| + |
SRC | up-regulates activity 
phosphorylation
|
STAP2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247333 |
Tyr22 |
GVLPSHYyESFLEKK |
Homo sapiens |
|
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase Tyr-22 and Tyr-322 are the major tyrosine phosphorylation sites by v-Src. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247337 |
Tyr322 |
GDGPAVDyENQDVAS |
Homo sapiens |
|
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase Tyr-22 and Tyr-322 are the major tyrosine phosphorylation sites by v-Src. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAP2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249371 |
Tyr250 |
PFLLDEDyEKVLGYV |
|
HEK-293 Cell |
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase |On the other hand, the phosphorylation levels of Y22F, Y310F, and Y322F by GST-JH1 were reduced to 8060% of the levels of wild-type STAP-2, which suggests that these three are potential phosphorylation sites by activated JAK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249372 |
Tyr310 |
LPNQEENyVTPIGDG |
|
HEK-293 Cell |
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase |On the other hand, the phosphorylation levels of Y22F, Y310F, and Y322F by GST-JH1 were reduced to 8060% of the levels of wild-type STAP-2, which suggests that these three are potential phosphorylation sites by activated JAK2. |
|
| Publications: |
2 |
| + |
PTK6 | up-regulates activity
phosphorylation
|
STAP2 |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247067 |
Tyr250 |
PFLLDEDyEKVLGYV |
Homo sapiens |
|
| pmid |
sentence |
| 19393627 |
Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates the signaling pathways downstream of them. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by Brk, using a series of STAP-2 YF mutants and anti-phospho-STAP-2 Tyr250 antibody. Furthermore, overexpression of the STAP-2 Y250F mutant protein affected Brk-mediated STAT3 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates
phosphorylation
|
STAP2 |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81489 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10980601 |
The phosphorylation of and association with bks by brk was also dependent on the sh2-like domain present within bks.bks is a substrate for the kinase activity of brk and has the characteristics of an adaptor protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STAP2
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