EPH receptor B2

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EPH receptor B2
Protein EPHB2 PDB 1b4f.png
PDB rendering based on 1b4f.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EPHB2 ; CAPB; DRT; EK5; EPHT3; ERK; Hek5; PCBC; Tyro5
External IDs OMIM600997 MGI99611 HomoloGene37925 ChEMBL: 3290 GeneCards: EPHB2 Gene
EC number 2.7.10.1
RNA expression pattern
PBB GE EPHB2 209588 at tn.png
PBB GE EPHB2 209589 s at tn.png
PBB GE EPHB2 210651 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2048 13844
Ensembl ENSG00000133216 ENSMUSG00000028664
UniProt P29323 A3KG01
RefSeq (mRNA) NM_004442 NM_010142
RefSeq (protein) NP_004433 NP_034272
Location (UCSC) Chr 1:
23.04 – 23.24 Mb
Chr 4:
136.65 – 136.84 Mb
PubMed search [1] [2]

Ephrin type-B receptor 2 is a protein that in humans is encoded by the EPHB2 gene.[1]

Function[edit]

Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.[2]

Animal studies[edit]

EphB2 is part of the NMDA signaling pathway and restoring expression rescues cognitive function in an animal model of Alzheimer's disease.[3]

A recessive EphB2 gene is responsible for the crested-feather mutation in pigeons.[4]

Interactions[edit]

EPH receptor B2 has been shown to interact with Src,[5][6] RAS p21 protein activator 1[7] and the Abl gene.[8]

References[edit]

  1. ^ Chan J, Watt VM (August 1991). "eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases". Oncogene 6 (6): 1057–61. PMID 1648701. 
  2. ^ "Entrez Gene: EPHB2 EPH receptor B2". 
  3. ^ Cissé M, Halabisky B, Harris J, Devidze N, Dubal DB, Sun B, Orr A, Lotz G, Kim DH, Hamto P, Ho K, Yu GQ, Mucke L (January 2011). "Reversing EphB2 depletion rescues cognitive functions in Alzheimer model". Nature 469 (7328): 47–52. doi:10.1038/nature09635. PMC 3030448. PMID 21113149. Lay summaryNHS Choices. 
  4. ^ Shapiro MD, Kronenberg Z, Li C, Domyan ET, Pan H, Campbell M, Tan H, Huff CD, Hu H, Vickrey AI, Nielsen SC, Stringham SA, Hu H, Willerslev E, Gilbert MT, Yandell M, Zhang G, Wang J (January 2013). "Genomic Diversity and Evolution of the Head Crest in the Rock Pigeon". Science. doi:10.1126/science.1230422. PMID 23371554. Lay summaryNew York Times. 
  5. ^ Zisch AH, Kalo MS, Chong LD, Pasquale EB (May 1998). "Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region". Oncogene 16 (20): 2657–70. doi:10.1038/sj.onc.1201823. PMID 9632142. 
  6. ^ Zisch AH, Pazzagli C, Freeman AL, Schneller M, Hadman M, Smith JW, Ruoslahti E, Pasquale EB (January 2000). "Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses". Oncogene 19 (2): 177–87. doi:10.1038/sj.onc.1203304. PMID 10644995. 
  7. ^ Holland SJ, Gale NW, Gish GD, Roth RA, Songyang Z, Cantley LC, Henkemeyer M, Yancopoulos GD, Pawson T (July 1997). "Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells". EMBO J. 16 (13): 3877–88. doi:10.1093/emboj/16.13.3877. PMC 1170012. PMID 9233798. 
  8. ^ Yu HH, Zisch AH, Dodelet VC, Pasquale EB (July 2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor". Oncogene 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. PMID 11494128. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.