+ |
MAPK9 | up-regulates quantity by stabilization
phosphorylation
|
PIN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277563 |
Ser115 |
SQFSDCSsAKARGDL |
Homo sapiens |
Cholangiocarcinoma Cell Line |
pmid |
sentence |
34048060 |
Mechanistically, the JNK kinases directly bind to and phosphorylate PIN1 at Ser115, and this phosphorylation prevents PIN1 mono-ubiquitination at Lys117 and its proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
H2AX |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160210 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
pmid |
sentence |
18158901 |
H2ax interacts with numerous proteins required for dna damage signaling and repair when phosphorylated on ser-140. Phosphorylation of ser-140 (h2ax139ph) in response to ionizing radiation is mediated by both atm and prkdc. Our data showed that h2ax is phosphorylated by uva-activated jnk. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
TOB1 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-91067 |
Ser152 |
PASSVSSsPSPPFGH |
Homo sapiens |
|
pmid |
sentence |
12151396 |
Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-88744 |
Ser154 |
SSVSSSPsPPFGHSA |
Homo sapiens |
|
pmid |
sentence |
12050114 |
Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-91071 |
Ser154 |
SSVSSSPsPPFGHSA |
Homo sapiens |
|
pmid |
sentence |
12151396 |
Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-88748 |
Ser164 |
FGHSAAVsPTFMPRS |
Homo sapiens |
|
pmid |
sentence |
12050114 |
Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-91075 |
Ser164 |
FGHSAAVsPTFMPRS |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
12151396 |
Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
BAZ1B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188168 |
Ser158 |
KSDGACDsPSSDKEN |
Homo sapiens |
|
pmid |
sentence |
19776015 |
Wstf, a specific component of two chromatin remodeling complexes (swi/snf-type winac and iswi-type wich), was phosphorylated by the stimulation of mapk cascades in vitro and in vivo. Ser-158 residue in the wac (wstf/acf1/cbpq46) domain, located close to the n terminus of wstf, was identified as a major phosphorylation target |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation, relocalization
|
NFATC3 |
0.698 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53364 |
Ser163 |
SYRESSLsPSPASSI |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
9374467 |
Ser163 and ser165 represent the major sites of in vitro phosphorylation of nfat4 by jnk. / the negative regulation of nfat4 nuclear accumulation caused by jnk provides a mechanism for cell type?specific Responses to extracellular stimulation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53368 |
Ser165 |
RESSLSPsPASSISS |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
9374467 |
Ser163 and ser165 represent the major sites of in vitro phosphorylation of nfat4 by jnk. / the negative regulation of nfat4 nuclear accumulation caused by jnk provides a mechanism for cell type?specific Responses to extracellular stimulation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103360 |
|
|
Homo sapiens |
|
pmid |
sentence |
14517246 |
Jnks directly phosphorylate nuclear factor of activated t-cell (nfat) transcription factors, thus antagonizing the effects of calcium-regulated signaling through the protein phosphatase calcineurin. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
CDC25C |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164093 |
Ser168 |
SEMKYLGsPITTVPK |
Homo sapiens |
|
pmid |
sentence |
20220133 |
Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
YWHAZ |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124031 |
Ser184 |
FYYEILNsPEKACSL |
Homo sapiens |
|
pmid |
sentence |
15071501 |
Jnk phosphorylates 14-3-3zetaat ser-184 and 14-3-3sigmaat ser-188 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
SFN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124027 |
Ser186 |
FHYEIANsPEEAISL |
Homo sapiens |
|
pmid |
sentence |
15071501 |
Jnk phosphorylates 14-3-3zeta_ at ser-184 and 14-3-3sigma_ at ser-189 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
CTNNB1 |
0.657 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178258 |
Ser191 |
SRHAIMRsPQMVSAI |
Homo sapiens |
|
pmid |
sentence |
