hmrbase

hmrbase curates detailed information on hormones, hormone receptors, and hormone–receptor interactions to support studies of endocrine signaling.

Key Features:

• Extensive Data Collection: Compiles information from literature sources and public databases documenting approximately 2,000 hormones and 3,000 hormone receptors, including hormone functions, source organisms, receptor sequences, subcellular localizations, ligands, and post-translational modifications.
• Hormone-Receptor Pair Information: Provides detailed records of approximately 4,100 hormone–receptor pairs to support analysis of specificity and signaling mechanisms.
• Integrated Computational Tools: Includes keyword search, structure-based search, peptide mapping, and sequence similarity search for analysis and comparison of hormones and receptors.
• Pfam Domain Annotations: Supplies Pfam domain annotations for hormone and receptor proteins to aid interpretation of functional domains.
• External Links and Resources: Links entries to other relevant databases and external resources for cross-referencing biological information.
• DrugPedia Linkage: Integrates with DrugPedia to associate hormones and receptors with potential therapeutic and drug-related information.
• Categorical Browsing Options: Organizes data for browsing by categories relevant to hormones and receptors.
• Online Data Submission: Accepts community-contributed data submissions for incorporation into the database.

Scientific Applications:

• Endocrine signaling research: Supports exploration of hormone–receptor interactions and signaling pathways at molecular and systems levels.
• Disease-focused studies: Enables investigation of hormonal roles in conditions such as cancer, osteoporosis, and diabetes where endocrine imbalance is implicated.
• Therapeutic target analysis: Facilitates elucidation of molecular mechanisms and identification of targets for development of targeted therapies.

Methodology:

Data were compiled by curation of literature and public databases and integrated with online computational tools and external resources, with Pfam domain annotations provided for protein entries.