The human DEPhOsphorylation Database
Names
More detailed information about this field from each metasource.
The human DEPhOsphorylation Database
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
DEPOD
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
DEPhOsphorylation Database
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
Human Dephosphorylation Database (DEPOD)
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
Names
More detailed information about this field from each metasource.
The human DEPhOsphorylation Database
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
DEPOD
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
DEPhOsphorylation Database
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
Human Dephosphorylation Database (DEPOD)
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
Other names: DEPOD, DEPhOsphorylation Database, Human Dephosphorylation Database (DEPOD)
Names
More detailed information about this field from each metasource.
The human DEPhOsphorylation Database
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
DEPOD
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
DEPhOsphorylation Database
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
Human Dephosphorylation Database (DEPOD)
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
DEPOD - the human DEPhOsphorylation Database is a manually curated database collecting human active and inactive phosphatases, their experimentally verified protein and non-protein substrates, and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates.
Description
More detailed information about this field from each metasource.
DEPOD - the human DEPhOsphorylation Database is a manually curated database collecting human active and inactive phosphatases, their experimentally verified protein and non-protein substrates, and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates.
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
DEPOD - the human DEPhOsphorylation Database (version 1.1) is a manually curated database collecting human active and inactive phosphatases, their experimentally verified protein and non-protein substrates, and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates. DEPOD aims to be a valuable resource for studying human phosphatases and their substrate specificities and molecular mechanisms; phosphatase-targeted drug discovery and development; connecting phosphatases with kinases through their common substrates; completing the human phosphorylation/dephosphorylation network.
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
DEPOD - the human DEPhOsphorylation Database (version 1.1) is a manually curated database collecting human active phosphatases, their experimentally verified protein and non-protein substrates and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates. DEPOD aims to be a valuable resource for studying human phosphatases and their substrate specificities and molecular mechanisms; phosphatase-targeted drug discovery and development; connecting phosphatases with kinases through their common substrates; completing the human phosphorylation/dephosphorylation network.
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
DEPOD - the human DEPhOsphorylation Database, is a manually curated database collecting human phosphatases, their experimentally verified substrates and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates.
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
Webpage:
http://www.depod.org/Webpage
More detailed information about this field from each metasource.
http://www.depod.org/
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
http://www.depod.org
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
http://depod.bioss.uni-freiburg.de/
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
Licence:
Name: CopyrightsLicence name
More detailed information about this field from each metasource.
Copyrights
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
Licence URL
More detailed information about this field from each metasource.
https://www.ebi.ac.uk/about/terms-of-use
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
Publications:
Publications
More detailed information about this field from each metasource.
Elucidating human phosphatase-substrate networks
PMID: 23674824
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
The human DEPhOsphorylation database DEPOD: a 2015 update
PMID: 25332398
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
The human DEPhOsphorylation Database DEPOD: 2019 update
PMID: 31836896
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
http://dx.doi.org/10.1093/nar/gku1009
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
Publications
More detailed information about this field from each metasource.
Elucidating human phosphatase-substrate networks
PMID: 23674824
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
The human DEPhOsphorylation database DEPOD: a 2015 update
PMID: 25332398
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
The human DEPhOsphorylation Database DEPOD: 2019 update
PMID: 31836896
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
http://dx.doi.org/10.1093/nar/gku1009
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
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Elucidating human phosphatase-substrate networks
PubMed citations: 57.
