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Search results 201 to 281 out of 281 for Tsg101

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Type Details Score
Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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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: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: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: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: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
- | 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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Protein
Q61187
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein Domain
IPR022008 | EABR
Type: Domain
Description: This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.
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Publication
12559917 | J:81924
First Author: Timmins J
Year: 2003
Journal: J Mol Biol
Title: Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4.
Volume: 326
Issue: 2
Pages: 493-502
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Publication
30884248 | J:291999
First Author: Essandoh K
Year: 2019
Journal: FASEB J
Title: Tsg101 positively regulates physiologic-like cardiac hypertrophy through FIP3-mediated endosomal recycling of IGF-1R.
Volume: 33
Issue: 6
Pages: 7451-7466
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Publication
9465061 | J:46158
First Author: Xie W
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: Cell cycle-dependent subcellular localization of the TSG101 protein and mitotic and nuclear abnormalities associated with TSG101 deficiency.
Volume: 95
Issue: 4
Pages: 1595-600
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Publication
17940959 | J:219096
 
First Author: Silvestri LS
Year: 2007
Journal: J Infect Dis
Title: Involvement of vacuolar protein sorting pathway in Ebola virus release independent of TSG101 interaction.
Volume: 196 Suppl 2
Pages: S264-70
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Publication
9241264 | J:42049
First Author: Koonin EV
Year: 1997
Journal: Nat Genet
Title: TSG101 may be the prototype of a class of dominant negative ubiquitin regulators.
Volume: 16
Issue: 4
Pages: 330-1
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Interaction Experiment
Jiao J (2009)
Description: Abnormal regulation of TSG101 in mice with spongiform neurodegeneration.
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Protein
Q8BT07
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q99JG7
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q80VZ7
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
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Publication
16552148 | -
First Author: Palencia A
Year: 2006
Journal: Acta Crystallogr D Biol Crystallogr
Title: Structure of human TSG101 UEV domain.
Volume: 62
Issue: Pt 4
Pages: 458-64
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Publication
12006492 | -
First Author: Pornillos O
Year: 2002
Journal: EMBO J
Title: Structure and functional interactions of the Tsg101 UEV domain.
Volume: 21
Issue: 10
Pages: 2397-406
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Interaction Experiment
Auth T (2009)
Description: The TSG101 protein binds to connexins and is involved in connexin degradation.
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Publication
12525615 | -
First Author: Licata JM
Year: 2003
Journal: J Virol
Title: Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4.
Volume: 77
Issue: 3
Pages: 1812-9
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Publication
17229889 | -
First Author: Kim BY
Year: 2007
Journal: Mol Biol Cell
Title: Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates TSG101 and regulates endosomal trafficking.
Volume: 18
Issue: 4
Pages: 1129-42
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Allele
Tg(Wap-Tsg101)4389Kuw | MGI:3710126
Name: transgene insertion 4389, Kay-Uwe Wagner
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Publication
15908698 | -
First Author: Segura-Morales C
Year: 2005
Journal: J Biol Chem
Title: Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding.
Volume: 280
Issue: 29
Pages: 27004-12
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Strain
MGI:3710659 | FVB/N-Tg(Wap-Tsg101)4389Kuw
Attribute String: coisogenic, mutant strain, targeted mutation
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Strain
MGI:4430730 | FVB/N-Tg(Wap-Tsg101)4389Kuw/Mmmh
Attribute String: coisogenic, mutant strain, transgenic
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Genotype
Genotype
Symbol: Tg(Wap-Tsg101)4389Kuw/?
Background: FVB/N-Tg(Wap-Tsg101)4389Kuw
Zygosity: ot
Has Mutant Allele: true
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Publication
16234236 | -
First Author: Fossen T
Year: 2005
Journal: J Biol Chem
Title: Solution structure of the human immunodeficiency virus type 1 p6 protein.
Volume: 280
Issue: 52
Pages: 42515-27
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Protein Domain
IPR014817 | Gag_p6
Type: Domain
Description: HIV protein p6 contains two late-budding domains (L domains) which are short sequence motifs essential for viral particle release. p6 interacts with the endosomal sorting complex and represents a docking site for several cellular and binding factors []. The PTAP motif interacts with the cellular budding factor TSG101 []. This domain is also found in some chimpanzee immunodeficiency virus (SIV-cpz) proteins.
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Genotype
Genotype
Symbol: Tsg101/Tsg101 Tg(Wap-cre)11738Mam/? Tg(Wap-Tsg101)4389Kuw/?
Background: involves: 129S1/Sv * 129X1/SvJ * C57BL/6 * FVB/N * SJL
Zygosity: cn
Has Mutant Allele: true
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Publication
23166352 | J:195246
First Author: Lee SM
Year: 2012
Journal: J Cell Biol
Title: Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking.
Volume: 199
Issue: 5
Pages: 799-816
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Publication
27882925 | J:243067
 
First Author: Villarroya-Beltri C
Year: 2016
Journal: Nat Commun
Title: ISGylation controls exosome secretion by promoting lysosomal degradation of MVB proteins.
Volume: 7
Pages: 13588
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Publication
12900395 | J:224742
First Author: Bache KG
Year: 2003
Journal: J Cell Biol
Title: Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes.
Volume: 162
Issue: 3
Pages: 435-42
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Publication
10944105 | -
First Author: Dessen A
Year: 2000
Journal: EMBO J
Title: Crystal structure of the matrix protein VP40 from Ebola virus.
Volume: 19
Issue: 16
Pages: 4228-36
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Protein Domain
IPR038057 | EV_matrix_sf
Type: Homologous_superfamily
Description: Ebola virus sp. are non-segmented, negative-strand RNA viruses that causes severe haemorrhagic fever in humans with high rates of mortality. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins associate with cellular membranes, interact with the cytoplasmic tails of glycoproteins, and bind to the ribonucleoprotein complex. The VP40 monomer consists of two domains, the N-terminal oligomerization domain and the C-terminal membrane-binding domain, connected by a flexible linker. Both the N- and C-terminal domains fold into beta sandwich structures of similar topology []. Within the N-terminal domain are two overlapping L-domains with the sequences PTAP and PPEY at residues 7 to13, which are required for efficient budding []. L-domains are thought to mediate their function in budding through their interaction with specific host cellular proteins, such as tsg101 and vps-4 []. This entry represents the N- and C-terminal domains of the VP40 matrix protein.
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Protein Domain
IPR035092 | EV_matrix_protein_C
Type: Homologous_superfamily
Description: Ebola virus sp. are non-segmented, negative-strand RNA viruses that causes severe haemorrhagic fever in humans with high rates of mortality. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins associate with cellular membranes, interact with the cytoplasmic tails of glycoproteins, and bind to the ribonucleoprotein complex. The VP40 monomer consists of two domains, the N-terminal oligomerization domain and the C-terminal membrane-binding domain, connected by a flexible linker. Both the N- and C-terminal domains fold into beta sandwich structures of similar topology []. Within the N-terminal domain are two overlapping L-domains with the sequences PTAP and PPEY at residues 7 to13, which are required for efficient budding []. L-domains are thought to mediate their function in budding through their interaction with specific host cellular proteins, such as tsg101 and vps-4 []. This entry describes the VP40 C-terminal domain.
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Protein Domain
IPR008986 | EV_matrix
Type: Family
Description: Ebola virus sp. are non-segmented, negative-strand RNA viruses that causes severe haemorrhagic fever in humans with high rates of mortality. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins associate with cellular membranes, interact with the cytoplasmic tails of glycoproteins, and bind to the ribonucleoprotein complex. The VP40 monomer consists of two domains, the N-terminal oligomerization domain and the C-terminal membrane-binding domain, connected by a flexible linker. Both the N- and C-terminal domains fold into beta sandwich structures of similar topology []. Within the N-terminal domain are two overlapping L-domains with the sequences PTAP and PPEY at residues 7 to13, which are required for efficient budding []. L-domains are thought to mediate their function in budding through their interaction with specific host cellular proteins, such as tsg101 and vps-4 [].
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Publication
20176808 | J:161709
First Author: Iwamori T
Year: 2010
Journal: Mol Cell Biol
Title: TEX14 interacts with CEP55 to block cell abscission.
Volume: 30
Issue: 9
Pages: 2280-92
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Publication
35017633 | J:318737
First Author: Nørgård MØ
Year: 2022
Journal: Sci Rep
Title: A new transgene mouse model using an extravesicular EGFP tag enables affinity isolation of cell-specific extracellular vesicles.
Volume: 12
Issue: 1
Pages: 496
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Publication
32084266 | J:288249
First Author: Mighty J
Year: 2020
Journal: Invest Ophthalmol Vis Sci
Title: Analysis of Adult Neural Retina Extracellular Vesicle Release, RNA Transport and Proteomic Cargo.
Volume: 61
Issue: 2
Pages: 30
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Publication
33262120 | J:306295
First Author: Yan C
Year: 2021
Journal: Diabetes
Title: A High-Fat Diet Attenuates AMPK α1 in Adipocytes to Induce Exosome Shedding and Nonalcoholic Fatty Liver Development In Vivo.
Volume: 70
Issue: 2
Pages: 577-588
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Publication
36918692 | J:340857
First Author: Kuchitsu Y
Year: 2023
Journal: Nat Cell Biol
Title: STING signalling is terminated through ESCRT-dependent microautophagy of vesicles originating from recycling endosomes.
Volume: 25
Issue: 3
Pages: 453-466
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Publication
9253709 | -
First Author: Ponting CP
Year: 1997
Journal: J Mol Med (Berl)
Title: The breast cancer gene product TSG101: a regulator of ubiquitination?
Volume: 75
Issue: 7
Pages: 467-9
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Protein Domain
IPR043079 | EV_matrix_protein_N
Type: Homologous_superfamily
Description: Ebola virus sp. are non-segmented, negative-strand RNA viruses that causes severe haemorrhagic fever in humans with high rates of mortality. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins associate with cellular membranes, interact with the cytoplasmic tails of glycoproteins, and bind to the ribonucleoprotein complex. The VP40 monomer consists of two domains, the N-terminal oligomerization domain and the C-terminal membrane-binding domain, connected by a flexible linker. Both the N- and C-terminal domains fold into beta sandwich structures of similar topology []. Within the N-terminal domain are two overlapping L-domains with the sequences PTAP and PPEY at residues 7 to13, which are required for efficient budding []. L-domains are thought to mediate their function in budding through their interaction with specific host cellular proteins, such as tsg101 and vps-4 []. This entry describes the VP40 N-terminal domain. It is the region of the protein where the two VP40 monomers bind.
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Protein Domain
IPR008883 | UEV_N
Type: Domain
Description: The N-terminal ubiquitin E2 variant (UEV) domain is ~145 amino acid residues in length and shows significant sequence similarity to E2 ubiquitin ligases but is unable to catalyze ubiquitin transfer as it lacks the active site cysteine that forms the transient thioester bond with the C terminus of ubiquitin (Ub). Nevertheless, at least some UEVs have retained the ability to bind Ub, and appear to act either as cofactors in ubiquitylation reactions, or as ubiquitin sensors. UEV domains also frequently contain other protein recognition motifs, and may generally serve to couple protein and Ub binding functions to facilitate the formation of multiprotein complexes [, , , ]. The UEV domain consists of a twisted four-stranded antiparallel β-sheet having a meander topology, with four α-helices packed against one face of the sheet. The UEV fold is generally similar to canonical E2 ligases in the hydrophobic core and 'active site' regions, but differs significantly at both its N- and C-termini [, ]. The UEV domain is found in the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other Homo sapiens malignancies. However, the involvement of this gene in neoplastic transformation and tumourigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but this gene is not a tumour suppressor for sporadic forms of breast cancer [].
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Publication
22025668 | J:191540
First Author: Street JM
Year: 2011
Journal: J Physiol
Title: Exosomal transmission of functional aquaporin 2 in kidney cortical collecting duct cells.
Volume: 589
Issue: Pt 24
Pages: 6119-27
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Publication
27169926 | J:251175
First Author: Diaz-Hidalgo L
Year: 2016
Journal: Biochim Biophys Acta
Title: Transglutaminase type 2-dependent selective recruitment of proteins into exosomes under stressful cellular conditions.
Volume: 1863
Issue: 8
Pages: 2084-92
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Protein
D3Z2V5
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: true
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Protein
A0A1B0GS10
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
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Protein
A0A1B0GRX2
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
D3Z0S9
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
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Protein
A0A1B0GSG9
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: false
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Publication
15044434 | -
First Author: Teo H
Year: 2004
Journal: J Biol Chem
Title: Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins.
Volume: 279
Issue: 27
Pages: 28689-96
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Publication
15611048 | -
First Author: Puertollano R
Year: 2005
Journal: J Biol Chem
Title: Interactions of TOM1L1 with the multivesicular body sorting machinery.
Volume: 280
Issue: 10
Pages: 9258-64
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Publication
14563850 | J:148073
First Author: Yamakami M
Year: 2003
Journal: J Biol Chem
Title: Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin.
Volume: 278
Issue: 52
Pages: 52865-72
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Publication
15056867 | -
First Author: Yamakami M
Year: 2004
Journal: Biol Pharm Bull
Title: Tom1 (target of Myb 1) is a novel negative regulator of interleukin-1- and tumor necrosis factor-induced signaling pathways.
Volume: 27
Issue: 4
Pages: 564-6
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Protein Domain
IPR014645 | TOM1
Type: Family
Description: Tom1 (target of Myb 1) and its related proteins (Tom1L1 and Tom1L2) constitute a protein family and share an N-terminal VHS (Vps27p/Hrs/Stam) domain followed by a GAT (GGA and Tom1) domain.VHS domains are found at the N termini of select proteins involved in intracellular membrane trafficking and are often localized to membranes. The three dimensional structure of human TOM1 VHS domain reveals eight helices arranged in a superhelix. The surface of the domain has two main features: (1) a basic patch on one side due to several conserved positively charged residues on helix 3 and (2) a negatively charged ridge on the opposite side, formed by residues on helix 2 []. The basic patch is thought to mediate membrane binding.It was demonstrated that the GAT domain of both Tom1 and Tom1L1 binds ubiquitin, suggesting that these proteins might participate in the sorting of ubiquitinated proteins into multivesicular bodies (MVB) []. Moreover, Tom1L1 interacts with members of the MVB sorting machinery. Specifically, the VHS domain of Tom1L1 interacts with Hrs (hepatocyte growth factor-regulated tyrosine kinase substrate), whereas a PTAP motif, located between the VHS and GAT domains of Tom1L1, is responsible for binding to TSG101 (tumour susceptibility gene 101). Myc epitope-tagged Tom1L1 is recruited to endosomes following Hrs expression. In addition, Tom1L1 possesses several tyrosine motifs at the C-terminal region that mediate interactions with members of the Src family kinases and other signalling proteins such as Grb2 and p85. Expression of a constitutively active form of Fyn kinase promotes the recruitment of Tom1L1 to enlarged endosomes. It is proposed that Tom1L1 could act as an intermediary between the signalling and degradative pathways [].Over expression of Tom1 suppresses activation of the transcription factors NF-kappaB and AP-1, induced by either IL-1beta or tumour necrosis factor (TNF)-alpha, and the VHS domain of Tom1 is indispensable for this suppressive activity. This suggests that Tom1 is a common negative regulator of signalling pathways induced by IL-1beta and TNF-alpha [].
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Protein
A0A1B0GS09
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: true
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Protein
Q3UCW0
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
Q3UK08
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
Q3U1V6
Organism: Mus musculus/domesticus
Length: 471  
Fragment?: false
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Publication
10985773 | -
First Author: Misra S
Year: 2000
Journal: Biochemistry
Title: Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes.
Volume: 39
Issue: 37
Pages: 11282-90
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Protein
Q923U0
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
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Protein
O88746
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
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Protein
Q5SRX1
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
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Protein
Q7TNI6
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
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Protein
Q8BZR6
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
Q3UDC3
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: false
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Protein
Q5SXA4
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q5SXA5
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
Q561M4
Organism: Mus musculus/domesticus
Length: 492  
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