18423204 |
Beta-catenin, upon entering the nucleus, in turn activates transcription of downstream target genes. Jnk2 phosphorylates Beta-catenin on critical residues (ser191 and ser605). Jnk activity is required for Beta-catenin nuclear localization in response to wnt. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178262 |
Ser605 |
LFVQLLYsPIENIQR |
Homo sapiens |
|
pmid |
sentence |
18423204 |
Beta-catenin, upon entering the nucleus, in turn activates transcription of downstream target genes. Jnk2 phosphorylates Beta-catenin on critical residues (ser191 and ser605). Jnk activity is required for Beta-catenin nuclear localization in response to wnt. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
TP53 |
0.738 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-115835 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
|
pmid |
sentence |
11896587 |
These findings strongly suggest that jnks are the major direct signaling mediators of uvb-induced p53 phosphorylation at serine 20. furthermore, phosphorylation of p53 at serine 20 by uvb-activated jnks and uvb-induced p53-dependent transcriptional activity were suppressed in jnk1 or jnk2 knockout (jnk1(-/-) or jnk2(-/-)) cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155209 |
Ser6 |
sDPSVEPP |
Homo sapiens |
|
pmid |
sentence |
17525747 |
Our studies revealed a novel mechanism in which phosphorylation of jnk2 is mediated by jnk1 before phosphorylation of p53, and then p53 is directly phosphorylated by jnk2 at ser6. |Role of map kinases in uvb-induced phosphorylation of p53 at serine 20. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates activity
phosphorylation
|
RXRA |
0.249 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145301 |
Ser260 |
NMGLNPSsPNDPVTN |
Homo sapiens |
|
pmid |
sentence |
16551633 |
Under stress conditions, hyperphosphorylated by activated jnk on ser-56, ser-70, thr-82 and ser-260. These findings indicate that inflammation-mediated cell signaling leads to rapid and profound reductions in nuclear rxralpha levels, via a multistep, jnk-dependent mechanism involving ser260, nuclear export, and proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
MFN2 |
0.358 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198054 |
Ser27 |
HMAEVNAsPLKHFVT |
Homo sapiens |
|
pmid |
sentence |
22748923 |
Jnk phosphorylation of mitofusin 2 in response to cellular stress leads to recruitment of the ubiquitin ligase (e3) huwe1/mule/arf-bp1/hecth9/e3histone/lasu1 to mitofusin 2, with the bh3 domain of huwe1 implicated in this interaction. This results in ubiquitin-mediated proteasomal degradation of mitofusin 2these data establish that mfn2 is phosphorylated on ser27 in response to a variety of cellular stresses and implicate jnk in this process |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
IRS1 |
0.698 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118881 |
Ser307 |
TRRSRTEsITATSPA |
Homo sapiens |
|
pmid |
sentence |
14579029 |
Map kinases and mtor mediate insulin-induced phosphorylation ofinsulinreceptor substrate-1 on serine residues 307, 612 and 632 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-52696 |
Ser315 |
ITATSPAsMVGGKPG |
Homo sapiens |
|
pmid |
sentence |
9335553 |
These results indicate that activation of protein kinase c stimulates a kinase which can phosphorylate insulin receptor substrate-1 at serine 612, resulting in an inhibition of insulin signaling in the cell these data suggest that: 1) activation of pkctheta contributes to ikk and jnk activation by ffas;2) ikk and jnk mediate pkctheta signals for irs-1 serine phosphorylation and degradation; ser-302 phosphorylation is dependent on pi 3-kinase/mtor, whereas ser-307 depends on c-jun nh2-terminal kinase to inhibit irs1 tyrosine phosphorylation. Ser-636 is located around the pi 3-kinase binding site and, therefore, thought to inhibit pi 3-kinase signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118873 |
Tyr612 |
TLHTDDGyMPMSPGV |
Homo sapiens |
|
pmid |
sentence |
14579029 |
Map kinases and mtor mediate insulin-induced phosphorylation of insulin receptor substrate-1 on serine residues 307, 612 and 632 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118877 |
Tyr632 |
GRKGSGDyMPMSPKS |
Homo sapiens |
|
