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1.
Proteomics ; 5(13): 3531-6, 2005 Aug.
Article in English | MEDLINE | ID: mdl-16041672

ABSTRACT

Plasma is one of the best studied compartments in the human body and serves as an ideal body fluid for the diagnosis of diseases. This report provides a detailed functional annotation of all the plasma proteins identified to date. In all, gene products encoded by 3778 distinct genes were annotated based on proteins previously published in the literature as plasma proteins and the identification of multiple peptides from proteins under HUPO's Plasma Proteome Project. Our analysis revealed that 51% of these genes encoded more than one protein isoform. All single nucleotide polymorphisms involving protein-coding regions were mapped onto the protein sequences. We found a number of examples of isoform-specific subcellular localization as well as tissue expression. This database is an attempt at comprehensive annotation of a complex subproteome and is available on the web at http://www.plasmaproteomedatabase.org.


Subject(s)
Blood Proteins/chemistry , Blood Proteins/genetics , Databases, Protein , Proteomics/methods , Amino Acid Motifs , Computational Biology/methods , Genome, Human , Humans , Mass Spectrometry , Peptides/chemistry , Polymorphism, Single Nucleotide , Protein Isoforms , Protein Structure, Tertiary , Time Factors
3.
Nucleic Acids Res ; 32(Database issue): D497-501, 2004 Jan 01.
Article in English | MEDLINE | ID: mdl-14681466

ABSTRACT

The rapid pace at which genomic and proteomic data is being generated necessitates the development of tools and resources for managing data that allow integration of information from disparate sources. The Human Protein Reference Database (http://www.hprd.org) is a web-based resource based on open source technologies for protein information about several aspects of human proteins including protein-protein interactions, post-translational modifications, enzyme-substrate relationships and disease associations. This information was derived manually by a critical reading of the published literature by expert biologists and through bioinformatics analyses of the protein sequence. This database will assist in biomedical discoveries by serving as a resource of genomic and proteomic information and providing an integrated view of sequence, structure, function and protein networks in health and disease.


Subject(s)
Databases, Protein , Proteins/metabolism , Proteomics , Computational Biology , Disease , Genomics , Humans , Information Storage and Retrieval , Internet , Protein Binding , Protein Processing, Post-Translational , Proteins/chemistry , Proteins/genetics , Proteome/chemistry , Proteome/genetics , Proteome/metabolism , Substrate Specificity , Vocabulary, Controlled
4.
Genome Res ; 13(10): 2363-71, 2003 Oct.
Article in English | MEDLINE | ID: mdl-14525934

ABSTRACT

Human Protein Reference Database (HPRD) is an object database that integrates a wealth of information relevant to the function of human proteins in health and disease. Data pertaining to thousands of protein-protein interactions, posttranslational modifications, enzyme/substrate relationships, disease associations, tissue expression, and subcellular localization were extracted from the literature for a nonredundant set of 2750 human proteins. Almost all the information was obtained manually by biologists who read and interpreted >300,000 published articles during the annotation process. This database, which has an intuitive query interface allowing easy access to all the features of proteins, was built by using open source technologies and will be freely available at http://www.hprd.org to the academic community. This unified bioinformatics platform will be useful in cataloging and mining the large number of proteomic interactions and alterations that will be discovered in the postgenomic era.


Subject(s)
Databases, Protein/trends , BRCA1 Protein/physiology , Computational Biology/methods , Genetics, Medical/methods , Humans , Macromolecular Substances , Protein Interaction Mapping/trends , Protein Processing, Post-Translational/physiology , Protein Structure, Quaternary/physiology , Protein Structure, Tertiary/physiology , Substrate Specificity/physiology
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