Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to e...
| Class:Id | Summation:372682 |
|---|---|
| _displayName | SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to e... |
| _timestamp | 2019-01-14 20:18:49 |
| created | [InstanceEdit:372670] Garapati, P V, 2008-06-27 10:19:56 |
| literatureReference | [LiteratureReference:372665] p130Cas: a versatile scaffold in signaling networks |
| modified | [InstanceEdit:373163] Garapati, P V, 2008-07-14 14:11:18 [InstanceEdit:8941456] Garapati, Phani Vijay, 2016-10-03 [InstanceEdit:9634747] Rothfels, Karen, 2019-01-14 |
| text | SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to enhanced tyrosine phosphorylation of BCAR1 at multiple sites. The Cas substrate domain contains 15 separate YxxP motifs, a main site of tyrosine phosphorylation on the BCAR1 molecule. Once phosphorylated, this domain serves as a docking site for the SH2 domains of CRK or NCK adaptor proteins that affect the downstream MAPK signalling pathway, resulting in cell survival and increased motility. |
| (summation) | [Reaction:372693] Phosphorylation of BCAR1 by SRC-PTK2 complex [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to e... (372682)
