|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 200 out of 216 for Vapb

<< First    < Previous  |  Next >    Last >>
0.032s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
•
•
•
•
•
Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
•
•
•
•
•
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
•
•
•
•
•
Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
•
•
•
•
•
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
•
•
•
•
•
Publication
23771029 | J:202148
First Author: Aliaga L
Year: 2013
Journal: Hum Mol Genet
Title: Amyotrophic lateral sclerosis-related VAPB P56S mutation differentially affects the function and survival of corticospinal and spinal motor neurons.
Volume: 22
Issue: 21
Pages: 4293-305
•
•
•
•
•
Transgene
MGI:5544192 | Tg(Thy1-VAPB*P56S,-EGFP)D3Cai
Type: transgene
Organism: mouse, laboratory
•
•
•
•
•
Publication
18555774 | J:139754
First Author: Tsuda H
Year: 2008
Journal: Cell
Title: The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors.
Volume: 133
Issue: 6
Pages: 963-77
•
•
•
•
•
Protein Domain
IPR019239 | VapB_antitoxin
Type: Family
Description: VapB is the antitoxin of a bacterial toxin-antitoxin gene pair. The cognate toxin is VapC (). The family contains several related antitoxins from Cyanobacteria and Actinobacterial families. Antitoxins of this class carry an N-terminal ribbon-helix-helix domain, RHH, that is highly conserved across all type II bacterial antitoxins, which dimerises with the RHH domain of a second VapB molecule. A hinge section follows the RHH, with an additional pair of flexible alpha helices at the C terminus. This C terminus is the Toxin-binding region of the dimer, and so is specific to the cognate toxin, whereas the RHH domain has the specific function of lying across the RNA-binding groove of the toxin dimer and inactivating the active-site - a more general function of all antitoxins [, ].
•
•
•
•
•
Genotype
Genotype
Symbol: Tg(Thy1-VAPB*P56S,-EGFP)D3Cai/?
Background: C57BL/6-Tg(Thy1-VAPB*P56S,-EGFP)D3Cai
Zygosity: ot
Has Mutant Allele: true
•
•
•
•
•
Publication
20011113 | -
First Author: Ramage HR
Year: 2009
Journal: PLoS Genet
Title: Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution.
Volume: 5
Issue: 12
Pages: e1000767
•
•
•
•
•
DO Term
DOID:0050752 | amyotrophic lateral sclerosis type 8
•
•
•
•
•
Interaction Experiment
Tsuda H (2008)
Description: The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors.
•
•
•
•
•
Interaction Experiment
Kirmiz M (2018)
Description: Identification of VAPA and VAPB as Kv2 Channel-Interacting Proteins Defining Endoplasmic Reticulum-Plasma Membrane Junctions in Mammalian Brain Neurons.
•
•
•
•
•
Publication
18606735 | -
First Author: Letek M
Year: 2008
Journal: J Bacteriol
Title: Evolution of the Rhodococcus equi vap pathogenicity island seen through comparison of host-associated vapA and vapB virulence plasmids.
Volume: 190
Issue: 17
Pages: 5797-805
•
•
•
•
•
Publication
15718296 | -
First Author: Pandey DP
Year: 2005
Journal: Nucleic Acids Res
Title: Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes.
Volume: 33
Issue: 3
Pages: 966-76
•
•
•
•
•
Allele
Vapb<Gt(OST284921)Lex> | MGI:5085882
Name: vesicle-associated membrane protein, associated protein B and C; gene trap OST284921, Lexicon Genetics
Allele Type: Gene trapped
Attribute String: Null/knockout, Reporter
•
•
•
•
•
DO Term
DOID:0111194 | autosomal dominant adult-onset proximal spinal muscular atrophy
•
•
•
•
•
Publication
19445953 | -
First Author: Robson J
Year: 2009
Journal: J Mol Biol
Title: The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation.
Volume: 390
Issue: 3
Pages: 353-67
•
•
•
•
•
Publication
25047537 | -
First Author: Lopes AP
Year: 2014
Journal: PLoS One
Title: VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.
Volume: 9
Issue: 7
Pages: e101678
•
•
•
•
•
Protein Domain
IPR011660 | VapB-like
Type: Family
Description: This entry includes a group of antitoxins, including vapB from Mycobacterium smegmatis. VapB is an antitoxin component of a type II toxin-antitoxin (TA) module that controls growth via inhibition of translation [, ].
