From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
EPHB1
Identifiers
Aliases
EPHB1 , Ephb1, 9330129L11, AW488255, C130099E04Rik, Cek6, ENSMUSG00000074119, Elk, Elkh, Hek6, Net, EPHT2, EPH receptor B1, ELK, NETExternal IDs
OMIM :
600600 ;
MGI :
1096337 ;
HomoloGene :
20936 ;
GeneCards :
EPHB1 ;
OMA :
EPHB1 - orthologs
RNA expression pattern
Bgee
Human
Mouse (ortholog)
Top expressed in endothelial cell ganglionic eminence Brodmann area 23 secondary oocyte cerebellum cerebellar cortex ventricular zone cerebellar hemisphere primary visual cortex right hemisphere of cerebellum
Top expressed in otic vesicle lumbar subsegment of spinal cord otolith organ utricle inferior colliculus substantia nigra deep cerebellar nuclei superior colliculus Rostral migratory stream medial ganglionic eminence
More reference expression data
BioGPS
Wikidata
Ephrin type-B receptor 1 is a
protein that in humans is encoded by the EPHB1
gene .
[5]
[6]
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]
Interactions
EPH receptor B1 has been shown to
interact with:
References
^
a
b
c
GRCh38: Ensembl release 89: ENSG00000154928 –
Ensembl , May 2017
^
a
b
c
GRCm38: Ensembl release 89: ENSMUSG00000032537 –
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 .
^ Tang XX, Biegel JA, Nycum LM, Yoshioka A, Brodeur GM, Pleasure DE, Ikegaki N (1995).
"cDNA cloning, molecular characterization, and chromosomal localization of NET(EPHT2), a human EPH-related receptor protein-tyrosine kinase gene preferentially expressed in brain" . Genomics . 29 (2): 426–37.
doi :
10.1006/geno.1995.9985 .
PMID
8666391 .
^
a
b
"Entrez Gene: EPHB1 EPH receptor B1" .
^ Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (Mar 1998).
"Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses" . Genes Dev . 12 (5): 667–78.
doi :
10.1101/gad.12.5.667 .
PMC
316584 .
PMID
9499402 .
^ Han DC, Shen TL, Miao H, Wang B, Guan JL (Nov 2002).
"EphB1 associates with Grb7 and regulates cell migration" . J. Biol. Chem . 277 (47): 45655–61.
doi :
10.1074/jbc.M203165200 .
PMID
12223469 .
^ Stein E, Huynh-Do U, Lane AA, Cerretti DP, Daniel TO (Jan 1998).
"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase" . J. Biol. Chem . 273 (3): 1303–8.
doi :
10.1074/jbc.273.3.1303 .
PMID
9430661 .
^ Williams, SE; Mann, F; Erskine, L (2003).
"Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm" . Neuron . 39 (6): 919–935.
doi :
10.1016/j.neuron.2003.08.017 .
PMID
12971893 .
S2CID
18565204 .
Further reading
Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annu. Rev. Neurosci . 21 : 309–45.
doi :
10.1146/annurev.neuro.21.1.309 .
PMID
9530499 .
Zhou R (1998). "The Eph family receptors and ligands". Pharmacol. Ther . 77 (3): 151–81.
doi :
10.1016/S0163-7258(97)00112-5 .
PMID
9576626 .
Abrahamson DR, Robert B, Hyink DP, St John PL, Daniel TO (1998).
"Origins and formation of microvasculature in the developing kidney" . Kidney Int. Suppl . 67 : S7-11.
doi :
10.1046/j.1523-1755.1998.06702.x .
PMID
9736245 .
Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development . 126 (10): 2033–44.
doi :
10.1242/dev.126.10.2033 .
PMID
10207129 .
Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol . International Review of Cytology. 196 : 177–244.
doi :
10.1016/S0074-7696(00)96005-4 .
ISBN
9780123646002 .
PMID
10730216 .
Xu Q, Mellitzer G, Wilkinson DG (2000).
"Roles of Eph receptors and ephrins in segmental patterning" . Philos. Trans. R. Soc. Lond. B Biol. Sci . 355 (1399): 993–1002.
doi :
10.1098/rstb.2000.0635 .
PMC
1692797 .
PMID
11128993 .
Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci . 2 (3): 155–64.
doi :
10.1038/35058515 .
PMID
11256076 .
S2CID
205014301 .
Larose L, Gish G, Shoelson S, Pawson T (1993). "Identification of residues in the beta platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-gamma 1". Oncogene . 8 (9): 2493–9.
PMID
7689724 .
