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HSPIR: a manually annotated heat shock protein information resource.


ABSTRACT: 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.http://pdslab.biochem.iisc.ernet.in/hspir/

SUBMITTER: R RK 

PROVIDER: S-EPMC3476333 | biostudies-other | 2012 Nov

REPOSITORIES: biostudies-other

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HSPIR: a manually annotated heat shock protein information resource.

R Ratheesh Kumar RK   N S Nagarajan N   S P Arunraj A   Sinha Devanjan D   Veedin Rajan Vinoth Babu VB   Esthaki Vinoth Kumar VK   D'Silva Patrick P  

Bioinformatics (Oxford, England) 20120824 21


<h4>Summary</h4>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. Mo  ...[more]

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