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Search results 101 to 155 out of 155 for Snx1

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Type Details Score
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
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
GXD Expression
Probe: MGI:7541025
Assay Type: Immunohistochemistry
Annotation Date: 2023-10-18
Strength: Present
Sex: Not Specified
Emaps: EMAPS:381337
Pattern: Not Specified
Stage: TS07
Assay Id: MGI:7541123
Age: embryonic day 5.5
Image: 3e/f
Note: Coexpressed with Snx1 in the early endocytic compartments in the subapical cytoplasm. Less expression in the apical vacuoles (Lamp2+).
Specimen Label: 3e/f
Detected: true
Specimen Num: 3
Protein Domain
Type: Family
Description: Sorting nexin-2 (SNX2) belongs to the sorting nexin family, which contains a conserved PX (phox homology) domain that is responsible for binding to specific phosphoinositides []. SNX1 and SNX2 are orthologues of yeast Vps5, which is a component of retromercomplex that is essential in endosome-to-Golgi retrograde transport []. The mammalian retromer complex is composed of the SNX1/2 alternative heterodimer or homodimer and the a Vps26-Vps29-Vps35 obligate heterotrimer []. Like SNX1, SNX2 also has an additional C-terminal BAR domain. SNX1 and SNX2 play interchangeable but essential roles in retromer structure and function [].
Protein Domain
Type: Domain
Description: Sorting nexin-2 (SNX2) belongs to the sorting nexin family, which contains a conserved PX (phox homology) domain that is responsible for binding to specific phosphoinositides []. SNX1 and SNX2 are orthologues of yeast Vps5, which is a component of retromer complex that is essential in endosome-to-Golgi retrograde transport []. The mammalian retromer complex is composed of the SNX1/2 alternative heterodimer or homodimer and the a Vps26-Vps29-Vps35 obligate heterotrimer []. Like SNX1, SNX2 also has an additional C-terminal BAR domain. SNX1 and SNX2 play interchangeable but essential roles in retromer structure and function [].This entry represents the PX domain of SNX2.
GO Term
GO Term
Publication  
First Author: Vergés M
Year: 2008
Journal: Int Rev Cell Mol Biol
Title: Retromer: multipurpose sorting and specialization in polarized transport.
Volume: 271
Pages: 153-98
Protein Domain
Type: Domain
Description: The Phox Homology (PX) domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds phosphoinositides (PIs) and targets the protein to PI-enriched membranes [, ]. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway [, , ].SNX1 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1 []. SNX1 is components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi []. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex [].This entry represents the SNX1 PX domain.
Publication
First Author: Horazdovsky BF
Year: 1997
Journal: Mol Biol Cell
Title: A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor.
Volume: 8
Issue: 8
Pages: 1529-41
Protein Domain
Type: Domain
Description: Sorting nexins (SNXs) are Phox homology (PX) domain-containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains []. The PX-BAR structural unit determines the specific membrane targeting of SNXs [].Vsp5 is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10, as well as other later-Golgi proteins [, , ].
Protein
Organism: Mus musculus/domesticus
Length: 40  
Fragment?: false
Protein Domain
Type: Domain
Description: Sorting nexins (SNXs) are hydrophilic molecules that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domains () or through protein-protein interactions with membrane-associated protein complexes []. Indeed, several of the SNXs require several targeting motifs for their appropriate cellular localization. In almost every case studied, mammalian SNXs can be shown to have a role in protein sorting, with the most commonly used experimental model being plasma-membrane receptor endocytosis and sorting through the endosomal pathway. However, it is equally probable that SNXs sort vesicles that are not derived from the plasma membrane, and have a function in the accurate targeting of these vesicles and their cargo. The N-terminal domain appears to be specific to sorting nexins 1 and 2. SNX1 and SNX2 are members of the retromer complex involved in protein sorting within the endocytic pathway []. SNX1 is both membrane-associated and cytosolic, where it probably exists as a tetramer in large protein complexes and may hetero-oligomerize with SNX2.
Protein Domain
Type: Domain
Description: The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system [, ]. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway [, , ].Vsp5 is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5 binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1 [].
HT Experiment
Series Id: GSE14984
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
Publication  
First Author: Follett J
Year: 2019
Journal: Neurosci Lett
Title: DNAJC13 p.Asn855Ser, implicated in familial parkinsonism, alters membrane dynamics of sorting nexin 1.
Volume: 706
Pages: 114-122
Publication
First Author: Koliwer J
Year: 2015
Journal: J Biol Chem
Title: The golgi-associated PDZ domain protein PIST/GOPC stabilizes the β1-adrenergic receptor in intracellular compartments after internalization.
Volume: 290
Issue: 10
Pages: 6120-9
Publication
First Author: Nielsen MS
Year: 2007
Journal: Mol Cell Biol
Title: Sorting by the cytoplasmic domain of the amyloid precursor protein binding receptor SorLA.
Volume: 27
Issue: 19
Pages: 6842-51
Publication
First Author: Ding F
Year: 2010
Journal: PLoS One
Title: Neonatal maternal deprivation response and developmental changes in gene expression revealed by hypothalamic gene expression profiling in mice.
Volume: 5
Issue: 2
Pages: e9402
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Seaman MN
Year: 2002
Journal: Mol Biol Cell
Title: Identification of the functional domains of yeast sorting nexins Vps5p and Vps17p.
Volume: 13
Issue: 8
Pages: 2826-40
Publication
First Author: Teasdale RD
Year: 2012
Journal: Biochem J
Title: Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease.
Volume: 441
Issue: 1
Pages: 39-59
Protein
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Carlton J
Year: 2005
Journal: Traffic
Title: Sorting nexins--unifying trends and new perspectives.
Volume: 6
Issue: 2
Pages: 75-82
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Mas C
Year: 2014
Journal: J Biol Chem
Title: Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.
Volume: 289
Issue: 41
Pages: 28554-68
Publication
First Author: Cullen PJ
Year: 2011
Journal: Nat Cell Biol
Title: Sorting nexins provide diversity for retromer-dependent trafficking events.
Volume: 14
Issue: 1
Pages: 29-37
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Seaman MN
Year: 1998
Journal: J Cell Biol
Title: A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast.
Volume: 142
Issue: 3
Pages: 665-81
Publication
First Author: Worby CA
Year: 2002
Journal: Nat Rev Mol Cell Biol
Title: Sorting out the cellular functions of sorting nexins.
Volume: 3
Issue: 12
Pages: 919-31
Publication
First Author: Seet LF
Year: 2006
Journal: Biochim Biophys Acta
Title: The Phox (PX) domain proteins and membrane traffic.
Volume: 1761
Issue: 8
Pages: 878-96
Publication
First Author: Wishart MJ
Year: 2001
Journal: Cell
Title: Phoxy lipids: revealing PX domains as phosphoinositide binding modules.
Volume: 105
Issue: 7
Pages: 817-20
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory