TMOD1

Tropomodulin 1

Identifiers

TMOD1 ; D9S57E; ETMOD; TMOD

External IDs

OMIM: 190930 MGI: 98775 HomoloGene: 20701 GeneCards: TMOD1 Gene

Gene ontology
Molecular function	• actin binding • tropomyosin binding
Cellular component	• cytosol • COP9 signalosome • membrane • myofibril • cortical cytoskeleton
Biological process	• adult locomotory behavior • muscle filament sliding • myofibril assembly
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 9:
100.26 – 100.36 Mb

Chr 4:
46.04 – 46.12 Mb

PubMed search

Tropomodulin-1 is a protein that in humans is encoded by the TMOD1 gene.^[1]^[2]^[3]

References

↑ Sung LA, Fowler VM, Lambert K, Sussman MA, Karr D, Chien S (Mar 1992). "Molecular cloning and characterization of human fetal liver tropomodulin. A tropomyosin-binding protein". J Biol Chem 267 (4): 2616–21. PMID 1370827.
↑ Sung LA, Fan Y, Lin CC (Dec 1996). "Gene assignment, expression, and homology of human tropomodulin". Genomics 34 (1): 92–6. doi:10.1006/geno.1996.0245. PMID 8661028.
↑ "Entrez Gene: TMOD1 tropomodulin 1".

Ursitti JA, Fowler VM (1994). "Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons.". J. Cell. Sci. 107 (6): 1633–9. PMID 7962203.
Sung LA, Lin JJ (1994). "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene.". Biochem. Biophys. Res. Commun. 201 (2): 627–34. doi:10.1006/bbrc.1994.1747. PMID 8002995.
Sussman MA; Bilak M; Kedes L et al. (1994). "Tropomodulin is highly concentrated at the postsynaptic domain of human and rat neuromuscular junctions". Exp. Cell Res. 209 (2): 388–91. doi:10.1006/excr.1993.1325. PMID 8262158.
Lench NJ; Telford EA; Andersen SE et al. (1997). "An EST and STS-based YAC contig map of human chromosome 9q22.3". Genomics 38 (2): 199–205. doi:10.1006/geno.1996.0616. PMID 8954802.
Vera C; Sood A; Gao KM et al. (2000). "Tropomodulin-binding site mapped to residues 7-14 at the N-terminal heptad repeats of tropomyosin isoform 5". Arch. Biochem. Biophys. 378 (1): 16–24. doi:10.1006/abbi.2000.1802. PMID 10871039.
McElhinny AS; Kolmerer B; Fowler VM et al. (2001). "The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments". J. Biol. Chem. 276 (1): 583–92. doi:10.1074/jbc.M005693200. PMID 11016930.
Chu X, Thompson D, Yee LJ, Sung LA (2001). "Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments". Gene 256 (1–2): 271–81. doi:10.1016/S0378-1119(00)00327-9. PMID 11054557.
Greenfield NJ, Fowler VM (2002). "Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin". Biophys. J. 82 (5): 2580–91. doi:10.1016/S0006-3495(02)75600-2. PMC 1302047. PMID 11964245.
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.
Rho SB; Chun T; Lee SH et al. (2004). "The interaction between E-tropomodulin and thymosin beta-10 rescues tumor cells from thymosin beta-10 mediated apoptosis by restoring actin architecture". FEBS Lett. 557 (1–3): 57–63. doi:10.1016/S0014-5793(03)01438-8. PMID 14741341.
Pawlak G; McGarvey TW; Nguyen TB et al. (2004). "Alterations in tropomyosin isoform expression in human transitional cell carcinoma of the urinary bladder". Int. J. Cancer 110 (3): 368–73. doi:10.1002/ijc.20151. PMID 15095301.
Humphray SJ; Oliver K; Hunt AR et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
Gerhard DS; Wagner L; Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Vera C, Lao J, Hamelberg D, Sung LA (2006). "Mapping the tropomyosin isoform 5 binding site on human erythrocyte tropomodulin: further insights into E-Tmod/TM5 interaction". Arch. Biochem. Biophys. 444 (2): 130–8. doi:10.1016/j.abb.2005.10.002. PMID 16297372.
Kong KY, Kedes L (2006). "Leucine 135 of tropomodulin-1 regulates its association with tropomyosin, its cellular localization, and the integrity of sarcomeres". J. Biol. Chem. 281 (14): 9589–99. doi:10.1074/jbc.M512064200. PMID 16434395.

Proteins of the cytoskeleton

Human

Microfilaments
(ABPs)

Myofilament

Actins	A1 A2 B C1 G1 G2

Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1

Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Wiskott-Aldrich syndrome protein
Fibrillin
Filamin
- FLNA
- FLNB
- FLNC
Espin
TRIOBP

IFs

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 7 8 9

Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86

Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80

Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Lamin A
B

Microtubules/
MAPs

Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3

Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3

Other	Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3

Catenins

Membrane

Dystrophin
- Dystroglycan
Utrophin
Ankyrin
- ANK1
- ANK2
- ANK3
Spectrin
- SPTA1
- SPTAN1
- SPTB
- SPTBN1
- SPTBN2
- SPTBN4
- SPTBN5

Other

Nonhuman

See also: cytoskeletal defects

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

TMOD1

References

Further reading