| + |
PRKD1 |
phosphorylation
|
RIN1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170877 |
Ser292 |
QLLRRESsVGYRVPA |
Homo sapiens |
|
| pmid |
sentence |
| 21209314 |
Here, we report the identification of serine 292 in rin1 as an in vivo pkd phosphorylation site. we demonstrate that phosphorylation at serine 292 controls rin1-mediated inhibition of cell migration by modulating the activation of abl kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113964 |
Ser351 |
RPLLRSMsAAFCSLL |
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
Serine 351 is a substrate for protein kinase d (pkd [also known as pkcmu]) in vitro and in vivo. These data suggest that the normal localization and function of rin1, as well as its ability to compete with raf, are regulated in part by 14-3-3 binding, which in turn is controlled by pkd phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates 
phosphorylation
|
RIN1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113960 |
Ser351 |
RPLLRSMsAAFCSLL |
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
Rin1 also binds to 14-3-3 proteins through a sequence including serine 351. Mutation of this residue abolished the 14-3-3 binding capacity of rin1 and led to more efficient blockade of ras-mediated transformation. The mutant protein, rin1(s351a), showed a shift in localization to the plasma membrane. Serine 351 is a substrate for protein kinase d (pkd [also known as pkcmu]) in vitro and in vivo. These data suggest that the normal localization and function of rin1, as well as its ability to compete with raf, are regulated in part by 14-3-3 binding, which in turn is controlled by pkd phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RLF | up-regulates activity 
binding
|
RIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-220920 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10545207 |
Rit and Rin were found to interact with the known Ras binding proteins RalGDS, Rlf, and AF-6/Canoe. These interactions were GTP and effector domain dependent and suggest that RalGDS, Rlf, and AF-6 are Rit and Rin effectors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIN1 | up-regulates
phosphorylation
|
ABL2 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136961 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15886098 |
Rin1 binds to the abl sh3 and sh2 domains, and these inetractions stimulate abl2 catalytic activity. This leads to increased phosphorylation of crk and crkl |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
RIN1 | up-regulates
binding
|
HRAS |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
We demonstrate that the ras effector protein rin1 binds to activated ras with an affinity (k(d), 22 nm) similar to that observed for raf1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RALGDS | up-regulates activity
binding
|
RIN1 |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-220923 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10545207 |
Rit and Rin were found to interact with the known Ras binding proteins RalGDS, Rlf, and AF-6/Canoe. These interactions were GTP and effector domain dependent and suggest that RalGDS, Rlf, and AF-6 are Rit and Rin effectors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL2 | up-regulates activity
phosphorylation
|
RIN1 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15886098 |
These findings suggested that RIN1 is phosphorylated by both ABL1 and ABL2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AFDN | up-regulates activity
binding
|
RIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-220926 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10545207 |
Rit and Rin were found to interact with the known Ras binding proteins RalGDS, Rlf, and AF-6/Canoe. These interactions were GTP and effector domain dependent and suggest that RalGDS, Rlf, and AF-6 are Rit and Rin effectors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
RIN1 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48142 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9144171 |
We also report that the amino-terminal domain of rin1 contains sequences that can mediate interactions with the abl tyrosine kinase and that rin1 is itself tyrosine phosphorylated by c-abl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIN1 | up-regulates
binding
|
EGFR |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101530 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12783862 |
The interaction between egfr and rin1 delineates a novel signal transduction pathway between egfr and its effectors, rin1, rab5a, and ras, which together coordinate and regulate both signaling and membrane trafficking. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIN1 | up-regulates
binding
|
KRAS |
0.612 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113970 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
We demonstrate that the ras effector protein rin1 binds to activated ras with an affinity (k(d), 22 nm) similar to that observed for raf1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
RIN1
- 
- 