•
•
•
•
•
Strain
MGI:5560801 | B6;129S5-Vapb<Gt(OST284921)Lex>/Mmucd
Attribute String: mutant stock, targeted mutation
•
•
•
•
•
Genotype
Genotype
Symbol: Vapb/Vapb
Background: involves: 129S5/SvEvBrd * C57BL/6J
Zygosity: hm
Has Mutant Allele: true
•
•
•
•
•
Strain
MGI:5544438 | C57BL/6-Tg(Thy1-VAPB*P56S,-EGFP)D3Cai
Attribute String: coisogenic, mutant strain, transgenic
•
•
•
•
•
Protein
Q3V4A2
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
•
•
•
•
•
Publication
18468439 | -
First Author: Lev S
Year: 2008
Journal: Trends Cell Biol
Title: The VAP protein family: from cellular functions to motor neuron disease.
Volume: 18
Issue: 6
Pages: 282-90
•
•
•
•
•
Publication
19207211 | -
First Author: Saravanan RS
Year: 2009
Journal: Plant J
Title: The targeting of the oxysterol-binding protein ORP3a to the endoplasmic reticulum relies on the plant VAP33 homolog PVA12.
Volume: 58
Issue: 5
Pages: 817-30
•
•
•
•
•
Publication
15668246 | -
First Author: Loewen CJ
Year: 2005
Journal: J Biol Chem
Title: A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins.
Volume: 280
Issue: 14
Pages: 14097-104
•
•
•
•
•
Protein Domain
IPR016763 | VAP
Type: Family
Description: This entry represents a family of vesicle-associated membrane-protein-associated proteins (VAPs) and plant VAP homologs (PVAPs) []. VAPs (VAPA and VAPB in humans, VAPA, VAPB and VAPC in other mammals []) are endoplasmic reticulum (ER) proteins that play roles in vesicle trafficking, neurotransmitter release, microtubule organisation, lipid transport and unfolded protein response []. VAP proteins contain an MSP domain in their N-terminal half, which has been shown to interact with proteins containing a FFAT motif, such as members of the oxysterol-binding protein (OSBP) family or the phosphatidylinositol transfer proteins from the PITPNM family []. Yeast VAP homologues are known as Scs2 and Scs22 [].
•
•
•
•
•
Protein
F6V527
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: true
•
•
•
•
•
Protein Domain
IPR002716 | PIN_dom
Type: Domain
Description: PIN domains are small protein domains identified by the presence of three strictly conserved acidic residues. Apart from these three residues, there is poor sequence conservation []. PIN domains are found in eukaryotes, eubacteria and archaea. In eukaryotes they are ribonucleases involved in nonsense mediated mRNA decay []and in processing of 18S ribosomal RNA []. In prokaryotes, they are the toxic components of toxin-antitoxin (TA) systems, their toxicity arising by virtue of their ribonuclease activity. The PIN domain TA systems are now called VapBC TAs(virulence associated proteins), where VapB is the inhibitor and VapC, the PIN-domain ribonuclease toxin [].
•
•
•
•
•
Protein
Q9DBQ9
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: false
•
•
•
•
•
Publication
30741620 | J:313400
First Author: Mao D
Year: 2019
Journal: Autophagy
Title: VAMP associated proteins are required for autophagic and lysosomal degradation by promoting a PtdIns4P-mediated endosomal pathway.
Volume: 15
Issue: 7
Pages: 1214-1233
•
•
•
•
•
Publication
31594866 | J:283057
First Author: Kirmiz M
Year: 2019
Journal: J Biol Chem
Title: Neuronal ER-plasma membrane junctions organized by Kv2-VAP pairing recruit Nir proteins and affect phosphoinositide homeostasis.
Volume: 294
Issue: 47
Pages: 17735-17757
•
•
•
•
•
Publication
27418313 | J:236016
First Author: Stoica R
Year: 2016
Journal: EMBO Rep
Title: ALS/FTD-associated FUS activates GSK-3β to disrupt the VAPB-PTPIP51 interaction and ER-mitochondria associations.
Volume: 17
Issue: 9
Pages: 1326-42
•
•
•
•
•
Protein
Q6A0A9
Organism: Mus musculus/domesticus
Length: 1112  
Fragment?: false
•
•
•
•
•
Protein
Q6RI63
Organism: Mus musculus/domesticus
Length: 786  
Fragment?: false
•
•
•
•
•
Protein
A0A087WNN6
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: false
•
•
•
•
•
Publication
17053788 | -
First Author: Glavan F
Year: 2006
Journal: EMBO J
Title: Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex.
Volume: 25
Issue: 21
Pages: 5117-25
•
•
•
•
•
Publication
19706509 | -
First Author: Lamanna AC
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain.
Volume: 106
Issue: 34
Pages: 14259-64
•
•
•
•
•
Publication
25930206 | -
First Author: Derré I
Year: 2015
Journal: Cell Microbiol
Title: Chlamydiae interaction with the endoplasmic reticulum: contact, function and consequences.
Volume: 17
Issue: 7
Pages: 959-66
•
•
•
•
•
Protein Domain
IPR038296 | ParD_sf
Type: Homologous_superfamily
Description: ParD is the antitoxin of a bacterial toxin-antitoxin gene pair. The cognate toxin is ParE in . The superfamily contains several related antitoxins from Cyanobacteria, Proteobacteria and Actinobacteria. Antitoxins of this class carry an N-terminal ribbon-helix-helix domain, RHH, that is highly conserved across all type II bacterial antitoxins, which dimerises with the RHH domain of a second VapB molecule. A hinge section follows the RHH, with an additional pair of flexible alpha helices at the C terminus. This C terminus is the toxin-binding region of the dimer, and so is specific to the cognate toxin, whereas the RHH domain has the specific function of lying across the RNA-binding groove of the toxin dimer and inactivating the active-site - a more general function of all type II antitoxins [, , ].
•
•
•
•
•
Protein Domain
IPR022789 | ParD
Type: Family
Description: ParD is the antitoxin of a bacterial toxin-antitoxin gene pair. The cognate toxin is ParE in . The family contains several related antitoxins from Cyanobacteria, Proteobacteria and Actinobacteria. Antitoxins of this class carry an N-terminal ribbon-helix-helix domain, RHH, that is highly conserved across all type II bacterial antitoxins, which dimerises with the RHH domain of a second VapB molecule. A hinge section follows the RHH, with an additional pair of flexible alpha helices at the C terminus. This C terminus is the toxin-binding region of the dimer, and so is specific to the cognate toxin, whereas the RHH domain has the specific function of lying across the RNA-binding groove of the toxin dimer and inactivating the active-site - a more general function of all type II antitoxins [, , ].
•
•
•
•
•
Protein Domain
IPR029060 | PIN-like_dom_sf
Type: Homologous_superfamily
Description: This superfamily represents a domain sharing protein structural similarity with the PIN domain. This domain can also be found in the N-terminal of the 5'3'-exonuclease, which has a 3-layer α/β/α core structure and contains an α-helical arch [].PIN domains are small protein domains identified by the presence of three strictly conserved acidic residues. Apart from these three residues, there is poor sequence conservation []. PIN domains are found in eukaryotes, eubacteria and archaea. In eukaryotes they are ribonucleases involved in nonsense mediated mRNA decay []and in processing of 18S ribosomal RNA []. In prokaryotes, they are the toxic components of toxin-antitoxin (TA) systems, their toxicity arising by virtue of their ribonuclease activity. The PIN domain TA systems are now called VapBC TAs(virulence associated proteins), where VapB is the inhibitor and VapC, the PIN-domain ribonuclease toxin [].
•
•
•
•
•
Protein Domain
IPR035117 | IncD
Type: Family
Description: The chlamydial inclusion membrane is extensively modified by the insertion of type III secreted effector proteins []. These inclusion membrane proteins (Incs) have two major characteristics: an N-terminal type III secretion signal that is necessary for their secretion out of the bacterium and a hydrophobic region consisting of at least two trans-membrane helices that allows insertion into the inclusion membrane. Generally, both the N- and C-terminal regions of the Inc are exposed to the host cell cytosol [].This family has members such as the IncD proteins found in Chlamydia trachomatis. This C. trachomatis effector protein IncD has been shown to recruit the lipid transfer protein CERT to the inclusion membrane by directly interacting with CERT PH domain, which mediates the FFAT motif-dependent recruitment of the ER-resident protein VAPB (vesicle-associated membrane protein-associated protein) to the inclusion [].
•
•
•
•
•
Publication
9920726 | J:52046
First Author: Nishimura Y
Year: 1999
Journal: Biochem Biophys Res Commun
Title: Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins.
Volume: 254
Issue: 1
Pages: 21-6
•
•
•
•
•
Publication
20143871 | -
First Author: Dalton KM
Year: 2010
Journal: Biochemistry
Title: A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex.
Volume: 49
Issue: 10
Pages: 2205-15
•
•
•
•
•
Protein
Q9CTH6
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
•
•
•
•
•
Protein
E9Q186
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
•
•
•
•
•
Protein
E9PW56
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
•
•
•
•
•
Protein
Q8BW77
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: false
•
•
•
•
•
Protein
D3Z5Y3
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
•
•
•
•
•
Publication
20487277 | -
First Author: Fiebig A
Year: 2010
Journal: Mol Microbiol
Title: Interaction specificity, toxicity and regulation of a paralogous set of ParE/RelE-family toxin-antitoxin systems.
Volume: 77
Issue: 1
Pages: 236-51
•
•
•
•
•
Protein
Q8BIR2
Organism: Mus musculus/domesticus
Length: 672  
Fragment?: false
•
•
•
•
•
Protein
Q8C3F2
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
•
•
•
•
•
Protein
Q9CX11
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
•
•
•
•
•
Protein
B7ZW94
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
•
•
•
•
•
Protein
Q3V3X9
Organism: Mus musculus/domesticus
Length: 1000  
Fragment?: true
•
•
•
•
•
Protein
H3BLN7
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
•
•
•
•
•
Publication
21036780 | -
First Author: Arcus VL
Year: 2011
Journal: Protein Eng Des Sel
Title: The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array.
Volume: 24
Issue: 1-2
Pages: 33-40
•
•
•
•
•
Publication
18398909 | -
First Author: Bunker RD
Year: 2008
Journal: Proteins
Title: Crystal structure of PAE0151 from Pyrobaculum aerophilum, a PIN-domain (VapC) protein from a toxin-antitoxin operon.
Volume: 72
Issue: 1
Pages: 510-8
•
•
•
•
•
Protein Domain
IPR044153 | PIN_Pae0151-like
Type: Domain
Description: This PIN domain can be found in the Pyrobaculum aerophilum proteins, Pae0151 (also known as VapC3) and Pae2754 (also known as VapC9), and their homologues []. They are similar to the PIN domains of the Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB toxins of the prokaryotic toxin/antitoxin operons, VapBC and FitAB, respectively, which are believed to be involved in growth inhibition by regulating translation. These toxins are nearly always co-expressed with an antitoxin, a cognate protein inhibitor, forming an inert protein complex. Disassociation of the protein complex activates the ribonuclease activity of the toxin by an, as yet undefined mechanism [, ].PIN domains are small protein domains identified by the presence of three strictly conserved acidic residues. Apart from these three residues, there is poor sequence conservation []. PIN domains are found in eukaryotes, eubacteria and archaea. In eukaryotes they are ribonucleases involved in nonsense mediated mRNA decay []and in processing of 18S ribosomal RNA []. In prokaryotes, they are the toxic components of toxin-antitoxin (TA) systems, their toxicity arising by virtue of their ribonuclease activity. The PIN domain TA systems are now called VapBC TAs(virulence associated proteins), where VapB is the inhibitor and VapC, the PIN-domain ribonuclease toxin [].
•
•
•
•
•
Protein Domain
IPR033411 | Ribonuclease_PIN
Type: Domain
Description: This is a PIN domain found in eukaryotic ribonuclease Nob1 and archaeal ribonuclease VapC1 []. RNA-binding protein NOB1 has a nuclear location []and contains a PIN domain and binds a single zinc ion. Budding yeast Nob1 is involved in proteasomal and 40S ribosomal subunit biogenesis []. It is also required for maturation of the small subunit ribosomal RNA by catalyzing cleavage at site D after export of the preribosomal subunit into the cytoplasm. Nob1 is also found in archaea, where it is manganese-dependent and also processes RNA-substrates []. This domain can also be found in VapC1, which is a toxic component and a ribonuclease of a toxin-antitoxin (TA) module [].PIN domains are small protein domains identified by the presence of three strictly conserved acidic residues. Apart from these three residues, there is poor sequence conservation []. PIN domains are found in eukaryotes, eubacteria and archaea. In eukaryotes they are ribonucleases involved in nonsense mediated mRNA decay []and in processing of 18S ribosomal RNA []. In prokaryotes, they are the toxic components of toxin-antitoxin (TA) systems, their toxicity arising by virtue of their ribonuclease activity. The PIN domain TA systems are now called VapBC TAs(virulence associated proteins), where VapB is the inhibitor and VapC, the PIN-domain ribonuclease toxin [].
•
•
•
•
•
Protein
Q8BW10
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
•
•
•
•
•
Protein
Q9CSH3
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
•
•
•
•
•
Protein
Q148S3
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
•
•
•
•
•
Protein
A0A2I3BR78
Organism: Mus musculus/domesticus
Length: 566  
Fragment?: false
•
•
•
•
•
Protein
Q8R2P7
Organism: Mus musculus/domesticus
Length: 566  
Fragment?: false
•
•
•
•
•
Protein
F6YBB8
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: true
•
•
•
•
•
Publication
10675611 | -
First Author: Tone Y
Year: 2000
Journal: Gene
Title: Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells.
Volume: 243
Issue: 1-2
Pages: 37-45
•
•
•
•
•
Publication
22156373 | -
First Author: Veith T
Year: 2012
Journal: Nucleic Acids Res
Title: Structural and functional analysis of the archaeal endonuclease Nob1.
Volume: 40
Issue: 7
Pages: 3259-74
•
•
•
•
•
Publication
25391136 | -
First Author: Hamilton B
Year: 2014
Journal: PLoS One
Title: Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active site.
Volume: 9
Issue: 11
Pages: e112921
•
•
•
•
•
Publication
8657312 | -
First Author: Ceska TA
Year: 1996
Journal: Nature
Title: A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease.
Volume: 382
Issue: 6586
Pages: 90-3
•
•
•
•
•
Publication
16172919 | -
First Author: Zhang Y
Year: 2005
Journal: Mol Biol Rep
Title: Cloning, expression and characterization of the human NOB1 gene.
Volume: 32
Issue: 3
Pages: 185-9
•
•
•
•
•
Protein
P61406
Organism: Mus musculus/domesticus
Length: 1418  
Fragment?: false
•
•
•
•
•
Protein
Q8BGG6
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
•
•
•
•
•
Protein
Q9WV55
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
•
•
•
•
•
Protein
Q9QY76
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
•
•
•
•
•
Protein
Q9D8A4
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
•
•
•
•
•
Protein
Q8BVR1
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
•
•
•
•
•
Protein
Q05DT5
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
•
•
•
•
•
Protein
Q3TU78
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: true
•
•
•
•
•
Protein
D3Z1F3
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
•
•
•
•
•
Protein
A0A3B2W837
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
•
•
•
•
•
Protein
Q3TA54
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: true
•
•
•
•
•
Protein
Q8BH80
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
•
•
•
•
•
Protein
Q6ZPY2
Organism: Mus musculus/domesticus
Length: 1017  
Fragment?: false
•
•
•
•
•
Protein
Q3UZS1
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: false
•
•
•
•
•
Publication
23696825 | -
First Author: Mital J
Year: 2013
Journal: PLoS One
Title: Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis.
Volume: 8
Issue: 5
Pages: e63426
•
•
•
•
•
Publication
25717440 | -
 
First Author: Gauliard E
Year: 2015
Journal: Front Cell Infect Microbiol
Title: Characterization of interactions between inclusion membrane proteins from Chlamydia trachomatis.
Volume: 5
Pages: 13
•
•
•
•
•
Protein
A0A1W2P876
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P7L4
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P7J7
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
•
•
•
•
•
Protein
A0A0A6YX74
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
•
•
•
•
•
Protein
A0A1W2P6M6
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: true
•
•
•
•
•
Protein
P39749
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
•
•
•
•
•
Protein
Q9QZ11
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
•
•
•
•
•
Protein
P35689
Organism: Mus musculus/domesticus
Length: 1170  
Fragment?: false
•
•
•
•
•
Protein
Q8BMI4
Organism: Mus musculus/domesticus
Length: 908  
Fragment?: false
•
•
•
•
•
Protein
Q6P9Q0
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: true
•
•
•
•
•




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