TPM1

From Wikipedia, the free encyclopedia

Tropomyosin 1 (alpha)

PDB rendering based on 1c1g.

Available structures: 1c1g, 1ic2, 1mv4, 2g9j, 2tma

Identifiers

Symbol(s)

TPM1; TMSA; HTM-alpha; TPM1-alpha; TPM1-kappa

External IDs

OMIM: 191010 MGI: 98809 HomoloGene: 88552

Gene ontology
Molecular Function:	• actin binding • structural constituent of cytoskeleton • structural constituent of muscle
Cellular Component:	• cytoskeleton • muscle thin filament tropomyosin
Biological Process:	• cell motility • regulation of muscle contraction • regulation of heart contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000366 (mRNA)
NP_000357 (protein)

NM_024427 (mRNA)
NP_077745 (protein)

Location

Chr 15: 61.12 - 61.15 Mb

Chr 9: 66.82 - 66.85 Mb

Pubmed search

[1]

[2]

Tropomyosin 1 (alpha), also known as TPM1, is a human gene.

This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy.^[1]

[edit] References

^ Entrez Gene: TPM1 tropomyosin 1 (alpha).

[edit] Further reading

Lees-Miller JP, Helfman DM (1992). "The molecular basis for tropomyosin isoform diversity.". Bioessays 13 (9): 429-37. doi:10.1002/bies.950130902. PMID 1796905.
Balvay L, Fiszman MY (1995). "[Analysis of the diversity of tropomyosin isoforms]". C. R. Seances Soc. Biol. Fil. 188 (5-6): 527-40. PMID 7780795.
Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis.". Anat. Embryol. 195 (4): 311-5. PMID 9108196.
Perry SV (2002). "Vertebrate tropomyosin: distribution, properties and function.". J. Muscle Res. Cell. Motil. 22 (1): 5-49. PMID 11563548.
Perry SV (2004). "What is the role of tropomyosin in the regulation of muscle contraction?". J. Muscle Res. Cell. Motil. 24 (8): 593-6. PMID 14870975.
Jääskeläinen P, Miettinen R, Kärkkäinen P, et al. (2004). "Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes.". Ann. Med. 36 (1): 23-32. PMID 15000344.
Mak A, Smillie LB, Bárány M (1978). "Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle.". Proc. Natl. Acad. Sci. U.S.A. 75 (8): 3588-92. PMID 278975.
Höner B, Shoeman RL, Traub P (1992). "Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease.". Cell Biol. Int. Rep. 16 (7): 603-12. PMID 1516138.
Chevray PM, Nathans D (1992). "Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun.". Proc. Natl. Acad. Sci. U.S.A. 89 (13): 5789-93. PMID 1631061.
Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease.". FEBS Lett. 278 (2): 199-203. PMID 1991513.
Cho YJ, Liu J, Hitchcock-DeGregori SE (1990). "The amino terminus of muscle tropomyosin is a major determinant for function.". J. Biol. Chem. 265 (1): 538-45. PMID 2136742.
Colote S, Widada JS, Ferraz C, et al. (1988). "Evolution of tropomyosin functional domains: differential splicing and genomic constraints.". J. Mol. Evol. 27 (3): 228-35. PMID 3138425.
Lin CS, Leavitt J (1988). "Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts.". Mol. Cell. Biol. 8 (1): 160-8. PMID 3336357.
MacLeod AR, Gooding C (1988). "Human hTM alpha gene: expression in muscle and nonmuscle tissue.". Mol. Cell. Biol. 8 (1): 433-40. PMID 3336363.
Mische SM, Manjula BN, Fischetti VA (1987). "Relation of streptococcal M protein with human and rabbit tropomyosin: the complete amino acid sequence of human cardiac alpha tropomyosin, a highly conserved contractile protein.". Biochem. Biophys. Res. Commun. 142 (3): 813-8. PMID 3548719.
Heeley DH, Golosinska K, Smillie LB (1987). "The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C.". J. Biol. Chem. 262 (21): 9971-8. PMID 3611073.
Brown HR, Schachat FH (1985). "Renaturation of skeletal muscle tropomyosin: implications for in vivo assembly.". Proc. Natl. Acad. Sci. U.S.A. 82 (8): 2359-63. PMID 3857586.
Tanokura M, Ohtsuki I (1984). "Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and troponin C.". J. Biochem. 95 (5): 1417-21. PMID 6746613.
Pearlstone JR, Smillie LB (1983). "Effects of troponin-I plus-C on the binding of troponin-T and its fragments to alpha-tropomyosin. Ca2+ sensitivity and cooperativity.". J. Biol. Chem. 258 (4): 2534-42. PMID 6822572.