pmid |
sentence |
14579029 |
Map kinases and mtor mediate insulin-induced phosphorylation ofinsulinreceptor substrate-1 on serine residues 307, 612 and 632 |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
PSEN1 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179676 |
Ser319 |
NSKYNAEsTERESQD |
Homo sapiens |
|
pmid |
sentence |
18667537 |
This jnk phosphorylation of ps1 at ser(319)thr(320) enhances the stability of the ps1 c-terminal fragment that is necessary for gamma-secretase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179680 |
Thr320 |
SKYNAEStERESQDT |
Homo sapiens |
|
pmid |
sentence |
18667537 |
This jnk phosphorylation of ps1 at ser(319)thr(320) enhances the stability of the ps1 c-terminal fragment that is necessary for gamma-secretase activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK9 |
phosphorylation
|
SH3BP5 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250142 |
Ser351 |
PGSLDLPsPVSLSEF |
in vitro |
|
pmid |
sentence |
15158451 |
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: |
1 |
Organism: |
In Vitro |
+ |
MAPK9 | down-regulates
phosphorylation
|
STMN1 |
0.259 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166698 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
pmid |
sentence |
20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates activity
phosphorylation
|
ELK1 |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-247062 |
Ser389 |
LSPIAPRsPAKLSFQ |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
8846788 |
However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 |
phosphorylation
|
MAPK9 |
0.222 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83711 |
Ser407 |
STEQTLAsDTDSSLD |
Homo sapiens |
|
pmid |
sentence |
11062067 |
The phosphorylation of thr-404 and ser-407 is not increased in response to other agonists that activate mkk7 and sapk1/jnk, suggesting that phosphorylation of these residues is catalysed by another protein kinase, such as ck2, which also phosphorylates thr-404 and ser-407 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83715 |
Thr404 |
SSMSTEQtLASDTDS |
Homo sapiens |
|
pmid |
sentence |
11062067 |
The phosphorylation of thr-404 and ser-407 is not increased in response to other agonists that activate mkk7 and sapk1/jnk, suggesting that phosphorylation of these residues is catalysed by another protein kinase, such as ck2, which also phosphorylates thr-404 and ser-407 in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAP2K7 | up-regulates activity
phosphorylation
|
MAPK9 |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251416 |
Ser407 |
STEQTLAsDTDSSLD |
in vitro |
|
pmid |
sentence |
11062067 |
MKK7 also phosphorylates JNK2 alpha 2 at Thr-404 and Ser-407 in vitro. Stress-activated protein kinase 1 (SAPK1), also called c-Jun N-terminal kinase (JNK), becomes activated in vivo in response to pro-inflammatory cytokines or cellular stresses. Its full activation requires the phosphorylation of a threonine and a tyrosine residue in a Thr-Pro-Tyr motif, which can be catalysed by the protein kinases mitogen-activated protein kinase kinase (MKK)4 and MKK7. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251417 |
Thr183 |
ACTNFMMtPYVVTRY |
in vitro |
|
pmid |
sentence |
11062067 |
MKK7 phosphorylates SAPK2a p38 exclusively at Tyr-182. Stress-activated protein kinase 1 (SAPK1), also called c-Jun N-terminal kinase (JNK), becomes activated in vivo in response to pro-inflammatory cytokines or cellular stresses. Its full activation requires the phosphorylation of a threonine and a tyrosine residue in a Thr-Pro-Tyr motif, which can be catalysed by the protein kinases mitogen-activated protein kinase kinase (MKK)4 and MKK7. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251418 |
Thr404 |
SSMSTEQtLASDTDS |
in vitro |
|
pmid |
sentence |
11062067 |
MKK7 also phosphorylates JNK2 alpha 2 at Thr-404 and Ser-407 in vitro. Stress-activated protein kinase 1 (SAPK1), also called c-Jun N-terminal kinase (JNK), becomes activated in vivo in response to pro-inflammatory cytokines or cellular stresses. Its full activation requires the phosphorylation of a threonine and a tyrosine residue in a Thr-Pro-Tyr motif, which can be catalysed by the protein kinases mitogen-activated protein kinase kinase (MKK)4 and MKK7. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
