+ |
SYK | up-regulates activity
phosphorylation
|
LAT2 |
0.576 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273576 |
Tyr136 |
EDDDANSyENVLICK |
Mus musculus |
A20 Cell |
pmid |
sentence |
14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273575 |
Tyr193 |
EDEESEDyQNSASIH |
Mus musculus |
A20 Cell |
pmid |
sentence |
14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273577 |
Tyr233 |
EEDGEPDyVNGEVAA |
Mus musculus |
A20 Cell |
pmid |
sentence |
14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
Publications: |
3 |
Organism: |
Mus Musculus |