| + |
MAPKAPK5 | down-regulates activity 
phosphorylation
|
RHEB |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276313 |
Ser130 |
LHMERVIsYEEGKAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21336308 |
Phosphorylation of Rheb at Ser 130 by PRAK impairs the nucleotide-binding ability of Rheb and inhibits Rheb-mediated mTORC1 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK5 | up-regulates 
phosphorylation
|
DNAJB1 |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203456 |
Ser149 |
TNVNFGRsRSAQEPA |
Homo sapiens |
|
| pmid |
sentence |
| 24309468 |
Phosphorylation of heat shock protein 40 (hsp40/dnajb1) by mitogen-activated protein kinase-activated protein kinase 5 (mk5/prak). Mk5 phosphorylates hsp40/dnajb1 in vivo at ser-149 or/and ser-151 and ser-171 in the c-terminal domain of hsp40/dnajb1. Mk5 modestly stimulates the atp hydrolyse activity of hsp40/hsp70 complex and enhances the repression of heat shock factor 1 driven transcription by hsp40/dnajb1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203460 |
Ser151 |
VNFGRSRsAQEPARK |
Homo sapiens |
|
| pmid |
sentence |
| 24309468 |
Phosphorylation of heat shock protein 40 (hsp40/dnajb1) by mitogen-activated protein kinase-activated protein kinase 5 (mk5/prak). Mk5 phosphorylates hsp40/dnajb1 in vivo at ser-149 or/and ser-151 and ser-171 in the c-terminal domain of hsp40/dnajb1. Mk5 modestly stimulates the atp hydrolyse activity of hsp40/hsp70 complex and enhances the repression of heat shock factor 1 driven transcription by hsp40/dnajb1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203464 |
Ser171 |
VTHDLRVsLEEIYSG |
Homo sapiens |
|
| pmid |
sentence |
| 24309468 |
Phosphorylation of heat shock protein 40 (hsp40/dnajb1) by mitogen-activated protein kinase-activated protein kinase 5 (mk5/prak). Mk5 phosphorylates hsp40/dnajb1 in vivo at ser-149 or/and ser-151 and ser-171 in the c-terminal domain of hsp40/dnajb1. Mk5 modestly stimulates the atp hydrolyse activity of hsp40/hsp70 complex and enhances the repression of heat shock factor 1 driven transcription by hsp40/dnajb1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
TLK1 | up-regulates activity
phosphorylation
|
MAPKAPK5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276745 |
Ser160 |
NLLFKDNsLDAPVKL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 35064619 |
We established that TLK1 phosphorylates MK5 on three residues (S160, S354 and S386), resulting in MK5 activation, and additionally, mobility shifts of MK5 also supported its phosphorylation by TLK1 in transfected HEK 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276746 |
Ser354 |
VSLKPLHsVNNPILR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 35064619 |
We established that TLK1 phosphorylates MK5 on three residues (S160, S354 and S386), resulting in MK5 activation, and additionally, mobility shifts of MK5 also supported its phosphorylation by TLK1 in transfected HEK 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276747 |
Ser386 |
HENGAEDsNVALEKL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 35064619 |
We established that TLK1 phosphorylates MK5 on three residues (S160, S354 and S386), resulting in MK5 activation, and additionally, mobility shifts of MK5 also supported its phosphorylation by TLK1 in transfected HEK 293 cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK5 | up-regulates
phosphorylation
|
MAPK4 |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-17069 |
Ser186 |
YSHKGYLsEGLVTKW |
Homo sapiens |
|
| pmid |
sentence |
| 1319925 |
This is due to mk5-dependent phosphorylation and only this retarded erk4 species is both phosphorylated on ser(186) and co-immunoprecipitates with wild-type mk5. We conclude that binding between erk4 and mk5 facilitates phosphorylation of ser(186) and stabilization of the erk4-mk5 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK5 | up-regulates
phosphorylation
|
TH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95479 |
Ser19 |
KGFRRAVsELDAKQA |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Recombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation of both ser40 and ser19 induced a high-affinity binding of 14-3-3 proteins, but only the interaction of 14-3-3 with ser19 increased the hth1 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK5 | up-regulates
phosphorylation
|
TP53 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152847 |
Ser37 |
NVLSPLPsQAMDDLM |
Homo sapiens |
Skin Cancer Cell |
| pmid |
sentence |
| 17254968 |
Furthermore, we show that prak activates p53 by direct phosphorylation. prak phosphorylates p53 at ser37 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152850 |
|
|
Homo sapiens |
Skin Cancer Cell |
| pmid |
sentence |
| 17254968 |
Furthermore, we show that prak activates p53 by direct phosphorylation. We propose that phosphorylation of p53 by prak following activation of p38 mapk by ras plays an important role in ras-induced senescence and tumor suppression. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK5 |
phosphorylation
|
EEF2K |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249708 |
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 |
| + |
MAPKAPK5 | up-regulates activity
phosphorylation
|
KALRN |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263093 |
Ser487 |
DVLQRPLsPGNSESL |
in vitro |
|
| pmid |
sentence |
| 22508986 |
The brain-specific nucleotide exchange factor kalirin-7 (Kal7) was identified as an MK5 interaction partner and substrate protein. The MK5 substrate Kal7, a Rho GEF and known activator of Rac GTPases, further contributes to PAK activation and actin filament reorganization. Thus, the coordinated phosphorylation of Borg proteins and Kal7 by ERK3 and MK5 constitute a novel signaling cascade involving feed-forward circuits, multiple GTPases, and cytoskeletal elements. The fragment SR3-6, but not the mutated fragment SR3-6-S487A, is phosphorylated by MK5. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPKAPK5 | up-regulates activity
phosphorylation
|
PLA2G4A |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250162 |
Ser727 |
RQNPSRCsVSLSNVE |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 10978317 |
The p38-activated protein kinases MNK1, MSK1, and PRAK1 phosphorylate cPLA2 in vitro uniquely on Ser-727. By using Chinese hamster ovary, HeLa, and HEK293 cells stably transfected with wild type and phosphorylation site mutant forms of cPLA2, we show that phosphorylation of cPLA2 at both Ser-505 and Ser-727 and elevation of Ca(2+) leads to its activation in agonist-stimulated cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK11 | up-regulates
phosphorylation
|
MAPKAPK5 |
0.602 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58131 |
Thr182 |
IDQGDLMtPQFTPYY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9628874 |
Prak activity was regulated by p38alpha and p38beta both in vitro and in vivo and thr182 was shown to be the regulatory phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | up-regulates activity
phosphorylation
|
MAPKAPK5 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58135 |
Thr182 |
IDQGDLMtPQFTPYY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9628874 |
In hela cells, prak was activated in response to cellular stress and proinflammatory cytokines. Prak activity was regulated by p38alpha and p38beta both in vitro and in vivo and thr182 was shown to be the regulatory phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
MAPKAPK5 |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58127 |
Thr182 |
IDQGDLMtPQFTPYY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9628874 |
Activated following phosphorylation at thr-182 by p38-alpha/mapk14, p38-beta/mapk11, erk2/mapk1, erk3/mapk6, and erk4/mapk4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174076 |
Thr182 |
IDQGDLMtPQFTPYY |
Homo sapiens |
|
| pmid |
sentence |
| 21666810 |
Like mk2, mk5 could be phosphorylated and activated by p38mapk and erk2 in vitro, but not by sapk?/Jnk3 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
MAPKAPK5
- 
- 