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) [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 105,253,670 bp [2] End 105,282,778 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cerebellar hemisphere tibial nerve right coronary artery popliteal artery ascending aorta prefrontal cortex canal of the cervix ganglionic eminence Brodmann area 10 left uterine tube Top expressed in cerebellar cortex superior frontal gyrus cerebellar vermis prefrontal cortex piriform cortex lateral geniculate nucleus subiculum pontine nuclei hippocampus proper habenula More reference expression data BioGPS 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 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 Species Human Mouse Entrez 10612 55992 Ensembl ENSG00000110171 ENSMUSG00000036989 UniProt O75382 Q9R1R2 RefSeq (mRNA) NM_001248006 NM_001248007 NM_006458 NM_033278 NM_033279 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: 105.25 – 105.28 Mb PubMed search [3] [4]
Wikidata
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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]

TRIM3 binds to and ubiquitinates Estrogen receptor alpha (ERa) leading to receptor's stabilization. ^[8]

Moreover, TRIM3 interacts with P53 which promotes the formation of K48-linked poly-ubiquitin chains and degradation. ^[9]

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): 19771–19777. 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): 906–911. doi:10.1006/bbrc.1999.2045. PMID   10673389.
8. Zhuang T, Wang B, Tan X, Wu L, Li X, Li Z, et al. (April 2022). "TRIM3 facilitates estrogen signaling and modulates breast cancer cell progression". Cell Communication and Signaling. 20 (1): 45. doi:10.1186/s12964-022-00861-z. PMC   8991925 . PMID   35392925.
9. Wang X, Zhang Y, Pei X, Guo G, Xue B, Duan X, Dou D (November 2020). "TRIM3 inhibits P53 signaling in breast cancer cells". Cancer Cell International. 20 (1): 559. doi:10.1186/s12935-020-01630-z. PMC   7685606 . PMID   33292295.

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): 906–911. 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): 363–367. doi:10.1006/geno.2000.6452. PMID   11170753.
• Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, et al. (May 2001). "The tripartite motif family identifies cell compartments". The EMBO Journal. 20 (9): 2140–2151. 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): 61–64. 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): 2470–2482. 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): 635–648. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.