| + |
LCK | up-regulates activity 
phosphorylation
|
SH2D2A |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262888 |
Tyr280 |
PKPSNPIyNEPDEPI |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 18541536 |
Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262889 |
Tyr290 |
PDEPIAFyAMGRGSP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 18541536 |
Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262890 |
Tyr305 |
GEAPSNIyVEVEDEG |
Homo sapiens |
|
| pmid |
sentence |
| 18541536 |
Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DSCAM | up-regulates activity
binding
|
SH2D2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264279 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
Our findings now further suggest that STAT3 and the adaptor protein SH2D2A interact with tyrosine‐containing motifs within the DSCAM/L1 ICDs. The SH2 domains of both STAT3 and SH2D2A are known to bind to phosphorylated tyrosine residues in the context of such motifs. Thus, the interactions between DSCAMs and SH2‐domain containing proteins seem to play a central and conserved role in Dscam signaling in the context of dynamic changes of tyrosine‐phosphorylation levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SH2D2A
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