Evidence map›Paper›PMID 42117294›Full record

ArticleDatabase : the journal of biological databases and curation2026

CysDBase: a comprehensive database of cysteine post-translational modifications across protein sequence, structure, microenvironment, class, cellular localization, biological pathway, and taxonomy.

Devarakonda Himaja, Debashree Bandyopadhyay

Abstract read
In one paragraph

Article in Database : the journal of biological databases and curation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Devarakonda HimajaDepartment of Biological Sciences, Birla Institute of Technology and Science, Pilani, Hyderabad Campus, Hyderabad 500078, India.
Debashree BandyopadhyayDepartment of Biological Sciences, Birla Institute of Technology and Science, Pilani, Hyderabad Campus, Hyderabad 500078, India.ORCID 0000-0003-4131-907X

Funding

Department of Science and TechnologyIndian Council of Medical ResearchScience and Engineering Research Board EMR/2017/002953SRF BMI/11(99)/2022
6 · The paper itself

Abstract

The reactive thiol group of cysteine (Cys) acts as a nucleophile and undergoes many cysteine post-translational modifications (Cys-PTMs). Cys-PTMs, called protein redox switch, contribute to various cellular and physiological processes, including reactive oxygen species (ROS)-induced signalling, ROS mitigation, and scavenging. Consolidation of Cys-PTMs into a database would facilitate the mechanistic elucidation of biological processes and therapeutic applications. The existing databases store information on cysteine motifs, oxidation states, a few of the Cys-PTMs, etc., specific to species or kingdoms, and lack general applicability. There was no mention of the impact of the protein microenvironments and cellular localizations on the Cys-PTMs. The current study reports a database containing 7 Cys-PTMs (disulphide, S-nitrosylation, S-palmitoylation, S-glutathionylation, S-sulphenylation, metal-binding, and thioether), 11 features, 33 06 395 UniProt IDs, and 1 14 56 639 cysteine residues, across the taxonomy, encompassing cellular organelles, enzyme classes, sequence motifs, protein structures, and microenvironments. The maximum number of cysteine residues is reported here compared to 16 contemporary cysteine databases. Twenty-one types of metal-binding cysteines and thioether modifications are reported for the first time. Enzyme classes, cellular localization, taxonomic preferences, and microenvironment around Cys-PTMs were systematically analysed and curated, indicating the pathogenic involvement of those Cys-PTMs. The database has a web access (https://cysdbase.bits-hyderabad.ac.in/) and a programmatic access via GitHub link (https://github.com/devhimd19/CysDBase). The query inputs to the repositories are UniProt ID, biological pathway, location, or genus name. Query outputs are 11 biological features, namely, protein name, Cys-PTMs, cysteine residue number, cysteine sequence motif, cell organelle, biological pathway, protein microenvironment (buried fraction and relative hydrophobicity [rHpy]), EC number and enzyme class, secondary structure, organism, and PubMed ID.

Indexed as

Cellular MicroenvironmentCysteineDatabases, ProteinProtein Processing, Post-TranslationalProteinsAmino Acid SequenceAnimalsBiocurationHumansCysteineProteins

Identifiers

PMID42117294
PMCPMC13161762

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.