Analysis of the Functional Relationship of Protein Kinase Families Using Phospho-Proteomics Data

Author

David A. Parra Peña, The University of Texas Rio Grande Valley

Date of Award

8-2020

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Computer Science

First Advisor

Dr. Marzieh Ayati

Second Advisor

Dr. Zhixiang Chen

Third Advisor

Dr. Andres Figueroa

Abstract

As cancer research advances, Mass-spectrometry based proteomics is becoming a widely used technique for proteome characterization. Phosphoproteomics is a specific type of proteomics that characterizes proteins with the reversible post-translational modification of phosphorylation PTM), which has allowed the identifications of thousands of phosphorylation sites. These phosphorylation sites, also known as substrates, are known to interact with a protein type named kinases. Studies have shown that abnormal phosphorylation activity is related to cancer diseases. Moreover, these kinases are divided into families, based on the similarity of their catalytic domain, as this part of their amino acid sequence determines a large part of what their functions are. In this work, propose 2 new methods to assess the relationship of kinases based on the correlation of the phosphorylation pattern of their substrates. Using these metrics, we cluster the kinases and analyze their inter-family interactions.

Comments

Copyright 2020 by David A. Parra Peña. All Rights Reserved.

https://go.openathens.net/redirector/utrgv.edu?url=https://www.proquest.com/dissertations-theses/analysis-functional-relationship-protein-kinase/docview/2506328516/se-2?accountid=7119

Recommended Citation

Parra Peña, David A., "Analysis of the Functional Relationship of Protein Kinase Families Using Phospho-Proteomics Data" (2020). Theses and Dissertations. 564.
https://scholarworks.utrgv.edu/etd/564