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Wikipedia

RIMS1

La proteína de regulación de la exocitosis-1 de la membrana sináptica[3]​ (RIMS1) es una proteína que en los humanos está codificada por el gen RIMS1.[4][5][6]

RIMS1
Estructuras disponibles
PDBBuscar ortólogos: PDBe RCSB
Identificadores
Otros nombresRIMS1, CORD7, RAB3IP2, RIM, RIM1, regulating synaptic membrane exocytosis 1
Identificadores externosOMIM: 606629 MGI: 2152971 HomoloGene: 128399 GeneCards: RIMS1
Patrón de expresión RNA
More reference expression data
Ortólogos
EspeciesHumanoRatón
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001012623
NM_001012624
NM_001012625
NM_053270
NM_183018

RefSeq (proteína)

NP_001012641
NP_001012642
NP_001012643
NP_444500
NP_898839

Ubicación (UCSC)n/an/a
Búsqueda PubMed[1][2]
Wikidata
Ver/editar humanoVer/editar humano

Función

RAB3A (MIM 179490), miembro de la superfamilia de genes Ras, es una proteína de vesícula sináptica que regula la exocitosis de vesícula sináptica. MUNC13 (UNC13; MIM 605836) y sus isoformas son necesarias para preparar vesículas sinápticas para la exocitosis. La familia RIM de proteínas de la zona activa probablemente funcione como andamios de proteínas que ayudan a regular la exocitosis vesicular durante la plasticidad a corto plazo.[Suministrado por OMIM][6]

Interacciones

Se ha demostrado que RIMS1 interactúa con:

Referencias

  1. «Referencia Human PubMed:». National Center for Biotechnology Information, U.S. National Library of Medicine. 
  2. «Referencia Mouse PubMed:». National Center for Biotechnology Information, U.S. National Library of Medicine. 
  3. Plaza Serón, María del Carmen (2016). Reacciones de hipersensibilidad por intolerancia cruzada a antiinflamatorios no esteroideos: relación fenotipo-genotipo. Universidad de Málaga. p. 29. Consultado el 12 de febrero de 2020. 
  4. «Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro». DNA Res 4 (2): 141-50. September 1997. PMID 9205841. doi:10.1093/dnares/4.2.141. 
  5. «Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin». J Biol Chem 276 (35): 32756-62. August 2001. PMID 11438518. doi:10.1074/jbc.M100929200. 
  6. «Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1». 
  7. «Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release». J. Cell Biol. 164 (2): 301-11. January 2004. PMC 2172332. PMID 14734538. doi:10.1083/jcb.200307101. 
  8. «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. April 2003. PMID 12578829. doi:10.1074/jbc.M212341200. 
  9. «Protein unc-13 homolog A». UniProt. 
  10. «Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1». J. Cell Biol. 158 (3): 577-90. August 2002. PMC 2173811. PMID 12163476. doi:10.1083/jcb.200202083. 
  11. «Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming». Neuron 30 (1): 183-96. April 2001. PMID 11343654. doi:10.1016/s0896-6273(01)00272-0. 
  12. «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. October 2003. PMID 12871946. doi:10.1074/jbc.M212801200. 

Lectura adicional

  • «Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q». Am. J. Hum. Genet. 63 (1): 274-9. 1998. PMC 1377229. PMID 9634506. doi:10.1086/301905. 
  • «Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming». Neuron 30 (1): 183-96. 2001. PMID 11343654. doi:10.1016/S0896-6273(01)00272-0. 
  • «HIV Nef-mediated cellular phenotypes are differentially expressed as a function of intracellular Nef concentrations». J. Biol. Chem. 276 (35): 32763-70. 2001. PMID 11438519. doi:10.1074/jbc.M101025200. 
  • «Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond». J. Biol. Chem. 276 (35): 32771-8. 2001. PMID 11438520. doi:10.1074/jbc.M101229200. 
  • «Induction of neurite outgrowth in PC12 cells by alpha -phenyl-N-tert-butylnitron through activation of protein kinase C and the Ras-extracellular signal-regulated kinase pathway». J. Biol. Chem. 276 (35): 32779-85. 2001. PMID 11438521. doi:10.1074/jbc.M101403200. 
  • «Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain». J. Biol. Chem. 276 (40): 37472-81. 2001. PMID 11438522. doi:10.1074/jbc.M101502200. 
  • «RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone». Nature 415 (6869): 321-6. 2002. PMID 11797009. doi:10.1038/415321a. 
  • «Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1». J. Cell Biol. 158 (3): 577-90. 2002. PMC 2173811. PMID 12163476. doi:10.1083/jcb.200202083. 
  • «A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones». Proc. Natl. Acad. Sci. U.S.A. 99 (22): 14464-9. 2002. PMC 137906. PMID 12391317. doi:10.1073/pnas.182532999. 
  • «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. 2003. PMID 12578829. doi:10.1074/jbc.M212341200. 
  • «Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins( small star, filled )». Genomics 81 (2): 126-37. 2003. PMID 12620390. doi:10.1016/S0888-7543(02)00024-1. 
  • «Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7)». Genomics 81 (3): 304-14. 2003. PMID 12659814. doi:10.1016/S0888-7543(03)00010-7. 
  • «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. 2003. PMID 12871946. doi:10.1074/jbc.M212801200. 
  • «Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release». J. Cell Biol. 164 (2): 301-11. 2004. PMC 2172332. PMID 14734538. doi:10.1083/jcb.200307101. 
  • «Large-scale characterization of HeLa cell nuclear phosphoproteins». Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. 2004. PMC 514446. PMID 15302935. doi:10.1073/pnas.0404720101. 
  • «Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa». Ophthalmic Res. 37 (2): 89-93. 2005. PMID 15746564. doi:10.1159/000084250. 
  • «Genetic enhancement of cognition in a kindred with cone–rod dystrophy due to RIMS1 mutation». J. Med. Genet. 44 (6): 373-80. 2007. PMC 2740882. PMID 17237123. doi:10.1136/jmg.2006.047407. 
  •   Datos: Q18036647

rims1, proteína, regulación, exocitosis, membrana, sináptica, proteína, humanos, está, codificada, estructuras, disponiblespdbbuscar, ortólogos, pdbe, rcsblista, identificadores, pdb2cssidentificadoresotros, nombres, cord7, rab3ip2, rim1, regulating, synaptic,. La proteina de regulacion de la exocitosis 1 de la membrana sinaptica 3 RIMS1 es una proteina que en los humanos esta codificada por el gen RIMS1 4 5 6 RIMS1Estructuras disponiblesPDBBuscar ortologos PDBe RCSBLista de identificadores PDB2CSSIdentificadoresOtros nombresRIMS1 CORD7 RAB3IP2 RIM RIM1 regulating synaptic membrane exocytosis 1Identificadores externosOMIM 606629 MGI 2152971 HomoloGene 128399 GeneCards RIMS1Patron de expresion RNAMore reference expression dataOntologia genicaFuncion molecular GO 0005083 GTPase regulator activity metal ion binding GO 0001948 union a proteina plasmatica ion channel binding union a ARN RNA Componente celular citosol membrana membrana plasmatica sinapsis presynaptic active zone union celular presynaptic membrane cytoskeleton of presynaptic active zone presynaptic active zone cytoplasmic componentProceso biologico diferenciacion celular respuesta al estimulo synaptic vesicle exocytosis positive regulation of inhibitory postsynaptic potential membrane fusion regulation of neurotransmitter secretion secrecion glutamate secretion positive regulation of gene expression positive regulation of excitatory postsynaptic potential positive regulation of dendrite extension regulated exocytosis intracellular protein transport neurotransmitter transport GO 0010554 neurotransmitter secretion vision calcium ion regulated exocytosis exocitosis GO 0048552 regulation of catalytic activity regulacion de potencial de membrana calcium ion regulated exocytosis of neurotransmitter regulation of synaptic vesicle exocytosis transporte regulation of synaptic plasticity positive regulation of synaptic transmission protein containing complex assembly acrosomal vesicle exocytosisFuentes Amigo QuickGOOrtologosEspeciesHumanoRatonEntrez22999116837EnsemblENSG00000079841ENSMUSG00000041670UniProtQ86UR5Q99NE5RefSeq mRNA NM 001168407NM 001168408NM 001168409NM 001168410NM 001168411NM 014989NM 001012623NM 001012624NM 001012625NM 053270NM 183018RefSeq proteina NP 001161879NP 001161880NP 001161881NP 001161882NP 001161883NP 055804NP 001337340NP 001337341NP 001337342NP 001337343NP 001337344NP 001337345NP 001337346NP 001337347NP 001337348NP 001337349NP 001337350NP 001337351NP 001337352NP 001337353NP 001337354NP 001337355NP 001337356NP 001337357NP 001337358NP 001337359NP 001337360NP 001337361NP 001337362NP 001337363NP 001337364NP 001337365NP 001337366NP 001337367NP 001337368NP 001337369NP 001337370NP 001337371NP 001337372NP 001337373NP 001337374NP 001337375NP 001337376NP 001337377NP 001337378NP 001337379NP 001337381NP 001337383NP 001337384NP 001337385NP 001337386NP 001337387NP 001337388NP 001337389NP 001337390NP 001337391NP 001337392NP 001337393NP 001337394NP 001337395NP 001337396NP 001337397NP 001337398NP 001337399NP 001337400NP 001337401NP 001337402NP 001337403NP 001012641NP 001012642NP 001012643NP 444500NP 898839Ubicacion UCSC n an aBusqueda PubMed 1 2 WikidataVer editar humanoVer editar humano Indice 1 Funcion 2 Interacciones 3 Referencias 4 Lectura adicionalFuncion EditarRAB3A MIM 179490 miembro de la superfamilia de genes Ras es una proteina de vesicula sinaptica que regula la exocitosis de vesicula sinaptica MUNC13 UNC13 MIM 605836 y sus isoformas son necesarias para preparar vesiculas sinapticas para la exocitosis La familia RIM de proteinas de la zona activa probablemente funcione como andamios de proteinas que ayudan a regular la exocitosis vesicular durante la plasticidad a corto plazo Suministrado por OMIM 6 Interacciones EditarSe ha demostrado que RIMS1 interactua con ERC2 7 RAB3A 8 UNC13A 9 UNC13B 10 11 y YHHAH 12 Referencias Editar Referencia Human PubMed National Center for Biotechnology Information U S National Library of Medicine Referencia Mouse PubMed National Center for Biotechnology Information U S National Library of Medicine Plaza Seron Maria del Carmen 2016 Reacciones de hipersensibilidad por intolerancia cruzada a antiinflamatorios no esteroideos relacion fenotipo genotipo Universidad de Malaga p 29 Consultado el 12 de febrero de 2020 Prediction of the coding sequences of