PolarProtDb

PolarProtDb catalogs proteins involved in cellular polarity and provides curated experimental and homology-based annotations to support analysis of protein localization, transmembrane topology, post-translational modifications (e.g., glycosylations, phosphorylations), short linear motifs, and interaction partners in epithelial and other cell types.

Key Features:

• Comprehensive Data Collection: Compiles information from numerous scientific publications into a single resource with detailed records of proteins involved in maintaining cellular polarity, with emphasis on epithelial cells.
• Experimental Verification: Contains experimentally verified data to indicate evidence-backed protein polarization and related annotations.
• Homology-Based Inferences: Provides homology-based inferences based on evolutionary conservation across species to predict polarized behavior of proteins.
• Transmembrane Topology Information: Includes transmembrane topology data for applicable proteins to inform protein orientation and function within cellular membranes.
• Post-Translational Modifications (PTMs): Documents PTMs such as glycosylations and phosphorylations relevant to protein trafficking and function.
• Short Linear Motifs: Identifies known or predicted short linear motifs conserved across orthologs as potential regulatory elements for protein sorting and localization.
• Interaction Partners: Lists potential interaction partners to facilitate exploration of protein networks and pathways related to cellular polarity.

Scientific Applications:

• Cellular Polarity Studies: Supports investigation of apical-basal polarization mechanisms and the roles of specific proteins in epithelial cell function and organization.
• Viral Entry Research: Aids identification of proteins that may serve as receptors or facilitators of viral entry, including targets relevant to SARS-CoV-2.
• Experimental Design: Informs design of experiments probing protein trafficking, sorting mechanisms, and the functional impact of specific modifications.
• Comparative Analyses: Enables comparative studies across species to assess evolutionary conservation and divergence of polarized protein functions.

Methodology:

PolarProtDb integrates data from scientific publications and applies rigorous inclusion criteria, prioritizing experimentally validated findings while incorporating homology-based predictions.