Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

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.

Name Email address

Details on Person Starting in mitotic prometaphase, GTSE1 becomes phosphorylat...

Class:IdSummation:8852311
_displayNameStarting in mitotic prometaphase, GTSE1 becomes phosphorylat...
_timestamp2016-01-25 16:51:56
created[InstanceEdit:8852310] Orlic-Milacic, Marija, 2016-01-15
modified[InstanceEdit:8853810] Orlic-Milacic, Marija, 2016-01-25
[InstanceEdit:8853880] Orlic-Milacic, Marija, 2016-01-25
textStarting in mitotic prometaphase, GTSE1 becomes phosphorylated at threonine residues T513 and T526 (and possibly other sites), located adjacent to the two SKIP-like motifs involved in binding to MAPRE1 (EB1). Mitotic phosphorylation of GTSE1 inhibits its association with microtubule plus ends. CDK1 activity inhibits the association of recombinant human GTSE1 with microtubule plus ends in Xenopus extracts, but it is not certain whether CDK1 or another mitotic kinase phosphorylates GTSE1 (Scolz et al. 2012).
(summation)[Reaction:8852306] Mitotic phosphorylation-induced dissociation of GTSE1 from microtubule plus ends [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Starting in mitotic prometaphase, GTSE1 becomes phosphorylat... (8852311)