sorting nexin-25 isoform 1 [Mus musculus]
Protein Classification
PX domain-containing protein( domain architecture ID 10490416)
PX (Phox Homology) domain-containing protein with PXA (PX associated) and nexin C-terminal domains, may bind phosphoinositides; with similarity to sorting nexin-14 but lacking the regulator of G protein signaling (RGS) domain
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PX_SNX25 | cd06878 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ... |
648-770 | 7.64e-60 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. : Pssm-ID: 132788 Cd Length: 127 Bit Score: 200.29 E-value: 7.64e-60
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| RGS super family | cl02565 | Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ... |
437-545 | 1.40e-48 | ||||
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision. The actual alignment was detected with superfamily member cd08720: Pssm-ID: 470619 Cd Length: 110 Bit Score: 167.59 E-value: 1.40e-48
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| Nexin_C | pfam08628 | Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ... |
847-950 | 2.69e-37 | ||||
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787. : Pssm-ID: 462541 Cd Length: 111 Bit Score: 135.43 E-value: 2.69e-37
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| PXA | pfam02194 | PXA domain; This domain is associated with PX domains pfam00787. |
148-303 | 7.75e-25 | ||||
PXA domain; This domain is associated with PX domains pfam00787. : Pssm-ID: 460484 Cd Length: 181 Bit Score: 102.31 E-value: 7.75e-25
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| Name | Accession | Description | Interval | E-value | ||||
| PX_SNX25 | cd06878 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ... |
648-770 | 7.64e-60 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. Pssm-ID: 132788 Cd Length: 127 Bit Score: 200.29 E-value: 7.64e-60
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| RGS_SNX25 | cd08720 | Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 25 (SNX25) protein; ... |
437-545 | 1.40e-48 | ||||
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 25 (SNX25) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX25 (Sorting Nexin 25) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX25 is a member of the Dopamine receptors (DAR) signalplex and regulates the trafficking of D1 and D2 DARs. Pssm-ID: 188675 Cd Length: 110 Bit Score: 167.59 E-value: 1.40e-48
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| Nexin_C | pfam08628 | Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ... |
847-950 | 2.69e-37 | ||||
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787. Pssm-ID: 462541 Cd Length: 111 Bit Score: 135.43 E-value: 2.69e-37
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| PXA | pfam02194 | PXA domain; This domain is associated with PX domains pfam00787. |
148-303 | 7.75e-25 | ||||
PXA domain; This domain is associated with PX domains pfam00787. Pssm-ID: 460484 Cd Length: 181 Bit Score: 102.31 E-value: 7.75e-25
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| RGS | pfam00615 | Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ... |
434-546 | 5.05e-21 | ||||
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Pssm-ID: 459870 Cd Length: 117 Bit Score: 89.21 E-value: 5.05e-21
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| PXA | smart00313 | Domain associated with PX domains; unpubl. observations |
147-303 | 5.02e-17 | ||||
Domain associated with PX domains; unpubl. observations Pssm-ID: 214611 Cd Length: 176 Bit Score: 79.77 E-value: 5.02e-17
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| PX | pfam00787 | PX domain; PX domains bind to phosphoinositides. |
691-770 | 2.86e-13 | ||||
PX domain; PX domains bind to phosphoinositides. Pssm-ID: 459940 Cd Length: 84 Bit Score: 66.11 E-value: 2.86e-13
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| RGS | smart00315 | Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ... |
434-546 | 4.10e-12 | ||||
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Pssm-ID: 214613 Cd Length: 118 Bit Score: 63.83 E-value: 4.10e-12
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| PX | smart00312 | PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
688-768 | 8.85e-10 | ||||
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: 56.97 E-value: 8.85e-10
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| Name | Accession | Description | Interval | E-value | ||||
| PX_SNX25 | cd06878 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ... |
648-770 | 7.64e-60 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. Pssm-ID: 132788 Cd Length: 127 Bit Score: 200.29 E-value: 7.64e-60
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| RGS_SNX25 | cd08720 | Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 25 (SNX25) protein; ... |
437-545 | 1.40e-48 | ||||
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 25 (SNX25) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX25 (Sorting Nexin 25) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. SNX25 is a member of the Dopamine receptors (DAR) signalplex and regulates the trafficking of D1 and D2 DARs. Pssm-ID: 188675 Cd Length: 110 Bit Score: 167.59 E-value: 1.40e-48
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| Nexin_C | pfam08628 | Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ... |
847-950 | 2.69e-37 | ||||
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787. Pssm-ID: 462541 Cd Length: 111 Bit Score: 135.43 E-value: 2.69e-37
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| PXA | pfam02194 | PXA domain; This domain is associated with PX domains pfam00787. |
148-303 | 7.75e-25 | ||||
PXA domain; This domain is associated with PX domains pfam00787. Pssm-ID: 460484 Cd Length: 181 Bit Score: 102.31 E-value: 7.75e-25
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| RGS | pfam00615 | Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ... |
434-546 | 5.05e-21 | ||||
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Pssm-ID: 459870 Cd Length: 117 Bit Score: 89.21 E-value: 5.05e-21
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| PX_SNX14 | cd06877 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ... |
656-769 | 1.43e-17 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; 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. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. Pssm-ID: 132787 Cd Length: 119 Bit Score: 79.34 E-value: 1.43e-17
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| PXA | smart00313 | Domain associated with PX domains; unpubl. observations |
147-303 | 5.02e-17 | ||||
Domain associated with PX domains; unpubl. observations Pssm-ID: 214611 Cd Length: 176 Bit Score: 79.77 E-value: 5.02e-17
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| PX_domain | cd06093 | The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
658-768 | 2.87e-15 | ||||
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: 72.39 E-value: 2.87e-15
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| PX_SNX13 | cd06873 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ... |
658-769 | 1.46e-13 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; 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. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome. Pssm-ID: 132783 Cd Length: 120 Bit Score: 68.06 E-value: 1.46e-13
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| PX | pfam00787 | PX domain; PX domains bind to phosphoinositides. |
691-770 | 2.86e-13 | ||||
PX domain; PX domains bind to phosphoinositides. Pssm-ID: 459940 Cd Length: 84 Bit Score: 66.11 E-value: 2.86e-13
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| PX_MDM1p | cd06876 | The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ... |
657-768 | 3.97e-12 | ||||
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. 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. Pssm-ID: 132786 Cd Length: 133 Bit Score: 64.25 E-value: 3.97e-12
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| RGS | smart00315 | Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ... |
434-546 | 4.10e-12 | ||||
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Pssm-ID: 214613 Cd Length: 118 Bit Score: 63.83 E-value: 4.10e-12
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| PX | smart00312 | PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
688-768 | 8.85e-10 | ||||
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: 56.97 E-value: 8.85e-10
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| RGS | cd07440 | Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ... |
438-545 | 3.47e-09 | ||||
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision. Pssm-ID: 188659 [Multi-domain] Cd Length: 113 Bit Score: 55.48 E-value: 3.47e-09
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| PX_SNARE | cd06897 | The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ... |
676-768 | 3.49e-08 | ||||
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. Pssm-ID: 132807 Cd Length: 108 Bit Score: 52.27 E-value: 3.49e-08
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| RGS_RGS11 | cd08740 | Regulator of G protein signaling (RGS) domain found in the RGS11 protein; The RGS (Regulator ... |
434-547 | 1.39e-07 | ||||
Regulator of G protein signaling (RGS) domain found in the RGS11 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS11 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS9, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS11 is expressed exclusively in retinal ON-bipolar neurons in which it forms complexes with G-beta-5 and R7AP (RGS7 anchor protein ) and plays crucial roles in processing the light responses of retinal neurons. Pssm-ID: 188694 Cd Length: 126 Bit Score: 51.07 E-value: 1.39e-07
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| PX_SNX19_like_plant | cd06872 | The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ... |
657-768 | 8.14e-07 | ||||
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. Pssm-ID: 132782 Cd Length: 107 Bit Score: 48.29 E-value: 8.14e-07
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| PX_PI3K_C2 | cd06883 | The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ... |
695-770 | 3.32e-06 | ||||
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins. Pssm-ID: 132793 Cd Length: 109 Bit Score: 46.58 E-value: 3.32e-06
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| PX_CISK | cd06870 | The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ... |
688-767 | 1.05e-05 | ||||
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity. Pssm-ID: 132780 Cd Length: 109 Bit Score: 45.48 E-value: 1.05e-05
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| PX_SNX19 | cd06893 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ... |
690-768 | 1.44e-05 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; 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. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors. Pssm-ID: 132803 [Multi-domain] Cd Length: 132 Bit Score: 45.61 E-value: 1.44e-05
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| RGS_RGS6 | cd08737 | Regulator of G protein signaling (RGS) domain found in the RGS6 protein; The RGS (Regulator of ... |
434-547 | 1.69e-05 | ||||
Regulator of G protein signaling (RGS) domain found in the RGS6 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS6 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). Other members of the R7 subfamily (Neuronal RGS) include: RGS7, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS6 exists in multiple splice isoforms with identical RGS domains, but possess complete or incomplete GGL domains and distinct N- and C-terminal domains. RGS6 interacts with SCG10, a neuronal growth-associated protein and therefore regulates neuronal differentiation. Another RGS6-binding protein is DMAP1, a component of the Dnmt1 complex involved in repression of newly replicated genes. Mutations of a critical residue required for interaction of RGS6 protein with G proteins did not affect the ability of RGS6 to interact with both SCG10 and DMAP1. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Pssm-ID: 188691 Cd Length: 125 Bit Score: 45.39 E-value: 1.69e-05
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| RGS_RGS7 | cd08738 | Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of ... |
435-545 | 3.15e-05 | ||||
Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways. Pssm-ID: 188692 Cd Length: 121 Bit Score: 44.32 E-value: 3.15e-05
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| PX_IRAS | cd06875 | The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ... |
668-753 | 3.82e-05 | ||||
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. 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. 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. Pssm-ID: 132785 Cd Length: 116 Bit Score: 43.81 E-value: 3.82e-05
