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 Receptor autophosphorylation requires a lysine at position 1...

Class:IdSummation:74755
_displayNameReceptor autophosphorylation requires a lysine at position 1...
_timestamp2017-04-06 15:48:02
created[InstanceEdit:74816] 2003-07-28 10:05:14
literatureReference[LiteratureReference:5685347] Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mapping
modified[InstanceEdit:74806] Schmidt, EE, 2003-07-28 08:28:53
[InstanceEdit:74811] Schmidt, EE, 2003-07-28 10:05:13
[InstanceEdit:5685348] Jupe, Steve, 2015-03-27
[InstanceEdit:8984457] Duenas, Corina, 2017-04-06
textReceptor autophosphorylation requires a lysine at position 1057 to stabilize the gamma phosphate of ATP. The adenosine of ATP interacts with three glycines at residues 1030-1035. The first tyrosine residues to be autophosphorylated are 1185, 1189 and 1190 in the kinase domain. This is followed by 999 in the juxtamembrane domain, 1355 and 1361. These tyrosines fall into the three distinct tyrosine phosphorylation domains of the beta-subunit. In total there are 13 potential tyrosines that may be phosphorylated. The receptor phosphorylates itself in a trans rather than cis manner, where the beta-subunits phosphorylate each other rather than themselves (Tavaré et al. 1998).
(summation)[Reaction:74715] Autophosphorylation of insulin receptor [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Receptor autophosphorylation requires a lysine at position 1... (74755)
Follow Reactome