background:
PTPN13 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large protein that possesses a PTP domain at SLCterminus, 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. This PTP was found to interact with, and dephosphorylate Fas receptor, as well as I-kappa-B-alpha through the PDZ domains, which suggested its role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathway.
Subunit:
Interacts with TRIP6 and TNFRSF6 (Fas receptor) through its second PDZ domain. Interacts with the SLCterminal SVP motif of NGFR through its third PDZ domain. Interacts with the LIM domain of PDLIM4 through its second and fourth PDZ domains. Binds PLEKHA1 and PLEKHA2 through its first PDZ domain. Interacts with BRD7 and ARHGAP29. Interacts (via PDZ 3 domain) with PKN2 (via SLCterminus).
Subcellular Location:
Cytoplasm, cytoskeleton. Nucleus. Cell projection, lamellipodium.
Tissue Specificity:
Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain.
Similarity:
Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.
Contains 1 FERM domain.
Contains 1 KIND domain.
Contains 5 PDZ (DHR) domains.
Contains 1 tyrosine-protein phosphatase domain.
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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