Type |
Details |
Score |
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: |
The Gene Ontology Consortium |
Year: |
2010 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs |
|
|
|
|
•
•
•
•
•
|
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: |
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: |
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 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 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: |
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 Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
391
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
Abnormal regulation of TSG101 in mice with spongiform neurodegeneration. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
462
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
430
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
451
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
The TSG101 protein binds to connexins and is involved in connexin degradation. |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 4389, Kay-Uwe Wagner |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, transgenic |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(Wap-Tsg101)4389Kuw/? |
Background: |
FVB/N-Tg(Wap-Tsg101)4389Kuw |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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 []. |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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 []. |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
139
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
148
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
66
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
145
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
73
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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 []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
253
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
391
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
391
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
471
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
474
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
492
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
507
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
474
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
397
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
516
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
462
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
457
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
492
|
Fragment?: |
false |
|
•
•
•
•
•
|