TRIM3

TRIM3
Identifiers
Aliases	TRIM3, BERP, HAC1, RNF22, RNF97, tripartite motif containing 3
External IDs	MGI: 1860040 HomoloGene: 21290 GeneCards: TRIM3
Gene location (Human)
Chr.	Chromosome 11 (human)[1]
End	6,474,459 bp[1]
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)[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; • protein binding; • metal ion binding; • 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
	10612
	55992
	ENSG00000110171
	ENSMUSG00000036989
	O75382
	Q9R1R2
	NM_001248006; NM_001248007; NM_006458; NM_033278
	NM_001285870; NM_001285871; NM_001285873; NM_018880; NM_001360425
	NP_001234935; NP_001234936; NP_006449; NP_150594
	NP_001272799; NP_001272800; NP_001272802; NP_061368; NP_001347354
	Wikidata
View/Edit Human	View/Edit Mouse

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

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 2 3 GRCh38: Ensembl release 89: ENSG00000110171 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000036989 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ El-Husseini AE, Vincent SR (August 1999). "Cloning and characterization of a novel RING finger protein that interacts with class V myosins". J Biol Chem. 274 (28): 19771–7. doi:10.1074/jbc.274.28.19771. PMID 10391919.
1 2 "Entrez Gene: TRIM3 tripartite motif-containing 3".
↑ El-Husseini, A E; Kwasnicka D; Yamada T; Hirohashi S; Vincent S R (January 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochem. Biophys. Res. Commun. UNITED STATES. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. ISSN 0006-291X. PMID 10673389.

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. PMC 125245. 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. doi:10.1016/S0014-5793(01)02689-8. 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. Bibcode:2002PNAS...9916899M. 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.
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. PMC 1087250. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000110171 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000036989 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid10391919-5] El-Husseini AE, Vincent SR (August 1999). "Cloning and characterization of a novel RING finger protein that interacts with class V myosins". J Biol Chem. 274 (28): 19771–7. doi:10.1074/jbc.274.28.19771. PMID 10391919.

[entrez-6] 1 2 "Entrez Gene: TRIM3 tripartite motif-containing 3".

[pmid10673389-7] El-Husseini, A E; Kwasnicka D; Yamada T; Hirohashi S; Vincent S R (January 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochem. Biophys. Res. Commun. UNITED STATES. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. ISSN 0006-291X. PMID 10673389.

TRIM3

Interactions

References

Further reading