- Tropomyosin 3
Tropomyosin 3, also known as TPM3, is a human
gene .cite web | title = Entrez Gene: TPM3 tropomyosin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7170| accessdate = ]PBB_Summary
section_title =
summary_text = This gene encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in this gene result in autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are associated with cancer. Multiple transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: TPM3 tropomyosin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7170| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Lees-Miller JP, Helfman DM |title=The molecular basis for tropomyosin isoform diversity. |journal=Bioessays |volume=13 |issue= 9 |pages= 429–37 |year= 1992 |pmid= 1796905 |doi= 10.1002/bies.950130902
*cite journal | author=Pittenger MF, Kazzaz JA, Helfman DM |title=Functional properties of non-muscle tropomyosin isoforms. |journal=Curr. Opin. Cell Biol. |volume=6 |issue= 1 |pages= 96–104 |year= 1994 |pmid= 8167032 |doi=
*cite journal | author=Gunning P, Weinberger R, Jeffrey P |title=Actin and tropomyosin isoforms in morphogenesis. |journal=Anat. Embryol. |volume=195 |issue= 4 |pages= 311–5 |year= 1997 |pmid= 9108196 |doi=
*cite journal | author=Gunning PW, Schevzov G, Kee AJ, Hardeman EC |title=Tropomyosin isoforms: divining rods for actin cytoskeleton function. |journal=Trends Cell Biol. |volume=15 |issue= 6 |pages= 333–41 |year= 2006 |pmid= 15953552 |doi= 10.1016/j.tcb.2005.04.007
*cite journal | author=Rasmussen HH, van Damme J, Puype M, "et al." |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=
*cite journal | author=Höner B, Shoeman RL, Traub P |title=Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease. |journal=Cell Biol. Int. Rep. |volume=16 |issue= 7 |pages= 603–12 |year= 1992 |pmid= 1516138 |doi=
*cite journal | author=Morris CM, Hao QL, Heisterkamp N, "et al." |title=Localization of the TRK proto-oncogene to human chromosome bands 1q23-1q24. |journal=Oncogene |volume=6 |issue= 6 |pages= 1093–5 |year= 1991 |pmid= 1829807 |doi=
*cite journal | author=Winder SJ, Walsh MP |title=Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10148–55 |year= 1990 |pmid= 2161834 |doi=
*cite journal | author=Takahashi K, Hiwada K, Kokubu T |title=Vascular smooth muscle calponin. A novel troponin T-like protein. |journal=Hypertension |volume=11 |issue= 6 Pt 2 |pages= 620–6 |year= 1988 |pmid= 2455687 |doi=
*cite journal | author=Coulier F, Martin-Zanca D, Ernst M, Barbacid M |title=Mechanism of activation of the human trk oncogene. |journal=Mol. Cell. Biol. |volume=9 |issue= 1 |pages= 15–23 |year= 1989 |pmid= 2538716 |doi=
*cite journal | author=Martin-Zanca D, Hughes SH, Barbacid M |title=A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences. |journal=Nature |volume=319 |issue= 6056 |pages= 743–8 |year= 1986 |pmid= 2869410 |doi= 10.1038/319743a0
*cite journal | author=Reinach FC, MacLeod AR |title=Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene. |journal=Nature |volume=322 |issue= 6080 |pages= 648–50 |year= 1986 |pmid= 3018581 |doi= 10.1038/322648a0
*cite journal | author=MacLeod AR, Houlker C, Reinach FC, Talbot K |title=The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal tropomyosin. |journal=Nucleic Acids Res. |volume=14 |issue= 21 |pages= 8413–26 |year= 1987 |pmid= 3024106 |doi=
*cite journal | author=Clayton L, Reinach FC, Chumbley GM, MacLeod AR |title=Organization of the hTMnm gene. Implications for the evolution of muscle and non-muscle tropomyosins. |journal=J. Mol. Biol. |volume=201 |issue= 3 |pages= 507–15 |year= 1988 |pmid= 3418707 |doi=
*cite journal | author=MacLeod AR, Houlker C, Reinach FC, "et al." |title=A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 23 |pages= 7835–9 |year= 1986 |pmid= 3865200 |doi=
*cite journal | author=Butti MG, Bongarzone I, Ferraresi G, "et al." |title=A sequence analysis of the genomic regions involved in the rearrangements between TPM3 and NTRK1 genes producing TRK oncogenes in papillary thyroid carcinomas. |journal=Genomics |volume=28 |issue= 1 |pages= 15–24 |year= 1995 |pmid= 7590742 |doi= 10.1006/geno.1995.1100
*cite journal | author=Laing NG, Wilton SD, Akkari PA, "et al." |title=A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 249 |year= 1995 |pmid= 7663526 |doi= 10.1038/ng0695-249
*cite journal | author=Laing NG, Wilton SD, Akkari PA, "et al." |title=A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy. |journal=Nat. Genet. |volume=9 |issue= 1 |pages= 75–9 |year= 1995 |pmid= 7704029 |doi= 10.1038/ng0195-75
*cite journal | author=Wilton SD, Eyre H, Akkari PA, "et al." |title=Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by fluorescence in situ hybridisation. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 122–4 |year= 1994 |pmid= 7956350 |doi=PBB_Controls
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