PTMcode
Names
More detailed information about this field from each metasource.
PTMcode
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
PTMCode
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:49.339348
ptmcode
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:49.339348
Names
More detailed information about this field from each metasource.
PTMcode
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
PTMCode
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
ptmcode
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
Names
More detailed information about this field from each metasource.
PTMcode
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
PTMCode
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
ptmcode
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
PTMCode is a resource of known and predicted functional associations between protein post-translational modifications (PTMs) within and between interacting proteins.
Description
More detailed information about this field from each metasource.
PTMCode is a resource of known and predicted functional associations between protein post-translational modifications (PTMs) within and between interacting proteins.
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
Functional associations between posttranslational modifications within proteins
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
PTMCode is a resource of known and predicted functional associations between protein post-translational modifications (PTMs) within and between interacting proteins. It currently contains 316,546 modified sites from 69 different PTM types which are also propagated through ortholgs between 19 different eukaryotic species. A total of 1.6 million sites and 17 million functional associations more than 100,000 proteins can currently be explored.
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
Webpage:
http://ptmcode.embl.deWebpage
More detailed information about this field from each metasource.
http://ptmcode.embl.de
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
https://ptmcode.embl.de/
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
Licence:
Name: Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)Licence name
More detailed information about this field from each metasource.
Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
CC-BY-NC-SA-3.0
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
Licence URL
More detailed information about this field from each metasource.
https://creativecommons.org/licenses/by-nc-sa/3.0/
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
Publications:
Publications
More detailed information about this field from each metasource.
Deciphering a global network of functionally associated post-translational modifications
PMID: 22806145
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins
PMID: 23193284
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins
PMID: 25361965
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
http://dx.doi.org/10.1093/nar/gks1230
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:49.339348
Publications
More detailed information about this field from each metasource.
Deciphering a global network of functionally associated post-translational modifications
PMID: 22806145
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins
PMID: 23193284
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins
PMID: 25361965
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
http://dx.doi.org/10.1093/nar/gks1230
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:49.339348
-
Deciphering a global network of functionally associated post-translational modifications
PubMed citations: 97.
97 articles citing: Deciphering a global network of functionally associated post-translational modifications
A Text Mining and Machine Learning Protocol for Extracting Posttranslational Modifications of Proteins from PubMed: A Special Focus on Glycosylation, Acetylation, Methylation, Hydroxylation, and Ubiquitination. PMID:35713865
Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation. PMID:35696084
Carry-over effects of dry period heat stress on the mammary gland proteome and phosphoproteome in the subsequent lactation of dairy cows. PMID:35459770
Protein post-translational modifications in the regulation of cancer hallmarks. PMID:35393571
The auto-inhibition mechanism of transcription factor Ets-1 induced by phosphorylation on the intrinsically disordered region. PMID:35317227
Protein Persulfidation in Plants: Function and Mechanism. PMID:34679765
