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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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