionally rapidly by several SAPKs in vitro (Figure 4), and which is expressed in muscles and immune cells. Both MAPKAP-K2 and MAPKAP-K3 phosphorylated CapZIP at Ser-179 in vitro. An important clue to the function of CapZIP and its phosphorylation came from the finding that it binds to the actin-capping protein CapZ (Figure 7A), and that cellular stresses trigger the dissociation of these two proteins (Figure 7B).Such an effect is presumably lost when CapZIP is phosphorylated and dissociates from CapZ. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
MAPKAPK3 |
phosphorylation
|
EEF2K |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249709 |
Ser377 |
PPLLRPLsENSGDEN |
in vitro |
|
pmid |
sentence |
12171600 |
Identification of Ser-377 as the site on eEF2 kinase phosphorylated in vitro by MAPKAP-K2, MAPKAP-K3 and MAPKAP-K5. Maximal phosphorylation of eEF2 kinase by MAPKAP-K2 (Figure 5) or MAPKAP-K5 (results not shown) had no effect on its activity. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CREB5 | up-regulates quantity by expression
transcriptional regulation
|
MAPKAPK3 |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253807 |
|
|
Homo sapiens |
|
pmid |
sentence |
21132541 |
Our result verified CREB5 biological regulation module in the upstream of frontal cortex of HIVE-control patients (MAPKAPK3 activation; DGKG, LY96, TNFRSF11B inhibition) and downstream (ATP6V0E1, CFB, DGKG, MX1, TGFBR3 activation; LGALS3BP, RASGRP3, RDX, STAT1 inhibition), |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Chorda Gubernaculum |
+ |
MAPK14 | up-regulates activity
phosphorylation
|
MAPKAPK3 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235451 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11157753 |
These results, taken together, suggest the importance of the docking interaction in the efficient phosphorylation and activation of 3pk by p38. |
|
Publications: |
1 |
Organism: |
Mus Musculus |