Phospho-TENC1 (Y483) Antibody

1. Patients with low TNS2 expression showed poor relapse-free survival rates for breast and lung cancers. These results strongly suggest a role of tensin2 in suppressing cell transformation and reduction of tumorigenicity. PMID: 27203214
2. p62 expression increased but C1-Ten protein decreased during muscle differentiation, supporting a role for p62 as a physiological regulator of C1-Ten. PMID: 25101860
3. Pulldown studies in human cells using Myc-tagged Tensin2 constructs revealed that DISC1 specifically interacts with the C-terminal PTB domain of Tensin2 in a phosphorylation-independent manner. PMID: 23233134
4. Results identified tensin2 as a Syk-binding protein. PMID: 22019427
5. Here, we report complete chemical shift assignments of the SH2 domain of human tensin2 determined by triple resonance experiments. PMID: 21461930
6. Tensin2 is an important new mediator in TPO/c-Mpl pathway and has a positive affect on cellular growth, at least in part through its effect on the PI3K/Akt signaling. PMID: 21527831
7. Tensin2 SH2 domain was identified to interact with nonphosphorylated ligand (DLC-1) as well as phosphorylated ligand. PMID: 21765928
8. Tensin2, in addition to regulating cytoskeletal dynamics, influences phosphoinositide-Akt signalling through its PTPase domain. PMID: 20678486
9. Data suggest that the interaction between START-GAP1 and tensin2 occurs in a PTB domain-dependent manner. manner.ty=0 PMID: 19895840
10. Differential proteolytic cleavage of Tensin2 can liberate domains with discrete localisations and functions, which has implications for the role of Tensins in cancer cell survival and motility. PMID: 19747564
11. Interaction of Axl receptor tyrosine kinase with C1-TEN. PMID: 12470648
12. C1 domain-containing phosphatase and TENsin homologue (C1-TEN) appears to be a novel intracellular phosphatase that negatively regulates the Akt/Protein kinase B signaling cascade PMID: 15817639
13. variant 3 significantly promoted the cell growth and motility of HCC cells; clonal transfectants of variant 3 were more closely packed and resulted in a higher saturation density than in the control vector transfectants PMID: 17006924
14. Tensins may represent a novel group of metastasis suppressors in the kidney, the loss of which leads to greater tumor cell motility and consequent metastasis. PMID: 19194507
15. DLC1 interaction with tensin2 through this novel focal adhesion binding site contributes to the growth-suppressive activity of DLC1. PMID: 19440389

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HGNC: 19737

OMIM: 607717

KEGG: hsa:23371

STRING: 9606.ENSP00000319756

UniGene: Hs.343334