+ |
MAPK8 |
phosphorylation
|
MAPK8IP1 |
0.879 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250123 |
Ser15 |
GLGGGAAsPPAASPF |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250124 |
Ser197 |
DRVSRSSsPLKTGEQ |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250125 |
Ser29 |
FLGLHIAsPPNFRLT |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250126 |
Ser421 |
DNCASVSsPYESAIG |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250127 |
Thr205 |
PLKTGEQtPPHEHIC |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Publications: |
5 |
Organism: |
Chlorocebus Aethiops |
Pathways: | SAPK/JNK Signaling |
+ |
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 |
+ |
MAPK8 | up-regulates activity
phosphorylation
|
MAPK8IP1 |
0.879 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250128 |
Thr103 |
LIDATGDtPGAEDDE |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12756254 |
After mapping JNK-dependent JIP1 phosphorylation sites and testing their functional significance, 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. The data presented corroborates our previous observations using endogenous proteins, demonstrates that JNK binding to JIP1 is necessary for module activation, and shows that activation of JIP1-JNK module dynamics requires phosphorylation of JIP1 on Thr-103 by JNK. and Thr-205 are phosphorylated directly by JNK after JNK binds to JIP1. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
Pathways: | SAPK/JNK Signaling |
+ |
MAPK8IP1 | down-regulates
binding
|
MAPK8 |
0.879 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124727 |
|
|
Homo sapiens |
|
pmid |
sentence |
15141161 |
The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178655 |
|
|
Homo sapiens |
|
pmid |
sentence |
18486448 |
The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64175 |
|
|
Homo sapiens |
|
pmid |
sentence |
9922370 |
The jip proteins function by aggregating components of a map kinase module (including mlk, mkk7, and jnk) and facilitate signal transmission by the protein kinase cascade. Overexpression of jip1 deactivates the jnk pathway selectively by cytoplasmic retention of jnk and thereby inhibits gene expression mediated by jnk, which occurs in the nucleus |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70851 |
|
|
Homo sapiens |
|
pmid |
sentence |
10490659 |
These experiments demonstrated that 10 different jnk isoforms bound to both jip proteins. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | SAPK/JNK Signaling |
+ |
MAPK8IP1 | down-regulates
binding
|
MAP3K12 |
0.53 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109046 |
|
|
Homo sapiens |
|
pmid |
sentence |
11432832 |
Jip inhibits dlk dimerization. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP1 | down-regulates
binding
|
NOTCH1 |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165710 |
|
|
Homo sapiens |
|
pmid |
sentence |
20508646 |
Here, we show that jip1 suppresses notch1 activity. Jip1 was found to physically associate with either intracellular domain of notch1 or rbp-jk and interfere with the interaction between them. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP1 | up-regulates
binding
|
MAP3K10 |
0.519 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134552 |
|
|
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 |
+ |
MAPK8IP2 | up-regulates
binding
|
MAPK8IP1 |
0.643 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70863 |
|
|
Homo sapiens |
|
pmid |
sentence |
10490659 |
Deletion analysis demonstrated that the cooh-terminal regions of jip1 and jip2 were sufficient for the formation of hetero-oligomeric complexes |
|
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 |
+ |
SH3RF1 | up-regulates
binding
|
MAPK8IP1 |
0.288 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145393 |
|
|
Homo sapiens |
|
pmid |
sentence |
16571722 |
We find that posh and jips directly associate with one another to form a multiprotein complex, pjac (posh-jip apoptotic complex), that includes all of the known kinase components of the pathway. Our observations indicate that this complex is required for jnk activation and cell death in response to apoptotic stimuli. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SAPK/JNK Signaling |
+ |
MAPK8IP1 | down-regulates
binding
|
RBPJ |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165713 |
|
|
Homo sapiens |
|
pmid |
sentence |
20508646 |
Here, we show that jip1 suppresses notch1 activity. Jip1 was found to physically associate with either intracellular domain of notch1 or rbp-jk and interfere with the interaction between them. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DUSP16 | up-regulates
binding
|
MAPK8IP1 |
0.451 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97173 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
12524447 |
Here we report that jip-1 also binds the dual-specificity phosphatases mkp7 and m3/6 via a region independent of its jnk binding domain. when mkp7 is bound to jip-1 it reduces jnk activation leading to reduced phosphorylation of the jnk target c-jun |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP1 | down-regulates
binding
|
MAP4K2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-75385 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10702297 |
DLK mutants were used to demonstrate that a DLK leucine zipper-leucine zipper interaction is necessary for DLK dimerization and to show that DLK dimerization mediated by the leucine zipper domain is prerequisite for DLK activity and subsequent activation of stress-activated protein kinase (SAPK). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SAPK/JNK Signaling |
+ |
INPPL1 | up-regulates
|
MAPK8IP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178652 |
|
|
Homo sapiens |
|
pmid |
sentence |
18486448 |
Ship2 positively modulated the mlk3/jip1-mediated jnk1 activation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK8IP1 | up-regulates
binding
|
MAP2K7 |
0.715 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70848 |
|
|
Homo sapiens |
|
pmid |
sentence |
10490659 |
Both jip1 and jip2 selectively bind the mapkk isoform mkk7. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |