ArticlePloS one2014
mUbiSiDa: a comprehensive database for protein ubiquitination sites in mammals.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 66 citations in OpenAlex.
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- Methods to Study the Molecular Mechanism and Drive the Design of Protein Degraders.Chemical reviews · 2026Review
- E3 ubiquitin ligase SKP2 limits autophagosome formation duringFrontiers in cellular and infection microbiology · 2026Article
- Protein modification by a eukaryotic-like ubiquitin-related modifier in the hyperthermophilic archaeonmSystems · 2025Article
- Combining evidence from human genetic and functional screens to identify pathways altering obesity and fat distribution.American journal of human genetics · 2025Article
- Subversion of the host endocytic pathway by Legionella pneumophila-mediated ubiquitination of Rab5.The Journal of cell biology · 2025Article
- Insight into Protein Engineering: FromCurrent pharmaceutical design · 2025Review
- Towards the Targeted Protein Degradation of PRMT1.ChemMedChem · 2024Article
- GPS-SUMO 2.0: an updated online service for the prediction of SUMOylation sites and SUMO-interacting motifs.Nucleic acids research · 2024Article
- Bioinformatics analysis and alternative polyadenylation in Heat Shock Proteins 70 (HSP70) family members.International journal of physiology, pathophysiology and pharmacology · 2024Article
- A New Potential Therapeutic Target for Cancer in Ubiquitin-Like Proteins-UBL3.International journal of molecular sciences · 2023Review
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- ILRUN Promotes Atherosclerosis Through Lipid-Dependent and Lipid-Independent Factors.Arteriosclerosis, thrombosis, and vascular biology · 2022Article
- Targeting the mRNA endonuclease CPSF73 inhibits breast cancer cell migration, invasion, and self-renewal.iScience · 2022Article
- A versatile new tool derived from a bacterial deubiquitylase to detect and purify ubiquitylated substrates and their interacting proteins.PLoS biology · 2022Article
- CPLM 4.0: an updated database with rich annotations for protein lysine modifications.Nucleic acids research · 2022Article
- Mini-review: Recent advances in post-translational modification site prediction based on deep learning.Computational and structural biotechnology journal · 2022Review
- The PROTACtable genome.Nature reviews. Drug discovery · 2021Review
- On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3' End Nuclease.Trends in biochemical sciences · 2021Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
motivationProtein ubiquitination is one of the important post-translational modifications by attaching ubiquitin to specific lysine (K) residues in target proteins, and plays important regulatory roles in many cell processes. Recent studies indicated that abnormal protein ubiquitination have been implicated in many diseases by degradation of many key regulatory proteins including tumor suppressor, oncoprotein, and cell cycle regulator. The detailed information of protein ubiquitination sites is useful for scientists to investigate the mechanism of many cell activities and related diseases.
resultsIn this study we established mUbiSida for mammalian Ubiquitination Site Database, which provides a scientific community with a comprehensive, freely and high-quality accessible resource of mammalian protein ubiquitination sites. In mUbiSida, we deposited about 35,494 experimentally validated ubiquitinated proteins with 110,976 ubiquitination sites from five species. The mUbiSiDa can also provide blast function to predict novel protein ubiquitination sites in other species by blast the query sequence in the deposit sequences in mUbiSiDa. The mUbiSiDa was designed to be a widely used tool for biologists and biomedical researchers with a user-friendly interface, and facilitate the further research of protein ubiquitination, biological networks and functional proteomics. The mUbiSiDa database is freely available at http://reprod.njmu.edu.cn/mUbiSiDa.
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