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PhosphoPOINT specifications


Unique identifier OMICS_02955
Name PhosphoPOINT
Restrictions to use None
Community driven No
Data access Browse
User data submission Not allowed
Maintained No


  • Primates
    • Homo sapiens

Publication for PhosphoPOINT

PhosphoPOINT citations


Phosphoproteomics reveals network rewiring to a pro adhesion state in annexin 1 deficient mammary epithelial cells

PMCID: 5727667
PMID: 29233185
DOI: 10.1186/s13058-017-0924-4

[…] e base of experimentally derived kinase-substrate relationships (KSR) available from KSR-LIVE []. The integrated database combines KSRs from multiple repositories such as PhosphoSitePlus, PhosphoELM, PhosphoPOINT and the Human Protein Reference Database (HPRD). The derived upstream kinases along with the regulated phosphoproteins were analyzed using the search tool for the retrieval of interacting […]


Functional phosphatome requirement for protein homeostasis, networked mitochondria, and sarcomere structure in C. elegans muscle

PMCID: 5566650
PMID: 28508547
DOI: 10.1002/jcsm.12196

[…] a‐analyses of physical and functional interactions between the genes identified during the chronic and acute RNAi screen were extracted manually from the following databases: WormBase, GeneMANIA, and PhosphoPOINT. Only interactions between the genes identified to potentially regulate a specific process were searched to construct process‐specific network models. To use PhosphoPOINT data, a human or […]


Unraveling Kinase Activation Dynamics Using Kinase Substrate Relationships from Temporal Large Scale Phosphoproteomics Studies

PLoS One
PMCID: 4918924
PMID: 27336693
DOI: 10.1371/journal.pone.0157763

[…] The information from four databases were combined into one integrated ‘KSR knowledgebase’. The databases used were: PhosphoSitePlus (retrieved 06/2014), PhosphoELM (release 9.0), PhosphoPOINT (04/2014) and Human Protein Reference Database (release 9). Data from human and mouse was used, and the mouse proteins were mapped to human proteins using the Inparanoid ortholog database […]


The exploration of network motifs as potential drug targets from post translational regulatory networks

Sci Rep
PMCID: 4744934
PMID: 26853265
DOI: 10.1038/srep20558
call_split See protocol

[…] Human phosphorylation/dephosphorylation annotations were retrieved from five public resources, i.e. Phospho.ELM (v9.0), NetworKIN (v2.0), PhosphoPOINT (downloaded April 2011), Kinasource (downloaded March 2011) ( and PhosphoSitePlus (downloaded April 2011), as well as two systematic studies. As a result, we o […]


Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease related protein networks

Sci Rep
PMCID: 4676070
PMID: 26657352
DOI: 10.1038/srep18189

[…] to the DEPs or DPPs were chosen as the key regulators. To identify key kinases regulating the DPPs, 5,563 kinase-substrate interaction data were also collected from PhosphoSitePlus®, Phospho.ELM, and PhosphoPOINT (). The same method was applied to the kinase-substrate interaction data and the DPPs. Of the kinases with P < 0.05, the kinases belonging to the DEPs or DPPs were selected as key kinases […]


A reverse engineering approach to dissect post translational modulators of transcription factor’s activity from transcriptional data

BMC Bioinformatics
PMCID: 4559297
PMID: 26334955
DOI: 10.1186/s12859-015-0700-3

[…] ir differential Multi-Information and with an associated p-value ().In order to assess the predictive ability of DMI, we collected the known kinases modulating the activity of each of the 14 TFs from PhosphoPOINT [], NetworKIN [] and CEASAR []. We thus obtained a “Golden Standard” for each TF consisting of experimentally verified kinases (Material and Methods). We estimated the performance of DMI […]


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PhosphoPOINT institution(s)
Department of Computer Science and Information Engineering, Taipei, Taiwan, China; Graduate Institute of Biomedical Electronics and Bioinformatics, National Taiwan University, Taiwan, China; Graduate Institute of Networking and Multimedia, National Taiwan University, Taiwan, China; Graduate Institute of Life Sciences, National Defense Medical Center University, Taiwan, China; Division of Hematology and Oncology, Department of Medicine, Taipei Veterans General Hospital, Taipei, Taiwan, China; Institute of Bioinformatics, National Chiao-Tung University, Taiwan, China; Department of Life Science, Fu-Jen Catholic University, Taiwan, China; Department of Biochemistry, Faculty of Medicine, College of Medicine, Kaohsiung Medical University, Taiwan, China; Department of Proteomics Technology, Industrial Technology Research Institute, Taiwan, China; Institute of Clinical Medicine, National Yang-Ming University, Taipei 112, Taiwan, China; Institute of Bio-Pharmaceutical Sciences, National Yang-Ming University, , Taiwan, China; Institute of Biotechnology in Medicine, National Yang-Ming University, Taiwan, China
PhosphoPOINT funding source(s)
Supported by grants from NSC (NSC95-2627-B-400-002 and NSC95-2320-B-010-071-MY3) NSC95-2627-B-030-001, NSC95-2627-B-194-001, NSC95-2627-B-002-011, and NSC95-2221-E-002-126-MY3.

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