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PhosphoregDB: the tissue and sub-cellular distribution of mammalian protein kinases and phosphatases

Alistair R R Forrest, Darrin F Taylor, J Lynn Fink, M Milena Gongora, Cameron Flegg, Rohan D Teasdale, Harukazu Suzuki, Mutsumi Kanamori, Chikatoshi Kai, Yoshihide Hayashizaki, Sean M Grimmond
2006 BMC Bioinformatics  
The database lets users query where a specific kinase or phosphatase is expressed at both the tissue and sub-cellular levels.  ...  Protein kinases and protein phosphatases are the fundamental components of phosphorylation dependent protein regulatory systems.  ...  Acknowledgements We would like to acknowledge the following funding sources. A.F.  ... 
doi:10.1186/1471-2105-7-82 pmid:16504016 pmcid:PMC1395337 fatcat:yzkw5dpun5d3fbwqmulru7hkmq

Phospho.ELM: a database of phosphorylation sites update 2008

F. Diella, C. M. Gould, C. Chica, A. Via, T. J. Gibson
2007 Nucleic Acids Research  
The entries provide information about the phosphorylated proteins and the exact position of known phosphorylated instances, the kinases responsible for the modification (where known) and links to bibliographic  ...  The current release of Phospho.ELM (version 7.0, July 2007) contains 4078 phospho-protein sequences covering 12 025 phospho-serine, 2362 phospho-threonine and 2083 phospho-tyrosine sites.  ...  We are grateful to Lars Juhl-Jensen and Rune Linding for their insightful comments and suggestions. We are thankful to Niall Haslam for critical reading of the manuscript.  ... 
doi:10.1093/nar/gkm772 pmid:17962309 pmcid:PMC2238828 fatcat:m2gvdov5erhyneh2ot6grat6tu

PTP-central: A comprehensive resource of protein tyrosine phosphatases in eukaryotic genomes

Teri Hatzihristidis, Shaq Liu, Leszek Pryszcz, Andrew P. Hutchins, Toni Gabaldón, Michel L. Tremblay, Diego Miranda-Saavedra
2014 Methods  
Whereas protein tyrosine kinases have long been implicated in many diseases, aberrant protein tyrosine phosphatase (PTP) activity is increasingly being associated with a wide spectrum of conditions too  ...  Reversible tyrosine phosphorylation is a fundamental signaling mechanism controlling a diversity of cellular processes.  ...  Acknowledgements This work was supported by the Japan Society for the Promotion of Science (JSPS) through the WPI-IFReC Research Program and a Kakenhi grant; the Kishimoto Foundation; the ETHZ-JST Japanese  ... 
doi:10.1016/j.ymeth.2013.07.031 pmid:23911837 fatcat:coghdmyg3zgjdmq2ihvmudjkve

Proteomic databases and tools to decipher post-translational modifications

Karthik S. Kamath, Meghana S. Vasavada, Sanjeeva Srivastava
2011 Journal of Proteomics  
Amidst these complexities connecting the modifications with physiological and cellular cascade of events are still very challenging.  ...  Post-translational modifications (PTMs) are vital cellular control mechanism, which affect protein properties, including folding, conformation, activity and consequently, their functions.  ...  Includes information on other types of PTMs such as ubiquitination etc. 11 PhosphoregDB [84] http://phosphoreg.imb.uq.edu.au/ Tissue and sub-cellular distribution of mouse protein kinases and phosphatases  ... 
doi:10.1016/j.jprot.2011.09.014 pmid:21983556 fatcat:wf6nrct5jvd6hnzaobm6dttc5u