RIMS2

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; OMA:RIMS2 - orthologs
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	39,547,768 bp
RNA expression pattern
	n/a
	Top expressed in
	Rostral migratory stream; ; neural layer of retina; ; lateral geniculate nucleus; ; medial dorsal nucleus; ; cerebellar vermis; ; lobe of cerebellum; ; inferior colliculi; ; nucleus accumbens; ; lateral septal nucleus; ; medial geniculate nucleus;
	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
	9699
	116838
	ENSG00000176406
	ENSMUSG00000037386
	Q9UQ26
	Q9EQZ7
	NM_001100117; NM_001282881; NM_001282882; NM_014677
	NM_001256382; NM_001256383; NM_001256384; NM_053271
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
	Wikidata
View/Edit Human	View/Edit Mouse

Regulating synaptic membrane exocytosis protein 2 is a protein that in humans is encoded by the RIMS2 gene.^[4]^[5]^[6]

Interactions

RIMS2 has been shown to interact with YWHAH,^[7] RAPGEF4,^[8]^[9] and UNC13A.^[10]

References

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000037386 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (April 1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
^ Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J Biol Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
^ "Entrez Gene: RIMS2 regulating synaptic membrane exocytosis 2".
^ Sun, Lei; Bittner Mary A; Holz Ronald W (October 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). United States: 38301–9. doi:10.1074/jbc.M212801200. ISSN 0021-9258. PMID 12871946.
^ Shibasaki, Tadao; Sunaga Yasuhiro; Fujimoto Kei; Kashima Yasushige; Seino Susumu (February 2004). "Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis". J. Biol. Chem. 279 (9). United States: 7956–61. doi:10.1074/jbc.M309068200. ISSN 0021-9258. PMID 14660679.
^ Kashima, Y; Miki T; Shibasaki T; Ozaki N; Miyazaki M; Yano H; Seino S (Dec 2001). "Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated insulin secretion". J. Biol. Chem. 276 (49). United States: 46046–53. doi:10.1074/jbc.M108378200. ISSN 0021-9258. PMID 11598134.
^ "Protein unc-13 homolog A". UniProt.

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.

This article on a gene on human chromosome 8 is a stub. You can help Wikipedia by expanding it.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000037386 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9872452-4] Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (April 1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.

[pmid12578829-5] Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J Biol Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.

[entrez-6] "Entrez Gene: RIMS2 regulating synaptic membrane exocytosis 2".

[pmid12871946-7] Sun, Lei; Bittner Mary A; Holz Ronald W (October 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). United States: 38301–9. doi:10.1074/jbc.M212801200. ISSN 0021-9258. PMID 12871946.

[pmid14660679-8] Shibasaki, Tadao; Sunaga Yasuhiro; Fujimoto Kei; Kashima Yasushige; Seino Susumu (February 2004). "Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis". J. Biol. Chem. 279 (9). United States: 7956–61. doi:10.1074/jbc.M309068200. ISSN 0021-9258. PMID 14660679.

[pmid11598134-9] Kashima, Y; Miki T; Shibasaki T; Ozaki N; Miyazaki M; Yano H; Seino S (Dec 2001). "Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated insulin secretion". J. Biol. Chem. 276 (49). United States: 46046–53. doi:10.1074/jbc.M108378200. ISSN 0021-9258. PMID 11598134.

[10] "Protein unc-13 homolog A". UniProt.

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Interactions

References

Further reading