title: PhosphoPOINT: a comprehensive human kinase interactome and phospho-protein database.
abstract: BACKGROUND
  To fully understand how a protein kinase regulates biological processes, it is imperative to first identify its substrate(s) and interacting protein(s). However, of the 518 known human serine/threonine/tyrosine kinases, 35% of these have known substrates, while 14% of the kinases have identified substrate recognition motifs. In contrast, 85% of the kinases have protein-protein interaction (PPI) datasets, raising the possibility that we might reveal potential kinase-substrate pairs from these PPIs.
  
  
  RESULTS
  PhosphoPOINT, a comprehensive human kinase interactome and phospho-protein database, is a collection of 4195 phospho-proteins with a total of 15 738 phosphorylation sites. PhosphoPOINT annotates the interactions among kinases, with their down-stream substrates and with interacting (phospho)-proteins to modulate the kinase-substrate pairs. PhosphoPOINT implements various gene expression profiles and Gene Ontology cellular component information to evaluate each kinase and their interacting (phospho)-proteins/substrates. Integration of cSNPs that cause amino acids change with the proteins with the phosphoprotein dataset reveals that 64 phosphorylation sites result in a disease phenotypes when changed; the linked phenotypes include schizophrenia and hypertension. PhosphoPOINT also provides a search function for all phospho-peptides using about 300 known kinase/phosphatase substrate/binding motifs. Altogether, PhosphoPOINT provides robust annotation for kinases, their downstream substrates and their interaction (phospho)-proteins and this should accelerate the functional characterization of kinomemediated signaling.
  
  
  BACKGROUND
  PhosphoPOINT can be freely accessed in http://kinase. bioinformatics.tw/.
  
  
  BACKGROUND
  Supplementary data are available at Bioinformatics online.
authors.affiliation: Department of Computer Science and Information Engineering, National Taiwan University, Taipei 106, Taiwan, Republic of China.
authors.forename: Chia-Ying
authors.initials: CY
authors.lastname: Yang
authors.forename: Chao-Hui
authors.initials: CH
authors.lastname: Chang
authors.forename: Ya-Ling
authors.initials: YL
authors.lastname: Yu
authors.forename: Tsu-Chun Emma
authors.initials: TC
authors.lastname: Lin
authors.forename: Sheng-An
authors.initials: SA
authors.lastname: Lee
authors.forename: Chueh-Chuan
authors.initials: CC
authors.lastname: Yen
authors.forename: Jinn-Moon
authors.initials: JM
authors.lastname: Yang
authors.forename: Jin-Mei
authors.initials: JM
authors.lastname: Lai
authors.forename: Yi-Ren
authors.initials: YR
authors.lastname: Hong
authors.forename: Tzu-Ling
authors.initials: TL
authors.lastname: Tseng
authors.forename: Kun-Mao
authors.initials: KM
authors.lastname: Chao
authors.forename: Chi-Ying F
authors.initials: CY
authors.lastname: Huang
mesh_terms: D001665:Binding Sites; D030562:Databases, Protein; D006801:Humans; D016247:Information Storage and Retrieval / Q000379:methods; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D020543:Proteome / Q000737:chemistry / Q000378:metabolism*; D014584:User-Computer Interface
chemical_list: D010750:Phosphoproteins; D020543:Proteome; D010770:Phosphotransferases