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ephrin-B2 isoform 3 precursor [Homo sapiens]
Ephrin-B_Ectodomain domain-containing protein( domain architecture ID 10179620)
Ephrin-B_Ectodomain domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
Ephrin-B_Ectodomain | cd10426 | Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ... |
29-165 | 8.74e-103 | |||
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model. : Pssm-ID: 259897 Cd Length: 137 Bit Score: 296.28 E-value: 8.74e-103
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Name | Accession | Description | Interval | E-value | |||
Ephrin-B_Ectodomain | cd10426 | Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ... |
29-165 | 8.74e-103 | |||
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model. Pssm-ID: 259897 Cd Length: 137 Bit Score: 296.28 E-value: 8.74e-103
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Ephrin | pfam00812 | Ephrin; |
27-164 | 2.06e-73 | |||
Ephrin; Pssm-ID: 459947 Cd Length: 139 Bit Score: 221.78 E-value: 2.06e-73
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Name | Accession | Description | Interval | E-value | |||
Ephrin-B_Ectodomain | cd10426 | Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ... |
29-165 | 8.74e-103 | |||
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model. Pssm-ID: 259897 Cd Length: 137 Bit Score: 296.28 E-value: 8.74e-103
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Ephrin | pfam00812 | Ephrin; |
27-164 | 2.06e-73 | |||
Ephrin; Pssm-ID: 459947 Cd Length: 139 Bit Score: 221.78 E-value: 2.06e-73
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Ephrin_ectodomain | cd02675 | Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ... |
30-165 | 3.84e-67 | |||
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrins contain a highly conserved ectodomain for receptor binding, which is characterized by this domain hierarchy. Pssm-ID: 259861 Cd Length: 136 Bit Score: 205.60 E-value: 3.84e-67
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Ephrin-A_Ectodomain | cd10425 | Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ... |
32-138 | 9.51e-27 | |||
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors. Pssm-ID: 259896 Cd Length: 130 Bit Score: 101.62 E-value: 9.51e-27
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