Davis S, Gale NW, Aldrich TH, Maisonpierre PC, Lhotak V, Pawson T, Goldfarb M, Yancopoulos GD (1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science . 266 (5186): 816–9.
Bibcode :
1994Sci...266..816D .
doi :
10.1126/science.7973638 .
PMID
7973638 .
Beckmann MP, Cerretti DP, Baum P, Vanden Bos T, James L, Farrah T, Kozlosky C, Hollingsworth T, Shilling H, Maraskovsky E (1994).
"Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors" . EMBO J . 13 (16): 3757–62.
doi :
10.1002/j.1460-2075.1994.tb06685.x .
PMC
395287 .
PMID
8070404 .
Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (1995).
"Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases" . Mol. Immunol . 32 (16): 1197–205.
doi :
10.1016/0161-5890(95)00108-5 .
PMID
8559144 .
Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD (1996).
"Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis" . Neuron . 17 (1): 9–19.
doi :
10.1016/S0896-6273(00)80276-7 .
PMID
8755474 .
S2CID
1075856 .
Stein E, Cerretti DP, Daniel TO (1996).
"Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells" . J. Biol. Chem . 271 (38): 23588–93.
doi :
10.1074/jbc.271.38.23588 .
PMID
8798570 .
Bonaldo MF, Lennon G, Soares MB (1996).
"Normalization and subtraction: two approaches to facilitate gene discovery" . Genome Res . 6 (9): 791–806.
doi :
10.1101/gr.6.9.791 .
PMID
8889548 .
Kozlosky CJ, VandenBos T, Park L, Cerretti DP, Carpenter MK (1997). "LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain". Cytokine . 9 (8): 540–9.
doi :
10.1006/cyto.1997.0199 .
PMID
9245480 .
Ephnomenclaturecommittee (1997).
"Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee" . Cell . 90 (3): 403–4.
doi :
10.1016/S0092-8674(00)80500-0 .
PMID
9267020 .
S2CID
26773768 .
Stein E, Huynh-Do U, Lane AA, Cerretti DP, Daniel TO (1998).
"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase" . J. Biol. Chem . 273 (3): 1303–8.
doi :
10.1074/jbc.273.3.1303 .
PMID
9430661 .
Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (1998).
"Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses" . Genes Dev . 12 (5): 667–78.
doi :
10.1101/gad.12.5.667 .
PMC
316584 .
PMID
9499402 .
Angiopoietin
CNTF
EGF (ErbB)
FGF
FGFR1
FGFR2
Agonists:
Ersofermin
FGF (
1 ,
2 (bFGF) ,
3 ,
4 ,
5 ,
6 ,
7 (
KGF ),
8 ,
9 ,
10 (KGF2) ,
17 ,
18 ,
22 )
Palifermin
Repifermin
Selpercatinib
Sprifermin
Trafermin
FGFR3
FGFR4 Unsorted
HGF (c-Met)
IGF
LNGF (p75NTR )
PDGF
RET (GFL)
SCF (c-Kit)
TGFβ
Trk
TrkA
Negative allosteric modulators:
VM-902A
TrkB
Agonists:
3,7-DHF
3,7,8,2'-THF
4'-DMA-7,8-DHF
7,3'-DHF
7,8-DHF
7,8,2'-THF
7,8,3'-THF
Amitriptyline
BDNF
BNN-20
Deoxygedunin
Deprenyl
Diosmetin
DMAQ-B1
HIOC
LM22A-4
N-Acetylserotonin
NT-3
NT-4
Norwogonin (5,7,8-THF)
R7
R13
TDP6
TrkC
VEGF Others
Additional growth factors:
Adrenomedullin
Colony-stimulating factors (see
here instead)
Connective tissue growth factor (CTGF)
Ephrins (
A1 ,
A2 ,
A3 ,
A4 ,
A5 ,
B1 ,
B2 ,
B3 )
Erythropoietin (see
here instead)
Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF)
Glia maturation factor (GMF)
Hepatoma-derived growth factor (HDGF)
Interleukins /
T-cell growth factors (see
here instead)
Leukemia inhibitory factor (LIF)
Macrophage-stimulating protein (MSP; HLP, HGFLP)
Midkine (NEGF2)
Migration-stimulating factor (MSF; PRG4)
Oncomodulin
Pituitary adenylate cyclase-activating peptide (PACAP)
Pleiotrophin
Renalase
Thrombopoietin (see
here instead)
Wnt signaling proteins
Additional growth factor receptor modulators:
Cerebrolysin (neurotrophin mixture)