Title: Phosphoregulation homepage
Date Reviewed: May 4th, 2006
Description: This is an interesting database that catalogues all known phosphorylation sites/events on proteins at their serine, threonine or tyrosine residues. The site allows three different flavors of searches: by protein name (Swissprot), to find the phosphorylation sites available on it; by kinase, to find which substrates are available to to it; and by phosphorylations binding motifs to find which phosphorylation sites it binds to. The results page includes an amino acid sequence showing the site of phosphorylation, the literature the information came from as well as a description of its function and links out to the pfam database which has additional information and sources.
Strengths: This is a thorough site with most of its information coming from swissprot and the literature. The information is inputted manually to prevent computational error and has resulted in a viable database of over 5000 phosphorylations.
Weaknesses: The kinase search and binding motif search are dependent on the element you are interested in being present in the website's database. Te results page appears a little empty but this may not be negligence on the part of th creators, it may be genuine holes in the literature (I didn't check this thoroughly)
Comprehensiveness: The list of kinases and binding motifs are impressive but extra links out to more information (PDB or KEGG for example) are a little lacking.
Timeliness: (how often is the site updated) At the time of review, the website had not been updated for 6 months.
Ease of Use: Easy to use search bars right on the homepage. Choosing which topic you wish to search by (through the three search engines) is a welcome addition.
Responsiveness: Pages downloaded instantaneously
Similar or Related Sites: Protein phosphorylation database (http://vigen.biochem.vt.edu/xpd/xpdindex.htm) A little harder to use but, in my mind, a lot more specific and thorough, I'd use this one first.
Overall Evaluation: 3 Stars
Reviewer: Paul Everill
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