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Ephrin type-B receptor 2 (EC 2.7.10.1) (Neural kinase) (Nuk receptor tyrosine kinase) (Tyrosine-protein kinase receptor EPH-3) (Tyrosine-protein kinase receptor SEK-3)

 EPHB2_MOUSE             Reviewed;         986 AA.
P54763; A3KG00; A3KG01; A3KG02; A3KG89; A3KG90; Q62213; Q6GTQ7;
Q6P5F1; Q9QVY4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 3.
28-FEB-2018, entry version 188.
RecName: Full=Ephrin type-B receptor 2 {ECO:0000305};
EC=2.7.10.1;
AltName: Full=Neural kinase;
AltName: Full=Nuk receptor tyrosine kinase;
AltName: Full=Tyrosine-protein kinase receptor EPH-3;
AltName: Full=Tyrosine-protein kinase receptor SEK-3;
Flags: Precursor;
Name=Ephb2 {ECO:0000312|MGI:MGI:99611};
Synonyms=Epth3, Nuk {ECO:0000303|PubMed:8134103},
Sek3 {ECO:0000312|MGI:MGI:99611};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-986 (ISOFORM 3).
PubMed=8134103;
Henkemeyer M., Marengere L.E., McGlade J., Olivier J.P., Conlon R.A.,
Holmyard D.P., Letwin K., Pawson T.;
"Immunolocalization of the Nuk receptor tyrosine kinase suggests roles
in segmental patterning of the brain and axonogenesis.";
Oncogene 9:1001-1014(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 508-986 (ISOFORM 2).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=7947319; DOI=10.1016/0925-4773(94)90091-4;
Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P.,
Nieto A., Wilkinson D.G., Charnay P., Gilardi P.;
"Several receptor tyrosine kinase genes of the Eph family are
segmentally expressed in the developing hindbrain.";
Mech. Dev. 47:3-17(1994).
[5]
DISRUPTION PHENOTYPE, FUNCTION IN COMMISSURAL AXON GUIDANCE,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=8689685; DOI=10.1016/S0092-8674(00)80075-6;
Henkemeyer M., Orioli D., Henderson J.T., Saxton T.M., Roder J.,
Pawson T., Klein R.;
"Nuk controls pathfinding of commissural axons in the mammalian
central nervous system.";
Cell 86:35-46(1996).
[6]
FUNCTION IN AXON GUIDANCE, AND FUNCTION IN PALATE DEVELOPMENT.
PubMed=8947026;
Orioli D., Henkemeyer M., Lemke G., Klein R., Pawson T.;
"Sek4 and Nuk receptors cooperate in guidance of commissural axons and
in palate formation.";
EMBO J. 15:6035-6049(1996).
[7]
INTERACTION WITH PICK1 AND GRIP1, AND IDENTIFICATION OF PDZ-BINDING
MOTIF.
PubMed=9883737; DOI=10.1016/S0896-6273(00)80663-7;
Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
"PDZ proteins bind, cluster, and synaptically colocalize with Eph
receptors and their ephrin ligands.";
Neuron 21:1453-1463(1998).
[8]
FUNCTION IN ANGIOGENESIS, AND DEVELOPMENTAL STAGE.
PubMed=9990854; DOI=10.1101/gad.13.3.295;
Adams R.H., Wilkinson G.A., Weiss C., Diella F., Gale N.W.,
Deutsch U., Risau W., Klein R.;
"Roles of ephrinB ligands and EphB receptors in cardiovascular
development: demarcation of arterial/venous domains, vascular
morphogenesis, and sprouting angiogenesis.";
Genes Dev. 13:295-306(1999).
[9]
DEVELOPMENTAL STAGE.
PubMed=10704386;
Imondi R., Wideman C., Kaprielian Z.;
"Complementary expression of transmembrane ephrins and their receptors
in the mouse spinal cord: a possible role in constraining the
orientation of longitudinally projecting axons.";
Development 127:1397-1410(2000).
[10]
DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE, FUNCTION IN INNER EAR
DEVELOPMENT, INTERACTION WITH AQP1, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=10839360; DOI=10.1016/S0896-6273(00)81174-5;
Cowan C.A., Yokoyama N., Bianchi L.M., Henkemeyer M., Fritzsch B.;
"EphB2 guides axons at the midline and is necessary for normal
vestibular function.";
Neuron 26:417-430(2000).
[11]
FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY
SYNAPSE FORMATION, AND SUBCELLULAR LOCATION.
PubMed=14691139; DOI=10.1083/jcb.200306033;
Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.;
"Multiple EphB receptor tyrosine kinases shape dendritic spines in the
hippocampus.";
J. Cell Biol. 163:1313-1326(2003).
[12]
FUNCTION IN URORECTAL DEVELOPMENT.
