TRIM3

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)
End	6,474,459 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	105,282,778 bp
RNA expression pattern
	Top expressed in
	cerebellar hemisphere; ; cerebellum; ; cerebellar vermis; ; superior frontal gyrus; ; sural nerve;
	More reference expression data
	; ; ; ;
	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 anatomical structure; 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_033279
	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[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000110171 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036989 - Ensembl, May 2017
^ "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.
^ 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.
^ ^a ^b "Entrez Gene: TRIM3 tripartite motif-containing 3".
^ 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. S2CID 42977319.
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. S2CID 7827573.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by .

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

[refGRCm38Ensembl-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.

[pmid10391919-5] 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.

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

[pmid10673389-7] 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.

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