A Web-Accessible Resource of Information on
Protein Tyrosine Phosphatases

This website aims to provide a peer-reviewed compendium on Protein Tyrosine Phosphatases (PTPs) that integrates sequence and structure information with cellular and biological function. Together with our analyses published in Mol & Cell Biol (2001), FASEB Journal (2004) and Methods (2004, in press), it provides a resource for annotation and classification of the classic, tyrosine-specific PTPs.
 
The classic, tyrosine-specific PTPs are encoded by 38 genes in humans and belong to a larger family of cysteine-dependent phosphatases that totals approximately 100 human members and numerous pseudogenes.  The cysteine-dependent phosphatases utilize a conserved 'C[X]5R’ sequence motif to hydrolyze phosphoester bonds in proteins and non-protein substrates. Based on structural homology and substrate specificity, they are divided into five categories: (i) classic, tyrosine-specific phosphatases (PTPs); (ii) dual-specificity phosphatases (DSPs); (iii) Cdc25 phosphatases; (iv) myotubularin-related; and (iv) low molecular weight phosphatases.

At this website, which is a collaborative project between researches at Novo Nordisk and Cold Spring Harbor Laboratory, the reader can explore the diversity of the PTP family and download files such our non-redundant database of PTP accession numbers, multiple sequence alignments, phylogenetic trees, structure files, annotated molecular graphics files, chromosomal mapping data including analysis of exon structure, pseudogenes and information on possible links between PTPs and human diseases.

The PTP database can be searched by keywords and by sequence similarity using our BLAST server which also provides a tool for phylogenetic classification of anonymously submitted sequences based on PTP domain sequence homology and neighbor-joining (NJ) trees. Finally, we provide a section on online bioinformatics resources that have been described in Handbook of Cell Signalling and in our ‘Practical guide to Bioinformatics and Data Resources’ (Methods 2004, in press).

For any questions or suggestions, please contact Jannik N. Andersen.

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