SwissPalm 2: Protein S-Palmitoylation Database

Mathieu Blanc; Fabrice P A David; F Gisou van der Goot

doi:10.1007/978-1-4939-9532-5_16

SwissPalm 2: Protein S-Palmitoylation Database

Methods Mol Biol. 2019:2009:203-214. doi: 10.1007/978-1-4939-9532-5_16.

Authors

Mathieu Blanc¹, Fabrice P A David², F Gisou van der Goot³

Affiliations

¹ Global Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
² Global Health Institute, Gene Expression Core Facility, SV-IT, School of Life Sciences, EPFL, Lausanne, Switzerland.
³ Global Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland. gisou.vandergoot@epfl.ch.

PMID: 31152406
DOI: 10.1007/978-1-4939-9532-5_16

Abstract

Protein S-palmitoylation is increasingly recognized as an important posttranslational modification, present in all eukaryotic organisms, involved in the regulation of many biological processes. The SwissPalm database centralizes the large and increasing number of published palmitoyl-proteome datasets, provides tools to compare them, and includes curated data from the literature on the identification and analysis of palmitoylated proteins. SwissPalm 2 provides an updated version, with 38 palmitoyl-proteomes at the time of release, from 17 different species, and new features such as the inclusion of orthologs.

Keywords: Confidence; DHHC; Database; Palmitoyl-proteomes; Palmitoylation; Posttranslational modification; Proteomics; S-acylation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Databases, Protein*
Humans
Lipoylation*
Protein Processing, Post-Translational*
Proteome* / chemistry
Proteome* / genetics
Proteome* / metabolism

Substances

Proteome