EPH receptor B2

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

Ephrin type-B receptor 2 is a protein that in humans is encoded by the EPHB2 gene.[5]

PDBOrtholog search: PDBe RCSB
AliasesEPHB2, Ephb2, Cek5, Drt, ETECK, Erk, Hek5, Nuk, Prkm5, Qek5, Sek3, Tyro5, CAPB, EK5, EPHT3, PCBC, EPH receptor B2, DRT, ERK, BDPLT22
Quick facts EPHB2, Available structures ...
EPHB2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEPHB2, Ephb2, Cek5, Drt, ETECK, Erk, Hek5, Nuk, Prkm5, Qek5, Sek3, Tyro5, CAPB, EK5, EPHT3, PCBC, EPH receptor B2, DRT, ERK, BDPLT22
External IDsOMIM: 600997; MGI: 99611; HomoloGene: 37925; GeneCards: EPHB2; OMA:EPHB2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001309192
NM_001309193
NM_004442
NM_017449

NM_001290753
NM_010142

RefSeq (protein)

NP_001296121
NP_001296122
NP_004433
NP_059145

NP_001277682
NP_034272

Location (UCSC)Chr 1: 22.71 – 22.92 MbChr 4: 136.37 – 136.56 Mb
PubMed search[3][4]
Wikidata
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Function

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 two 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.[6]

Animal studies

EphB2 is part of the NMDA signaling pathway and restoring expression rescues cognitive function in an animal model of Alzheimer's disease.[7]

A recessive EphB2 gene is responsible for the crested-feather mutation in pigeons.[8]

Interactions

EPH receptor B2 has been shown to interact with:

References

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