Abstract 5146: Phosphositeplus® and protein modifications in cancer, a case study: profiling tyrosine phosphorylated sites in AML and CML.

Abstract PhosphoSitePlus® (PSP) is an open, comprehensive, manually curated, and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses over 250,000 non-redundant modification sites, primarily phosphorylation, ubiquitinylation and acetylation. The results of thousands of mass spec experiments, many from various cancers, are aggregated and available for downloading from PSP. The cancers that are most widely represented in PSP include non-small cell lung cancer (NSCLC), chronic myelogenous leukemia (CML), acute myelogenous leukemia (AML), breast cancer (BRC), and gastric (GAC) cancer. In order to determine if the sort of binary data in PSP can be useful in identifying sites that are differentially tyrosine phosphorylated between various cancers, 284 CML and 160 AML datasets were downloaded from PSP and analyzed. Differences in the expression of tyrosine phosphorylation were observed: sites that were elevated in AML included PAG1 Tyr317/359/417, WASP Tyr291, SHP-1 Tyr536, and E-Syt1 Tyr822. Sites that were elevated in CML included Bcr and Abl sites as expected, as well as DYRK1A Tyr145, VASP Tyr39, CD2AP Tyr88, SHIP-2 Tyr986/1135/1162. These meta-analyses demonstrate that PSP provides a rich source of easily accessible data that enables proteomic profiling of multiple cancers. See www.phosposite.org Supported by NIH R44 CA126080, R43 GM65768, and R44 AA014848 Citation Format: Peter Hornbeck, Bin Zhang, Beth Murray, Elzbieta Skrzypek, Jon Kornhauser, Vaughan Latham. Phosphositeplus® and protein modifications in cancer, a case study: profiling tyrosine phosphorylated sites in AML and CML. [abstract]. In: Proceedings of the 104th Annual Meeting of the American Association for Cancer Research; 2013 Apr 6-10; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2013;73(8 Suppl):Abstract nr 5146. doi:10.1158/1538-7445.AM2013-5146