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TNS3 (Tensin-3) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Prostate cancer and Basal cell carcinoma.
May act as a protein phosphatase and/or a lipid phosphatase. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1.
Open Targets scores its association with cancer at 0.57 (direct and indirect evidence; datatypes literature 0.80, animal model 0.31, genetic association 0.72).
In plain words · TNS3 (Tensin-3) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Prostate cancer and Basal cell carcinoma.
TNS3 (Tensin-3) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Prostate cancer and Basal cell carcinoma.
May act as a protein phosphatase and/or a lipid phosphatase. Involved in the dissociation of the integrin-tensin-actin complex.
No product in this corpus aims at TNS3 yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
First described 2001. Earliest sequence paper UniProt cites for the protein: Carson-Walter E.B. et al, Cancer Res, 2001, "Cell surface tumor endothelial markers are conserved in mice and humans". Source.
Sources: HGNC HGNC:21616 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q68CZ2 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000136205 (association with cancer (MONDO_0004992) 0.57; per-cancer scores at or above 0.5: prostate cancer 0.52, basal cell carcinoma 0.51 (GraphQL API, CC0))
May act as a protein phosphatase and/or a lipid phosphatase. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organisation. Enhances RHOA activation in the presence of DLC1. Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation. Location: Cell junction, focal adhesion; Cell projection, podosome (UniProt). Locus 7p12.3 (HGNC).
Query for this target: (TITLE:"TNS3" OR ABSTRACT:"TNS3" OR TITLE:"tensin 3" OR ABSTRACT:"tensin 3" OR TITLE:"Tensin-3" OR ABSTRACT:"Tensin-3" OR TITLE:"TEM6" OR ABSTRACT:"TEM6" OR TITLE:"H_NH0549I23.2" OR ABSTRACT:"H_NH0549I23.2" OR TITLE:"FLJ13732" OR ABSTRACT:"FLJ13732") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about TNS3, not a curated reading list.