BoMiProt

BoMiProt provides a curated repository of bovine milk proteins, consolidating proteomic data from over 300 publications on composition changes driven by seasons, lactation stages, breeds, health status, and milk fractions, and supplying structural and functional annotations to support studies of mammary gland physiology and protein structure–function relationships.

Key Features:

• Extensive Protein Compilation: Contains information on more than 7,459 proteins identified from milk fractions including whey, fat globule membranes, and exosomes, compiled from peer-reviewed publications.
• Detailed Cross-Referencing: Each protein entry includes annotations of protein function, biochemical properties, post-translational modifications, and reported significance in milk.
• Secondary and Structural Annotations: Includes 1,392 proteins annotated with domains, fold information, AlphaFold predicted models, and available crystal structures.
• Structural Models Gallery: Reports over 199 proteins with homology models and crystal structure galleries providing three-dimensional insights.
• Search and Filtering: Supports retrieval by protein name, accession IDs, or FASTA sequences and filtering by milk fraction, post-translational modifications, and structural annotation.

Scientific Applications:

• Milk Proteome Reference: Provides a unified reference of bovine milk proteome identifications for comparative and meta-analyses.
• Mammary Gland Pathophysiology: Enables investigation of proteomic changes associated with mammary gland physiology and disease states.
• Dairy Nutrition and Health Effects: Facilitates studies on the nutritional quality of dairy products and potential health effects of milk proteins.
• Structural and Functional Studies: Supports structural biology investigations linking sequence, AlphaFold models, and crystal structures to protein function.

Methodology:

Data were manually curated from published proteomic studies (over 300 publications), extracting protein identifications and associated annotations and updating the database with newly identified proteins and additional structural and functional entries.