RIMS2

Regulating synaptic membrane exocytosis protein 2 is a protein that in humans is encoded by the RIMS2 gene.

RIMS2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1V27, 1WFG
Identifiers
Aliases	RIMS2, OBOE, RAB3IP3, RIM2, regulating synaptic membrane exocytosis 2
External IDs	OMIM: 606630 MGI: 2152972 HomoloGene: 81639 GeneCards: RIMS2
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 B3.1|15 15.45 cM Start 39,061,656 bp End 39,547,768 bp
RNA expression pattern Bgee Human Mouse (ortholog) n/a Top expressed in lateral geniculate nucleus medial dorsal nucleus cerebellar vermis inferior colliculus nucleus accumbens medial geniculate nucleus motor neuron substantia nigra olfactory tubercle ventromedial nucleus BioGPS More reference expression data
Gene ontology Molecular function metal ion binding protein binding transmembrane transporter binding Cellular component membrane plasma membrane synapse intracellular anatomical structure presynaptic active zone cell junction extracellular exosome presynaptic membrane cytoskeleton of presynaptic active zone presynaptic active zone cytoplasmic component Biological process cell differentiation spontaneous neurotransmitter secretion positive regulation of inhibitory postsynaptic potential insulin secretion regulation of exocytosis positive regulation of gene expression positive regulation of excitatory postsynaptic potential positive regulation of dendrite extension intracellular protein transport cAMP-mediated signaling calcium-ion regulated exocytosis regulation of membrane potential calcium ion-regulated exocytosis of neurotransmitter regulation of synaptic vesicle exocytosis exocytosis regulation of synaptic plasticity positive regulation of synaptic transmission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9699 116838 Ensembl ENSG00000176406 ENSMUSG00000037386 UniProt Q9UQ26 Q9EQZ7 RefSeq (mRNA) NM_001100117 NM_001282881 NM_001282882 NM_014677 NM_001256382 NM_001256383 NM_001256384 NM_053271 RefSeq (protein) NP_001093587 NP_001269810 NP_001269811 NP_055492 NP_001335413 NP_001335414 NP_001335415 NP_001335416 NP_001335417 NP_001335418 NP_001335419 NP_001335420 NP_001335421 NP_001335422 NP_001335423 NP_001335424 NP_001335425 NP_001335426 NP_001335427 NP_001335428 NP_001335429 NP_001335430 NP_001335431 NP_001335432 NP_001335433 NP_001335434 NP_001335435 NP_001335436 NP_001335437 NP_001335438 NP_001243311 NP_001243312 NP_001243313 NP_444501 Location (UCSC) n/a Chr 15: 39.06 – 39.55 Mb PubMed search
Wikidata
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Interactions

RIMS2 has been shown to interact with YWHAH, RAPGEF4, and UNC13A.

Further reading

• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Fenster SD, Chung WJ, Zhai R, et al. (2000). "Piccolo, a presynaptic zinc finger protein structurally related to bassoon". Neuron. 25 (1): 203–14. doi:10.1016/S0896-6273(00)80883-1. PMID 10707984. S2CID 10177138.
• Kashima Y, Miki T, Shibasaki T, et al. (2002). "Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated insulin secretion". J. Biol. Chem. 276 (49): 46046–53. doi:10.1074/jbc.M108378200. PMID 11598134.
• 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.
• Wang Y, Südhof TC (2003). "Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins( small star, filled )". Genomics. 81 (2): 126–37. doi:10.1016/S0888-7543(02)00024-1. PMID 12620390.
• Sun L, Bittner MA, Holz RW (2003). "Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus". J. Biol. Chem. 278 (40): 38301–9. doi:10.1074/jbc.M212801200. PMID 12871946.
• Shibasaki T, Sunaga Y, Fujimoto K, et al. (2004). "Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis". J. Biol. Chem. 279 (9): 7956–61. doi:10.1074/jbc.M309068200. PMID 14660679.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• 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.
• Gérard HC, Whittum-Hudson JA, Schumacher HR, Hudson AP (2006). "Synovial Chlamydia trachomatis up regulates expression of a panel of genes similar to that transcribed by Mycobacterium tuberculosis during persistent infection". Ann. Rheum. Dis. 65 (3): 321–7. doi:10.1136/ard.2005.042226. PMC 1798071. PMID 16192289.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.