sorting nexin family protein [Saccharomyces cerevisiae S288C]
Protein Classification
PX and BAR domain-containing protein( domain architecture ID 10246345)
PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| BAR_SNX | cd07596 | The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
361-580 | 4.22e-40 | ||||
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. : Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 145.58 E-value: 4.22e-40
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| PX_domain super family | cl02563 | The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
136-243 | 1.77e-12 | ||||
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting. The actual alignment was detected with superfamily member cd06861: Pssm-ID: 470617 Cd Length: 112 Bit Score: 63.91 E-value: 1.77e-12
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| Name | Accession | Description | Interval | E-value | ||||
| BAR_SNX | cd07596 | The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
361-580 | 4.22e-40 | ||||
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 145.58 E-value: 4.22e-40
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| Vps5 | pfam09325 | Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
351-579 | 9.70e-16 | ||||
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain. Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 76.94 E-value: 9.70e-16
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| PX_Vps5p | cd06861 | The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ... |
136-243 | 1.77e-12 | ||||
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; 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. Vsp5p 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 Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p 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. Pssm-ID: 132771 Cd Length: 112 Bit Score: 63.91 E-value: 1.77e-12
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| PX | smart00312 | PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
121-241 | 2.48e-11 | ||||
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform. Pssm-ID: 214610 Cd Length: 105 Bit Score: 60.44 E-value: 2.48e-11
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| PX | pfam00787 | PX domain; PX domains bind to phosphoinositides. |
139-243 | 3.07e-09 | ||||
PX domain; PX domains bind to phosphoinositides. Pssm-ID: 459940 Cd Length: 84 Bit Score: 53.78 E-value: 3.07e-09
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| Name | Accession | Description | Interval | E-value | ||||
| BAR_SNX | cd07596 | The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
361-580 | 4.22e-40 | ||||
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. 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. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 145.58 E-value: 4.22e-40
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| BAR_Vps5p | cd07627 | The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ... |
378-552 | 2.13e-18 | ||||
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. 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. Vsp5p 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 Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. Pssm-ID: 153311 [Multi-domain] Cd Length: 216 Bit Score: 84.28 E-value: 2.13e-18
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| Vps5 | pfam09325 | Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ... |
351-579 | 9.70e-16 | ||||
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain. Pssm-ID: 430527 [Multi-domain] Cd Length: 236 Bit Score: 76.94 E-value: 9.70e-16
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| PX_Vps5p | cd06861 | The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ... |
136-243 | 1.77e-12 | ||||
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; 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. Vsp5p 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 Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p 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. Pssm-ID: 132771 Cd Length: 112 Bit Score: 63.91 E-value: 1.77e-12
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| PX | smart00312 | PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
121-241 | 2.48e-11 | ||||
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform. Pssm-ID: 214610 Cd Length: 105 Bit Score: 60.44 E-value: 2.48e-11
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| PX | pfam00787 | PX domain; PX domains bind to phosphoinositides. |
139-243 | 3.07e-09 | ||||
PX domain; PX domains bind to phosphoinositides. Pssm-ID: 459940 Cd Length: 84 Bit Score: 53.78 E-value: 3.07e-09
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| PX_SNX1_2_like | cd06859 | The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ... |
146-239 | 5.39e-09 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; 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. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor 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 and SNX2 are 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 effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Pssm-ID: 132769 [Multi-domain] Cd Length: 114 Bit Score: 54.12 E-value: 5.39e-09
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| PX_domain | cd06093 | The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
136-188 | 4.28e-05 | ||||
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting. Pssm-ID: 132768 [Multi-domain] Cd Length: 106 Bit Score: 42.73 E-value: 4.28e-05
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