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Search results 1 to 86 out of 86 for Vps28

0.023s
Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: frog, western clawed
Protein Domain
Type: Family
Description: The Endosomal Sorting Complex Required for Transport (ESCRT) complexes form the machinery driving protein sorting from endosomes to lysosomes. ESCRT complexes are central to receptor down-regulation, lysosome biogenesis, and budding of HIV. Yeast ESCRT-I consists of three protein subunits, Vps23, Vps28, and Vps37. In humans, ESCRT-I comprises TSG101, VPS28, and one of four potential human VPS37 homologues. The main role of ESCRT-I is to recognise ubiquitinated cargo via the UEV domain of the VPS23/TSG101 subunit. The assembly of the ESCRT-I complex is directed by the C-terminal steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C-terminal half of VPS37. The structure is primarily composed of three long, parallel helical hairpins, each corresponding to a different subunit. The additional domains and motifs extending beyond the core serve as gripping tools for ESCRT-I critical functions [, ].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
Publication
First Author: Kostelansky MS
Year: 2006
Journal: Cell
Title: Structural and functional organization of the ESCRT-I trafficking complex.
Volume: 125
Issue: 1
Pages: 113-26
Publication
First Author: Teo H
Year: 2006
Journal: Cell
Title: ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.
Volume: 125
Issue: 1
Pages: 99-111
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication    
First Author: Strausberg R
Year: 2001
Journal: GenBank Submission
Title: Mus musculus, RIKEN cDNA 1110014J03 gene, clone MGC: 19216 IMAGE: 4239189, mRNA, complete cds
Pages: BC013535
Publication
First Author: Cho SG
Year: 2003
Journal: J Cell Biol
Title: Identification of a novel antiapoptotic protein that antagonizes ASK1 and CAD activities.
Volume: 163
Issue: 1
Pages: 71-81
Publication
First Author: Suzuki H
Year: 2001
Journal: Genome Res
Title: Protein-protein interaction panel using mouse full-length cDNAs.
Volume: 11
Issue: 10
Pages: 1758-65
Publication      
First Author: Centre for Modeling Human Disease
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the NorCOMM project by the Centre for Modeling Human Disease (Cmhd), Institute of Biomaterials & Biomedical Engineering, University of Toronto
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: RIKEN Data Curation in Mouse Genome Informatics
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
Publication
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
Publication        
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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 Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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
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: Bishop N
Year: 2001
Journal: J Biol Chem
Title: TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes.
Volume: 276
Issue: 15
Pages: 11735-42
Publication
First Author: Borlak J
Year: 2018
Journal: Biochim Biophys Acta Mol Basis Dis
Title: Serum proteome mapping of EGF transgenic mice reveal mechanistic biomarkers of lung cancer precursor lesions with clinical significance for human adenocarcinomas.
Volume: 1864
Issue: 10
Pages: 3122-3144
Publication
First Author: Singh SR
Year: 2021
Journal: Autophagy
Title: A high-throughput screening identifies ZNF418 as a novel regulator of the ubiquitin-proteasome system and autophagy-lysosomal pathway.
Volume: 17
Issue: 10
Pages: 3124-3139
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
Protein Domain
Type: Domain
Description: A key aspect of eukaryotic intracellular trafficking is the sorting of cell-surface proteins into multi-vesicular endosomes or bodies (MVBs), which eventually fuse with the lysosome, where they are degraded by lipases and peptidases. This is the primary mechanism for down-regulation of signaling via transmembrane receptors and removal of misfolded or defective membrane proteins. This process is also utilised by several viruses (e.g. HIV-1) to facilitate budding of their virions from the cell-membrane. Studies in animals and fungi have shown that it depends on an intricate series of interactions, which is initiated via ubiquitination (typically one or more mono-ubiquitinations) of the cytoplasmic tails of membrane proteins by specific E3 ligases. Ubiquitinated membrane proteins are then captured into endosomes by the ESCRT system and prevented from being recycled back to the plasma membrane via the retrograde trafficking system. The ESCRT system also folds the endosomal membranes into invaginations that are concentrated in these ubiquitinated targets and catalyzes their abscission into intra-luminal-vesicles inside the endosome. This largely seals the fate of these membrane proteins as targets for lysosomal degradation. The ESCRT system is comprised of 4 major protein complexes, ESCRT-0 to ESCRT-III, which are successively involved in the above-described steps [].ESCRT-I contains three subunits that are conserved between yeast and animals, namely the inactive E2-ligase protein TSG101/VPS23, VPS28 and VPS37. Additionally, both yeast and metazoan ESCRT-I contain a fourth subunit termed MVB12 (multivesicular body sorting factor of 12 kD); however, the MVB12 subunits from the two lineages do not show significant sequence similarity. The metazoan MVB12 proteins contain two distinct conserved domains that occur independently in various proteins. The C-terminal region of MVB12, which is shared with ubiquitin associated protein-1 (UBAP1), forms the UBAP1-MVB12 associated (UMA) domain. Human UBAP1 is implicated in nasopharyngeal carcinoma risk and fronto-temporal lobar degeneration. The UMA domain is also found in several other poorly characterised proteins, including at leat one orthologous group of proteins conserved in vertebrates prototyped be the human protein LOC390595 and another group conserved across Metazoa typified by human tcag7.903. The UMA domain found in MVB12 and UBAP1 defines a novel adaptor that might recruit diverse targets to ESCRT-I. The different UMA proteins might function as alternative as MVB12-like subunit that recruit different targets via their specific intercation modules (such as MABP) or UBA or the specific extensions) to the ESCRT-I complex [].This entry represents the UMA domain, which contains a conserved proline followed by a hydrophobic residue in the N terminus and a nearly absolutely conserved glutamate at the C terminus. It is predicted to adopt an alpha+beta fold [].
