TRIM63

Tripartite motif containing 63, E3 ubiquitin protein ligase
PDB rendering based on 2d8u.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2D8U​, 3DDT​, 4M3L​
Identifiers
Symbols	TRIM63 ; IRF; MURF1; MURF2; RNF28; SMRZ
External IDs	OMIM: 606131 MGI: 2447992 HomoloGene: 41878 GeneCards: TRIM63 Gene
Gene ontology Molecular function • signal transducer activity • protein binding • zinc ion binding • ligase activity • titin binding • ubiquitin protein ligase activity Cellular component • nucleus • cytoplasm • microtubule • Z disc • M band Biological process • muscle contraction • signal transduction • regulation of gene expression • skeletal muscle atrophy • response to electrical stimulus involved in regulation of muscle adaptation • protein ubiquitination • proteasome-mediated ubiquitin-dependent protein catabolic process • response to interleukin-1 • cellular response to dexamethasone stimulus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	84676	433766
Ensembl	ENSG00000158022	ENSMUSG00000028834
UniProt	Q969Q1	Q38HM4
RefSeq (mRNA)	NM_032588	NM_001039048
RefSeq (protein)	NP_115977	NP_001034137
Location (UCSC)	Chr 1: 26.05 – 26.07 Mb	Chr 4: 134.32 – 134.33 Mb
PubMed search

E3 ubiquitin-protein ligase TRIM63 is an enzyme that in humans is encoded by the TRIM63 gene.^[1][2][3]

This gene encodes a member of the RING zinc finger protein family found in striated muscle and iris. The product of this gene is localized to the Z-line and M-line lattices of myofibrils, where titin's N-terminal and C-terminal regions respectively bind to the sarcomere. In vitro binding studies have shown that this protein also binds directly to titin near the region of titin containing kinase activity. Another member of this protein family binds to microtubules. Since these family members can form heterodimers, this suggests that these proteins may serve as a link between titin kinase and microtubule-dependent signal pathways in muscle.^[3]

Interactions

TRIM63 has been shown to interact with Titin,^[1] GMEB1^[4] and SUMO2.^[2]

References

1. 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.
2. Dai KS, Liew CC (Jun 2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". J Biol Chem 276 (26): 23992–9. doi:10.1074/jbc.M011208200. PMID 11283016.
3. "Entrez Gene: TRIM63 tripartite motif-containing 63".
4. McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC (April 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.

Further reading

• Bodine SC, Latres E, Baumhueter S, et al. (2001). "Identification of ubiquitin ligases required for skeletal muscle atrophy.". Science 294 (5547): 1704–8. doi:10.1126/science.1065874. PMID 11679633.
• 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.
• Wistow G, Bernstein SL, Ray S, et al. (2002). "Expressed sequence tag analysis of adult human iris for the NEIBank Project: steroid-response factors and similarities with retinal pigment epithelium.". Mol. Vis. 8: 185–95. PMID 12107412.
• 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.
• Kedar V, McDonough H, Arya R, et al. (2005). "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I.". Proc. Natl. Acad. Sci. U.S.A. 101 (52): 18135–40. doi:10.1073/pnas.0404341102. PMC 539735. PMID 15601779.
• 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.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
• Doucet M, Russell AP, Léger B, et al. (2007). "Muscle atrophy and hypertrophy signaling in patients with chronic obstructive pulmonary disease.". Am. J. Respir. Crit. Care Med. 176 (3): 261–9. doi:10.1164/rccm.200605-704OC. PMID 17478621.