RIMS2

Regulating synaptic membrane exocytosis 2

PDB rendering based on 1v27.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1V27, 1WFG

Identifiers

Symbols

RIMS2 ; OBOE; RAB3IP3; RIM2

External IDs

OMIM: 606630 HomoloGene: 81639 GeneCards: RIMS2 Gene

Gene ontology
Molecular function	• protein binding • Rab GTPase binding • ion channel binding • metal ion binding
Cellular component	• intracellular • cell junction • presynaptic membrane • presynaptic active zone • extracellular exosome
Biological process	• intracellular protein transport • positive regulation of gene expression • calcium ion-dependent exocytosis • regulation of exocytosis • cAMP-mediated signaling • insulin secretion • regulation of membrane potential • calcium ion-dependent exocytosis of neurotransmitter • spontaneous neurotransmitter secretion • positive regulation of inhibitory postsynaptic potential • positive regulation of dendrite extension • positive regulation of excitatory postsynaptic potential
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
103.5 – 104.26 Mb

Chr 15:
39.2 – 39.68 Mb

PubMed search

Regulating synaptic membrane exocytosis protein 2 is a protein that in humans is encoded by the RIMS2 gene.^[1]^[2]^[3]

Interactions

RIMS2 has been shown to interact with YWHAH^[4] and RAPGEF4.^[5]^[6]

References

↑ 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. (United States) 278 (40): 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. (United States) 279 (9): 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. (United States) 276 (49): 46046–53. doi:10.1074/jbc.M108378200. ISSN 0021-9258. PMID 11598134.

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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.
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. 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.
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.

PDB gallery

1v27: Solution structure of the first C2 domain of RIM2

1wfg: PDZ domain of human RIM2B

2bwq: CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION

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RIMS2

Interactions

References

Further reading