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Search results 101 to 182 out of 182 for Vps13c

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0.027s
Type Details Score
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication        
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
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 Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
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
Protein
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
UniProt Feature
Begin: 1
Description: Intermembrane lipid transfer protein VPS13C
Type: chain
End: 3748
Protein
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 3748  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3708  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3623  
Fragment?: false
Publication
First Author: Kumar N
Year: 2018
Journal: J Cell Biol
Title: VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites.
Volume: 217
Issue: 10
Pages: 3625-3639
Allele
Name: vacuolar protein sorting 13C; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
DO Term
Allele
Name: vacuolar protein sorting 13C; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Publication
First Author: Mizuno E
Year: 2007
Journal: Biochem Biophys Res Commun
Title: Brain-specific transcript variants of 5' and 3' ends of mouse VPS13A and VPS13C.
Volume: 353
Issue: 4
Pages: 902-7
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Publication
First Author: Samaranayake HS
Year: 2011
Journal: Eukaryot Cell
Title: Vacuolar protein sorting protein 13A, TtVPS13A, localizes to the tetrahymena thermophila phagosome membrane and is required for efficient phagocytosis.
Volume: 10
Issue: 9
Pages: 1207-18
Protein
Organism: Mus musculus/domesticus
Length: 1457  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1429  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
Publication
First Author: Valverde DP
Year: 2019
Journal: J Cell Biol
Title: ATG2 transports lipids to promote autophagosome biogenesis.
Volume: 218
Issue: 6
Pages: 1787-1798
Protein Domain
Type: Domain
Description: This domain lies towards the N terminus, just downstream from . This domain is involved in lipid binding and transport [, , ]. This domain specifically interacts with phosphatidic acid and phosphorylated forms of phosphatidyl inositol [].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].
Protein Domain
Type: Domain
Description: This entry represents a domain reminiscent of a DH domain (DH-Like domain) found adjacent the C-terminal PH-like domain of VPS13 proteins [, , , ]. DHL-PH domains has been identified as the mitochondria-binding region of VPS13A and the lipid droplet-binding region of both proteins. These two domains contain a region of high similarity to ATG2, which also binds lipid droplets [, ].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].
Protein Domain
Type: Domain
Description: This entry represents the repeating region of VPS13. This repeating region shares a common core element that includes a well-conserved P-X4-P-X13-17-G sequence [, ]. This region contains a FFAT motif which mediates VAMP binding and tethering of the ER.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].
Protein Domain
Type: Domain
Description: This is the N-terminal chorein domain of VPS13 and ATG2 proteins, which is highly conserved. ATG2 proteins are involved in autophagosome assembly, playing a key role in nonvesicular lipid transfer [, , , ]. This domain has a scoop shape whose concave surface is lined by hydrophobic residues which bind glycerophospholipids.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].
Publication
First Author: Bean BDM
Year: 2018
Journal: J Cell Biol
Title: Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites.
Volume: 217
Issue: 10
Pages: 3593-3607
Publication    
First Author: Yeshaw WM
Year: 2019
Journal: Elife
Title: Human VPS13A is associated with multiple organelles and influences mitochondrial morphology and lipid droplet motility.
Volume: 8
Publication  
First Author: Muñoz-Braceras S
Year: 2019
Journal: Dis Model Mech
Title: VPS13A is closely associated with mitochondria and is required for efficient lysosomal degradation.
Volume: 12
Issue: 2
Publication
First Author: Leonzino M
Year: 2021
Journal: Biochim Biophys Acta Mol Cell Biol Lipids
Title: Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport.
Volume: 1866
Issue: 10
Pages: 159003
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1078  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 2339  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: true
Publication
First Author: Koizumi K
Year: 2013
Journal: Development
Title: Identification of SHRUBBY, a SHORT-ROOT and SCARECROW interacting protein that controls root growth and radial patterning.
Volume: 140
Issue: 6
Pages: 1292-300
Publication
First Author: De M
Year: 2017
Journal: J Cell Biol
Title: The Vps13p-Cdc31p complex is directly required for TGN late endosome transport and TGN homotypic fusion.
Volume: 216
Issue: 2
Pages: 425-439
Protein Domain
Type: Domain
Description: This entry represents the VPS13 adaptor binding (VAB) domain, previously known as SHR-BD, found in VPS13 []. These proteins interact with membrane-specific adaptor proteins such as Ypt35, Spo71 and the mitochondrial membrane protein Mcp1, to be recruited to different membranes. This domain interacts with Ypt35 which recruits VPS13 to endosomal and vacuolar membranes, and with Mcp1 to target VPS13 at mitochondria []. In plants, this domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY () [].This domain likely adopts an elongated structure consisting of β-sheets. It has been described as a β-propeller/WD40-like structure [, ], however, based on structural models, it does not seem to have that 3D arrangement.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].
Protein
Organism: Mus musculus/domesticus
Length: 3993  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
Publication
First Author: Velayos-Baeza A
Year: 2004
Journal: Genomics
Title: Analysis of the human VPS13 gene family.
Volume: 84
Issue: 3
Pages: 536-49
Protein
Organism: Mus musculus/domesticus
Length: 3166  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3748  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4359  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4390  
Fragment?: false
Publication  
First Author: Kolakowski D
Year: 2021
Journal: Int J Mol Sci
Title: The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus.
Volume: 22
Issue: 22
Protein
Organism: Mus musculus/domesticus
Length: 1914  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2075  
Fragment?: false
Publication
First Author: Mousavy Gharavy SN
Year: 2021
Journal: Diabetologia
Title: Sexually dimorphic roles for the type 2 diabetes-associated C2cd4b gene in murine glucose homeostasis.
Volume: 64
Issue: 4
Pages: 850-864
Protein
Organism: Mus musculus/domesticus
Length: 921  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 857  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1186  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 757  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 3211  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1918  
Fragment?: true
Publication
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 4
Pages: 167-80
Publication
First Author: Sweet SM
Year: 2009
Journal: Mol Cell Proteomics
Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.
Volume: 8
Issue: 5
Pages: 904-12
Publication
First Author: Guo A
Year: 2014
Journal: Mol Cell Proteomics
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
Volume: 13
Issue: 1
Pages: 372-87
Publication
First Author: Trost M
Year: 2009
Journal: Immunity
Title: The phagosomal proteome in interferon-gamma-activated macrophages.
Volume: 30
Issue: 1
Pages: 143-54
Publication
First Author: Villén J
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Large-scale phosphorylation analysis of mouse liver.
Volume: 104
Issue: 5
Pages: 1488-93
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112