TRIM11

Tripartite motif containing 11
Identifiers
Symbols	TRIM11 ; BIA1; RNF92
External IDs	OMIM: 607868 MGI: 2137355 HomoloGene: 14225 GeneCards: TRIM11 Gene
Gene ontology Molecular function • protein binding • transcription factor binding • zinc ion binding • ligase activity • protein domain specific binding • ubiquitin protein ligase activity Cellular component • nucleus • cytoplasm Biological process • protein ubiquitination • negative regulation of viral transcription • innate immune response • negative regulation of transcription, DNA-templated • negative regulation of viral entry into host cell • positive regulation of viral entry into host cell • negative regulation of neurogenesis • defense response to virus • negative regulation of viral release from host cell Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	81559	94091
Ensembl	ENSG00000154370	ENSMUSG00000020455
UniProt	Q96F44	Q99PQ2
RefSeq (mRNA)	NM_145214	NM_001290988
RefSeq (protein)	NP_660215	NP_001277917
Location (UCSC)	Chr 1: 228.39 – 228.41 Mb	Chr 11: 58.98 – 58.99 Mb
PubMed search

Tripartite motif-containing protein 11 is a protein that in humans is encoded by the TRIM11 gene.^[1][2]

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. 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 the nucleus and the cytoplasm. Its function has not been identified.^[2]

References

1. 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". EMBO J 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
2. "Entrez Gene: TRIM11 tripartite motif-containing 11".

Further reading

• Ishikawa H, Tachikawa H, Miura Y, Takahashi N (2006). "TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system.". FEBS Lett. 580 (20): 4784–92. doi:10.1016/j.febslet.2006.07.066. PMID 16904669.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Cooper ST, Hanson IM (2006). "A screen for proteins that interact with PAX6: C-terminal mutations disrupt interaction with HOMER3, DNCL1 and TRIM11.". BMC Genet. 6: 43. doi:10.1186/1471-2156-6-43. PMC 1208879. PMID 16098226.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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.
• Niikura T, Hashimoto Y, Tajima H, et al. (2003). "A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults.". Eur. J. Neurosci. 17 (6): 1150–8. doi:10.1046/j.1460-9568.2003.02553.x. PMID 12670303.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.