57 articles citing: Elucidating human phosphatase-substrate networks
Cryptococcus neoformans Infection Induces IL-17 Production by Promoting STAT3 Phosphorylation in CD4+ T Cells. PMID:35720334
Differential mRNA Expression Profiling Reveals the Role of MiR-375 in Inflammation of Bovine Mammary Epithelial Cells. PMID:35681895
The phosphorylation to acetylation/methylation cascade in transcriptional regulation: how kinases regulate transcriptional activities of DNA/histone-modifying enzymes. PMID:35659740
Designing bioresponsive nanomaterials for intracellular self-assembly. PMID:35382500
Unconventional protein post-translational modifications: the helmsmen in breast cancer. PMID:35216622
PTPN2, A Key Predictor of Prognosis for Pancreatic Adenocarcinoma, Significantly Regulates Cell Cycles, Apoptosis, and Metastasis. PMID:35154122
Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs. PMID:34989786
Regulation of Viral Restriction by Post-Translational Modifications. PMID:34835003
Higher-order phosphatase-substrate contacts terminate the integrated stress response. PMID:34625748
Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling. PMID:34526379
Protein Phosphatase 1 Regulates Human Cytomegalovirus Protein Translation by Restraining AMPK Signaling. PMID:34335531
Computational Phosphorylation Network Reconstruction: An Update on Methods and Resources. PMID:34270057
Protein Kinase C-Mediated Phosphorylation and α2δ-1 Interdependently Regulate NMDA Receptor Trafficking and Activity. PMID:34252035
Phosphorylation of TRIP13 at Y56 induces radiation resistance but sensitizes head and neck cancer to cetuximab. PMID:34111559
Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions. PMID:34100859
Phosphoregulation of the autophagy machinery by kinases and phosphatases. PMID:33970777
Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics. PMID:33909430
Integrated Proteomic and Phosphoproteomics Analysis of DKK3 Signaling Reveals Activated Kinase in the Most Aggressive Gallbladder Cancer. PMID:33670899
Serine/threonine phosphatases in osteoclastogenesis and bone resorption. PMID:33338510
Integrative proteomics reveals principles of dynamic phosphosignaling networks in human erythropoiesis. PMID:33259127
In vitro and in silico evaluation of the inhibitory effect of a curcumin-based oxovanadium (IV) complex on alkaline phosphatase activity and bacterial biofilm formation. PMID:33191462
Modular bioengineered kinase sensors via scaffold protein-mediated split-luciferase complementation. PMID:32874496
Characterization of Kinase Expression Related to Increased Migration of PC-3M Cells Using Global Comparative Phosphoproteome Analysis. PMID:32859632
Dissecting the sequence determinants for dephosphorylation by the catalytic subunits of phosphatases PP1 and PP2A. PMID:32681005
The expression patterns and the diagnostic/prognostic roles of PTPN family members in digestive tract cancers. PMID:32536826
Turn and Face the Strange: A New View on Phosphatases. PMID:32341996
Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide. PMID:31841001
The human DEPhOsphorylation Database DEPOD: 2019 update. PMID:31836896
Machine learning empowers phosphoproteome prediction in cancers. PMID:31410451
Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin. PMID:31375679
Identifying New Substrates and Functions for an Old Enzyme: Calcineurin. PMID:31308145
The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell-cell adhesion. PMID:30924770
Calcineurin dephosphorylates Kelch-like 3, reversing phosphorylation by angiotensin II and regulating renal electrolyte handling. PMID:30718414
Protein phosphatases in the regulation of mitosis. PMID:30446607
iEKPD 2.0: an update with rich annotations for eukaryotic protein kinases, protein phosphatases and proteins containing phosphoprotein-binding domains. PMID:30380109
Interrogating Protein Phosphatases with Chemical Activity Probes. PMID:29338103
Kinetic characterization of the inhibition of protein tyrosine phosphatase-1B by Vanadyl (VO2+) chelates. PMID:29071441
Functional Genomics Approach Identifies Novel Signaling Regulators of TGFα Ectodomain Shedding. PMID:29018056
Miklós Bodanszky Award Lecture: Advances in the selective targeting of protein phosphatase-1 and phosphatase-2A with peptides. PMID:28876538
The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review). PMID:28656226
Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1). PMID:28522851
A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. PMID:28065597
Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM. PMID:27974827
Modulation of VEGF receptor 2 signaling by protein phosphatases. PMID:27888154
Phosphoprotein Phosphatase 1 Is Required for Extracellular Calcium-Induced Keratinocyte Differentiation. PMID:27340655
Prediction and verification of novel peptide targets of protein tyrosine phosphatase 1B. PMID:27025565
Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases. PMID:26617522
Phosphotyrosine Substrate Sequence Motifs for Dual Specificity Phosphatases. PMID:26302245
Procyanidins Negatively Affect the Activity of the Phosphatases of Regenerating Liver. PMID:26226290
Integrating phosphoproteomics in systems biology. PMID:25349677
The human DEPhOsphorylation database DEPOD: a 2015 update. PMID:25332398
Biochemical evaluation of virtual screening methods reveals a cell-active inhibitor of the cancer-promoting phosphatases of regenerating liver. PMID:25159123
The calcineurin signaling network evolves via conserved kinase-phosphatase modules that transcend substrate identity. PMID:24930733
Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways. PMID:24847354
Quantitative phosphoproteomics unveils temporal dynamics of thrombin signaling in human endothelial cells. PMID:24501219
EKPD: a hierarchical database of eukaryotic protein kinases and protein phosphatases. PMID:24214991
Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery. PMID:23969317 -
The human DEPhOsphorylation database DEPOD: a 2015 update
PubMed citations: 34.
34 articles citing: The human DEPhOsphorylation database DEPOD: a 2015 update
Mini-review: Recent advances in post-translational modification site prediction based on deep learning. PMID:35860402
Proteogenomic characterization of pancreatic ductal adenocarcinoma. PMID:34534465
Computational Phosphorylation Network Reconstruction: An Update on Methods and Resources. PMID:34270057
Protein tyrosine phosphatases in cell adhesion. PMID:33710332
Proteogenomic and metabolomic characterization of human glioblastoma. PMID:33577785
Using phosphoproteomics data to understand cellular signaling: a comprehensive guide to bioinformatics resources. PMID:32676006
Turn and Face the Strange: A New View on Phosphatases. PMID:32341996
Proteogenomic Characterization of Endometrial Carcinoma. PMID:32059776
The human DEPhOsphorylation Database DEPOD: 2019 update. PMID:31836896
NicheNet: modeling intercellular communication by linking ligands to target genes. PMID:31819264
Global redox proteome and phosphoproteome analysis reveals redox switch in Akt. PMID:31792197
Ouabain-regulated phosphoproteome reveals molecular mechanisms for Na+, K+-ATPase control of cell adhesion, proliferation, and survival. PMID:31199885
Mapping connections in signaling networks with ambiguous modularity. PMID:31149348
Phosphoproteome Analysis of Cells Infected with Adapted and Nonadapted Influenza A Virus Reveals Novel Pro- and Antiviral Signaling Networks. PMID:30996098
The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell-cell adhesion. PMID:30924770
A deep proteome and transcriptome abundance atlas of 29 healthy human tissues. PMID:30777892
Clinically Relevant Post-Translational Modification Analyses-Maturing Workflows and Bioinformatics Tools. PMID:30577541
iEKPD 2.0: an update with rich annotations for eukaryotic protein kinases, protein phosphatases and proteins containing phosphoprotein-binding domains. PMID:30380109
Post-translational Modification-Based Regulation of HIV Replication. PMID:30254620
Petri net-based prediction of therapeutic targets that recover abnormally phosphorylated proteins in muscle atrophy. PMID:29506508
Phosphoproteomics-Based Profiling of Kinase Activities in Cancer Cells. PMID:29344887
KiPho: malaria parasite kinome and phosphatome portal. PMID:29220464
Functional Genomics Approach Identifies Novel Signaling Regulators of TGFα Ectodomain Shedding. PMID:29018056
Tartrate-resistant acid phosphatase (TRAP/ACP5) promotes metastasis-related properties via TGFβ2/TβR and CD44 in MDA-MB-231 breast cancer cells. PMID:28915803
Miklós Bodanszky Award Lecture: Advances in the selective targeting of protein phosphatase-1 and phosphatase-2A with peptides. PMID:28876538
Isoelectric point-based fractionation by HiRIEF coupled to LC-MS allows for in-depth quantitative analysis of the phosphoproteome. PMID:28674419
Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1). PMID:28522851
Tissue-Specific Signaling Networks Rewired by Major Somatic Mutations in Human Cancer Revealed by Proteome-Wide Discovery. PMID:28364002
Protein Bioinformatics Databases and Resources. PMID:28150231
The harmonizome: a collection of processed datasets gathered to serve and mine knowledge about genes and proteins. PMID:27374120
Enrichr: a comprehensive gene set enrichment analysis web server 2016 update. PMID:27141961
Unbiased identification of substrates of protein tyrosine phosphatase ptp-3 in C. elegans. PMID:27067626
Prediction and verification of novel peptide targets of protein tyrosine phosphatase 1B. PMID:27025565
DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites. PMID:27002216 -
The human DEPhOsphorylation Database DEPOD: 2019 update
PubMed citations: 11.