MAPK9 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250134 |
Ser59 |
GDSCPHGsPQGPLAP |
|
|
pmid |
sentence |
12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250135 |
Ser77 |
PGPFATRsPLFIFMR |
|
|
pmid |
sentence |
12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
Publications: |
2 |
+ |
MAPK9 | up-regulates
phosphorylation
|
MYC |
0.368 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-72104 |
Ser62 |
LLPTPPLsPSRRSGL |
Homo sapiens |
|
pmid |
sentence |
10551811 |
The jnk pathway is selectively involved in the c-myc-mediated apoptosis and that the apoptotic function of c-myc is directly regulated by jnk pathway through phosphorylation at ser-62 and ser-71. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-72108 |
Ser71 |
SRRSGLCsPSYVAVT |
Homo sapiens |
|
pmid |
sentence |
10551811 |
The jnk pathway is selectively involved in the c-myc-mediated apoptosis and that the apoptotic function of c-myc is directly regulated by jnk pathway through phosphorylation at ser-62 and ser-71. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation, binding
|
JUN |
0.881 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183017 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
pmid |
sentence |
19118012 |
Phosphorylation by activated jnk protects c-jun from ubiquitination;phosphorylation of c-jun on ser73 by jnk is sufficient to protect c-jun from ubiquitination c-jun is targeted for ubiquitination by its association with inactive c-jun nh2-terminal kinase (jnk). Phosphorylation by activated jnk protects c-jun from ubiquitination, thus by prolonging its half-life targets of the jnk signal transduction pathway include the transcription factors atf2 and c-jun apoptosis, altered;apoptosis, induced;transcription, altered;cell growth, altered;jnk1(disrupts);pin1(induces);dna(disrupts) transcription, altered;cell growth, altered;jnk1(disrupts);pin1(induces);dna(disrupts) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-88208 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
Neuron |
pmid |
sentence |
12040039 |
Stress in primary cultured cns neurons induces phosphorylation of c-jun serines 63 and 73 and increased c-jun protein. Jnk2/3 activity selectively targets c-jun. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-88212 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
Neuron |
pmid |
sentence |
12040039 |
Stress in primary cultured cns neurons induces phosphorylation of c-jun serines 63 and 73 and increased c-jun protein. Jnk2/3 activity selectively targets c-jun. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53791 |
|
|
Homo sapiens |
|
pmid |
sentence |
9405416 |
C-jun is targeted for ubiquitination by its association with inactive c-jun nh2-terminal kinase (jnk).Phosphorylation By activated jnk protects c-jun from ubiquitination. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250136 |
Ser69 |
GPLAPPAsPGPFATR |
|
|
pmid |
sentence |
18174237 |
Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome. |
|
Publications: |
1 |
+ |
MAPK9 | up-regulates
phosphorylation
|
STAT3 |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179275 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
|
pmid |
sentence |
18691976 |
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates activity
phosphorylation
|
ATN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-102402 |
Ser739 |
EEYETPEsPVPPARS |
Homo sapiens |
|
pmid |
sentence |
12812981 |
Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-jun nh2-terminal kinase. serine 734 of the drpla protein is a phospho-acceptor site by jnk. The phosphorylation may be coupled to the activation of a protease. The molecular size of drpla protein detected in the rat brain with the specific phosphopeptide antibody was 150_kda, which was slightly smaller than that expected from the sequence and the results with the human protein. The phosphorylated forms of ha-tagged human drpla gradually disappeared after osmotic treatment, |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
MAPK9 | down-regulates
phosphorylation
|
PPM1J |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178934 |
Ser93 |
HAGRAVQsPPDTGRR |
Homo sapiens |
|
