F33A35A6F52E196DB668DE2DE2B63697BB0898406231FC6BD4C8A595916C07DEAC9A465B1B9689CF7D57F44333769140

Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating angiogenic signals mediated by ANGPT1. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity).

Source:http://purl.uniprot.org/SHA-384/F33A35A6F52E196DB668DE2DE2B63697BB0898406231FC6BD4C8A595916C07DEAC9A465B1B9689CF7D57F44333769140

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
rdfs:comment
Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating angiogenic signals mediated by ANGPT1. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity).