PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPN13 is a large protein that possesses a PTP domain at C-terminus, and multiple noncatalytic domains, which include a domain with similarity to band 4.1 superfamily of cytoskeletal-associated proteins, a region consisting of five PDZ domains, and a leucine zipper motif. PTPN13 binds to a negative regulatory domain in Fas that inhibits Fas-induced apoptosis.
The Journal of biological chemistry, 269(39), 24082-24089 (1994-09-30)
A novel cytoplasmic protein tyrosine phosphatase (PTP), PTPL1, was identified and cloned using a polymerase chain reaction-based approach. Overlapping cDNA clones encompass an open reading frame of 7398 base pairs, predicting a protein of 2466 amino acid residues with a
PTPN13 is a protein tyrosine phosphatase that associates with the C-terminal negative regulatory domain in the Fas (APO-1/CD95) receptor. The PTPN13 protein contains six GLGF repeats that have been found in the rat postsynaptic density protein (PSD-95) and the Drosophila
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