Extensive regulation of enzyme activity by phosphorylation in Escherichia coli. PMID:34561442
The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation. PMID:34439914
A global map of associations between types of protein posttranslational modifications and human genetic diseases. PMID:34430807
Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review). PMID:34368858
Decoding Post-Translational Modification Crosstalk With Proteomics. PMID:34339852
Insulin signaling regulates longevity through protein phosphorylation in Caenorhabditis elegans. PMID:34315882
Co-occurrence of Protein Crotonylation and 2-Hydroxyisobutyrylation in the Proteome of End-Stage Renal Disease. PMID:34179622
Pan-methylarginine antibody generation using PEG linked GAR motifs as antigens. PMID:34107353
Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics. PMID:33909430
Physiological relevance of post-translational regulation of the spindle assembly checkpoint protein BubR1. PMID:33892776
NAA10 as a New Prognostic Marker for Cancer Progression. PMID:33126484
Ubiquitomics: An Overview and Future. PMID:33080838
Global chemical modifications comparison of human plasma proteome from two different age groups. PMID:32929118
SUMO conjugation regulates immune signalling. PMID:32777975
dBMHCC: A comprehensive hepatocellular carcinoma (HCC) biomarker database provides a reliable prediction system for novel HCC phosphorylated biomarkers. PMID:32497121
Utilization of microRNAs and their regulatory functions for improving biotic stress tolerance in tea plant [Camellia sinensis (L.) O. Kuntze]. PMID:32478595
Post-translational Modification Crosstalk and Hotspots in Sirtuin Interactors Implicated in Cardiovascular Diseases. PMID:32425973
Proteomics Approaches for Biomarker and Drug Target Discovery in ALS and FTD. PMID:31244593
Cellular consequences of arginine methylation. PMID:31101937
Adapting machine-learning algorithms to design gene circuits. PMID:31029103
Time-invariant biological networks with feedback loops: structural equation models and structural identifiability. PMID:30472690
Interaction modulation through arrays of clustered methyl-arginine protein modifications. PMID:30456387
Evolution of In Silico Strategies for Protein-Protein Interaction Drug Discovery. PMID:30082644
PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile. PMID:29989096
Site-specific characterization of endogenous SUMOylation across species and organs. PMID:29942033
PTMscape: an open source tool to predict generic post-translational modifications and map modification crosstalk in protein domains and biological processes. PMID:29876573
Integration of protein phosphorylation, acetylation, and methylation data sets to outline lung cancer signaling networks. PMID:29789295
Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones. PMID:29720613
Nuclear Signaling of Plant MAPKs. PMID:29696029
Identification of human glycosyltransferase genes expressed in erythroid cells predicts potential carbohydrate blood group loci. PMID:29662110
Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications. PMID:28570536
Parameter identifiability-based optimal observation remedy for biological networks. PMID:28472965
Co-occurring protein phosphorylation are functionally associated. PMID:28459814
Protein post-translational modifications: In silico prediction tools and molecular modeling. PMID:28458782
Curated protein information in the Saccharomyces genome database. PMID:28365727
Systematic identification of phosphorylation-mediated protein interaction switches. PMID:28346509
An Asymmetrically Balanced Organization of Kinases versus Phosphatases across Eukaryotes Determines Their Distinct Impacts. PMID:28135269
SUMO and the robustness of cancer. PMID:28134258
Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions. PMID:28079140
Caenorhabditis elegans as a model system to study post-translational modifications of human transthyretin. PMID:27869126
Untargeted metabolomics unravels functionalities of phosphorylation sites in Saccharomyces cerevisiae. PMID:27846849
Proteome-wide Structural Analysis of PTM Hotspots Reveals Regulatory Elements Predicted to Impact Biological Function and Disease. PMID:27697855
Evolutionary conservation of Ebola virus proteins predicts important functions at residue level. PMID:27659453
The Role of Genomic Profiling in Advanced Breast Cancer: The Two Faces of Janus. PMID:27547031
BioTriangle: a web-accessible platform for generating various molecular representations for chemicals, proteins, DNAs/RNAs and their interactions. PMID:27330567
