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FYN-binding protein 1 isoform X3 [Mus musculus]
FYN-binding protein 1( domain architecture ID 10983874)
FYN-binding protein 1 acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
hSH3 | pfam14603 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
739-827 | 8.47e-54 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. : Pssm-ID: 464216 Cd Length: 89 Bit Score: 180.95 E-value: 8.47e-54
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hSH3 super family | cl48258 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
496-591 | 4.63e-08 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. The actual alignment was detected with superfamily member pfam14603: Pssm-ID: 464216 Cd Length: 89 Bit Score: 51.14 E-value: 4.63e-08
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Name | Accession | Description | Interval | E-value | |||
hSH3 | pfam14603 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
739-827 | 8.47e-54 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. Pssm-ID: 464216 Cd Length: 89 Bit Score: 180.95 E-value: 8.47e-54
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hSH3_ADAP | cd11867 | Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
738-809 | 7.16e-38 | |||
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides. Pssm-ID: 212801 Cd Length: 77 Bit Score: 135.73 E-value: 7.16e-38
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hSH3 | pfam14603 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
496-591 | 4.63e-08 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. Pssm-ID: 464216 Cd Length: 89 Bit Score: 51.14 E-value: 4.63e-08
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SH3 | smart00326 | Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
500-556 | 2.40e-06 | |||
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations. Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 45.22 E-value: 2.40e-06
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SH3_Cortactin_like | cd11819 | Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ... |
503-557 | 5.22e-04 | |||
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212753 [Multi-domain] Cd Length: 54 Bit Score: 38.45 E-value: 5.22e-04
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Name | Accession | Description | Interval | E-value | |||
hSH3 | pfam14603 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
739-827 | 8.47e-54 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. Pssm-ID: 464216 Cd Length: 89 Bit Score: 180.95 E-value: 8.47e-54
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hSH3_ADAP | cd11867 | Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
738-809 | 7.16e-38 | |||
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides. Pssm-ID: 212801 Cd Length: 77 Bit Score: 135.73 E-value: 7.16e-38
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hSH3 | pfam14603 | Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
496-591 | 4.63e-08 | |||
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown. Pssm-ID: 464216 Cd Length: 89 Bit Score: 51.14 E-value: 4.63e-08
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SH3 | smart00326 | Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
500-556 | 2.40e-06 | |||
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations. Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 45.22 E-value: 2.40e-06
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SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
503-558 | 3.04e-06 | |||
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel. Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 44.89 E-value: 3.04e-06
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SH3_Cortactin_like | cd11819 | Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ... |
503-557 | 5.22e-04 | |||
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212753 [Multi-domain] Cd Length: 54 Bit Score: 38.45 E-value: 5.22e-04
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SH3 | cd00174 | Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
503-550 | 8.06e-04 | |||
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction. Pssm-ID: 212690 [Multi-domain] Cd Length: 51 Bit Score: 37.83 E-value: 8.06e-04
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SH3_SNX9_like | cd11763 | Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ... |
514-557 | 9.12e-04 | |||
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; 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. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212697 [Multi-domain] Cd Length: 55 Bit Score: 38.08 E-value: 9.12e-04
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SH3_Nck_3 | cd11767 | Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ... |
516-557 | 1.40e-03 | |||
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase. Pssm-ID: 212701 [Multi-domain] Cd Length: 56 Bit Score: 37.68 E-value: 1.40e-03
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SH3_SNX9 | cd11898 | Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a ... |
513-557 | 6.89e-03 | |||
Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX9 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212831 Cd Length: 57 Bit Score: 35.61 E-value: 6.89e-03
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SH3_Pex13p_fungal | cd11771 | Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ... |
514-557 | 7.46e-03 | |||
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212705 [Multi-domain] Cd Length: 60 Bit Score: 35.71 E-value: 7.46e-03
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Blast search parameters | ||||
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