| + |
MAPK12 | down-regulates activity 
phosphorylation
|
RCSD1 |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263083 |
Ser108 |
LPGASPKsPGLKAMV |
in vitro |
|
| pmid |
sentence |
| 15850461 |
Peptide T2 was sequenced and shown to comprise residues 79–112 of CapZIP, phosphorylated at Ser-108 (Figure 2B). The identity of peptide T1 is unknown. These experiments established that the SAPK3/p38γ substrate was CapZIP. Using this antibody, we showed by immunoblotting that bacterially expressed CapZIP was phosphorylated at Ser-108 by SAPK4/p38δ, JNK1α1 and ERK2 in vitro, as well as by SAPK3/p38γ (results not shown). 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: |
1 |
Organism: |
In Vitro |
| + |
MAPK12 | up-regulates 
phosphorylation
|
SNTA1 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67061 |
Ser193 |
GWDSPPAsPLQRQPS |
Homo sapiens |
|
| pmid |
sentence |
| 10212242 |
Sapk3 phosphorylates alpha1-syntrophin at serine residues 193 and 201 in vitro and phosphorylation is dependent on binding to the pdz domain of alpha1-syntrophin. The finding that sapk3 co-localizes with _1-syntrophin in skeletal muscle, that it binds to the pdz domain of _1-syntrophin, and that phosphorylation of _1-syntrophin depends on this interaction identifies a novel mechanism for targeting a protein kinase to its substrates. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67065 |
Ser201 |
PLQRQPSsPGPTPRN |
Homo sapiens |
|
| pmid |
sentence |
| 10212242 |
Sapk3 phosphorylates alpha1-syntrophin at serine residues 193 and 201 in vitro and phosphorylation is dependent on binding to the pdz domain of alpha1-syntrophin. The finding that sapk3 co-localizes with _1-syntrophin in skeletal muscle, that it binds to the pdz domain of _1-syntrophin, and that phosphorylation of _1-syntrophin depends on this interaction identifies a novel mechanism for targeting a protein kinase to its substrates. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
MAPK12 | up-regulates activity
phosphorylation
|
MYOD1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276274 |
Ser200 |
YSGDSDAsSPRSNCS |
Mus musculus |
C3H10T1/2 Clone 8 Cell |
| pmid |
sentence |
| 20026657 |
We determined that p38-gamma directly phosphorylated MyoD on Ser199 and Ser200, which results in enhanced occupancy of MyoD on the promoter of myogenin together with markedly decreased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276273 |
Ser201 |
SGDSDASsPRSNCSD |
Mus musculus |
C3H10T1/2 Clone 8 Cell |
| pmid |
sentence |
| 20026657 |
We determined that p38-gamma directly phosphorylated MyoD on Ser199 and Ser200, which results in enhanced occupancy of MyoD on the promoter of myogenin together with markedly decreased transcriptional activity. Phosphorylation of MyoD by p38-γ directs the assembly of a repressive transcriptional complex at the Myogenin promoter. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
MAPK12 | down-regulates quantity by destabilization
phosphorylation
|
NUP62 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277416 |
Ser272 |
SGTSTTTsTAATATA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30401435 |
We further show that imidazole propionate impairs insulin signaling at the level of insulin receptor substrate through the activation of p38γ MAPK, which promotes p62 phosphorylation and, subsequently, activation of mechanistic target of rapamycin complex 1 (mTORC1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277415 |
Thr269 |
GAASGTStTTSTAAT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30401435 |
We further show that imidazole propionate impairs insulin signaling at the level of insulin receptor substrate through the activation of p38γ MAPK, which promotes p62 phosphorylation and, subsequently, activation of mechanistic target of rapamycin complex 1 (mTORC1). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK12 |
phosphorylation
|
SH3BP5 |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250140 |
Ser351 |
PGSLDLPsPVSLSEF |
in vitro |
|
| pmid |
sentence |
| 15158451 |
Activated SAPK3 phosphorylates the mitochondrial protein Sab. we have identified serine 321 as the major site of phosphorylation by both SAPK3 and JNK2. SAPK3 but not JNK2 also phosphorylates serine 391 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250141 |
Ser421 |
SKSQSSTsPEGQALE |
in vitro |
|
| pmid |
sentence |
| 15158451 |
Activated SAPK3 phosphorylates the mitochondrial protein Sab. we have identified serine 321 as the major site of phosphorylation by both SAPK3 and JNK2. SAPK3 but not JNK2 also phosphorylates serine 391 |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPK12 |
phosphorylation
|
EEF2K |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250137 |
Ser396 |
TFDSLPSsPSSATPH |
in vitro |
|
| pmid |
sentence |
| 12171600 |
We have also shown that JNK11, JNK22 and SAPK3 p38 phosphorylate eEF2 kinase very poorly at Ser-396 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK12 | down-regulates activity
phosphorylation
|
MAPT |
0.504 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250084 |
Ser519 |
SGYSSPGsPGTPGSR |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250085 |
Ser637 |
VDLSKVTsKCGSLGN |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250086 |
Thr498 |
KTPPAPKtPPSSGEP |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250087 |
Thr522 |
SSPGSPGtPGSRSRT |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250088 |
Thr548 |
KKVAVVRtPPKSPSS |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
MAPK12 | down-regulates activity
phosphorylation
|
CARM1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255897 |
Ser595 |
GPAISMAsPMSIPTN |
Mus musculus |
|
| pmid |
sentence |
| 29681515 |
Here, we identify a role for the mitogen-activated protein kinase (MAPK) p38g/MAPK12 as a critical regulator of satellite stem cell fate through phosphorylation of Carm1. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK12 | up-regulates
phosphorylation
|
KRT8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114067 |
Ser74 |
TVNQSLLsPLVLEVD |
Homo sapiens |
|
| pmid |
sentence |
| 11788583 |