Structural identifiability of cyclic graphical models of biological networks with latent variables. PMID:27296452
dbPAF: an integrative database of protein phosphorylation in animals and fungi. PMID:27010073
Comparing Alzheimer's and Parkinson's diseases networks using graph communities structure. PMID:26935435
Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations. PMID:26659599
Systematic Analysis and Prediction of In Situ Cross Talk of O-GlcNAcylation and Phosphorylation. PMID:26601103
Histone H4 Lysine 20 (H4K20) Methylation, Expanding the Signaling Potential of the Proteome One Methyl Moiety at a Time. PMID:26598646
Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase. PMID:26350458
Prediction of Functionally Important Phospho-Regulatory Events in Xenopus laevis Oocytes. PMID:26312481
Post-translational modifications of the cardiac proteome in diabetes and heart failure. PMID:26140508
A Comparative Analysis and Review of lysyl Residues Affected by Posttranslational Modifications. PMID:26085811
Structural Analysis of PTM Hotspots (SAPH-ire)--A Quantitative Informatics Method Enabling the Discovery of Novel Regulatory Elements in Protein Families. PMID:26070665
Quantitative Profiling of Lysine Acetylation Reveals Dynamic Crosstalk between Receptor Tyrosine Kinases and Lysine Acetylation. PMID:25978619
Large-scale analysis of the evolutionary histories of phosphorylation motifs in the human genome. PMID:25949811
Metabolic dependencies drive species co-occurrence in diverse microbial communities. PMID:25941371
The roles of post-translational modifications in the context of protein interaction networks. PMID:25692714
Systematic characterization and prediction of post-translational modification cross-talk. PMID:25605461
Systematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues. PMID:25476580
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins. PMID:25361965
Integrating phosphoproteomics in systems biology. PMID:25349677
Exploiting holistic approaches to model specificity in protein phosphorylation. PMID:25324856
Fast and accurate discovery of degenerate linear motifs in protein sequences. PMID:25207816
Physicochemical mechanisms of protein regulation by phosphorylation. PMID:25147561
In silico analysis of protein Lys-N(𝜀)-acetylation in plants. PMID:25136347
Investigating co-evolution of functionally associated phosphosites in human. PMID:25005854
A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases. PMID:24974292
Engram formation in psychiatric disorders. PMID:24904262
The structural and functional signatures of proteins that undergo multiple events of post-translational modification. PMID:24888500
A Proteome-wide Domain-centric Perspective on Protein Phosphorylation. PMID:24830415
DoReMi: context-based prioritization of linear motif matches. PMID:24711967
SysPTM 2.0: an updated systematic resource for post-translational modification. PMID:24705204
Toward understanding the structure of the vertebrate nuclear pore complex. PMID:24699243
Functional divergence and evolutionary turnover in mammalian phosphoproteomes. PMID:24465218
Evolution and functional cross-talk of protein post-translational modifications. PMID:24366814
A novel pulse-chase SILAC strategy measures changes in protein decay and synthesis rates induced by perturbation of proteostasis with an Hsp90 inhibitor. PMID:24312217
wKinMut: an integrated tool for the analysis and interpretation of mutations in human protein kinases. PMID:24289158
Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation. PMID:24267725
PhosphoChain: a novel algorithm to predict kinase and phosphatase networks from high-throughput expression data. PMID:23832245
Monitoring of post-translational modification dynamics with genetically encoded fluorescent reporters. PMID:23576192
Perspectives on epigenetic-based immune intervention for rheumatic diseases. PMID:23510070
Dual coordination of post translational modifications in human protein networks. PMID:23505349
Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation. PMID:23418452
Concise review: new paradigms for Down syndrome research using induced pluripotent stem cells: tackling complex human genetic disease. PMID:23413375
Deciphering post-translational modification codes. PMID:23402885
STRING v9.1: protein-protein interaction networks, with increased coverage and integration. PMID:23203871
PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins. PMID:23193284
Cells, shared memory and breaking the PTM code. PMID:22866336 -
PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins
PubMed citations: 51.
