+ |
TEC | up-regulates activity
phosphorylation
|
STAP1 |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261817 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10518561 |
In 293 cells expressing recombinant BRDG1 and various PTKs, Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induced marked phosphorylation of BRDG1 on tyrosine residues. BRDG1 was also phosphorylated by Tec directly in vitro. Efficient phosphorylation of BRDG1 by Tec required the PH and SH2 domains as well as the kinase domain of the latter. Furthermore, BRDG1 was shown to participate in a positive feedback loop by increasing the activity of Tec. BRDG1 transcripts are abundant in the human B cell line Ramos, and the endogenous protein underwent tyrosine phosphorylation in response to BCR stimulation. BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTK2B | up-regulates activity
phosphorylation
|
STAP1 |
0.358 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261818 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10518561 |
In 293 cells expressing recombinant BRDG1 and various PTKs, Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induced marked phosphorylation of BRDG1 on tyrosine residues. BRDG1 was also phosphorylated by Tec directly in vitro. Furthermore, BRDG1 was shown to participate in a positive feedback loop by increasing the activity of Tec. BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAP1 | up-regulates activity
binding
|
TEC |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261819 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10518561 |
In 293 cells expressing recombinant BRDG1 and various PTKs, Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induced marked phosphorylation of BRDG1 on tyrosine residues. BRDG1 was also phosphorylated by Tec directly in vitro. Furthermore, BRDG1 was shown to participate in a positive feedback loop by increasing the activity of Tec. BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling. BRDG1 may activate Tec by disrupting an intramolecular interaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAP1 | up-regulates activity
binding
|
STAT5A |
0.395 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261821 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10679268 |
STAP-1 was tyrosine-phosphorylated by activated c-kit. An in vitro binding assay suggested that the STAP-1 SH2 domain interacted with several tyrosine-phosphorylated proteins including c-kit and STAT5. These suggest that STAP-1 functions as an adaptor molecule downstream of c-kit in hematopoietic stem cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAP1 | up-regulates activity
binding
|
KIT |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261822 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10679268 |
STAP-1 was tyrosine-phosphorylated by activated c-kit. An in vitro binding assay suggested that the STAP-1 SH2 domain interacted with several tyrosine-phosphorylated proteins including c-kit and STAT5. These suggest that STAP-1 functions as an adaptor molecule downstream of c-kit in hematopoietic stem cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KIT | up-regulates activity
phosphorylation
|
STAP1 |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261820 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10679268 |
STAP-1 was tyrosine-phosphorylated by activated c-kit. An in vitro binding assay suggested that the STAP-1 SH2 domain interacted with several tyrosine-phosphorylated proteins including c-kit and STAT5. These suggest that STAP-1 functions as an adaptor molecule downstream of c-kit in hematopoietic stem cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |