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Search results 401 to 500 out of 582 for Rab3a

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Type Details Score
GXD Expression    
Probe: MGI:7788255
Assay Type: Western blot
Annotation Date: 2024-12-18
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1735719
Stage: TS19
Assay Id: MGI:7788335
Age: embryonic day 11.5
Image: S3
Specimen Label: Mes
Detected: true
Specimen Num: 1
GXD Expression    
Probe: MGI:7788255
Assay Type: Western blot
Annotation Date: 2024-12-18
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3818419
Stage: TS19
Assay Id: MGI:7788335
Age: embryonic day 11.5
Image: S3
Specimen Label: Epi
Detected: false
Specimen Num: 2
GXD Expression    
Probe: MGI:1447853
Assay Type: RNA in situ
Annotation Date: 2023-09-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3271122
Pattern: Not Specified
Stage: TS22
Assay Id: MGI:7530844
Age: embryonic day 14.5
Specimen Label: Supplementary table 2
Detected: true
Specimen Num: 1
GXD Expression  
Probe: MGI:1447853
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1603923
Pattern: Ubiquitous
Stage: TS23
Assay Id: MGI:4827580
Age: embryonic day 14.5
Image: euxassay_006549_15
Specimen Label: euxassay_006549_15
Detected: true
Specimen Num: 1
GXD Expression
Probe: MGI:7788247
Assay Type: RNA in situ
Annotation Date: 2024-12-18
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1735719
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:7788329
Age: embryonic day 11.5
Image: 3D'
Note: Expression restricted to mesenchyme.
Specimen Label: 3D'
Detected: true
Specimen Num: 1
GXD Expression    
Probe: MGI:1447853
Assay Type: RNA in situ
Annotation Date: 2023-09-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1754722
Pattern: Not Specified
Stage: TS22
Assay Id: MGI:7530844
Age: embryonic day 14.5
Specimen Label: Supplementary table 2
Detected: true
Specimen Num: 1
GO Term
Allele  
Name: RAB3A interacting protein; gene trap Ayu21-W142, Institute of Molecular Embryology and Genetics
Allele Type: Gene trapped
Allele
Name: RAB3A interacting protein (rabin3)-like 1; targeted mutation 2e, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
Allele
Name: RAB3A interacting protein (rabin3)-like 1; targeted mutation 2a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
Allele  
Name: RAB3A interacting protein (rabin3)-like 1; gene trap 372H9, Centre for Modeling Human Disease
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST13513C11, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST13640F7, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST13778C5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST14248H8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST14383C5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST14502B2, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Allele  
Name: RAB3A interacting protein; gene trap IST14994B12, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Allele
Name: RAB3A interacting protein (rabin3)-like 1; endonuclease-mediated mutation 1, GemPharmatech Co., Ltd
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Allele
Name: RAB3A interacting protein (rabin3)-like 1; endonuclease-mediated mutation 2, GemPharmatech Co., Ltd
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Rab3ip/Rab3ip
Background: involves: C57BL/6 * CBA
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Rab3il1/Rab3il1
Background: C57BL/6NJ-Rab3il1/Mmjax
Zygosity: hm
Has Mutant Allele: true
Publication
First Author: Dalfó E
Year: 2004
Journal: Neurobiol Dis
Title: Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease.
Volume: 16
Issue: 1
Pages: 92-7
Publication
First Author: Wang J
Year: 2015
Journal: J Cell Sci
Title: The Arf and Rab11 effector FIP3 acts synergistically with ASAP1 to direct Rabin8 in ciliary receptor targeting.
Volume: 128
Issue: 7
Pages: 1375-85
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Rab3ip/Rab3ip<+>
Background: involves: C57BL/6 * CBA
Zygosity: ht
Has Mutant Allele: true
Genotype
Symbol: Rab3ip/Rab3ip<+>
Background: C57BL/6N-Rab3ip/J
Zygosity: ht
Has Mutant Allele: true
Publication
First Author: Fukuda M
Year: 2004
Journal: Genes Cells
Title: Alternative splicing in the first alpha-helical region of the Rab-binding domain of Rim regulates Rab3A binding activity: is Rim a Rab3 effector protein during evolution?
Volume: 9
Issue: 9
Pages: 831-42
Publication  
First Author: Elliott KH
Year: 2023
Journal: Development
Title: Identification of a heterogeneous and dynamic ciliome during embryonic development and cell differentiation.
Volume: 150
Issue: 8
Publication
First Author: Li L
Year: 2023
Journal: Acta Biochim Biophys Sin (Shanghai)
Title: A direct interaction between CENTLEIN and RABIN8 is required for primary cilium formation.
Volume: 55
Issue: 9
Pages: 1434-1444
Publication
First Author: Andres DA
Year: 1993
Journal: Cell
Title: cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein.
Volume: 73
Issue: 6
Pages: 1091-9
Protein Domain
Type: Family
Description: This entry includes Rabphilin and Doc2. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: Rabphilin contains an N-terminal Rab-binding domain (RBD), whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID) []. This entry also includes Noc2 (also known as Rabphilin-3A-like protein), which is a potential effector of Ras-associated binding proteins Rab3A and Rab27A. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains [].
Publication
First Author: Millar AL
Year: 2002
Journal: Histol Histopathol
Title: Rab3D: a regulator of exocytosis in non-neuronal cells.
Volume: 17
Issue: 3
Pages: 929-36
Protein Domain
Type: Family
Description: The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules []. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process [].
Publication
First Author: Kotake K
Year: 1997
Journal: J Biol Chem
Title: Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells.
Volume: 272
Issue: 47
Pages: 29407-10
Publication
First Author: Shanmugam C
Year: 2009
Journal: Biotech Histochem
Title: Immunohistochemical expression of rabphilin-3A-like (Noc2) in normal and tumor tissues of human endocrine pancreas.
Volume: 84
Issue: 2
Pages: 39-45
Publication
First Author: Manabe S
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Identification and characterization of Noc2 as a potential Rab3B effector protein in epithelial cells.
Volume: 316
Issue: 1
Pages: 218-25
Protein Domain
Type: Family
Description: Noc2, also known as Rabphilin-3A-like protein, is a potential effector of Ras-associated binding proteins Rab3A and Rab27A [, ]that is involved in the regulation of exocytosis in endocrine and exocrine cells [, , ]. Noc2 may regulate insulin secretion from pancreatic beta-cells and amylase secretion from pancreatic acini [].
Protein
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
Publication
First Author: Imai A
Year: 2006
Journal: Arch Biochem Biophys
Title: Functional involvement of Noc2, a Rab27 effector, in rat parotid acinar cells.
Volume: 455
Issue: 2
Pages: 127-35
Publication
First Author: Olkkonen VM
Year: 1994
Journal: Gene
Title: Isolation of a mouse cDNA encoding Rab23, a small novel GTPase expressed predominantly in the brain.
Volume: 138
Issue: 1-2
Pages: 207-11
Publication
First Author: Yamaguchi K
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: A GDP/GTP exchange protein for the Rab3 small G protein family up-regulates a postdocking step of synaptic exocytosis in central synapses.
Volume: 99
Issue: 22
Pages: 14536-41
Publication
First Author: Ishizaki H
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Role of rab GDP dissociation inhibitor alpha in regulating plasticity of hippocampal neurotransmission.
Volume: 97
Issue: 21
Pages: 11587-92
Publication  
First Author: Fukuda M
Year: 2005
Journal: Methods Enzymol
Title: Assay of the Rab-binding specificity of rabphilin and Noc2: target molecules for Rab27.