51 articles citing: PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins
Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation. PMID:35696084
Current status of PTMs structural databases: applications, limitations and prospects. PMID:35020020
UNFERTILIZED EMBRYO SAC 12 phosphorylation plays a crucial role in conferring salt tolerance. PMID:34904673
Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation. PMID:34738012
Decoding Post-Translational Modification Crosstalk With Proteomics. PMID:34339852
Physiological relevance of post-translational regulation of the spindle assembly checkpoint protein BubR1. PMID:33892776
A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications. PMID:33821625
The ubiquitin proteoform problem. PMID:33813043
Robust inference of kinase activity using functional networks. PMID:33608514
Dysregulation of USP18/FTO/PYCR1 signaling network promotes bladder cancer development and progression. PMID:33461172
Polyphyllin VII suppresses cell proliferation, the cell cycle and cell migration in colorectal cancer. PMID:33240431
NAA10 as a New Prognostic Marker for Cancer Progression. PMID:33126484
Hsp60 Post-translational Modifications: Functional and Pathological Consequences. PMID:32582761
Post-translational Modification Crosstalk and Hotspots in Sirtuin Interactors Implicated in Cardiovascular Diseases. PMID:32425973
MusiteDeep: a deep-learning based webserver for protein post-translational modification site prediction and visualization. PMID:32324217
Identification of dual histone modification-binding protein interaction by combining mass spectrometry and isothermal titration calorimetric analysis. PMID:31956440
Networking of predicted post-translational modification (PTM) sites in human EGFR. PMID:31485130
Clinically Relevant Post-Translational Modification Analyses-Maturing Workflows and Bioinformatics Tools. PMID:30577541
Time-invariant biological networks with feedback loops: structural equation models and structural identifiability. PMID:30472690
Post-translational modifications in MeHg-induced neurotoxicity. PMID:30385410
qPhos: a database of protein phosphorylation dynamics in humans. PMID:30380102
PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile. PMID:29989096
Estimating the Distribution of Protein Post-Translational Modification States by Mass Spectrometry. PMID:29945451
PTMscape: an open source tool to predict generic post-translational modifications and map modification crosstalk in protein domains and biological processes. PMID:29876573
Direct Profiling the Post-Translational Modification Codes of a Single Protein Immobilized on a Surface Using Cu-free Click Chemistry. PMID:29806008
YAAM: Yeast Amino Acid Modifications Database. PMID:29688347
Parameter identifiability-based optimal observation remedy for biological networks. PMID:28472965
Prediction of post-translational modification sites using multiple kernel support vector machine. PMID:28462053
Systematic identification of phosphorylation-mediated protein interaction switches. PMID:28346509
iPTMnet: Integrative Bioinformatics for Studying PTM Networks. PMID:28150246
yMap: an automated method to map yeast variants to protein modifications and functional regions. PMID:27797766
Proteome-wide Structural Analysis of PTM Hotspots Reveals Regulatory Elements Predicted to Impact Biological Function and Disease. PMID:27697855
A machine learning strategy for predicting localization of post-translational modification sites in protein-protein interacting regions. PMID:27534850
BioTriangle: a web-accessible platform for generating various molecular representations for chemicals, proteins, DNAs/RNAs and their interactions. PMID:27330567
Structural identifiability of cyclic graphical models of biological networks with latent variables. PMID:27296452
Systematic Analysis and Prediction of In Situ Cross Talk of O-GlcNAcylation and Phosphorylation. PMID:26601103
Nonsynonymous Single-Nucleotide Variations on Some Posttranslational Modifications of Human Proteins and the Association with Diseases. PMID:26495027
Post-translational modifications of the cardiac proteome in diabetes and heart failure. PMID:26140508
Structural Analysis of PTM Hotspots (SAPH-ire)--A Quantitative Informatics Method Enabling the Discovery of Novel Regulatory Elements in Protein Families. PMID:26070665
PEIMAN 1.0: Post-translational modification Enrichment, Integration and Matching ANalysis. PMID:25911152
The roles of post-translational modifications in the context of protein interaction networks. PMID:25692714
Tissue-aware data integration approach for the inference of pathway interactions in metazoan organisms. PMID:25431329
ProteomeScout: a repository and analysis resource for post-translational modifications and proteins. PMID:25414335
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins. PMID:25361965
SMART: recent updates, new developments and status in 2015. PMID:25300481
Human germline and pan-cancer variomes and their distinct functional profiles. PMID:25232094
Engram formation in psychiatric disorders. PMID:24904262
PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins. PMID:24857970
SysPTM 2.0: an updated systematic resource for post-translational modification. PMID:24705204
Regulation of transcription factor activity by interconnected post-translational modifications. PMID:24388790
Perspectives on epigenetic-based immune intervention for rheumatic diseases. PMID:23510070 -
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins
PubMed citations: 33.
