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Tripartite motif containing 3
Symbols TRIM3 ; BERP; HAC1; RNF22; RNF97
External IDs OMIM605493 MGI1860040 HomoloGene21290 GeneCards: TRIM3 Gene
RNA expression pattern
PBB GE TRIM3 204910 s at tn.png
PBB GE TRIM3 204911 s at tn.png
PBB GE TRIM3 213884 s at tn.png
More reference expression data
Species Human Mouse
Entrez 10612 55992
Ensembl ENSG00000110171 ENSMUSG00000036989
UniProt O75382 Q9R1R2
RefSeq (mRNA) NM_001248006 NM_001285870
RefSeq (protein) NP_001234935 NP_001272799
Location (UCSC) Chr 11:
6.47 – 6.5 Mb
Chr 7:
105.6 – 105.63 Mb
PubMed search [1] [2]

Tripartite motif-containing protein 3 is a protein that in humans is encoded by the TRIM3 gene.[1][2]

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.[2]


TRIM3 has been shown to interact with Actinin alpha 4.[3]


  1. ^ 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. 
  2. ^ a b "Entrez Gene: TRIM3 tripartite motif-containing 3". 
  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. 

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