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| PX_Bem1p | cd06890 | The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a ... |
691-770 | 4.06e-05 | ||||
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of Bem1p specifically binds phosphatidylinositol-4-phosphate (PI4P). Pssm-ID: 132800 Cd Length: 112 Bit Score: 43.82 E-value: 4.06e-05
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| PX_KIF16B_SNX23 | cd06874 | The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ... |
693-794 | 4.32e-05 | ||||
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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. Pssm-ID: 132784 Cd Length: 127 Bit Score: 43.91 E-value: 4.32e-05
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| PX_SNX1 | cd07281 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ... |
667-767 | 8.40e-05 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; 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. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component 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. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. Pssm-ID: 132814 Cd Length: 124 Bit Score: 43.12 E-value: 8.40e-05
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| PX_SNX16 | cd07276 | The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ... |
657-767 | 1.69e-04 | ||||
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; 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. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking. Pssm-ID: 132809 Cd Length: 110 Bit Score: 42.01 E-value: 1.69e-04
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| RGS_R7-like | cd08705 | Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins; The RGS ... |
432-543 | 2.51e-04 | ||||
Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins; The RGS (Regulator of G-protein Signaling) domain is an essential part of the R7 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R7 subfamily includes RGS6, RGS7, RGS9, and RGS11, all of which, in humans, are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes. In addition, R7 proteins were found to bind many other proteins outside of the G protein signaling pathways including: m-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, guanylyl cyclase, among others. Pssm-ID: 188660 Cd Length: 121 Bit Score: 41.84 E-value: 2.51e-04
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| PX_RUN | cd07277 | The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ... |
675-752 | 2.58e-04 | ||||
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways. Pssm-ID: 132810 Cd Length: 118 Bit Score: 41.56 E-value: 2.58e-04
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| PX_MONaKA | cd06871 | The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ... |
658-769 | 6.54e-04 | ||||
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes. Pssm-ID: 132781 Cd Length: 120 Bit Score: 40.42 E-value: 6.54e-04
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| RGS_AKAP2_2 | cd08721 | Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, ... |
442-545 | 8.10e-04 | ||||
Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, D-AKAP2; The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring protein), a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the second RGS domain. Pssm-ID: 188676 Cd Length: 121 Bit Score: 40.41 E-value: 8.10e-04
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| PX_YPT35 | cd07280 | The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ... |
697-769 | 1.11e-03 | ||||
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway. Pssm-ID: 132813 Cd Length: 120 Bit Score: 40.00 E-value: 1.11e-03
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| PX_UP2_fungi | cd06869 | The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ... |
695-768 | 1.96e-03 | ||||
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. Pssm-ID: 132779 Cd Length: 119 Bit Score: 39.19 E-value: 1.96e-03
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| RGS_Axin | cd08707 | Regulator of G protein signaling (RGS) domain found in the Axin protein; The RGS (Regulator of ... |
447-543 | 2.47e-03 | ||||
Regulator of G protein signaling (RGS) domain found in the Axin protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the Axin protein. Axin is a member of the RA/RGS subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, and skeletal and muscle development. The RGS domain of Axin is specifically interacts with the heterotrimeric G-alpha12 protein, but not with closely related G-alpha13, and provides a unique tool to regulate G-alpha12-mediated signaling processes. The RGS domain of Axin also interacts with the tumor suppressor protein APC (Adenomatous Polyposis Coli) in order to control the cytoplasmic level of the proto-oncogene, beta-catenin. Pssm-ID: 188662 Cd Length: 117 Bit Score: 38.60 E-value: 2.47e-03
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| RGS_RGS9 | cd08739 | Regulator of G protein signaling (RGS) domain found in the RGS9 protein; The RGS (Regulator of ... |
432-489 | 3.22e-03 | ||||
Regulator of G protein signaling (RGS) domain found in the RGS9 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS9 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS9 forms constitutive complexes with G-beta-5 subunit and controls such fundamental functions as vision and behavior. RGS9 exists in two splice isoforms: RGS9-1 which regulates phototransduction in rods and cones and RGS9-2 which regulates dopamine and opioid signaling in the basal ganglia. In addition, RGS9 was found to bind many other proteins outside of G protein signaling pathways including: mu-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, and guanylyl cyclase, among others. Pssm-ID: 188693 Cd Length: 121 Bit Score: 38.47 E-value: 3.22e-03
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| RGS_SNX13 | cd08719 | Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein; ... |
447-545 | 5.79e-03 | ||||
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX13 (Sorting Nexin 13) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. The RGS-domain of SNX13 plays a major role through attenuation of Galphas-mediated signaling and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. Snx13-null mice were embryonic lethal around midgestation which supports an essential role for SNX13 in mouse development and regulation of endocytosis dynamics. Pssm-ID: 188674 Cd Length: 135 Bit Score: 38.16 E-value: 5.79e-03
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