title: PhosphoregDB: the tissue and sub-cellular distribution of mammalian protein kinases and phosphatases.
abstract: BACKGROUND
  Protein kinases and protein phosphatases are the fundamental components of phosphorylation dependent protein regulatory systems. We have created a database for the protein kinase-like and phosphatase-like loci of mouse http://phosphoreg.imb.uq.edu.au that integrates protein sequence, interaction, classification and pathway information with the results of a systematic screen of their sub-cellular localization and tissue specific expression data mined from the GNF tissue atlas of mouse.
  
  
  RESULTS
  The database lets users query where a specific kinase or phosphatase is expressed at both the tissue and sub-cellular levels. Similarly the interface allows the user to query by tissue, pathway or sub-cellular localization, to reveal which components are co-expressed or co-localized. A review of their expression reveals 30% of these components are detected in all tissues tested while 70% show some level of tissue restriction. Hierarchical clustering of the expression data reveals that expression of these genes can be used to separate the samples into tissues of related lineage, including 3 larger clusters of nervous tissue, developing embryo and cells of the immune system. By overlaying the expression, sub-cellular localization and classification data we examine correlations between class, specificity and tissue restriction and show that tyrosine kinases are more generally expressed in fewer tissues than serine/threonine kinases.
  
  
  CONCLUSIONS
  Together these data demonstrate that cell type specific systems exist to regulate protein phosphorylation and that for accurate modelling and for determination of enzyme substrate relationships the co-location of components needs to be considered.
authors.affiliation: The Institute for Molecular Bioscience, University of Queensland, Brisbane 4072, Australia. a.forrest@imb.uq.edu.au
authors.forename: Alistair R R
authors.initials: AR
authors.lastname: Forrest
authors.forename: Darrin F
authors.initials: DF
authors.lastname: Taylor
authors.forename: J Lynn
authors.initials: JL
authors.lastname: Fink
authors.forename: M Milena
authors.initials: MM
authors.lastname: Gongora
authors.forename: Cameron
authors.initials: C
authors.lastname: Flegg
authors.forename: Rohan D
authors.initials: RD
authors.lastname: Teasdale
authors.forename: Harukazu
authors.initials: H
authors.lastname: Suzuki
authors.forename: Mutsumi
authors.initials: M
authors.lastname: Kanamori
authors.forename: Chikatoshi
authors.initials: C
authors.lastname: Kai
authors.forename: Yoshihide
authors.initials: Y
authors.lastname: Hayashizaki
authors.forename: Sean M
authors.initials: SM
authors.lastname: Grimmond
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002453:Cell Cycle; D019070:Cell Lineage; D016000:Cluster Analysis; D019295:Computational Biology / Q000379:methods*; D003593:Cytoplasm / Q000378:metabolism; D030562:Databases, Protein; D020224:Expressed Sequence Tags; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D007107:Immune System; D047468:Immunoprecipitation; D020407:Internet; D051379:Mice; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000096:biosynthesis*; D010766:Phosphorylation; D016133:Polymerase Chain Reaction; D011401:Promoter Regions, Genetic; D025941:Protein Interaction Mapping / Q000379:methods*; D011494:Protein Kinases / Q000096:biosynthesis*; D015398:Signal Transduction; D013379:Substrate Specificity; D014018:Tissue Distribution; D014162:Transfection
chemical_list: D011494:Protein Kinases; D010744:Phosphoric Monoester Hydrolases