TNS1

From Wikipedia, the free encyclopedia

Tensin 1

Identifiers

TNS1; MGC88584; TNS

External IDs

OMIM: 600076 MGI: 104552 HomoloGene: 11219

Gene ontology
Molecular Function:	• actin binding
Cellular Component:	• cytoskeleton • focal adhesion • cell-matrix junction
Biological Process:	• cell-substrate junction assembly • intracellular signaling cascade • cell migration

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_022648 (mRNA)
NP_072174 (protein)

XM_619639 (mRNA)
XP_619639 (protein)

Location

Chr 2: 218.38 - 218.52 Mb

Chr 1: 73.85 - 73.86 Mb

Pubmed search

[1]

[2]

Tensin 1, also known as TNS1, is a human gene.^[1]

The protein encoded by this gene localizes to focal adhesions, regions of the plasma membrane where the cell attaches to the extracellular matrix. This protein crosslinks actin filaments and contains a Src homology 2 (SH2) domain, which is often found in molecules involved in signal transduction. This protein is a substrate of calpain II. A second transcript from this gene has been described, but its full length nature has not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: TNS1 tensin 1.

[edit] Further reading

Jankowski SA, Gumucio DL (1996). "Genes for tensin, villin and desmin are linked on mouse chromosome 1.". Mamm. Genome 6 (10): 744-5. PMID 8563175.
Salgia R, Pisick E, Sattler M, et al. (1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene.". J. Biol. Chem. 271 (41): 25198-203. PMID 8810278.
Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491-6. PMID 10737800.
Katz BZ, Zohar M, Teramoto H, et al. (2000). "Tensin can induce JNK and p38 activation.". Biochem. Biophys. Res. Commun. 272 (3): 717-20. doi:10.1006/bbrc.2000.2853. PMID 10860821.
Chen H, Ishii A, Wong WK, et al. (2001). "Molecular characterization of human tensin.". Biochem. J. 351 Pt 2: 403-11. PMID 11023826.
Benzing T, Gerke P, Höpker K, et al. (2001). "Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2.". Proc. Natl. Acad. Sci. U.S.A. 98 (17): 9784-9. doi:10.1073/pnas.171269898. PMID 11493697.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Yamashita M, Horikoshi S, Asanuma K, et al. (2004). "Tensin is potentially involved in extracellular matrix production in mesangial cells.". Histochem. Cell Biol. 121 (3): 245-54. doi:10.1007/s00418-004-0626-8. PMID 14991332.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635-48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Eto M, Kirkbride J, Elliott E, et al. (2007). "Association of the tensin N-terminal protein-tyrosine phosphatase domain with the alpha isoform of protein phosphatase-1 in focal adhesions.". J. Biol. Chem. 282 (24): 17806-15. doi:10.1074/jbc.M700944200. PMID 17435217.