+ |
SRC | up-regulates activity
phosphorylation
|
FCRL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274008 |
Tyr650 |
PMELEPMySNVNPGD |
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274010 |
Tyr662 |
PGDSNPIySQIWSIQ |
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274007 |
Tyr692 |
HEELTVLySELKKTH |
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274009 |
Tyr722 |
EEDDEENyENVPRVL |
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Publications: |
4 |
Organism: |
In Vitro |
+ |
FCRL3 | up-regulates activity
binding
|
PTPN6 |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274013 |
|
|
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FCRL3 | up-regulates activity
binding
|
SYK |
0.359 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274011 |
|
|
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FCRL3 | up-regulates activity
binding
|
PTPN11 |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274014 |
|
|
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FCRL3 | up-regulates activity
binding
|
ZAP70 |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274012 |
|
|
in vitro |
|
pmid |
sentence |
12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
Publications: |
1 |
Organism: |
In Vitro |