33 articles citing: PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins
Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation. PMID:35696084
Current status of PTMs structural databases: applications, limitations and prospects. PMID:35020020
Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment. PMID:34924561
Mapping protein carboxymethylation sites provides insights into their role in proteostasis and cell proliferation. PMID:34795246
A global map of associations between types of protein posttranslational modifications and human genetic diseases. PMID:34430807
P2T2: Protein Panoramic annoTation Tool for the interpretation of protein coding genetic variants. PMID:34377961
Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment. PMID:34368138
Decoding Post-Translational Modification Crosstalk With Proteomics. PMID:34339852
Regulation of the Phosphoinositide Code by Phosphorylation of Membrane Readers. PMID:34069055
Advances on Plant Ubiquitylome-From Mechanism to Application. PMID:33114409
Co-phosphorylation networks reveal subtype-specific signaling modules in breast cancer. PMID:32730576
The Controversial Roles of ADP-Ribosyl Hydrolases MACROD1, MACROD2 and TARG1 in Carcinogenesis. PMID:32151005
Proteomics of Long-Lived Mammals. PMID:31737995
Clinically Relevant Post-Translational Modification Analyses-Maturing Workflows and Bioinformatics Tools. PMID:30577541
Kinome-wide identification of phosphorylation networks in eukaryotic proteomes. PMID:30016513
Unravelling the pathogenic role and genotype-phenotype correlation of the USH2A p.(Cys759Phe) variant among Spanish families. PMID:29912909
PTMscape: an open source tool to predict generic post-translational modifications and map modification crosstalk in protein domains and biological processes. PMID:29876573
Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones. PMID:29720613
iPTMnet: an integrated resource for protein post-translational modification network discovery. PMID:29145615
20 years of the SMART protein domain annotation resource. PMID:29040681
Co-occurring protein phosphorylation are functionally associated. PMID:28459814
Systematic identification of phosphorylation-mediated protein interaction switches. PMID:28346509
proGenomes: a resource for consistent functional and taxonomic annotations of prokaryotic genomes. PMID:28053165
yMap: an automated method to map yeast variants to protein modifications and functional regions. PMID:27797766
Molecular Principles of Gene Fusion Mediated Rewiring of Protein Interaction Networks in Cancer. PMID:27540857
Systems Level Analysis of Histone H3 Post-translational Modifications (PTMs) Reveals Features of PTM Crosstalk in Chromatin Regulation. PMID:27302890
Engineering of Methylation State Specific 3xMBT Domain Using ELISA Screening. PMID:27111853
Spatiotemporal variation of mammalian protein complex stoichiometries. PMID:26975353
In situ structural analysis of the human nuclear pore complex. PMID:26416747
Advances in computational approaches for prioritizing driver mutations and significantly mutated genes in cancer genomes. PMID:26307061
PEIMAN 1.0: Post-translational modification Enrichment, Integration and Matching ANalysis. PMID:25911152
Systematic characterization and prediction of post-translational modification cross-talk. PMID:25605461
The 2015 Nucleic Acids Research Database Issue and molecular biology database collection. PMID:25593347 - http://dx.doi.org/10.1093/nar/gks1230
Tags:
Tags
More detailed information about this field from each metasource.
functional association
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
post-translational protein modification
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
protein interaction
metasource: Fairsharing.org
version: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metabolic and signaling pathways
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
protein-protein interactions
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
bioinformatics
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:49.339348
Tags
More detailed information about this field from each metasource.
functional association
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
post-translational protein modification
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
protein interaction
metasource: Fairsharing.orgversion: FAIRsharing.org: PTMcode; PTMcode; DOI: https://doi.org/10.25504/FAIRsharing.96xqbf; Last edited: Jan. 8, 2019, 1:15 p.m.; Last accessed: Jan 03 2022 7:05 p.m.
metabolic and signaling pathways
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
protein-protein interactions
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
bioinformatics
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:49.339348
functional association post-translational protein modification protein interaction metabolic and signaling pathways protein-protein interactions bioinformatics
Need help integrating and/or managing biomedical data?