TNS1

From Wikipedia, the free encyclopedia

Tensin 1

Identifiers

TNS1; MST091; MST122; MST127; MSTP122; MSTP127; MXRA6; TNS

External IDs

OMIM: 600076 MGI: 104552 HomoloGene: 11219 GeneCards: TNS1 Gene

Gene Ontology
Molecular function	• actin binding • protein binding
Cellular component	• cytoplasm • cytoskeleton • focal adhesion
Biological process	• cell-substrate junction assembly • fibroblast migration
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000079308

ENSMUSG00000055322

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
218.66 – 218.87 Mb

Chr 1:
73.91 – 74.12 Mb

PubMed search

Tensin-1 is a protein that in humans is encoded by the TNS1 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]

External links

TNS1 Info with links in the Cell Migration Gateway

References

↑ 1.0 1.1 "Entrez Gene: TNS1 tensin 1".

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. doi:10.1007/BF00354299. 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. doi:10.1074/jbc.271.41.25198. 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. doi:10.1073/pnas.97.7.3491. PMC 16267. 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. PMC 1221376. 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. PMC 55530. 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. PMC 139241. 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.

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