| + |
HCK |
phosphorylation
|
ADAM15 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112927 |
Tyr715 |
LVMLGASyWYRARLH |
Homo sapiens |
|
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15 cytoplasmic domain in vitro in immune complex kinase assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates
phosphorylation
|
ADAM15 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112931 |
Tyr715 |
LVMLGASyWYRARLH |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112935 |
Tyr735 |
LKGPTCQyRAAQSGP |
Homo sapiens |
|
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates
phosphorylation
|
ADAM15 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112919 |
Tyr715 |
LVMLGASyWYRARLH |
Homo sapiens |
|
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112923 |
Tyr735 |
LKGPTCQyRAAQSGP |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ADAM15 | up-regulates activity
binding
|
SRC |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282630 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 31888763 |
Aspartate β-hydroxylase (ASPH) drives embryonic cell motility/invasion in pancreatic development/differentiation. We explored if dysregulated ASPH is critically involved in pancreatic cancer pathogenesis.Mechanistically, ASPH activates SRC cascade through direct physical interaction with ADAM12/ADAM15 independent of FAK. The ASPH-SRC axis enables invadopodia construction and initiates MMP-mediated ECM degradation/remodeling as executors for invasiveness. ADAM12 or ADAM15 interacts with SH3 domain of SRC [13–15], resulting in activation of the SRC cascade in pancreatic cancer cells (Fig. 2b). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
| up-regulates activity
binding
|
ADAM15 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282628 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 31888763 |
Aspartate β-hydroxylase (ASPH) drives embryonic cell motility/invasion in pancreatic development/differentiation. We explored if dysregulated ASPH is critically involved in pancreatic cancer pathogenesis.Mechanistically, ASPH activates SRC cascade through direct physical interaction with ADAM12/ADAM15 independent of FAK. The ASPH-SRC axis enables invadopodia construction and initiates MMP-mediated ECM degradation/remodeling as executors for invasiveness. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |