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Search results 1 to 88 out of 88 for Vps28

0.023s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Gene
51160 | VPS28
Type: gene
Organism: human
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Gene
112531894 | VPS28
Type: gene
Organism: chicken
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Gene
300052 | Vps28
Type: gene
Organism: rat
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Gene
464463 | VPS28
Type: gene
Organism: chimpanzee
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Gene
393562 | vps28
Type: gene
Organism: zebrafish
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Gene
607677 | VPS28
Type: gene
Organism: dog, domestic
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Gene
618785 | VPS28
Type: gene
Organism: cattle
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Gene
702412 | VPS28
Type: gene
Organism: macaque, rhesus
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Gene
549068 | vps28
Type: gene
Organism: frog, western clawed
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Protein Domain
IPR007143 | Vps28
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 [, ].
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Protein Coding Gene
MGI:1914164 | Vps28
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9D1C8
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
A0A2R8VKS6
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Protein
Q8BMZ7
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Publication
16615894 | -
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
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Publication
16615893 | -
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
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Protein Coding Gene
MGI_C57BL6J_1914164 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
- | J:76622
   
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
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Publication
14557248 | J:273504
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
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Publication
11591653 | J:103507
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
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Publication
- | J:165963
     
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
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Publication
- | J:68100
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: RIKEN Data Curation in Mouse Genome Informatics
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Publication
- | J:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:81858
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: Data Curation Using Mouse Genome Assembly
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Publication
- | J:155845
     
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
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Publication
18799693 | J:142754
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
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:342604
       
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
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
16602821 | J:162220
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
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Publication
11217851 | J:65060
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
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Publication
14610273 | J:86696
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
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
21677750 | J:173534
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
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Publication
- | J:141210
     
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
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Publication
- | J:342587
       
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
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
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
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
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
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
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).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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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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Publication
11134028 | J:218006
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
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Publication
29960043 | J:270733
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
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Publication
33249983 | J:338229
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
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Protein
E0CXP6
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
A0A1L1SRH2
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Protein
E0CX23
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
F6W646
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
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Protein
Q8C234
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
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Protein
B7ZWJ7
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
Q3TQY7
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein Domain
IPR023340 | UMA
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 [].
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Protein Domain
IPR023341 | MABP
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 [, ].
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Protein
Q6KAU4
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Protein
Q78HU3
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
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Protein
Q8BT99
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: false
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Protein
Q8C2W4
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: false
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Publication
20448139 | -
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
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Protein
A0A1D5RM52
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
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Protein
A2ARF0
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
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Protein
A0A1D5RLP2
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: false
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Protein
G3UW59
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
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Protein
Q8BH48
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
F6WHE1
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
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Protein
Q3TYW8
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
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Protein
Q3TZ11
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
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Publication
17717151 | -
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
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Protein
Q3U1Y4
Organism: Mus musculus/domesticus
Length: 1499  
Fragment?: false
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Protein
A6H8H2
Organism: Mus musculus/domesticus
Length: 1906  
Fragment?: false
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Protein
A0A0R4J172
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
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Protein
E9Q449
Organism: Mus musculus/domesticus
Length: 1615  
Fragment?: false
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Protein
E9Q8V6
Organism: Mus musculus/domesticus
Length: 1869  
Fragment?: false
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Protein
B9EKY0
Organism: Mus musculus/domesticus
Length: 1354  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom