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EPH receptor B2

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(Redirected from EphB2) Protein-coding gene in the species Homo sapiens
EPHB2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1B4F, 1F0M, 2QBX, 3ZFM

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
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for EPHB2Genomic location for EPHB2
Band1p36.12Start22,710,839 bp
End22,921,500 bp
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)
Chromosome 4 (mouse)Genomic location for EPHB2Genomic location for EPHB2
Band4 D3|4 69.0 cMStart136,374,850 bp
End136,563,299 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • ventricular zone

  • rectum

  • mucosa of transverse colon

  • cartilage tissue

  • mucosa of sigmoid colon

  • buccal mucosa cell

  • tendon of biceps brachii

  • duodenum

  • islet of Langerhans
Top expressed in
  • Rostral migratory stream

  • internal carotid artery

  • crypt of lieberkuhn of small intestine

  • tail of embryo

  • ventricular zone

  • genital tubercle

  • external carotid artery

  • Paneth cell

  • ganglionic eminence

  • efferent ductule
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2048

13844

Ensembl

ENSG00000133216

ENSMUSG00000028664

UniProt

P29323

P54763

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
Wikidata
View/Edit HumanView/Edit Mouse

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

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 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.

Animal studies

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

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

Interactions

EPH receptor B2 has been shown to interact with:

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000133216Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000028664Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. "Entrez Gene: EPHB2 EPH receptor B2".
  7. 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. Bibcode:2011Natur.469...47C. doi:10.1038/nature09635. PMC 3030448. PMID 21113149.
  8. 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. 339 (6123): 1063–7. Bibcode:2013Sci...339.1063S. doi:10.1126/science.1230422. PMC 3778192. PMID 23371554.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
PDB gallery
  • 1b4f: OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN 1b4f: OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN
  • 1f0m: MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN 1f0m: MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN
  • 1jpa: Crystal Structure of unphosphorylated EphB2 receptor tyrosine kinase and juxtamembrane region 1jpa: Crystal Structure of unphosphorylated EphB2 receptor tyrosine kinase and juxtamembrane region
  • 1kgy: Crystal Structure of the EphB2-ephrinB2 complex 1kgy: Crystal Structure of the EphB2-ephrinB2 complex
  • 1nuk: CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE 1nuk: CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE
  • 1sgg: THE SOLUTION STRUCTURE OF SAM DOMAIN FROM THE RECEPTOR TYROSINE KINASE EPHB2, NMR, 10 STRUCTURES 1sgg: THE SOLUTION STRUCTURE OF SAM DOMAIN FROM THE RECEPTOR TYROSINE KINASE EPHB2, NMR, 10 STRUCTURES
  • 1shw: EphB2 / EphrinA5 Complex Structure 1shw: EphB2 / EphrinA5 Complex Structure
  • 2hen: Crystal Structure of the EphB2 Receptor Kinase domain in complex with ADP 2hen: Crystal Structure of the EphB2 Receptor Kinase domain in complex with ADP
Protein kinases: tyrosine kinases (EC 2.7.10)
Receptor tyrosine kinases (EC 2.7.10.1)
Growth factor receptors
EGF receptor family
Insulin receptor family
PDGF receptor family
FGF receptor family
VEGF receptors family
HGF receptor family
Trk receptor family
EPH receptor family
LTK receptor family
TIE receptor family
ROR receptor family
DDR receptor family
PTK7 receptor family
RYK receptor family
MuSK receptor family
ROS receptor family
AATYK receptor family
AXL receptor family
RET receptor family
uncategorised
Non-receptor tyrosine kinases (EC 2.7.10.2)
ABL family
ACK family
CSK family
FAK family
FES family
FRK family
JAK family
SRC-A family
SRC-B family
TEC family
SYK family
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:
Growth factor receptor modulators
Angiopoietin
CNTF
EGF (ErbB)
EGF
(ErbB1/HER1)
ErbB2/HER2
  • Agonists: Unknown/none
ErbB3/HER3
ErbB4/HER4
FGF
FGFR1
FGFR2
FGFR3
FGFR4
Unsorted
HGF (c-Met)
IGF
IGF-1
IGF-2
Others
LNGF (p75)
PDGF
RET (GFL)
GFRα1
GFRα2
GFRα3
GFRα4
Unsorted
SCF (c-Kit)
TGFβ
Trk
TrkA
  • Negative allosteric modulators: VM-902A
TrkB
TrkC
VEGF
Others
  • Additional growth factor receptor modulators: Cerebrolysin (neurotrophin mixture)

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


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