pmid |
sentence |
18553930 |
Specific phosphorylation of pp2czeta at ser (92) by stress-activated jnk attenuates its phosphatase activity in cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates activity
phosphorylation
|
MAPK8IP1 |
0.765 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-101201 |
Thr103 |
LIDATGDtPGAEDDE |
Homo sapiens |
COS-7 Cell |
pmid |
sentence |
12756254 |
Recruitment of jnk to jip1 and jnk-dependent jip1 phosphorylation regulates jnk module dynamics and activation it was observed that phosphorylation by jnk of jip1 on thr-103 and not other phosphorylated jip1 residues is necessary for the regulation of dlk association with jip1, dlk activation, and subsequent module activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP2K7 | up-regulates
phosphorylation
|
MAPK9 |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83744 |
Thr183 |
ACTNFMMtPYVVTRY |
Homo sapiens |
|
pmid |
sentence |
11062067 |
Here we report that mkk4 shows a striking preference for the tyrosine residue (tyr-185), and mkk7 a striking preference for the threonine residue (thr-183) in three sapk1/jnk1 isoforms tested (jnk1 alpha 1, jnk2 alpha 2 and jnk3 alpha 1). These results indicate that hgk, a novel activator of the jnk pathway, may function through tak1, and that the hgk --> tak1 --> mkk4, mkk7 --> jnk kinase cascade may mediate the TNF-alphalpha signaling pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-63976 |
Thr183 |
ACTNFMMtPYVVTRY |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
9890973 |
Here we report that mkk4 shows a striking preference for the tyrosine residue (tyr-185), and mkk7 a striking preference for the threonine residue (thr-183) in three sapk1/jnk1 isoforms tested (jnk1 alpha 1, jnk2 alpha 2 and jnk3 alpha 1). These results indicate that hgk, a novel activator of the jnk pathway, may function through tak1, and that the hgk --> tak1 --> mkk4, mkk7 --> jnk kinase cascade may mediate the TNF-alphalpha signaling pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83748 |
Tyr185 |
TNFMMTPyVVTRYYR |
Homo sapiens |
|
pmid |
sentence |
11062067 |
In the present study, we found that mkk7 phosphorylates sapk2a/p38 exclusively at tyr-182, albeit at a low rate. Therefore one possibility is that the interaction of mkk7 and/or sapk1/jnk with another cellular protein alters the conformation of one of these enzymes in such a way as to facilitate phosphorylation of tyr-185 by mkk7 in vivo. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
MAP2K4 | up-regulates
phosphorylation
|
MAPK9 |
0.716 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260615 |
Thr183 |
ACTNFMMtPYVVTRY |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17761173 |
We next examined whether the phosphorylation of JNK at threonine 183 (Thr183) and tyrosine 185 (Tyr185) was enhanced by GRASP‐1 expression. Phosphorylation of Thr183 and Tyr185 by SEK1/MKK4, which is in turn phosphorylated and activated by several kinases including MEKK1, is known to activate JNK1/2/3 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197998 |
Tyr185 |
TNFMMTPyVVTRYYR |
Homo sapiens |
|
pmid |
sentence |
22730327 |
Mkk4, which activates p38gamma, p38delta, and jnk2 to phosphorylate p53 on ser-33 and cause a transient g(1) arrest. A map kinase kinase kinase (mapkkk), termed ask1, was identified that activated two different subs of map kinase kinases (mapkk), sek1 (or mkk4) and mkk3/mapkk6 (or mkk6), which in turn activated stress-activated protein kinase (sapk, also known as jnk;c-jun amino-terminal kinase) here we report that mkk4 shows a striking preference for the tyrosine residue (tyr-185), and mkk7 a striking preference for the threonine residue (thr-183) in three sapk1/jnk1 isoforms tested (jnk1 alpha 1, jnk2 alpha 2 and jnk3 alpha 1) |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Breast, Prostate Gland |
+ |
MAPK9 | down-regulates
phosphorylation
|
RRN3 |
0.487 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134878 |
Thr200 |
IARYVPStPWFLMPI |
Homo sapiens |
|
pmid |
sentence |
15805466 |
Inactivation is due to phosphorylation of tif-ia by c-jun n-terminal kinase (jnk) at a single threonine residue (thr 200). Phosphorylation at thr 200 impairs the interaction of tif-ia with pol i and the tbp-containing factor tif-ib/sl1, thereby abrogating initiation complex formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
