TRIM55

TRIM55
Identifiers
Aliases	TRIM55, MURF-2, RNF29, muRF2, tripartite motif containing 55
External IDs	MGI: 3036269 HomoloGene: 13205 GeneCards: TRIM55
Gene ontology Molecular function • zinc ion binding • protein binding • signal transducer activity • metal ion binding • identical protein binding Cellular component • cytoplasm • microtubule • intracellular • nucleus Biological process • signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84675	381485
Ensembl	ENSG00000147573	ENSMUSG00000060913
UniProt	Q9BYV6	n/a
RefSeq (mRNA)	NM_033058 NM_184085 NM_184086 NM_184087	NM_001081281
RefSeq (protein)	NP_149047.2 NP_908973.1 NP_908974.1 NP_908975.1	n/a
Location (UCSC)	Chr 8: 66.13 – 66.18 Mb	Chr 3: 19.64 – 19.69 Mb
PubMed search	[1]	[2]
Wikidata

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Tripartite motif-containing protein 55 is a protein that in humans is encoded by the TRIM55 gene.^[3][4]

The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein associates transiently with microtubules, myosin, and titin during muscle sarcomere assembly. It may act as a transient adaptor and plays a regulatory role in the assembly of sarcomeres. Four alternatively spliced transcript variants encoding distinct isoforms have been described.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Centner T, Yano J, Kimura E, McElhinny AS, Pelin K, Witt CC, Bang ML, Trombitas K, Granzier H, Gregorio CC, Sorimachi H, Labeit S (Mar 2001). "Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain". J Mol Biol. 306 (4): 717–26. doi:10.1006/jmbi.2001.4448. PMID 11243782.
4. "Entrez Gene: TRIM55 tripartite motif-containing 55".

Further reading

• McElhinny AS, Kakinuma K, Sorimachi H, et al. (2002). "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1". J. Cell Biol. 157 (1): 125–36. doi:10.1083/jcb.200108089. PMC 2173255. PMID 11927605.
• Pizon V, Iakovenko A, Van Der Ven PF, et al. (2003). "Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein". J. Cell. Sci. 115 (Pt 23): 4469–82. doi:10.1242/jcs.00131. PMID 12414993.
• 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.
• 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.
• Kim J, Bhinge AA, Morgan XC, Iyer VR (2005). "Mapping DNA-protein interactions in large genomes by sequence tag analysis of genomic enrichment". Nat. Methods. 2 (1): 47–53. doi:10.1038/nmeth726. PMID 15782160.
• Lange S, Xiang F, Yakovenko A, et al. (2005). "The kinase domain of titin controls muscle gene expression and protein turnover". Science. 308 (5728): 1599–603. doi:10.1126/science.1110463. PMID 15802564.
• Witt SH, Granzier H, Witt CC, Labeit S (2005). "MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination". J. Mol. Biol. 350 (4): 713–22. doi:10.1016/j.jmb.2005.05.021. PMID 15967462.