TRIM9

TRIM9
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DB8
Identifiers
Aliases	TRIM9 , RNF91, SPRING, tripartite motif containing 9
External IDs	OMIM: 606555 MGI: 2137354 HomoloGene: 9045 GeneCards: TRIM9
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q22.1 Start 50,975,262 bp [1] End 51,096,061 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12|12 C2 Start 70,291,307 bp [2] End 70,394,388 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 23 Brodmann area 9 Region I of hippocampus proper middle temporal gyrus nucleus accumbens caudate nucleus cingulate gyrus endothelial cell prefrontal cortex putamen Top expressed in piriform cortex primary motor cortex superior frontal gyrus subiculum olfactory tubercle medial dorsal nucleus substantia nigra cingulate gyrus Region I of hippocampus proper medial geniculate nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding zinc ion binding protein binding protein homodimerization activity transferase activity protein domain specific binding ubiquitin-protein transferase activity SNARE binding Cellular component cytoplasm cytoplasmic vesicle cell junction dendrite cell projection synapse cytoskeleton synaptic vesicle intracellular anatomical structure cytosol presynaptic cytosol Biological process negative regulation of calcium ion-dependent exocytosis protein ubiquitination negative regulation of SNARE complex assembly synaptic vesicle exocytosis proteasome-mediated ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 114088 94090 Ensembl ENSG00000100505 ENSMUSG00000021071 UniProt Q9C026 Q8C7M3 RefSeq (mRNA) NM_015163 NM_052978 NM_001110202 NM_001110203 NM_001286386 NM_001286387 NM_001286388 NM_053167 RefSeq (protein) NP_055978 NP_443210 NP_001103672 NP_001103673 NP_001273315 NP_001273316 NP_001273317 NP_444397 NP_001392290 NP_001392291 NP_001392292 NP_001392293 NP_001392294 NP_001392295 NP_001392296 NP_001392297 NP_001392298 NP_001392299 NP_001392300 NP_001392301 NP_001392302 NP_001392303 NP_001392304 NP_001392305 NP_001392306 NP_001392307 NP_001392308 NP_001392309 NP_001392310 NP_001392311 NP_001392312 NP_001392313 NP_001392314 NP_001392315 NP_001392316 Location (UCSC) Chr 14: 50.98 – 51.1 Mb Chr 12: 70.29 – 70.39 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Tripartite motif-containing protein 9 is a protein that in humans is encoded by the TRIM9 gene. ^{[5] [6] [7]}

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. ^[7]

Interactions

TRIM9 has been shown to interact with SNAP-25. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000100505 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021071 - 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. 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.
6. 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.
7. "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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.