HIstome
HIstome catalogs a manually curated relational database of 55 human histone proteins, 106 post-translational modification (PTM) sites, and 152 histone-modifying enzymes to support analysis of histone variants, PTMs, and enzyme-mediated chromatin regulation.
Key Features:
- Histone Proteins: Contains detailed entries for 55 human histone proteins, including histone variants.
- Post-Translational Modifications (PTMs): Catalogs 106 distinct PTM sites associated with those histones.
- Histone-Modifying Enzymes: Includes data on 152 enzymes responsible for addition and removal of histone modifications, categorized by catalytic function.
- Categorizations: Organizes entries into five types of histones, eight types of PTMs, and fourteen categories of modifying enzymes.
- Relational Database Structure: Implements a relational schema linking histone proteins, PTM sites, and modifying enzymes to enable cross-referenced queries.
Scientific Applications:
- Epigenetics research: Supports analysis of histone variants and PTM patterns underlying chromatin structure and gene regulation.
- Pharmacology and target discovery: Facilitates identification and annotation of histone-modifying enzymes relevant to drug development.
- Clinical and translational studies: Enables investigation of histone modification patterns and enzyme dysregulation in pathological conditions.
- Gene regulation studies: Aids exploration of how specific PTMs and modifying enzymes contribute to transcriptional control.
Methodology:
Manually curated from up-to-date scientific literature and implemented as a relational database linking histone proteins, PTM sites, and modifying enzymes.
Topics
Details
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Programming Languages:
- SQL
- Added:
- 3/30/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Khare SP, Habib F, Sharma R, Gadewal N, Gupta S, Galande S. HIstome--a relational knowledgebase of human histone proteins and histone modifying enzymes. Nucleic Acids Research. 2011;40(D1):D337-D342. doi:10.1093/nar/gkr1125. PMID:22140112. PMCID:PMC3245077.