MAPK8IP3 |
0.652 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134568 |
Thr265 |
GQSSAAAtPSTTGTK |
Homo sapiens |
|
pmid |
sentence |
15767678 |
Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134572 |
Thr275 |
TTGTKSNtPTSSVPS |
Homo sapiens |
|
pmid |
sentence |
15767678 |
Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134576 |
Thr286 |
SVPSAAVtPLNESLQ |
Homo sapiens |
|
pmid |
sentence |
15767678 |
Phosphoamino acid analysis confirmed that jnk caused thr phosphorylation of jip3 (fig. _(fig.3c).3c). This phosphorylation on thr was markedly decreased when thr266, thr276, and thr287 were replaced with ala. These data indicate that jnk phosphorylated jip3 on thr266, thr276, and thr287 in vitro. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
phosphorylation
|
ATF2 |
0.686 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163262 |
Thr69 |
SVIVADQtPTPTRFL |
Homo sapiens |
|
pmid |
sentence |
20068231 |
Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-32429 |
Thr69 |
SVIVADQtPTPTRFL |
Homo sapiens |
|
pmid |
sentence |
7737130 |
Stimulation of atf-2-dependent transactivation by genotoxic agents requires the presence of threonines 69 and 71 located in the n-terminal transactivation domain. These sites are the target of p54 and p46 stress-activated protein kinases (sapks) which bind to, and phosphorylate atf-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-32433 |
Thr71 |
IVADQTPtPTRFLKN |
Homo sapiens |
|
pmid |
sentence |
7737130 |
Stimulation of atf-2-dependent transactivation by genotoxic agents requires the presence of threonines 69 and 71 located in the n-terminal transactivation domain. These sites are the target of p54 and p46 stress-activated protein kinases (sapks) which bind to, and phosphorylate atf-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163266 |
Thr71 |
IVADQTPtPTRFLKN |
Homo sapiens |
|
pmid |
sentence |
20068231 |
Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP2 | up-regulates
binding
|
MAPK9 |
0.556 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70866 |
|
|
Homo sapiens |
|
pmid |
sentence |
10490659 |
These experiments demonstrated that 10 different jnk isoforms bound to both jip proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
anthra[1,9-cd]pyrazol-6(2H)-one | down-regulates
chemical inhibition
|
MAPK9 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111986 |
|
|
Homo sapiens |
|
pmid |
sentence |
11717429 |
We report the identification of an anthrapyrazolone series with significant jnk1, -2, and -3 (k(i) = 0.19 microm). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP3 | up-regulates
binding
|
MAPK9 |
0.652 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134561 |
|
|
Homo sapiens |
|
pmid |
sentence |
15767678 |
The c-jun nh2-terminal kinase (jnk)-interacting protein (jip) group of scaffold proteins (jip1, jip2, and jip3) can interact with components of the jnk signaling pathway and potently activate jnk. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DUSP4 | down-regulates
dephosphorylation
|
MAPK9 |
0.601 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-40929 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
8626452 |
We assayed the relative ability of mkp-2, pac1, and mkp-1 to dephosphorylate erk2 and the other related map kinases, jnk2 and p38. . Mkp-2 had detectable activity against jnk2, although full inactivation of jnk2 was not observed even at the higher phosphatase concentration. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8 | up-regulates
phosphorylation
|
MAPK9 |
0.574 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155205 |
|
|
Homo sapiens |
|
pmid |
sentence |
17525747 |
Our studies revealed a novel mechanism in which phosphorylation of jnk2 is mediated by jnk1 before phosphorylation of p53, and then p53 is directly phosphorylated by jnk2 at ser6. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
phosphorylation
|
NFATC2 |
0.557 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118223 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
14517246 |
Jnks directly phosphorylate nuclear factor of activated t-cell (nfat) transcription factors, thus antagonizing the effects of calcium-regulated signaling through the protein phosphatase calcineurin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP3K11 | up-regulates
|
MAPK9 |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-59884 |
|
|
Homo sapiens |
|
pmid |
sentence |
9733513 |
This scaffold protein selectively enhanced jnk activation by the mlk signaling pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IL1R1 | up-regulates activity
phosphorylation
|
MAPK9 |
0.286 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249514 |
|
|
Homo sapiens |
Macrophage |
pmid |
sentence |
9625767 |
Il-1 binding to its receptor triggers a cascade of signaling events, including activation of the stress-activated mitogen-activated protein (map) kinases, c-jun nh2-terminal kinase (jnk) and p38 map kinase, as well as transcription factor nuclear factor kappab (nf-kappab |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP1 | down-regulates
binding
|
MAPK9 |
0.765 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70854 |
|
|
Homo sapiens |
|
pmid |
sentence |
10490659 |
These experiments demonstrated that 10 different jnk isoforms bound to both jip proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-3-[(5-nitro-2-thiazolyl)thio]-1H-1,2,4-triazol-5-one | down-regulates
chemical inhibition
|
MAPK9 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-181650 |
|
|
Homo sapiens |
|
pmid |
sentence |
18922779 |
Bi-78d3, dose-dependently inhibits the phosphorylation of jnk substrates both in vitro and in cell. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP2K6 | up-regulates
phosphorylation
|
MAPK9 |
0.451 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45369 |
|
|
Homo sapiens |
|
pmid |
sentence |
8974401 |
A map kinase kinase kinase (mapkkk), termed ask1, was identified that activated two different subs of map kinase kinases (mapkk), sek1 (or mkk4) and mkk3/mapkk6 (or mkk6), which in turn activated stress-activated protein kinase (sapk, also known as jnk;c-jun amino-terminal kinase) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNFRSF17 | up-regulates
|
MAPK9 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-79507 |
|
|
Homo sapiens |
|
pmid |
sentence |
10903733 |
Overexpression of bcma activates jnk |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DUSP1 | down-regulates
dephosphorylation
|
MAPK9 |
0.671 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-40879 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
8626452 |
We assayed the relative ability of mkp-2, pac1, and mkp-1 to dephosphorylate erk2 and the other related map kinases, jnk2 and p38. the dual specific phosphatases pac1 and mkp-1 previously have been implicated in the in vivo inactivation of erk or of erk and jnk, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates
binding
|
JUNB |
0.671 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53827 |
|
|
Homo sapiens |
|
pmid |
sentence |
9405416 |
Jnk targets junb ubiquitination |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | up-regulates
|
BAX |
0.303 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124023 |
|
|
Homo sapiens |
|
pmid |
sentence |
15071501 |
Demonstrate that jnk-mediated phosphorylation of 14-3-3 induces the release of bax from 14-3-3 and triggers its translocation to the mitochondria;these results strongly indicate that jnk regulates the activity of bax by phosphorylating 14-3-3 proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK9 | down-regulates activity
phosphorylation
|
ELK3 |
0.328 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250138 |
|
|
|
|
pmid |
sentence |
11042694 |
JNK binds to the J box in the middle of the protein, and binding is required for phosphorylation of the adjacent EXport motif. Both the binding and phosphorylation sites (the JEX element) are important for Net export. |
|
Publications: |
1 |
+ |
RAC1 | up-regulates
binding
|
MAPK9 |
0.503 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178265 |
|
|
Homo sapiens |
|
pmid |
sentence |
18423204 |
We show that rac1 activates jnk2 that in turn phosphorylates beta-catenin on critical residues and controls its nuclear translocation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |