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 RUNX2, presumably in complex with CBFB, can be phosphorylate...
| Class:Id | Summation:9009279 |
|---|---|
| _displayName | RUNX2, presumably in complex with CBFB, can be phosphorylate... |
| _timestamp | 2017-06-21 14:45:23 |
| created | [InstanceEdit:9009280] Orlic-Milacic, Marija, 2017-06-16 |
| modified | [InstanceEdit:9009287] Orlic-Milacic, Marija, 2017-06-16 [InstanceEdit:9009399] Orlic-Milacic, Marija, 2017-06-16 [InstanceEdit:9009654] Orlic-Milacic, Marija, 2017-06-21 |
| text | RUNX2, presumably in complex with CBFB, can be phosphorylated by the complex of CDK1 and cyclin B. The interaction was demonstrated between endogenous human RUNX2 and CDK1:CCNB1. It was also shown in human cells that RUNX2 undergoes CDK1:CCNB1-mediated phosphorylation on serine residue S451 of RUNX2-P2 isoform. This residue corresponds to the mouse Runx-P1 serine residue S472 (Qiao et al. 2006, Rajgopal et al. 2007). At mitotic exit, RUNX2 is dephosphorylated by unidentified PP1 or PP2A phosphatase (Rajgopal et al. 2007). |
| (summation) | [Reaction:9009282] CDK1 phosphorylates RUNX2 [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by RUNX2, presumably in complex with CBFB, can be phosphorylate... (9009279)