11 articles citing: The human DEPhOsphorylation Database DEPOD: 2019 update
Evolutionary genomic relationships and coupling in MK-STYX and STYX pseudophosphatases. PMID:35264672
Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs. PMID:34989786
Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling. PMID:34526379
Proteome Landscape of Epithelial-to-Mesenchymal Transition (EMT) of Retinal Pigment Epithelium Shares Commonalities With Malignancy-Associated EMT. PMID:34455105
DTL-DephosSite: Deep Transfer Learning Based Approach to Predict Dephosphorylation Sites. PMID:34249915
A data-independent acquisition-based global phosphoproteomics system enables deep profiling. PMID:33953186
Integrated intra- and intercellular signaling knowledge for multicellular omics analysis. PMID:33749993
Alterations in the Global Proteome and Phosphoproteome in Third Generation EGFR TKI Resistance Reveal Drug Targets to Circumvent Resistance. PMID:33727228
canSAR: update to the cancer translational research and drug discovery knowledgebase. PMID:33219674
l-Lactate Dehydrogenase Identified as a Protein Tyrosine Phosphatase 1B Substrate by Using K-BIPS. PMID:33002308
Turn and Face the Strange: A New View on Phosphatases. PMID:32341996 - http://dx.doi.org/10.1093/nar/gku1009
Tags:
Tags
More detailed information about this field from each metasource.
phosphoprotein
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
phosphorylation
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
post-translational protein modification
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein expression profiling
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
regulation of post-translational protein modification
metasource: Fairsharing.org
version: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein sequence databases
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
databases of individual protein families
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
bioinformatics
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
enzyme
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
non-protein substrates
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
phosphatase
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
protein substrates
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
proteomics
metasource: re3data.org
version: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
protein interactions
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
data submission, annotation and curation
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
database management
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
small molecules
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
sequence sites, features and motifs
metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:32.140470
Tags
More detailed information about this field from each metasource.
phosphoprotein
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
phosphorylation
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
post-translational protein modification
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein expression profiling
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
regulation of post-translational protein modification
metasource: Fairsharing.orgversion: FAIRsharing.org: DEPOD; The human DEPhOsphorylation Database; DOI: https://doi.org/10.25504/FAIRsharing.q9j2e3; Last edited: Jan. 8, 2019, 1:21 p.m.; Last accessed: Jan 03 2022 7:09 p.m.
protein sequence databases
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
databases of individual protein families
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
bioinformatics
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
enzyme
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
non-protein substrates
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
phosphatase
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
protein substrates
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
proteomics
metasource: re3data.orgversion: re3data.org: DEPOD; editing status 2022-05-13; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3GP9F last accessed: 2022-11-04
protein interactions
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
data submission, annotation and curation
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
database management
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
small molecules
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
sequence sites, features and motifs
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:29:32.140470
phosphoprotein phosphorylation post-translational protein modification protein protein expression profiling regulation of post-translational protein modification protein sequence protein family bioinformatics enzyme non-protein substrates phosphatase protein substrates proteomics protein interaction data submission, annotation and curation data management small molecule sequence sites, features and motifs
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