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Search results 201 to 260 out of 260 for Rab3c

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Type Details Score
Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q920F0
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: true
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HT Experiment
GSE150388 | ATACseq, CutnRun and RNAseq data from Merkel cell and Touch dome epithelial progenitor cells, from wild type and Pou4f3-mutant epidermis
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
12168804 | -
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
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Publication
14716293 | -
First Author: Efimova EV
Year: 2004
Journal: Oncogene
Title: IG20, in contrast to DENN-SV, (MADD splice variants) suppresses tumor cell survival, and enhances their susceptibility to apoptosis and cancer drugs.
Volume: 23
Issue: 5
Pages: 1076-87
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Publication
9115275 | -
First Author: Schievella AR
Year: 1997
Journal: J Biol Chem
Title: MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase.
Volume: 272
Issue: 18
Pages: 12069-75
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Publication
9136770 | -
First Author: Iwasaki K
Year: 1997
Journal: Neuron
Title: aex-3 encodes a novel regulator of presynaptic activity in C. elegans.
Volume: 18
Issue: 4
Pages: 613-22
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Protein Domain
IPR039980 | MADD
Type: Family
Description: MAP kinase-activating death domain protein (MADD) regulates cell proliferation, survival and death through alternative mRNA splicing. Different isoforms have different effects: isoform 5 increases cell proliferation whereas isoform 2 decreases it; isoform 1 is susceptible to inducing apoptosis, isoform 5 is resistant []. MADD activates RAB3A, RAB3C and RAB3D by converting them from GDP-bound inactive forms to GTP-bound active forms []. MADD is a component of the TNFRSF1A signaling complex, linking the type 1 tumor necrosis factor receptor TNFRSF1A with MAP kinase activation []. MADD contains a tripartite DENN domain. In the nematode Caenorhabditis elegans, MADD is also known as regulator of presynaptic activity aex-3 [].
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Protein Domain
IPR037872 | Rab3
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 [].
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Protein
Q80UJ7
Organism: Mus musculus/domesticus
Length: 981  
Fragment?: false
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Protein
Q8BMG7
Organism: Mus musculus/domesticus
Length: 1366  
Fragment?: false
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Protein
E9QKE4
Organism: Mus musculus/domesticus
Length: 1387  
Fragment?: false
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Protein
A0A1D5RLG3
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: false
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Protein
A0A0A6YWM5
Organism: Mus musculus/domesticus
Length: 1367  
Fragment?: false
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Protein
Q3UYK8
Organism: Mus musculus/domesticus
Length: 982  
Fragment?: false
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Protein Domain
IPR026147 | Rab3GAP1_conserved
Type: Domain
Description: This entry represents a conserved domain found in the Rab3 GTPase-activating protein catalytic subunit (Rab3GAP1).Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein Domain
IPR026059 | Rab3GAP2
Type: Family
Description: This family represents the regulatory subunit of the Rab3GAP complex, also known as Rab3GAP2. Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein Domain
IPR032839 | RAB3GAP_N
Type: Domain
Description: This family includes the N terminus of the Rab3 GTPase-activating protein (GAP) non-catalytic subunit.Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein Domain
IPR029257 | RAB3GAP2_C
Type: Domain
Description: This entry represents the C terminus of the Rab3 GTPase-activating protein non-catalytic subunit.Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein Domain
IPR045698 | Rab3GAP1_C
Type: Domain
Description: This entry represents the C-terminal domain found in the Rab3 GTPase-activating protein catalytic subunit (Rab3GAP1) predominantly in animals.Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein Domain
IPR045700 | Rab3GAP1
Type: Family
Description: Small G proteins of the Rab family are regulators of intracellular vesicle traffic. Their rate of GTP hydrolysis is enhanced by specific GTPase-activating proteins (GAPs) that switch G proteins to their inactive form []. Rab3GAP1 (catalytic subunit) has been shown to form a heterodimeric complex with Rab3GAP2 (the regulatory subunit), and this complex acts as a guanosine nucleotide exchange factor for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3GAP complex may participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters [, ]. It also activates Rab18 and promotes autolysosome maturation through the Vps34 Complex I [].Mutations in the Rab3GAP1/2 gene cause Warburg micro syndrome (WMS), a hereditary autosomal neuromuscular disorder [].
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Protein
Q8BYZ6
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: true
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Protein
Q3UEY3
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: true
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Publication
15696165 | -
First Author: Aligianis IA
Year: 2005
Journal: Nat Genet
Title: Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro syndrome.
Volume: 37
Issue: 3
Pages: 221-3
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Publication
9030515 | -
First Author: Fukui K
Year: 1997
Journal: J Biol Chem
Title: Isolation and characterization of a GTPase activating protein specific for the Rab3 subfamily of small G proteins.
Volume: 272
Issue: 8
Pages: 4655-8
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Publication
9852129 | -
First Author: Oishi H
Year: 1998
Journal: J Biol Chem
Title: Localization of the Rab3 small G protein regulators in nerve terminals and their involvement in Ca2+-dependent exocytosis.
Volume: 273
Issue: 51
Pages: 34580-5
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Publication
10859313 | -
First Author: Clabecq A
Year: 2000
Journal: J Biol Chem
Title: Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP.
Volume: 275
Issue: 41
Pages: 31786-91
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Publication
32248620 | -
First Author: Takáts S
Year: 2021
Journal: FEBS J
Title: The Warburg Micro Syndrome-associated Rab3GAP-Rab18 module promotes autolysosome maturation through the Vps34 Complex I.
Volume: 288
Issue: 1
Pages: 190-211
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Publication
10407024 | J:56293
First Author: Schlüter OM
Year: 1999
Journal: J Neurosci
Title: Rabphilin knock-out mice reveal that rabphilin is not required for rab3 function in regulating neurotransmitter release.
Volume: 19
Issue: 14
Pages: 5834-46
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Protein
A6PWP7
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
Q99LH6
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
P63011
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
Q9CZT8
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
P62823
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
P35276
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
Q3TU26
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
Q0PD62
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
A0A286YDR2
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
Q543Q4
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
Q0PD63
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Publication
20937701 | -
First Author: Yoshimura S
Year: 2010
Journal: J Cell Biol
Title: Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors.
Volume: 191
Issue: 2
Pages: 367-81
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Protein
Q80U28
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
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Protein
E9QN47
Organism: Mus musculus/domesticus
Length: 1627  
Fragment?: false
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Protein
A2AGQ6
Organism: Mus musculus/domesticus
Length: 1602  
Fragment?: false
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Protein
A2AGQ9
Organism: Mus musculus/domesticus
Length: 1574  
Fragment?: false
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Protein
A2AGR0
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
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Protein
A2AGQ8
Organism: Mus musculus/domesticus
Length: 1562  
Fragment?: false
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Protein
A2AGQ4
Organism: Mus musculus/domesticus
Length: 1632  
Fragment?: false
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Protein
A2AGQ7
Organism: Mus musculus/domesticus
Length: 1573  
Fragment?: false
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Protein
A2AGQ3
Organism: Mus musculus/domesticus
Length: 1541  
Fragment?: false
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Protein
A0A0R4J1F4
Organism: Mus musculus/domesticus
Length: 1558  
Fragment?: false
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Protein
A6PWP8
Organism: Mus musculus/domesticus
Length: 1115  
Fragment?: false
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Protein
A2AGQ2
Organism: Mus musculus/domesticus
Length: 1554  
Fragment?: false
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Protein
A2AGQ5
Organism: Mus musculus/domesticus
Length: 1593  
Fragment?: false
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Protein
A2AGR1
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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Cambridge CB2 3EH, United Kingdom