Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2 (PubMed:14516276). Interacts (via the second PDZ domain) with TNFRSF6 (Fas receptor) (via C-terminus) (PubMed:10704206). Interacts (via the second PDZ domain) with TRIP6 (via the third LIM domain and C-terminus) (PubMed:10826496, PubMed:10400701). Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP motif) and PKN2 (via C-terminus) (PubMed:10544233, PubMed:11356191). Interacts (via the second or fourth PDZ domains) with PDLIM4 (via C-terminus only or via combined C-terminus and LIM domain, but not LIM domain only). Found in a complex with PDLIM4 and TRIP6 (By similarity). Interacts with PDLIM4; this interaction results in dephosphorylation of SRC 'Tyr-419' by this protein leading to its inactivation (PubMed:19307596). Interacts with BRD7 (By similarity). Interacts with RAPGEF6 (PubMed:12095257). Interacts with ARHGAP29 (PubMed:9305890). Interacts with PIK3R2; dephosphorylates PIK3R2 (PubMed:23604317). Interacts with FBXL2 (PubMed:23604317). Interacts (via the FERM domain) with ENTR1 (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1 (PubMed:23108400). Colocalizes with F-actin (PubMed:10826496). Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover (PubMed:11356191). Expressed in keratinocytes (at protein level) (PubMed:29043977). Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain. May be due to a competing donor splice site. Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Contaminating sequence. Potential poly-A sequence.