A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database

mtcPTM is an online repository of human and mouse phosphosites in which data are hierarchically organized to preserve biologically relevant experimental information, thus allowing straightforward comparisons of phosphorylation patterns found under different conditions. The database also contains the...

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Autores principales: Jiménez, José L, Hegemann, Björn, Hutchins, James RA, Peters, Jan-Michael, Durbin, Richard
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Software
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1929158/
https://www.ncbi.nlm.nih.gov/pubmed/17521420
http://dx.doi.org/10.1186/gb-2007-8-5-r90
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author Jiménez, José L
Hegemann, Björn
Hutchins, James RA
Peters, Jan-Michael
Durbin, Richard
author_facet Jiménez, José L
Hegemann, Björn
Hutchins, James RA
Peters, Jan-Michael
Durbin, Richard
author_sort Jiménez, José L
collection PubMed
description mtcPTM is an online repository of human and mouse phosphosites in which data are hierarchically organized to preserve biologically relevant experimental information, thus allowing straightforward comparisons of phosphorylation patterns found under different conditions. The database also contains the largest available collection of atomic models of phosphorylatable proteins. Detailed analysis of this structural dataset reveals that phosphorylation sites are found in a heterogeneous range of structural and sequence contexts. mtcPTM is available on the web .
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spelling pubmed-19291582007-07-21 A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database Jiménez, José L Hegemann, Björn Hutchins, James RA Peters, Jan-Michael Durbin, Richard Genome Biol Software mtcPTM is an online repository of human and mouse phosphosites in which data are hierarchically organized to preserve biologically relevant experimental information, thus allowing straightforward comparisons of phosphorylation patterns found under different conditions. The database also contains the largest available collection of atomic models of phosphorylatable proteins. Detailed analysis of this structural dataset reveals that phosphorylation sites are found in a heterogeneous range of structural and sequence contexts. mtcPTM is available on the web . BioMed Central 2007 2007-05-23 /pmc/articles/PMC1929158/ /pubmed/17521420 http://dx.doi.org/10.1186/gb-2007-8-5-r90 Text en Copyright © 2007 Jiménez et al. licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Software
Jiménez, José L
Hegemann, Björn
Hutchins, James RA
Peters, Jan-Michael
Durbin, Richard
A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title_full A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title_fullStr A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title_full_unstemmed A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title_short A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database
title_sort systematic comparative and structural analysis of protein phosphorylation sites based on the mtcptm database
topic Software
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1929158/
https://www.ncbi.nlm.nih.gov/pubmed/17521420
http://dx.doi.org/10.1186/gb-2007-8-5-r90
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