Contents

Search

Ephrin type-B receptor 2; tyrosine-protein kinase receptor EPH-3; DRT; receptor protein-tyrosine kinase HEK5; ERK; tyrosine-protein kinase TYRO5; renal carcinoma antigen NY-REN-47 (EPHB2; DRT; EPHT3; EPTH3; ERK; HEK5; TYRO5)

Function: - receptor for members of the ephrin-B family - acts as a tumor suppressor - ligand-activated form interacts with multiple proteins, including GTPase-activating protein (RASGAP) through its SH2 domain - binds RASGAP through the juxtamembrane Tyr - interacts with PRKCABP & GRIP1 (putative) - ligand (ephrin B2) binding of the ephB2 receptor in the postsynaptic membrane leads to binding of a src family protein to the ephB2 receptor, activation of src & phosphorylation of the NR2B subunit of the NMDA receptor at 3 phospho-Tyr sites; this in turn leads to an increase in Ca+2 permeability of the NMDA receptor; through this mechanism, the ephB2 receptor may be involved in synaptic plasticity [2] - EphB2 receptors may also induce clustering of NMDA receptors Structure: - belongs to the protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily - contains 2 fibronectin F3 modules - contains 1 protein kinase domain - contains 1 SAM (sterile alpha motif) domain Compartment: membrane Alternative splicing: named isoforms=3 Expression: - expressed in brain, heart, lung, kidney, placenta, pancreas, liver & skeletal muscle - preferentially expressed in fetal brain Pathology: - defects in EPHB2 a) progression of prostate cancer b) prostate cancer metastasis to the brain

General

ephB receptor glycoprotein

Properties

SIZE: entity length = 1055 aa MW = 117 kD COMPARTMENT: cellular membrane STATE: active state MOTIF: signal sequence {1-18} cysteine-rich region {184-324} MOTIF: N-glycosylation site {N265} fibronectin type III domain or F3 module {325-426} MOTIF: N-glycosylation site {N336} N-glycosylation site {N428} fibronectin type III domain or F3 module {432-527} MOTIF: N-glycosylation site {N482} transmembrane domain {544-564} kinase domain SITE: 621-884 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 627-635 ATP-binding site NAME: ATP-binding site SITE: 653-653 aspartate residue {D746} Thr phosphorylation site {T775} Ser phosphorylation site {S776} sterile alpha motif NAME: sterile alpha motif SITE: 913-977 PDZ recognition motif NAME: PDZ recognition motif SITE: 984-986 FOR-BINDING-VIA: PDZ domain

Database Correlations

OMIM correlations MORBIDMAP 600997 UniProt P29323 PFAM correlations Entrez Gene 2048 Kegg hsa:2048 ENZYME 2.7.10.1

References

  1. Eph Nomenclature Committee. Cell 90:403-4 1997
  2. Ghosh A. Neurobiology. Learning more about NMDA receptor regulation. Science. 2002 Jan 18;295(5554):449-51. No abstract available. PMID: 11799227
  3. UniProt :accession P29323