| + |
ASAP2 | up-regulates activity 
gtpase-activating protein
|
ARF6 |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269706 |
|
|
in vitro |
|
| pmid |
sentence |
| 10022920 |
Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Pap protein exhibits Arf GAP activity in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ASAP2 | up-regulates activity
gtpase-activating protein
|
ARF1 |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269705 |
|
|
in vitro |
|
| pmid |
sentence |
| 10022920 |
Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Pap protein exhibits Arf GAP activity in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ASAP2 | up-regulates activity
gtpase-activating protein
|
ARF5 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269707 |
|
|
in vitro |
|
| pmid |
sentence |
| 10022920 |
Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Pap protein exhibits Arf GAP activity in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTK2B | up-regulates activity
phosphorylation
|
ASAP2 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269704 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10022920 |
Tyrosine phosphorylation of Pap by Pyk2 or Src kinases. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ASAP2
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