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The UAB Proteomics Database.

Aubrey Hill1, Helen Kim

  • 1UAB Comprehensive Cancer Center, UAB Mass Spectrometry and Proteomics Shared Facility, University of Alabama at Birmingham, 1530 3rd Ave South, Kaul 602A, Birmingham, AL 35294, USA. ahill@uab.edu

Bioinformatics (Oxford, England)
|November 5, 2003
PubMed
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The University of Alabama at Birmingham (UAB) Proteomics Database (UPD) offers a centralized repository for 2D gel images and mass spectrometry data. This resource facilitates protein research by linking gel data with comprehensive analysis information.

Area of Science:

  • Proteomics
  • Bioinformatics
  • Molecular Biology

Background:

  • The University of Alabama at Birmingham (UAB) Proteomics Database (UPD) is accessible online.
  • It serves as a crucial resource for researchers in the field of proteomics.

Purpose of the Study:

  • To establish a comprehensive repository for storing and linking 2D gel electrophoresis images.
  • To integrate mass spectrometry data associated with proteins identified from these gels.
  • To create a user-friendly interface for accessing and navigating proteomic information.

Main Methods:

  • Development of a web interface for data access.
  • Implementation of a relational database for data storage and management.
  • Creation of image maps and hyperlinks for seamless navigation.

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  • Integration of links to external databases like the National Center for Biotechnology Information (NCBI).

    • Main Results:

    • The UPD currently houses data on 44 individual proteins from four distinct experiments.
    • Direct access to 2D gel images is provided through embedded hyperlinks.
    • The database facilitates the linkage of gel images with mass spectrometry analysis results.

    Conclusions:

    • The UAB Proteomics Database (UPD) provides a valuable, integrated resource for proteomics research.
    • It enhances data accessibility and facilitates the correlation of proteomic data with visual gel information.
    • The database structure supports the expansion and integration of future proteomic datasets.