Cargando…
SwissPalm: Protein Palmitoylation database
Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000Research
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4544385/ https://www.ncbi.nlm.nih.gov/pubmed/26339475 http://dx.doi.org/10.12688/f1000research.6464.1 |
_version_ | 1782386664782430208 |
---|---|
author | Blanc, Mathieu David, Fabrice Abrami, Laurence Migliozzi, Daniel Armand, Florence Bürgi, Jérôme van der Goot, Françoise Gisou |
author_facet | Blanc, Mathieu David, Fabrice Abrami, Laurence Migliozzi, Daniel Armand, Florence Bürgi, Jérôme van der Goot, Françoise Gisou |
author_sort | Blanc, Mathieu |
collection | PubMed |
description | Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species. As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm ( http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation. |
format | Online Article Text |
id | pubmed-4544385 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | F1000Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-45443852015-09-02 SwissPalm: Protein Palmitoylation database Blanc, Mathieu David, Fabrice Abrami, Laurence Migliozzi, Daniel Armand, Florence Bürgi, Jérôme van der Goot, Françoise Gisou F1000Res Research Article Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species. As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm ( http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation. F1000Research 2015-07-16 /pmc/articles/PMC4544385/ /pubmed/26339475 http://dx.doi.org/10.12688/f1000research.6464.1 Text en Copyright: © 2015 Blanc M et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Blanc, Mathieu David, Fabrice Abrami, Laurence Migliozzi, Daniel Armand, Florence Bürgi, Jérôme van der Goot, Françoise Gisou SwissPalm: Protein Palmitoylation database |
title | SwissPalm: Protein Palmitoylation database |
title_full | SwissPalm: Protein Palmitoylation database |
title_fullStr | SwissPalm: Protein Palmitoylation database |
title_full_unstemmed | SwissPalm: Protein Palmitoylation database |
title_short | SwissPalm: Protein Palmitoylation database |
title_sort | swisspalm: protein palmitoylation database |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4544385/ https://www.ncbi.nlm.nih.gov/pubmed/26339475 http://dx.doi.org/10.12688/f1000research.6464.1 |
work_keys_str_mv | AT blancmathieu swisspalmproteinpalmitoylationdatabase AT davidfabrice swisspalmproteinpalmitoylationdatabase AT abramilaurence swisspalmproteinpalmitoylationdatabase AT migliozzidaniel swisspalmproteinpalmitoylationdatabase AT armandflorence swisspalmproteinpalmitoylationdatabase AT burgijerome swisspalmproteinpalmitoylationdatabase AT vandergootfrancoisegisou swisspalmproteinpalmitoylationdatabase |