Keratin 8 (k8) serine 73 occurs within a relatively conserved type ii keratin motif . Here we show that ser-73 is exclusively phosphorylated in vitro by p38 mitogen-activated protein kinase. The ser-73 --> ala-associated filament reorganization defect is rescued by a ser-73 --> asp mutation. Also, disease-causing keratin mutations can modulate keratin phosphorylation and organization, which may affect disease pathogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK12 | down-regulates activity
phosphorylation
|
TP53BP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264448 |
Thr1609 |
LGPYEAVtPLTKAAD |
in vitro |
|
| pmid |
sentence |
| 24703952 |
Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif.|Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks |phosphorylation of T1609 is likely to be mediated by p38 MAPK |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAP2K6 | up-regulates
phosphorylation
|
MAPK12 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184134 |
Thr183 |
RQADSEMtGYVVTRW |
Homo sapiens |
|
| pmid |
sentence |
| 19230643 |
Mapkk6 was shown to phosphorylate and specifically activate the p38/mpk2 sub of the mitogen-activated protein kinase superfamily . the p38 mapkinasekinasemkk6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma mapkinaseisoforms . p38mapks are activated by dual phosphorylation on a t-x-y motif in the activation loop through the action of map kinase kinases |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184138 |
Tyr185 |
ADSEMTGyVVTRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 19230643 |
Mapkk6 was shown to phosphorylate and specifically activate the p38/mpk2 sub of the mitogen-activated protein kinase superfamily . the p38 mapkinasekinasemkk6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma mapkinaseisoforms . p38mapks are activated by dual phosphorylation on a t-x-y motif in the activation loop through the action of map kinase kinases |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates
dephosphorylation
|
MAPK12 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135976 |
Thr183 |
RQADSEMtGYVVTRW |
Homo sapiens |
|
| pmid |
sentence |
| 15870257 |
Ppm1d selectively inhibits p38 activation by dephosphorylating thr 180. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNTB1 | down-regulates
binding,
|
MAPK12 |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255901 |
|
|
Mus musculus |
Satellite Cell |
| pmid |
sentence |
| 29681515 |
Basal localization of the p38g/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through b1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38g/b1-syntrophin interactions are abrogated, resulting in enhanced Carm1 phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255903 |
|
|
Mus musculus |
Satellite Cell |
| pmid |
sentence |
| 29681515 |
[...] suggesting that, during an asymmetric cell division, p38gamma localization would be basally restricted by the DGC complex via its interaction with beta-1-syntrophin. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
TRIM27 | up-regulates 
|
MAPK12 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102025 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12807881 |
We found rfp-mediated activation of both exogenous and endogenous forms of the other stress-activated mapk, p38. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
MAPK12 | up-regulates quantity by expression
transcriptional regulation
|
Satellite_cells_self-renewal |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255902 |
|
|
Mus musculus |
Satellite Cell |
| pmid |
sentence |
| 29681515 |
[...] we observed a significant diminution in the number of symmetric satellite stem cell (YFP–) divisions in p38 gamma siRNA-treated fibers, suggesting that p38 gamma is required for symmetric stem cell maintenance. Thus, loss of p38gamma greatly skewed the ratio of asymmetric to symmetric satellite stem cell divisions to favor asymmetric divisions and myogenic commitment at the expense of self-renewal |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
MAPK12 | up-regulates
phosphorylation
|
ATF2 |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65589 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10085140 |
Our results indicate that atf-2 not only directly binds to smad3/4 hetero-oligomers but also that atf-2 is phosphorylated by tgf-beta signaling via tak1 and p38. The two pathways, smad and tak1, synergistically enhance the activity of atf-2 which acts as their common nuclear target |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNFRSF17 | up-regulates
|
MAPK12 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79498 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10903733 |
Overexpression of bcma activates the p38 mapk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAP2K3 | up-regulates
phosphorylation
|
MAPK12 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83718 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11062067 |
Mkk3, mkk4 and mkk6 all show a strong preference for phosphorylation of the tyrosine residue of the thr-gly-tyr motifs in their known substrates sapk2a/p38, sapk3/p38 gamma and sapk4/p38 delta. we therefore examined the phosphorylation of sapk2a/p38, sapk3/p38? And sapk4/p38? By mkk3, mkk4 and mkk6, which are all known to be capable of activating these enzymes in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK12 | up-regulates quantity by expression
transcriptional regulation
|
JUNB |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67532 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10330170 |
Moreover, in addition to jnk, erk5, p38alpha, and p38gamma were found to stimulate the c-jun promoter by acting on distinct responsive elements. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK12 | form complex 
binding
|
MAPK12/CARM1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255981 |
|
|
|
|
| pmid |
sentence |
| 29681515 |
Basal localization of the p38γ/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through β1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38γ/β1-syntrophin interactions are abrogated |
|
| Publications: |
1 |
3.0
MAPK12
- 
- 