unidentified human genes VII The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro DNA Res 4 2 141 50 September 1997 PMID 9205841 doi 10 1093 dnares 4 2 141 Direct interaction of the Rab3 effector RIM with Ca2 channels SNAP 25 and synaptotagmin J Biol Chem 276 35 32756 62 August 2001 PMID 11438518 doi 10 1074 jbc M100929200 a b Entrez Gene RIMS1 regulating synaptic membrane exocytosis 1 Physical and functional interaction of the active zone proteins CAST RIM1 and Bassoon in neurotransmitter release J Cell Biol 164 2 301 11 January 2004 PMC 2172332 PMID 14734538 doi 10 1083 jcb 200307101 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 April 2003 PMID 12578829 doi 10 1074 jbc M212341200 Protein unc 13 homolog A UniProt Cast a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13 1 J Cell Biol 158 3 577 90 August 2002 PMC 2173811 PMID 12163476 doi 10 1083 jcb 200202083 Functional interaction of the active zone proteins Munc13 1 and RIM1 in synaptic vesicle priming Neuron 30 1 183 96 April 2001 PMID 11343654 doi 10 1016 s0896 6273 01 00272 0 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 October 2003 PMID 12871946 doi 10 1074 jbc M212801200 Lectura adicional Editar Localization of a gene CORD7 for a dominant cone rod dystrophy to chromosome 6q Am J Hum Genet 63 1 274 9 1998 PMC 1377229 PMID 9634506 doi 10 1086 301905 Functional interaction of the active zone proteins Munc13 1 and RIM1 in synaptic vesicle priming Neuron 30 1 183 96 2001 PMID 11343654 doi 10 1016 S0896 6273 01 00272 0 HIV Nef mediated cellular phenotypes are differentially expressed as a function of intracellular Nef concentrations J Biol Chem 276 35 32763 70 2001 PMID 11438519 doi 10 1074 jbc M101025200 Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2 ATPase result in a complete loss of Ca2 transport activity without a loss of Ca2 dependent ATPase activity Role of the CYS876 CYS888 disulfide bond J Biol Chem 276 35 32771 8 2001 PMID 11438520 doi 10 1074 jbc M101229200 Induction of neurite outgrowth in PC12 cells by alpha phenyl N tert butylnitron through activation of protein kinase C and the Ras extracellular signal regulated kinase pathway J Biol Chem 276 35 32779 85 2001 PMID 11438521 doi 10 1074 jbc M101403200 Actin cytoskeletal association of cytohesin 1 is regulated by specific phosphorylation of its carboxyl terminal polybasic domain J Biol Chem 276 40 37472 81 2001 PMID 11438522 doi 10 1074 jbc M101502200 RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone Nature 415 6869 321 6 2002 PMID 11797009 doi 10 1038 415321a Cast a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13 1 J Cell Biol 158 3 577 90 2002 PMC 2173811 PMID 12163476 doi 10 1083 jcb 200202083 A family of RIM binding proteins regulated by alternative splicing Implications for the genesis of synaptic active zones Proc Natl Acad Sci U S A 99 22 14464 9 2002 PMC 137906 PMID 12391317 doi 10 1073 pnas 182532999 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 2003 PMID 12578829 doi 10 1074 jbc M212341200 Genomic definition of RIM proteins evolutionary amplification of a family of synaptic regulatory proteins small star filled Genomics 81 2 126 37 2003 PMID 12620390 doi 10 1016 S0888 7543 02 00024 1 Genomic organisation and alternative splicing of human RIM1 a gene implicated in autosomal dominant cone rod dystrophy CORD7 Genomics 81 3 304 14 2003 PMID 12659814 doi 10 1016 S0888 7543 03 00010 7 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 2003 PMID 12871946 doi 10 1074 jbc M212801200 Physical and functional interaction of the active zone proteins CAST RIM1 and Bassoon in neurotransmitter release J Cell Biol 164 2 301 11 2004 PMC 2172332 PMID 14734538 doi 10 1083 jcb 200307101 Large scale characterization of HeLa cell nuclear phosphoproteins Proc Natl Acad Sci U S A 101 33 12130 5 2004 PMC 514446 PMID 15302935 doi 10 1073 pnas 0404720101 Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa Ophthalmic Res 37 2 89 93 2005 PMID 15746564 doi 10 1159 000084250 Genetic enhancement of cognition in a kindred with cone rod dystrophy due to RIMS1 mutation J Med Genet 44 6 373 80 2007 PMC 2740882 PMID 17237123 doi 10 1136 jmg 2006 047407 Datos Q18036647Obtenido de https es wikipedia org w index php title RIMS1 amp oldid 131617746, 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