Tripartite motif-containing protein 55 is a
protein that in humans is encoded by the TRIM55gene.[5][6]
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.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
PMID11243782.
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.
PMID12414993.
S2CID16068484.
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.
PMID15782160.
S2CID6135437.
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.
PMID15967462.