PubMed=15223334; DOI=10.1016/j.ydbio.2004.03.027;
Dravis C., Yokoyama N., Chumley M.J., Cowan C.A., Silvany R.E.,
Shay J., Baker L.A., Henkemeyer M.;
"Bidirectional signaling mediated by ephrin-B2 and EphB2 controls
urorectal development.";
Dev. Biol. 271:272-290(2004).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-482.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION IN EXCITATORY SYNAPSE FORMATION, FUNCTION IN PHOSPHORYLATION
OF ARHGEF15, AND INTERACTION WITH ARHGEF15.
PubMed=21029865; DOI=10.1016/j.cell.2010.09.038;
Margolis S.S., Salogiannis J., Lipton D.M., Mandel-Brehm C.,
Wills Z.P., Mardinly A.R., Hu L., Greer P.L., Bikoff J.B., Ho H.Y.,
Soskis M.J., Sahin M., Greenberg M.E.;
"EphB-mediated degradation of the RhoA GEF Ephexin5 relieves a
developmental brake on excitatory synapse formation.";
Cell 143:442-455(2010).
[17]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
[18]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-196.
PubMed=9853759; DOI=10.1038/24904;
Himanen J.-P., Henkemeyer M., Nikolov D.B.;
"Crystal structure of the ligand-binding domain of the receptor
tyrosine kinase EphB2.";
Nature 396:486-491(1998).
[19]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-200 IN COMPLEX WITH EFNB2,
AND DISULFIDE BOND.
PubMed=11780069; DOI=10.1038/414933a;
Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A.,
Henkemeyer M., Nikolov D.B.;
"Crystal structure of an Eph receptor-ephrin complex.";
Nature 414:933-938(2001).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-199 IN COMPLEX WITH EFNA5.
PubMed=15107857; DOI=10.1038/nn1237;
Himanen J.P., Chumley M.J., Lackmann M., Li C., Barton W.A.,
Jeffrey P.D., Vearing C., Geleick D., Feldheim D.A., Boyd A.W.,
Henkemeyer M., Nikolov D.B.;
"Repelling class discrimination: ephrin-A5 binds to and activates
EphB2 receptor signaling.";
Nat. Neurosci. 7:501-509(2004).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
transmembrane ephrin-B family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. Functions in axon guidance during development. Involved
in the guidance of commissural axons, that form a major
interhemispheric connection between the 2 temporal lobes of the
cerebral cortex. Also involved in guidance of contralateral inner
ear efferent growth cones at the midline and of retinal ganglion
cell axons to the optic disk. In addition to axon guidance, also
regulates dendritic spines development and maturation and
stimulates the formation of excitatory synapses. Upon activation
by EFNB1, abolishes the ARHGEF15-mediated negative regulation on
excitatory synapse formation. Controls other aspects of
development including angiogenesis, palate development and in
inner ear development through regulation of endolymph production.
Forward and reverse signaling through the EFNB2/EPHB2 complex
regulate movement and adhesion of cells that tubularize the
urethra and septate the cloaca. May function as a tumor
suppressor. {ECO:0000269|PubMed:10839360,
ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:15223334,
ECO:0000269|PubMed:21029865, ECO:0000269|PubMed:8689685,
ECO:0000269|PubMed:8947026, ECO:0000269|PubMed:9990854}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Heterotetramer upon binding of the ligand. The
heterotetramer is composed of an ephrin dimer and a receptor
dimer. Oligomerization is probably required to induce biological
responses (By similarity). Interacts (via PDZ-binding motif) with
GRIP1 and PICK1 (via PDZ domain) (By similarity). Interacts with
ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and
degradation by the proteasome. Interacts with AQP1; involved in
endolymph production in the inner ear. {ECO:0000250,
ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:11780069,
ECO:0000269|PubMed:15107857, ECO:0000269|PubMed:21029865,
ECO:0000269|PubMed:9883737}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-537711, EBI-537711;
Q5FWH6-2:Arhgef15; NbExp=3; IntAct=EBI-537711, EBI-2943608;
Q03137:Epha4; NbExp=3; IntAct=EBI-537711, EBI-1539152;
Q925T6:Grip1; NbExp=2; IntAct=EBI-537711, EBI-537752;
P34152:Ptk2; NbExp=3; IntAct=EBI-537711, EBI-77070;
P05480:Src; NbExp=3; IntAct=EBI-537711, EBI-298680;
Q13009:TIAM1 (xeno); NbExp=3; IntAct=EBI-537711, EBI-1050007;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell projection, axon. Cell projection, dendrite.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3 {ECO:0000305};
IsoId=P54763-3; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=P54763-2; Sequence=VSP_057933;
Note=No experimental confirmation available.;
Name=4 {ECO:0000305};
IsoId=P54763-4; Sequence=VSP_057932;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the epithelial dark cells of the
inner ear. Expressed in the region of the proximal tubules of the
kidney nephron. Expressed in myogenic progenitor cells
(PubMed:27446912). {ECO:0000269|PubMed:10839360,
ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: Highly expressed in ventral cells of the
neural tube and within axons of the peripheral nervous system
during development. Expressed in the vestibulo-acoustic system and
hindbrain as early as E11.5. Detected in the spinal cord at E12.
Expressed in cells of the developing outer retina. Also expressed
in mesenchyme adjacent to vessels. In myogenic progenitor cells,
highly expressed during early development (E11.5) and
progressively repressed as developments proceeds
(PubMed:27446912). {ECO:0000269|PubMed:10704386,
ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:27446912,
ECO:0000269|PubMed:8689685, ECO:0000269|PubMed:9990854}.
-!- DISRUPTION PHENOTYPE: Mice are long-lived and fertile. They
display strain-specific circling behavior, are hyperactive and
exhibit rapid head bobbing and twirled excessively when picked-up
by the tail. This is probably due to abnormal vestibular function.
{ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:8689685}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA72411.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH62924.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AL627214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL627345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC043088; AAH43088.2; -; mRNA.
EMBL; BC062924; AAH62924.1; ALT_INIT; mRNA.
EMBL; L25890; AAA72411.1; ALT_INIT; mRNA.
EMBL; X76011; CAA53598.1; -; mRNA.
RefSeq; NP_001277682.1; NM_001290753.2. [P54763-4]
RefSeq; NP_034272.1; NM_010142.4. [P54763-3]
RefSeq; XP_006538594.1; XM_006538531.3. [P54763-2]
UniGene; Mm.250981; -.
PDB; 1JPA; X-ray; 1.91 A; A/B=587-898.
PDB; 1KGY; X-ray; 2.70 A; A/B/C/D=20-199.
PDB; 1NUK; X-ray; 2.90 A; A=20-202.
PDB; 1SHW; X-ray; 2.20 A; B=19-199.
PDB; 2HEN; X-ray; 2.60 A; A/B/C/D=614-898.
PDB; 3ETP; X-ray; 2.00 A; A=20-199.
PDBsum; 1JPA; -.
PDBsum; 1KGY; -.
PDBsum; 1NUK; -.
PDBsum; 1SHW; -.
PDBsum; 2HEN; -.
PDBsum; 3ETP; -.
ProteinModelPortal; P54763; -.
SMR; P54763; -.
CORUM; P54763; -.
DIP; DIP-34917N; -.
IntAct; P54763; 13.
MINT; P54763; -.
STRING; 10090.ENSMUSP00000101471; -.
BindingDB; P54763; -.
ChEMBL; CHEMBL5961; -.
GuidetoPHARMACOLOGY; 1831; -.
iPTMnet; P54763; -.
PhosphoSitePlus; P54763; -.
SwissPalm; P54763; -.
MaxQB; P54763; -.
PaxDb; P54763; -.
PRIDE; P54763; -.
DNASU; 13844; -.
Ensembl; ENSMUST00000059287; ENSMUSP00000058135; ENSMUSG00000028664. [P54763-4]
Ensembl; ENSMUST00000105845; ENSMUSP00000101471; ENSMUSG00000028664. [P54763-3]
Ensembl; ENSMUST00000105846; ENSMUSP00000101472; ENSMUSG00000028664. [P54763-2]
GeneID; 13844; -.
KEGG; mmu:13844; -.
UCSC; uc008vim.2; mouse.
UCSC; uc008vin.2; mouse.
CTD; 2048; -.
MGI; MGI:99611; Ephb2.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P54763; -.
KO; K05111; -.
OMA; VCRGCPS; -.
OrthoDB; EOG091G00W0; -.
TreeFam; TF315608; -.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
ChiTaRS; Ephb2; mouse.
EvolutionaryTrace; P54763; -.
PRO; PR:P54763; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028664; -.
CleanEx; MM_EPHB2; -.
ExpressionAtlas; P54763; baseline and differential.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045202; C:synapse; NAS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
GO; GO:0005003; F:ephrin receptor activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044877; F:macromolecular complex binding; IPI:ARUK-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; IPI:MGI.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0007411; P:axon guidance; IDA:MGI.
GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB.
GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB.
GO; GO:0022038; P:corpus callosum development; IMP:UniProtKB.
GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB.
GO; GO:0060997; P:dendritic spine morphogenesis; IDA:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0051389; P:inactivation of MAPKK activity; IDA:ARUK-UCL.
GO; GO:0042472; P:inner ear morphogenesis; IMP:UniProtKB.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
GO; GO:0050771; P:negative regulation of axonogenesis; IDA:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; IMP:ARUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:ARUK-UCL.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:ARUK-UCL.
