Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
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•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
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•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
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•
•
•
•
•
|
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 |
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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 []. |
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•
•
•
•
•
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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. |
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GO Term |
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•
•
•
•
•
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GO Term |
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•
•
•
•
•
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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 |
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•
•
•
•
•
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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. |
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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 |
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•
•
•
•
•
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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 [, , ]. |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
40
 |
Fragment?: |
false |
|
•
•
•
•
•
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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. |
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•
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•
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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 []. |
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HT Experiment |
Series Id: |
GSE14984 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
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•
•
•
•
•
|
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 |
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•
•
•
•
|
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 |
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•
•
•
•
•
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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 |
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•
•
•
•
•
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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 |
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•
•
•
•
•
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Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
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•
•
•
•
|
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 |
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•
•
•
•
•
|
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 |
|
•
•
•
•
•
|