+ |
MAPK10 | down-regulates
phosphorylation
|
CDC25C |
0.247 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164085 |
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 |
+ |
MAPK10 | down-regulates
phosphorylation
|
NFATC1 |
0.425 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-74556 |
Ser172 |
YRDPSCLsPASSLSS |
Homo sapiens |
|
pmid |
sentence |
10652349 |
We show that jnk, erk, and p38 physically associate with the nfatc n-terminal regulatory domain and can directly phosphorylate functionally important residues involved in regulating nfatc subcellular localization, namely ser(172) and the conserved nfatc ser-pro repeats. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | down-regulates activity
phosphorylation
|
KIF5C |
0.326 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262950 |
Ser176 |
CTERFVSsPEEVMDV |
in vitro |
|
pmid |
sentence |
19525941 |
Mass spectrometry identified a residue in the kinesin-1 motor domain that was phosphorylated by JNK3 and this modification reduced kinesin-1 binding to microtubules. JNK3 phosphorylates kinesin-1 at Ser176 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPK10 | down-regulates
phosphorylation
|
YWHAZ |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124009 |
Ser184 |
FYYEILNsPEKACSL |
Homo sapiens |
|
pmid |
sentence |
15071501 |
Jnk phosphorylates 14-3-3zetaat ser-184 and 14-3-3sigmaat ser-190 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | down-regulates
phosphorylation
|
SFN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124005 |
Ser186 |
FHYEIANsPEEAISL |
Homo sapiens |
|
pmid |
sentence |
15071501 |
Here we demonstrate that activated jnk promotes bax translocation to mitochondria through phosphorylation of 14-3-3, a cytoplasmic anchor of bax. Phosphorylation of 14-3-3 led to dissociation of bax from this protein.Jnk phosphorylates 14-3-3zeta_ at ser-184 and 14-3-3sigma_ at ser-191 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | up-regulates activity
phosphorylation
|
HNRNPK |
0.345 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250081 |
Ser216 |
ILDLISEsPIKGRAQ |
Homo sapiens |
|
pmid |
sentence |
11259409 |
JNK Phosphorylation of HnRNP K Increases Its Transcriptional Activity. the primary site for JNK phosphorylation consists of serines 216 and 353 on the K protein. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250083 |
Ser353 |
DSAIDTWsPSEWQMA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11259409 |
JNK Phosphorylation of HnRNP K Increases Its Transcriptional Activity. the primary site for JNK phosphorylation consists of serines 216 and 353 on the K protein. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | down-regulates activity
phosphorylation
|
HNRNPK |
0.345 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250082 |
Ser284 |
RRDYDDMsPRRGPPP |
|
|
pmid |
sentence |
11231586 |
Mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) efficiently phosphorylates hnRNP-K both in vitro and in vivo at serines 284 and 353. Our results establish the role of MAPK/ERK in phosphorylation-dependent cellular localization of hnRNP-K, which is required for its ability to silence mRNA translation. |
|
Publications: |
1 |
+ |
MAPK10 | down-regulates
phosphorylation
|
STMN1 |
0.307 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166690 |
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 |
+ |
MAPK10 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.677 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250130 |
Ser59 |
GDSCPHGsPQGPLAP |
Mus musculus |
|
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-250131 |
Ser77 |
PGPFATRsPLFIFMR |
Mus musculus |
|
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 |
Organism: |
Mus Musculus |
+ |
MAPK10 | down-regulates
phosphorylation
|
STMN2 |
0.455 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112110 |
Ser62 |
ELILKPPsPISEAPR |
Homo sapiens |
|
pmid |
sentence |
11718727 |
We demonstrate that purified scg10 can be phosphorylated by two subclasses of mitogen-activated protein (map) kinases, c-jun n-terminal/stress-activated protein kinase (jnk/sapk) and p38 map kinase;jnk3/sapkbeta phosphorylation occurs at ser-62 and ser-73, residues that result in reduced microtubule-destabilizing activity for scg10. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112114 |
Ser73 |
EAPRTLAsPKKKDLS |
Homo sapiens |
|
pmid |
sentence |
11718727 |
We demonstrate that purified scg10 can be phosphorylated by two subclasses of mitogen-activated protein (map) kinases, c-jun n-terminal/stress-activated protein kinase (jnk/sapk) and p38 map kinase;jnk3/sapkbeta phosphorylation occurs at ser-62 and ser-73, residues that result in reduced microtubule-destabilizing activity for scg10. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | up-regulates
phosphorylation
|
JUN |
0.883 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164800 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
pmid |
sentence |
20395206 |
With epidermal growth factor treatment, overexpression of erk8 in jb6 cl41 cells caused an increased phosphorylation of c-jun at ser(63) and ser(73), resulting in increased activator protein-1 transactivation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164804 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
|
pmid |
sentence |
20395206 |
With epidermal growth factor treatment, overexpression of erk8 in jb6 cl41 cells caused an increased phosphorylation of c-jun at ser(63) and ser(73), resulting in increased activator protein-1 transactivation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.677 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250080 |
Ser69 |
GPLAPPAsPGPFATR |
in vitro |
|
pmid |
sentence |
15486195 |
Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPK10 | down-regulates activity
phosphorylation
|
ATN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-102394 |
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 |
+ |
MAPK10 | down-regulates
phosphorylation
|
PPM1J |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178926 |
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 |
+ |
MAPK10 | up-regulates
phosphorylation
|
BCL2L11 |
0.677 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178683 |
Thr116 |
SCDKSTQtPSPPCQA |
Homo sapiens |
|
pmid |
sentence |
18498746 |
Jnk is the physiogically relevant uv-stimulated kinase that phosphorylates bimel on thr-112/jnk-induced bim apoptotic activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
MAPK10 |
0.351 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250668 |
Thr131 |
ISLLNVFtPQKTLEE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11823425 |
Here, we show that cdk5 directly phosphorylates c-Jun N-terminal kinase 3 (JNK3) on Thr131 and inhibits its kinase activity, leading to reduced c-Jun phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP2K7 | up-regulates activity
phosphorylation
|
MAPK10 |
0.564 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251422 |
Thr221 |
AGTSFMMtPYVVTRY |
in vitro |
|
pmid |
sentence |
10715136 |
Activation of JNK3 alpha 1 requires both MKK4 and MKK7. both MKK4 and MKK7 were required for bisphosphorylation and maximal enzyme activity. a processive mechanism for JNK3R1 activation that requires phosphorylation of Thr 221 by MKK7 prior to phosphorylation of Tyr 223 by MKK4 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAP2K7 | up-regulates
phosphorylation
|
MAPK10 |
0.564 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137609 |
Thr221 |
AGTSFMMtPYVVTRY |
Homo sapiens |
|
pmid |
sentence |
15911620 |
Two mapkks, sek1 and mkk7, synergistically activate jnk. Sek1 prefers the tyr-185 residue, and mkk7 prefers the thr-183 residue (17, 19). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-63972 |
|
|
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-83732 |
|
|
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. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
MAP2K4 | up-regulates
phosphorylation
|
MAPK10 |
0.732 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260614 |
Thr221 |
AGTSFMMtPYVVTRY |
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-137605 |
Tyr223 |
TSFMMTPyVVTRYYR |
Homo sapiens |
|
pmid |
sentence |
15911620 |
Two mapkks, sek1 and mkk7, synergistically activate jnk. Sek1 prefers the tyr-185 residue, and mkk7 prefers the thr-183 residue (17, 19). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45360 |
|
|
Homo sapiens |
|
pmid |
sentence |
8974401 |
A map kinase kinase kinase (mapkkk), termed ask1, was identified that activated two different subgroups 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) and p38 subgroups of map kinases, respectively. 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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105692 |
|
|
Homo sapiens |
|
pmid |
sentence |
11242034 |
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) and p38 subs of map kinases, respectively. 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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83721 |
|
|
Homo sapiens |
|
pmid |
sentence |
11062067 |
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) and p38 subs of map kinases, respectively. 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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-75792 |
|
|
Homo sapiens |
|
pmid |
sentence |
10715136 |
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) and p38 subs of map kinases, respectively. 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: |
6 |
Organism: |
Homo Sapiens |
+ |
MAPK10 | up-regulates
phosphorylation
|
MAPK8IP3 |
0.738 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134529 |
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-134533 |
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-134537 |
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 |
+ |
MAPK10 | up-regulates
phosphorylation
|
APP |
0.565 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204671 |
Thr743 |
VEVDAAVtPEERHLS |
Homo sapiens |
|
pmid |
sentence |
24610780 |
Phosphorylation of amyloid precursor protein at threonine 668 is essential for its copper-responsive trafficking in sh-sy5y neuroblastoma cells. is regulated by jnk3 via phosphorylation of app at thr668 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP2K4 | up-regulates activity
phosphorylation
|
MAPK10 |
0.732 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251423 |
Tyr223 |
TSFMMTPyVVTRYYR |
in vitro |
|
pmid |
sentence |
10715136 |
Activation of JNK3 alpha 1 requires both MKK4 and MKK7. both MKK4 and MKK7 were required for bisphosphorylation and maximal enzyme activity. a processive mechanism for JNK3R1 activation that requires phosphorylation of Thr 221 by MKK7 prior to phosphorylation of Tyr 223 by MKK4 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
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
|
MAPK10 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-181644 |
|
|
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 |
+ |
MAPK10 | up-regulates
phosphorylation
|
TP53 |
0.616 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-120552 |
|
|
Homo sapiens |
|
pmid |
sentence |
14699954 |
The targets of jnk include the transcription factors p53. P75ntr-mediated apoptosis was shown to be dependent of p53 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NGFR | up-regulates
|
MAPK10 |
0.426 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-120561 |
|
|
Homo sapiens |
|
pmid |
sentence |
14699954 |
Jnk3 is expressed exclusively in the nervous system and recent evidence indicates that this jnk isoform may be required for p75ntr-mediated cell death |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP3 | up-regulates
binding
|
MAPK10 |
0.738 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134555 |
|
|
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 |
+ |
profenamine | down-regulates
chemical inhibition
|
MAPK10 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184443 |
|
|
Homo sapiens |
|
pmid |
sentence |
19261605 |
Indazole-based inhibitors exemplified by sr-3737 were potent inhibitors of both jnk3 (ic50 12 nm). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
MAPK10 | down-regulates
phosphorylation
|
DIABLO |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157280 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17686459 |
Here we demonstrate that jnk3 can phosphorylate smac. Phosphorylation of smac by jnk3 attenuates its interaction with xiap. These results suggest that jnk3 activity can attenuate the progression of apoptosis through a novel mechanism of action, the down-regulation of interaction between smac and xiap. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK14 | down-regulates
|
MAPK10 |
0.402 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166608 |
|
|
Homo sapiens |
|
pmid |
sentence |
20626350 |
Jnk and p38 mapk activation have antagonistic effects in many cases. Froma a mechanicistic point of view, the p38 mapk pathway can negatively regulate jnk activity at the level of map3ks, either by phosphorylating mlk3 or the tak1 regulatory subunit tab1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNFRSF17 | up-regulates
|
MAPK10 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-79492 |
|
|
Homo sapiens |
|
pmid |
sentence |
10903733 |
Overexpression of bcma activates jnk |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
anthra[1,9-cd]pyrazol-6(2H)-one | down-regulates
chemical inhibition
|
MAPK10 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111980 |
|
|
Homo sapiens |
|
pmid |
sentence |
11717429 |
We report the identification of an anthrapyrazolone series with significant jnk1, -2, and -3 (k(i) = 0.19 microm). To determine whether jnk activity is required for stress-induced translocation of bax to the mitochondria, we examined the effect of sp600125, a jnk inhibitor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124034 |
|
|
Homo sapiens |
|
pmid |
sentence |
15071501 |
We report the identification of an anthrapyrazolone series with significant jnk1, -2, and -3 (k(i) = 0.19 microm). To determine whether jnk activity is required for stress-induced translocation of bax to the mitochondria, we examined the effect of sp600125, a jnk inhibitor. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
IL1R1 | up-regulates activity
phosphorylation
|
MAPK10 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249515 |
|
|
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 |
+ |
MAPK10 | up-regulates
|
BAX |
0.263 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124001 |
|
|
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 |
+ |
MAP2K6 | up-regulates
phosphorylation
|
MAPK10 |
0.441 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45363 |
|
|
Homo sapiens |
|
pmid |
sentence |
8974401 |
A map kinase kinase kinase (mapkkk), termed ask1, was identified that activated two different subgroups 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 |