RIMS2

Gene of the species Homo sapiens
RIMS2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1V27, 1WFG

Identifiers
AliasesRIMS2, OBOE, RAB3IP3, RIM2, regulating synaptic membrane exocytosis 2
External IDsOMIM: 606630; MGI: 2152972; HomoloGene: 81639; GeneCards: RIMS2; OMA:RIMS2 - orthologs
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[1]
Chromosome 15 (mouse)
Genomic location for RIMS2
Genomic location for RIMS2
Band15 B3.1|15 15.45 cMStart39,061,656 bp[1]
End39,547,768 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
    n/a
Top expressed in
  • Rostral migratory stream

  • neural layer of retina

  • lateral geniculate nucleus

  • medial dorsal nucleus

  • cerebellar vermis

  • lobe of cerebellum

  • inferior colliculus

  • nucleus accumbens

  • lateral septal nucleus

  • medial geniculate 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
SpeciesHumanMouse
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/aChr 15: 39.06 – 39.55 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/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

  1. ^ a b c 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.
  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.
  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.
  6. ^ "Entrez Gene: RIMS2 regulating synaptic membrane exocytosis 2".
  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.
  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.
  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.

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
  • e
  • 1v27: Solution structure of the first C2 domain of RIM2
    1v27: Solution structure of the first C2 domain of RIM2
  • 1wfg: PDZ domain of human RIM2B
    1wfg: PDZ domain of human RIM2B
  • 2bwq: CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION
    2bwq: CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION


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