Abstract
Summary: Heat shock protein information resource (HSPIR) is a concerted database of six major heat shock proteins (HSPs), namely, Hsp70, Hsp40, Hsp60, Hsp90, Hsp100 and small HSP. The HSPs are essential for the survival of all living organisms, as they protect the conformations of proteins on exposure to various stress conditions. They are a highly conserved group of proteins involved in diverse physiological functions, including de novo folding, disaggregation and protein trafficking. Moreover, their critical role in the control of disease progression made them a prime target of research. Presently, limited information is available on HSPs in reference to their identification and structural classification across genera. To that extent, HSPIR provides manually curated information on sequence, structure, classification, ontology, domain organization, localization and possible biological functions extracted from UniProt, GenBank, Protein Data Bank and the literature. The database offers interactive search with incorporated tools, which enhances the analysis. HSPIR is a reliable resource for researchers exploring structure, function and evolution of HSPs.Availability: http://pdslab.biochem.iisc.ernet.in/hspir/Contact: patrick@biochem.iisc.ernet.inSupplementary information: Supplementary data are available at Bioinformatics online.
Highlights
Heat shock proteins (HSPs) are a specialized group of proteins robustly synthesized in all living organisms in response to various conditions of stress, including elevated temperatures
Heat shock protein information resource (HSPIR) provides a comprehensive collection of information on six major HSP families across various genomes, with detailed subclassification based on their domain, structural organization and localization
Protein records can be viewed by clicking the accession ID, or have been added to the HSPIR cart for downloading and further analysis
Summary
Heat shock proteins (HSPs) are a specialized group of proteins robustly synthesized in all living organisms in response to various conditions of stress, including elevated temperatures. HSPs are critical for cell survival both constitutively and in times of stress to ensure proper folding of non-native states of proteins (Bukau et al, 2006; Parsell and Lindquist, 1993). Based on their nature of functions and molecular mass, HSPs are classified broadly into six major families, namely, Hsp, Hsp (J-proteins), Hsp (chaperonins), Hsp, Hsp100 (Clp proteins) and small HSPs. (Lund 2001; Kampinga and Craig, 2010) They function cooperatively by forming an intricate molecular network, thereby maintaining the overall cellular protein homeostasis (Lund, 2001). The database currently holds 10 000 hand-curated entries from six kingdoms, covering all the major model organisms and 295 3D structures
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