| + |
FYN | up-regulates activity 
phosphorylation
|
SLAMF1 |
0.647 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251181 |
Tyr281 |
EKKSLTIyAQVQKPG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11806999 |
All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251182 |
Tyr307 |
QDPCTTIyVAATEPV |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11806999 |
All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251183 |
Tyr327 |
ETNSITVyASVTLPE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11806999 |
All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
LYN |
phosphorylation
|
SLAMF1 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127997 |
Tyr327 |
ETNSITVyASVTLPE |
Homo sapiens |
|
| pmid |
sentence |
| 15315965 |
Cd150-mediated akt phosphorylation required syk and sh2d1a, was negatively regulated by lyn and btk, but was ship independent. Lyn directly phosphorylated y327 in cd150, but the akt pathway did not depend on cd150 tyrosine phosphorylation and cd150-shp-2 association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARCHF9 | down-regulates quantity by destabilization 
ubiquitination
|
SLAMF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271537 |
|
|
Homo sapiens |
B-lymphocyte Cell Line |
| pmid |
sentence |
| 19457934 |
MARCH9, a member of the RING-CH family of transmembrane E3 ubiquitin ligases, down-regulates CD4, major histocompatibility complex-I (MHC), and ICAM-1 in lymphoid cells. To identify novel MARCH9 substrates, we used high throughput flow cytometry and quantitative mass spectrometry by stable isotope labeling by amino acids in cell culture (SILAC) to determine the differential expression of plasma membrane proteins in a MARCH9-expressing B cell line. This combined approach identified 13 potential new MARCH9 targets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SLAMF1
- 
- 