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TRIM3

From Wikipedia, the free encyclopedia
TRIM3
Identifiers
AliasesTRIM3, BERP, HAC1, RNF22, RNF97, tripartite motif containing 3
External IDsOMIM: 605493; MGI: 1860040; HomoloGene: 21290; GeneCards: TRIM3; OMA:TRIM3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 7: 105.25 – 105.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

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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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110171Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036989Ensembl, 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. ^ a b "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

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