RIMS2

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RIMS2

Protein RIMS2 PDB 1v27.png

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1V27, 1WFG

Identifiers

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)^[1]

Band	15 B3.1\|15 15.45 cM	Start	39,061,656 bp^[1]
Band	15 B3.1\|15 15.45 cM	End	39,547,768 bp^[1]

RNA expression pattern


n/a


More reference expression data

Gene ontology
Molecular function	metal ion binding GO:0001948 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


9699


116838

Ensembl


ENSG00000176406


ENSMUSG00000037386


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

^[2]

^[3]

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. 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.
^ "Protein unc-13 homolog A". UniProt.

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.

v t 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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