Tyrosine-protein phosphatase non-receptor type 13 is an enzyme that in humans is encoded by the PTPN13gene.[5][6]
The protein encoded by this gene 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 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. This PTP was found to interact with, and dephosphorylate Fas receptor, as well as IkappaBalpha 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. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.[6]
Inazawa J, Ariyama T, Abe T, et al. (1997). "PTPN13, a fas-associated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3". Genomics. 31 (2): 240–242. doi:10.1006/geno.1996.0039. PMID8824809.
Ekiel I, Banville D, Shen SH, et al. (1999). "Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor". J. Biomol. NMR. 12 (3): 455–456. doi:10.1023/A:1008267807859. PMID9835052. S2CID19976473.
Lee SH, Shin MS, Park WS, et al. (2000). "Immunohistochemical localization of FAP-1, an inhibitor of Fas-mediated apoptosis, in normal and neoplastic human tissues". APMIS. 107 (12): 1101–1108. doi:10.1111/j.1699-0463.1999.tb01515.x. PMID10660140. S2CID24672576.
Kozlov G, Gehring K, Ekiel I (2000). "Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor". Biochemistry. 39 (10): 2572–2580. doi:10.1021/bi991913c. PMID10704206.
Cuppen E, van Ham M, Wansink DG, et al. (2000). "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL". Eur. J. Cell Biol. 79 (4): 283–293. doi:10.1078/S0171-9335(04)70031-X. PMID10826496.
Nakai Y, Irie S, Sato TA (2001). "Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1". Eur. J. Biochem. 267 (24): 7170–7175. doi:10.1046/j.1432-1327.2000.01818.x. PMID11106428.
1d5g: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E COMPLEXED WITH A PEPTIDE
1gm1: SECOND PDZ DOMAIN (PDZ2) OF PTP-BL
1ozi: The alternatively spliced PDZ2 domain of PTP-BL
1q7x: Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)
1vj6: PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
1wch: CRYSTAL STRUCTURE OF PTPL1 HUMAN TYROSINE PHOSPHATASE MUTATED IN COLORECTAL CANCER - EVIDENCE FOR A SECOND PHOSPHOTYROSINE SUBSTRATE RECOGNITION POCKET
3pdz: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E