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.

Documentation