Yang, C.-Y. et al.C.-Y. et al.YangChang, C.-H.C.-H.ChangYu, Y.-L.Y.-L.YuLin, T.-C.E.T.-C.E.LinLee, S.-A.S.-A.LeeYen, C.-C.C.-C.YenYang, J.-M.J.-M.YangLai, J.-M.J.-M.LaiHong, Y.-R.Y.-R.HongTseng, T.-L.T.-L.TsengKUN-MA0 CHAOHuang, Chi-Ying F.Chi-Ying F.Huang2020-04-162020-04-162008https://scholars.lib.ntu.edu.tw/handle/123456789/484550Motivation: 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. ? The Author 2008. Published by Oxford University Press. All rights reserved.[SDGs]SDG3ATM protein; aurora A kinase; cyclin dependent kinase 5; G protein coupled receptor kinase; mitogen activated protein kinase 1; mitogen activated protein kinase 3; phosphoprotein; phosphotransferase; protein p53; rhodopsin kinase; amino acid substitution; computer program; conference paper; controlled study; enzyme substrate complex; gene expression profiling; human; hypertension; phenotypic variation; priority journal; protein database; protein motif; protein phosphorylation; protein protein interaction; schizophrenia; signal transduction; single nucleotide polymorphism; Binding Sites; Databases, Protein; Humans; Information Storage and Retrieval; Phosphoproteins; Phosphorylation; Phosphotransferases; Protein Binding; Protein Interaction Mapping; Proteome; User-Computer Interfaceconference paper10.1093/bioinformatics/btn2972-s2.0-49549121853https://www.scopus.com/inward/record.uri?eid=2-s2.0-49549121853&doi=10.1093%2fbioinformatics%2fbtn297&partnerID=40&md5=76b64f288a974aa8e4744034021c864f