Volume: 403
Pages: 469-81
Protein Domain
Type: Domain
Description: Rab effector Noc2 (also known as RPH3AL) is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells []. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells [, ]. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains. The FYVE domain of Noc2 resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif [].
Publication
First Author: Bhartur SG
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Genomic structure of murine Rab11 family members.
Volume: 269
Issue: 2
Pages: 611-7
Publication
First Author: Kukimoto-Niino M
Year: 2008
Journal: Structure
Title: Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases.
Volume: 16
Issue: 10
Pages: 1478-90
Publication
First Author: Yasuda T
Year: 2010
Journal: Cell Metab
Title: Rim2alpha determines docking and priming states in insulin granule exocytosis.
Volume: 12
Issue: 2
Pages: 117-29
Publication
First Author: Adachi R
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Genomic organization, chromosomal localization, and expression of the murine RAB3D gene.
Volume: 273
Issue: 3
Pages: 877-83
Publication
First Author: Encarnação M
Year: 2016
Journal: J Cell Biol
Title: A Rab3a-dependent complex essential for lysosome positioning and plasma membrane repair.
Volume: 213
Issue: 6
Pages: 631-40
Protein
Organism: Mus musculus/domesticus
Length: 1960  
Fragment?: false
Publication
First Author: van Bokhoven H
Year: 1994
Journal: Hum Mol Genet
Title: Cloning and characterization of the human choroideremia gene.
Volume: 3
Issue: 7
Pages: 1041-6
Publication
First Author: Cremers FP
Year: 1990
Journal: Nature
Title: Cloning of a gene that is rearranged in patients with choroideraemia.
Volume: 347
Issue: 6294
Pages: 674-7
Publication
First Author: Merry DE
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Isolation of a candidate gene for choroideremia.
Volume: 89
Issue: 6
Pages: 2135-9
Protein Domain
Type: Domain
Description: This entry represents the Rab-binding domain.Rab are small GTPases implicated in vesicle trafficking. Like the other smallGTPases, Rab proteins act as molecular switches, with an active GTP-bound formthat interacts with its target or effector protein and an inactive GDP-boundform. A subgroup of Rab effectors contain in their N-terminal part a conservedregion of around 70 amino acid residues, the Rab-binding domain (RabBD). Insome Rab effector domains an atypical FYVE-type zinc finger is inserted in thecentral part [].The crystal structure of the Rab effector domain of Rabphilin-3A in complexwith Rab3A has been solved []. The structure consists of twolong helices separated by an atypical FYVE-type zinc finger which adopts aconformation similar to classical ones. The central zincfinger does not directly interact with Rab3A. The amino acids important forthis interaction are located around a short C-terminal motif (SGAWFF) and anacidic cluster in the N-terminal area.
Protein Domain
Type: Family
Description: Rab proteins constitute a family of small GTPases that serve a regulatory role in vesicular membrane traffic [, ]; C-terminal geranylgeranylation is crucial for their membrane association and function. This post-translational modification is catalysed by Rab geranylgeranyl transferase (Rab-GGTase), a multi-subunit enzyme that contains a catalytic heterodimer and an accessory component, termed Rab escort protein (REP)-1 [, ]. REP-1 presents newly-synthesised Rab proteins to the catalytic component, and forms a stable complex with the prenylated proteins following the transfer reaction.cDNA cloning of component A of rat Rab geranylgeranyl transferase (REP) confirms its resemblance to Rab3A guanine nucleotide dissociation inhibitor (GDI) and its identity with the human choroideremia gene product []. A genetic defect in REP underlies human choroideremia. Choroideraemia (or tapetochoroidal dystrophy) is a common form of X-linked blindness characterised by progressive dystrophy of the choroid, retinal pigment epithelium and retina [, , ].
Protein
Organism: Mus musculus/domesticus
Length: 83  
Fragment?: true
Publication
First Author: Nakayama T
Year: 1999
Journal: J Neurochem
Title: Localization and subcellular distribution of N-copine in mouse brain.
Volume: 72
Issue: 1
Pages: 373-9
Publication
First Author: Merrins MJ
Year: 2008
Journal: J Physiol
Title: Kinetics of Rab27a-dependent actions on vesicle docking and priming in pancreatic beta-cells.
Volume: 586
Issue: 22
Pages: 5367-81
Publication
First Author: Spencer B
Year: 2016
Journal: J Neurosci
Title: Reducing Endogenous α-Synuclein Mitigates the Degeneration of Selective Neuronal Populations in an Alzheimer's Disease Transgenic Mouse Model.
Volume: 36
Issue: 30
Pages: 7971-84
Publication
First Author: Castillo PE
Year: 2002
Journal: Nature
Title: RIM1alpha is required for presynaptic long-term potentiation.
Volume: 415
Issue: 6869
Pages: 327-30
Publication
First Author: Paulmann N
Year: 2009
Journal: PLoS Biol
Title: Intracellular serotonin modulates insulin secretion from pancreatic beta-cells by protein serotonylation.
Volume: 7
Issue: 10
Pages: e1000229
Publication
First Author: Smith GA
Year: 2014
Journal: Hum Mol Genet
Title: Progressive axonal transport and synaptic protein changes correlate with behavioral and neuropathological abnormalities in the heterozygous Q175 KI mouse model of Huntington's disease.
Volume: 23
Issue: 17
Pages: 4510-27
Publication
First Author: Tsetsenis T
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Rab3B protein is required for long-term depression of hippocampal inhibitory synapses and for normal reversal learning.
Volume: 108
Issue: 34
Pages: 14300-5
Publication  
First Author: Kang S
Year: 2018
Journal: Front Behav Neurosci
Title: Effects of a Dehydroevodiamine-Derivative on Synaptic Destabilization and Memory Impairment in the 5xFAD, Alzheimer's Disease Mouse Model.
Volume: 12
Pages: 273
Publication
First Author: Yi Z
Year: 2002
Journal: Mol Cell Biol
Title: The Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granules.
Volume: 22
Issue: 6
Pages: 1858-67
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 302  
Fragment?: false
Publication  
First Author: Mitra S
Year: 2018
Journal: Front Mol Neurosci
Title: Absence of Wdr13 Gene Predisposes Mice to Mild Social Isolation - Chronic Stress, Leading to Depression-Like Phenotype Associated With Differential Expression of Synaptic Proteins.
Volume: 11
Pages: 133
Protein
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Publication
First Author: tom Dieck S
Year: 1998
Journal: J Cell Biol
Title: Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals.
Volume: 142
Issue: 2
Pages: 499-509
Publication
First Author: Takao-Rikitsu E
Year: 2004
Journal: J Cell Biol
Title: Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release.
Volume: 164
Issue: 2
Pages: 301-11
Protein Domain
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding propertiesdepend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This (predicted) zinc finger is found in the bassoon and piccolo proteins, both of which are components of the presynaptic cytoskeletal matrix (PCM) assembled at the active zone of neurotransmitter release, where Piccolo plays a role in the trafficking of synaptic vesicles (SVs) [, , ]. The Piccolo zinc fingers were found to interact with the dual prenylated rab3A and VAMP2/Synaptobrevin II receptor PRA1. There are eight conserved cysteines in Piccolo-type zinc fingers, suggesting that they coordinates two zinc ligands.
Publication
First Author: Hong Y
Year: 2016
Journal: J Neurosci
Title: Mutant Huntingtin Impairs BDNF Release from Astrocytes by Disrupting Conversion of Rab3a-GTP into Rab3a-GDP.
Volume: 36
Issue: 34
Pages: 8790-801
Protein
Organism: Mus musculus/domesticus
Length: 529  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: true
Publication
First Author: Alexandrov K
Year: 1994
Journal: EMBO J
Title: Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes.
Volume: 13
Issue: 22
Pages: 5262-73
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true