TRIM9

Tripartite motif containing 9
PDB rendering based on 2db8.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2DB8​
Identifiers
Symbols	TRIM9 ; RNF91; SPRING
External IDs	OMIM: 606555 MGI: 2137354 HomoloGene: 9045 GeneCards: TRIM9 Gene
Gene ontology Molecular function • SNARE binding • ubiquitin-protein transferase activity • protein binding • zinc ion binding • ligase activity • protein homodimerization activity Cellular component • cytoplasm • cytoskeleton • synaptic vesicle • cell junction • dendrite Biological process • synaptic vesicle exocytosis • protein ubiquitination • negative regulation of SNARE complex assembly • proteasome-mediated ubiquitin-dependent protein catabolic process • negative regulation of calcium ion-dependent exocytosis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	114088	94090
Ensembl	ENSG00000100505	ENSMUSG00000021071
UniProt	Q9C026	Q8C7M3
RefSeq (mRNA)	NM_015163	NM_001110202
RefSeq (protein)	NP_055978	NP_001103672
Location (UCSC)	Chr 14: 50.98 – 51.1 Mb	Chr 12: 70.24 – 70.35 Mb
PubMed search

Tripartite motif-containing protein 9 is a protein that in humans is encoded by the TRIM9 gene.^[1][2][3]

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. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms.^[3]

Interactions

TRIM9 has been shown to interact with SNAP-25.^[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. Li Y, Chin LS, Weigel C, Li L (Oct 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". J Biol Chem 276 (44): 40824–33. doi:10.1074/jbc.M106141200. PMID 11524423.
3. "Entrez Gene: TRIM9 tripartite motif-containing 9".

Further reading

• Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Ohara O, Nagase T, Ishikawa K, et al. (1997). "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins.". DNA Res. 4 (1): 53–9. doi:10.1093/dnares/4.1.53. PMID 9179496.
• 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.
• 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.
• 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.
• 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.