| + |
SRC | up-regulates activity 
phosphorylation
|
BAIAP2L1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263037 |
Tyr156 |
GSRNALKyEHKEIEY |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263038 |
Tyr163 |
YEHKEIEyVETVTSR |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263039 |
Tyr274 |
SNVVRKDyDTLSKCS |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263040 |
Tyr293 |
PAPSGRAyTSPLIDM |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263041 |
Tyr37 |
LINLGKNyEKAVNAM |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263042 |
Tyr439 |
VVIPPPDyLECLSMG |
in vitro |
|
| pmid |
sentence |
| 21840312 |
Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility. |
|
| Publications: |
6 |
Organism: |
In Vitro |
3.0
BAIAP2L1
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