Protein Domain
Type: Domain
Description: A key aspect of eukaryotic intracellular trafficking is the sorting of cell-surface proteins into multi-vesicular endosomes or bodies (MVBs), which eventually fuse with the lysosome, where they are degraded by lipases and peptidases. This is the primary mechanism for down-regulation of signaling via transmembrane receptors and removal of misfolded or defective membrane proteins. This process is also utilised by several viruses (e.g. HIV-1) to facilitate budding of their virions from the cell-membrane. Studies in animals and fungi have shown that it depends on an intricate series of interactions, which is initiated via ubiquitination (typically one or more mono-ubiquitinations) of the cytoplasmic tails of membrane proteins by specific E3 ligases. Ubiquitinated membrane proteins are then captured into endosomes by the ESCRT system and prevented from being recycled back to the plasma membrane via the retrograde trafficking system. The ESCRT system also folds the endosomal membranes into invaginations that are concentrated in these ubiquitinated targets and catalyzes their abscission into intra-luminal-vesicles inside the endosome. This largely seals the fate of these membrane proteins as targets for lysosomal degradation. The ESCRT system is comprised of 4 major protein complexes, ESCRT-0 to ESCRT-III, which are successively involved in the above-described steps [].ESCRT-I contains three subunits that are conserved between yeast and animals, namely the inactive E2-ligase protein TSG101/VPS23, VPS28 and VPS37. Additionally, both yeast and metazoan ESCRT-I contain a fourth subunit termed MVB12 (multivesicular body sorting factor of 12 kD); however, the MVB12 subunits from the two lineages do not show significant sequence similarity. The metazoan MVB12 proteins contain two distinct conserved domains that occur independently in various proteins. The N-terminal region of MVB12 forms the MVB12-associated β-prism (MABP), which is also found in DENND4A/B/C from vertebrates, the membrane trafficking regulator Crag from Drosophila, bacterial proteins typified by the MAC/perforin (MACPF)-like protein plu1415 from Photorhabdus luminescens and uncharacterised proteins from choanoflagellates and stamenopiles. It has been suggested that the MABP domain has a membrane-associated function, perhaps even specific interactions with membrane components. It is plausible that the eukaryotic MABP domains are adaptators that help linking other associated domains found in the same polypeptide to vesicular membranes [].The MABP domain has an internal repeat structure of three homologous segments. Consitent with this, the structurally characterised representative Photorhabdus plu1415, showed that this region precisely corresponds to a type-I β-prism domain with an internal three fold symetry. Each of the three sub-domains of the β-prism structure is a distinctive three-stranded β-sheet. The MABP domain shares a triradial symmetry with β-sheets parallel to the prism axis. The β-prism fold is associated with membrane interaction. The majority of the eukaryotic MABP domain versions contain a conserved cysteine in the first and third subdomain of the β-prism [, ].
Protein
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: false
Publication
First Author: de Souza RF
Year: 2010
Journal: Bioinformatics
Title: UMA and MABP domains throw light on receptor endocytosis and selection of endosomal cargoes.
Volume: 26
Issue: 12
Pages: 1477-80
Protein
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
Publication
First Author: Rosado CJ
Year: 2007
Journal: Science
Title: A common fold mediates vertebrate defense and bacterial attack.
Volume: 317
Issue: 5844
Pages: 1548-51
Protein
Organism: Mus musculus/domesticus
Length: 1499  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1906  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1615  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1869  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1354  
Fragment?: false