Tropomyosin 3

Protein-coding gene in the species Homo sapiens
TPM3
Identifiers
AliasesTPM3, CAPM1, CFTD, HEL-189, HEL-S-82p, NEM1, OK/SW-cl.5, TM-5, TM3, TM30, TM30nm, TM5, TPMsk3, TRK, hscp30, Tropomyosin 3, TPM3nu
External IDsOMIM: 191030; MGI: 1890149; HomoloGene: 81889; GeneCards: TPM3; OMA:TPM3 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for TPM3
Genomic location for TPM3
Band1q21.3Start154,155,304 bp[1]
End154,194,648 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for TPM3
Genomic location for TPM3
Band3|3 F1Start89,979,956 bp[2]
End90,008,209 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • muscle of thigh

  • Skeletal muscle tissue of rectus abdominis

  • thoracic diaphragm

  • biceps brachii

  • gastrocnemius muscle

  • Skeletal muscle tissue of biceps brachii

  • glutes

  • vastus lateralis muscle

  • triceps brachii muscle

  • monocyte
Top expressed in
  • soleus muscle

  • tail of embryo

  • genital tubercle

  • granulocyte

  • ankle

  • plantaris muscle

  • intercostal muscle

  • yolk sac

  • extraocular muscle

  • thoracic diaphragm
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • actin binding
  • protein binding
  • structural constituent of muscle
  • actin filament binding
  • molecular function
Cellular component
  • cytoplasm
  • muscle thin filament tropomyosin
  • extracellular exosome
  • cytoskeleton
  • stress fiber
  • cytosol
  • actin filament
  • actin cytoskeleton
Biological process
  • muscle filament sliding
  • muscle contraction
  • actin filament organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7170

59069

Ensembl

ENSG00000143549

ENSMUSG00000027940

UniProt

P06753

P21107

RefSeq (mRNA)
NM_001043351
NM_001043352
NM_001043353
NM_001278188
NM_001278189

NM_001278190
NM_001278191
NM_152263
NM_153649
NM_001349679
NM_001364679
NM_001364680
NM_001364681
NM_001364682
NM_001364683

NM_001253738
NM_001253740
NM_001271764
NM_001293748
NM_001293749

NM_022314
NM_001357581

RefSeq (protein)
NP_001036816
NP_001036817
NP_001036818
NP_001265117
NP_001265118

NP_001265119
NP_001265120
NP_689476
NP_705935
NP_001336608
NP_001351608
NP_001351609
NP_001351610
NP_001351611
NP_001351612

NP_001240667
NP_001240669
NP_001258693
NP_001280677
NP_001280678

NP_071709
NP_001344510

Location (UCSC)Chr 1: 154.16 – 154.19 MbChr 3: 89.98 – 90.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143549 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027940 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Morris CM, Hao QL, Heisterkamp N, Fitzgerald PH, Groffen J (Aug 1991). "Localization of the TRK proto-oncogene to human chromosome bands 1q23-1q24". Oncogene. 6 (6): 1093–5. PMID 1829807.
  6. ^ a b "Entrez Gene: TPM3 tropomyosin 3".

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. S2CID 7958541.
  • Pittenger MF, Kazzaz JA, Helfman DM (1994). "Functional properties of non-muscle tropomyosin isoforms". Curr. Opin. Cell Biol. 6 (1): 96–104. doi:10.1016/0955-0674(94)90122-8. PMID 8167032.
  • Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis". Anat. Embryol. 195 (4): 311–5. doi:10.1007/s004290050050. PMID 9108196. S2CID 9692297.
  • Gunning PW, Schevzov G, Kee AJ, Hardeman EC (2006). "Tropomyosin isoforms: divining rods for actin cytoskeleton function". Trends Cell Biol. 15 (6): 333–41. doi:10.1016/j.tcb.2005.04.007. PMID 15953552.
  • Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667. S2CID 41855774.
  • 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. doi:10.1016/S0309-1651(06)80002-0. PMID 1516138.
  • Winder SJ, Walsh MP (1990). "Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation". J. Biol. Chem. 265 (17): 10148–55. doi:10.1016/S0021-9258(19)38792-7. PMID 2161834.
  • Takahashi K, Hiwada K, Kokubu T (1988). "Vascular smooth muscle calponin. A novel troponin T-like protein". Hypertension. 11 (6 Pt 2): 620–6. doi:10.1161/01.hyp.11.6.620. PMID 2455687.
  • Coulier F, Martin-Zanca D, Ernst M, Barbacid M (1989). "Mechanism of activation of the human trk oncogene". Mol. Cell. Biol. 9 (1): 15–23. doi:10.1128/mcb.9.1.15. PMC 362140. PMID 2538716.
  • Martin-Zanca D, Hughes SH, Barbacid M (1986). "A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences". Nature. 319 (6056): 743–8. Bibcode:1986Natur.319..743M. doi:10.1038/319743a0. PMID 2869410. S2CID 4316805.
  • Reinach FC, MacLeod AR (1986). "Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene". Nature. 322 (6080): 648–50. Bibcode:1986Natur.322..648R. doi:10.1038/322648a0. PMID 3018581. S2CID 4307865.
  • MacLeod AR, Houlker C, Reinach FC, Talbot K (1987). "The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal tropomyosin". Nucleic Acids Res. 14 (21): 8413–26. doi:10.1093/nar/14.21.8413. PMC 311868. PMID 3024106.
  • Clayton L, Reinach FC, Chumbley GM, MacLeod AR (1988). "Organization of the hTMnm gene. Implications for the evolution of muscle and non-muscle tropomyosins". J. Mol. Biol. 201 (3): 507–15. doi:10.1016/0022-2836(88)90633-X. PMID 3418707.
  • MacLeod AR, Houlker C, Reinach FC, et al. (1986). "A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism". Proc. Natl. Acad. Sci. U.S.A. 82 (23): 7835–9. doi:10.1073/pnas.82.23.7835. PMC 390864. PMID 3865200.
  • Butti MG, Bongarzone I, Ferraresi G, et al. (1995). "A sequence analysis of the genomic regions involved in the rearrangements between TPM3 and NTRK1 genes producing TRK oncogenes in papillary thyroid carcinomas". Genomics. 28 (1): 15–24. doi:10.1006/geno.1995.1100. PMID 7590742.
  • Laing NG, Wilton SD, Akkari PA, et al. (1995). "A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1". Nat. Genet. 10 (2): 249. doi:10.1038/ng0695-249a. PMID 7663526.
  • Laing NG, Wilton SD, Akkari PA, et al. (1995). "A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy". Nat. Genet. 9 (1): 75–9. doi:10.1038/ng0195-75. PMID 7704029. S2CID 40422785.
  • Wilton SD, Eyre H, Akkari PA, et al. (1994). "Assignment of the human a-tropomyosin gene TPM3 to 1q22→q23 by fluorescence in situ hybridisation". Cytogenet. Cell Genet. 68 (1–2): 122–4. doi:10.1159/000133905. PMID 7956350.

External links

  • GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy
  • v
  • t
  • e
  • 1mv4: TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated Alpha Tropomyosin
    1mv4: TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated Alpha Tropomyosin
  • 2g9j: Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain (""overlap region"") of tropomyosin
    2g9j: Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain (""overlap region"") of tropomyosin
  • v
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Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects
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