EPH receptor B2

EPHB2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1B4F, 1F0M, 2QBX, 3ZFM
Identifiers
Aliases	EPHB2, Ephb2, Cek5, Drt, ETECK, Erk, Hek5, Nuk, Prkm5, Qek5, Sek3, Tyro5, CAPB, EK5, EPHT3, PCBC, EPH receptor B2, DRT, ERK, BDPLT22
External IDs	OMIM: 600997 MGI: 99611 HomoloGene: 37925 GeneCards: EPHB2
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	22,921,500 bp[1]
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)[2]
End	136,563,299 bp[2]
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; rectum; ; duodenum; ; islet of Langerhans; ; cecum; ; appendix; ; pericardium; ; periodontal fiber; ; human penis; ; prefrontal cortex;
	Top expressed in
	internal carotid artery; ; crypt of lieberkuhn of small intestine; ; external carotid artery; ; Paneth cell; ; ganglionic eminence; ; maxillary prominence; ; abdominal wall; ; medial ganglionic eminence; ; vas deferens; ; left colon;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; transmembrane-ephrin receptor activity; kinase activity; protein binding; identical protein binding; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase activity; signaling receptor binding; ATP binding; axon guidance receptor activity; ephrin receptor activity; amyloid-beta binding; signaling receptor activity; protein-containing complex binding;
Cellular component	integral component of membrane; cytosol; cell projection; membrane; integral component of plasma membrane; extracellular region; axon; neuronal cell body; dendrite; nucleus; plasma membrane; neuron projection; receptor complex; postsynapse; glutamatergic synapse; integral component of postsynaptic membrane; integral component of presynaptic membrane;
Biological process	positive regulation of synapse assembly; roof of mouth development; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; optic nerve morphogenesis; ephrin receptor signaling pathway; learning; commissural neuron axon guidance; nervous system development; multicellular organism development; regulation of axonogenesis; dendritic spine development; dendritic spine morphogenesis; negative regulation of axonogenesis; protein phosphorylation; positive regulation of long-term neuronal synaptic plasticity; regulation of body fluid levels; inner ear morphogenesis; angiogenesis; cell morphogenesis; animal organ morphogenesis; regulation of neuronal synaptic plasticity; urogenital system development; peptidyl-tyrosine phosphorylation; corpus callosum development; central nervous system projection neuron axonogenesis; axonal fasciculation; camera-type eye morphogenesis; retinal ganglion cell axon guidance; axon guidance; trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; negative regulation of protein phosphorylation; learning or memory; positive regulation of gene expression; positive regulation of synaptic plasticity; negative regulation of Ras protein signal transduction; regulation of synapse assembly; negative regulation of ERK1 and ERK2 cascade; postsynaptic membrane assembly; neuron projection retraction; positive regulation of long-term synaptic potentiation; positive regulation of protein localization to plasma membrane; negative regulation of NMDA glutamate receptor activity; positive regulation of NMDA glutamate receptor activity;
	Sources:Amigo / QuickGO
Orthologs
	2048
	13844
	ENSG00000133216
	ENSMUSG00000028664
	P29323
	P54763
	NM_001309192; NM_001309193; NM_004442; NM_017449
	NM_001290753; NM_010142
	NP_001296121; NP_001296122; NP_004433; NP_059145
	NP_001277682; NP_034272
	Wikidata
View/Edit Human	View/Edit Mouse

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

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.[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

GRCh38: Ensembl release 89: ENSG00000133216 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000028664 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"Entrez Gene: EPHB2 EPH receptor B2".
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.
- "Protein provides Alzheimer's clue". NHS Choices. November 29, 2010. Archived from the original on 2011-05-18.
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.
- Carl Zimmer (February 4, 2013). "Pigeons Get a New Look". The New York Times.
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.
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.
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.
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.

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

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000133216 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028664 - Ensembl, 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.

[pmid1648701-5] 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".

[pmid21113149-7] 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.
"Protein provides Alzheimer's clue". NHS Choices. November 29, 2010. Archived from the original on 2011-05-18.

[8] "Protein provides Alzheimer's clue". NHS Choices. November 29, 2010. Archived from the original on 2011-05-18.

[pmid23371554-8] 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.
Carl Zimmer (February 4, 2013). "Pigeons Get a New Look". The New York Times.

[10] Carl Zimmer (February 4, 2013). "Pigeons Get a New Look". The New York Times.

[pmid11494128-9] 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.

[pmid9233798-10] 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.

[pmid9632142-11] 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.

[pmid10644995-12] 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.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)