TRIM3

Tripartite motif-containing protein 3 is a protein that in humans is encoded by the TRIM3 gene.[5][6]

TRIM3
Identifiers
Aliases	TRIM3, BERP, HAC1, RNF22, RNF97, tripartite motif containing 3
External IDs	OMIM: 605493 MGI: 1860040 HomoloGene: 21290 GeneCards: TRIM3
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p15.4 Start 6,448,613 bp[1] End 6,474,459 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 E3 Start 105,604,463 bp[2] End 105,633,571 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • zinc ion binding • protein C-terminus binding • GO:0001948 protein binding • metal ion binding • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • ubiquitin-protein transferase activity Cellular component • cytoplasm • endosome • early endosome • intracellular • Golgi apparatus • dendrite • cell projection Biological process • protein transport • protein ubiquitination • nervous system development • protein polyubiquitination • proteasome-mediated ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10612	55992
Ensembl	ENSG00000110171	ENSMUSG00000036989
UniProt	O75382	Q9R1R2
RefSeq (mRNA)	NM_001248006 NM_001248007 NM_006458 NM_033278	NM_001285870 NM_001285871 NM_001285873 NM_018880 NM_001360425
RefSeq (protein)	NP_001234935 NP_001234936 NP_006449 NP_150594	NP_001272799 NP_001272800 NP_001272802 NP_061368 NP_001347354
Location (UCSC)	Chr 11: 6.45 – 6.47 Mb	Chr 7: 105.6 – 105.63 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

TRIM3 has been shown to interact with Actinin alpha 4.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000110171 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000036989 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. El-Husseini AE, Vincent SR (July 1999). "Cloning and characterization of a novel RING finger protein that interacts with class V myosins". The Journal of Biological Chemistry. 274 (28): 19771–7. doi:10.1074/jbc.274.28.19771. PMID 10391919.
6. "Entrez Gene: TRIM3 tripartite motif-containing 3".
7. El-Husseini AE, Kwasnicka D, Yamada T, Hirohashi S, Vincent SR (January 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochemical and Biophysical Research Communications. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. PMID 10673389.

Further reading

• El-Husseini AE, Kwasnicka D, Yamada T, Hirohashi S, Vincent SR (January 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochemical and Biophysical Research Communications. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. PMID 10673389.
• El-Husseini AE, Fretier P, Vincent SR (February 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, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". The EMBO Journal. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
• Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S (August 2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme". FEBS Letters. 503 (1): 61–4. doi:10.1016/S0014-5793(01)02689-8. PMID 11513855.
• Yan Q, Sun W, Kujala P, Lotfi Y, Vida TA, Bean AJ (May 2005). "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling". Molecular Biology of the Cell. 16 (5): 2470–82. doi:10.1091/mbc.E04-11-1014. PMC 1087250. PMID 15772161.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 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.