TRIM3

From Wikipedia, the free encyclopedia

Tripartite motif-containing 3

Identifiers

TRIM3; BERP; FLJ16135; HAC1; RNF22; RNF97

External IDs

OMIM: 605493 MGI: 1860040 HomoloGene: 21290

Gene ontology
Molecular Function:	• protein binding • protein C-terminus binding • zinc ion binding • metal ion binding
Cellular Component:	• intracellular • cytoplasm
Biological Process:	• nervous system development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006458 (mRNA)
NP_006449 (protein)

XM_001000076 (mRNA)
XP_001000076 (protein)

Location

Chr 11: 6.43 - 6.45 Mb

Chr 7: 105.48 - 105.51 Mb

Pubmed search

[1]

[2]

Tripartite motif-containing 3, also known as TRIM3, is a human gene.^[1]

The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also called the 'RING-B-box-coiled-coil' (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to cytoplasmic filaments. It is similar to a rat protein which is a specific partner for the tail domain of myosin V, a class of myosins which are involved in the targeted transport of organelles. The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin V-mediated cargo transport. Alternatively spliced transcript variants encoding the same isoform have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: TRIM3 tripartite motif-containing 3.

[edit] Further reading

El-Husseini AE, Vincent SR (1999). "Cloning and characterization of a novel RING finger protein that interacts with class V myosins.". J. Biol. Chem. 274 (28): 19771–7. PMID 10391919.
El-Husseini AE, Kwasnicka D, Yamada T, et al. (2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4.". Biochem. Biophys. Res. Commun. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. PMID 10673389.
El-Husseini AE, Fretier P, Vincent SR (2001). "Cloning and characterization of a gene (RNF22) encoding a novel brain expressed ring finger protein (BERP) that maps to human chromosome 11p15.5.". Genomics 71 (3): 363–7. doi:10.1006/geno.2000.6452. PMID 11170753.
Reymond A, Meroni G, Fantozzi A, et al. (2001). "The tripartite motif family identifies cell compartments.". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMID 11331580.
Lee SJ, Choi JY, Sung YM, et al. (2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme.". FEBS Lett. 503 (1): 61–4. PMID 11513855.
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. 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.
Yan Q, Sun W, Kujala P, et al. (2005). "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling.". Mol. Biol. Cell 16 (5): 2470–82. doi:10.1091/mbc.E04-11-1014. PMID 15772161.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.