GO; GO:0106028; P:neuron projection retraction; IDA:ARUK-UCL.
GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
GO; GO:0060021; P:palate development; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:ARUK-UCL.
GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IMP:ARUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IGI:ARUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0050770; P:regulation of axonogenesis; IDA:MGI.
GO; GO:0050878; P:regulation of body fluid levels; IMP:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IMP:SynGO.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:MGI.
GO; GO:0001655; P:urogenital system development; IMP:UniProtKB.
CDD; cd10477; EphR_LBD_B2; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034238; EphB2_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF07699; Ephrin_rec_like; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Cell projection; Complete proteome; Developmental protein;
Disulfide bond; Glycoprotein; Kinase; Membrane; Neurogenesis;
Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 986 Ephrin type-B receptor 2. {ECO:0000255}.
/FTId=PRO_0000016828.
TOPO_DOM 19 543 Extracellular. {ECO:0000255}.
TRANSMEM 544 564 Helical. {ECO:0000255}.
TOPO_DOM 565 986 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 202 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 324 434 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 435 530 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 621 884 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 913 977 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 627 635 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 984 986 PDZ-binding.
COMPBIAS 184 321 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 653 653 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
DISULFID 62 184 {ECO:0000269|PubMed:11780069}.
DISULFID 97 107 {ECO:0000269|PubMed:11780069}.
VAR_SEQ 476 476 K -> KQ (in isoform 4). {ECO:0000305}.
/FTId=VSP_057932.
VAR_SEQ 566 566 N -> NR (in isoform 2).
{ECO:0000303|PubMed:7947319}.
/FTId=VSP_057933.
STRAND 20 25 {ECO:0000244|PDB:3ETP}.
HELIX 26 28 {ECO:0000244|PDB:3ETP}.
STRAND 36 39 {ECO:0000244|PDB:3ETP}.
STRAND 44 49 {ECO:0000244|PDB:3ETP}.
STRAND 55 61 {ECO:0000244|PDB:3ETP}.
STRAND 66 68 {ECO:0000244|PDB:3ETP}.
STRAND 71 74 {ECO:0000244|PDB:3ETP}.
STRAND 84 94 {ECO:0000244|PDB:3ETP}.
HELIX 97 99 {ECO:0000244|PDB:3ETP}.
STRAND 100 102 {ECO:0000244|PDB:1SHW}.
STRAND 110 121 {ECO:0000244|PDB:3ETP}.
STRAND 125 128 {ECO:0000244|PDB:3ETP}.
STRAND 130 132 {ECO:0000244|PDB:3ETP}.
STRAND 135 142 {ECO:0000244|PDB:3ETP}.
STRAND 147 152 {ECO:0000244|PDB:3ETP}.
STRAND 155 166 {ECO:0000244|PDB:3ETP}.
STRAND 171 182 {ECO:0000244|PDB:3ETP}.
STRAND 185 195 {ECO:0000244|PDB:3ETP}.
HELIX 599 601 {ECO:0000244|PDB:1JPA}.
STRAND 602 604 {ECO:0000244|PDB:1JPA}.
HELIX 605 612 {ECO:0000244|PDB:1JPA}.
HELIX 618 620 {ECO:0000244|PDB:1JPA}.
STRAND 621 629 {ECO:0000244|PDB:1JPA}.
STRAND 631 640 {ECO:0000244|PDB:1JPA}.
STRAND 643 645 {ECO:0000244|PDB:2HEN}.
STRAND 648 654 {ECO:0000244|PDB:1JPA}.
HELIX 661 674 {ECO:0000244|PDB:1JPA}.
STRAND 685 689 {ECO:0000244|PDB:1JPA}.
STRAND 691 694 {ECO:0000244|PDB:1JPA}.
STRAND 696 700 {ECO:0000244|PDB:1JPA}.
HELIX 707 712 {ECO:0000244|PDB:1JPA}.
TURN 713 716 {ECO:0000244|PDB:1JPA}.
HELIX 720 739 {ECO:0000244|PDB:1JPA}.
HELIX 749 751 {ECO:0000244|PDB:1JPA}.
STRAND 752 754 {ECO:0000244|PDB:1JPA}.
STRAND 760 762 {ECO:0000244|PDB:1JPA}.
HELIX 790 792 {ECO:0000244|PDB:1JPA}.
HELIX 795 799 {ECO:0000244|PDB:1JPA}.
HELIX 805 820 {ECO:0000244|PDB:1JPA}.
TURN 821 823 {ECO:0000244|PDB:2HEN}.
TURN 826 829 {ECO:0000244|PDB:1JPA}.
HELIX 832 840 {ECO:0000244|PDB:1JPA}.
HELIX 853 862 {ECO:0000244|PDB:1JPA}.
TURN 867 869 {ECO:0000244|PDB:1JPA}.
HELIX 873 885 {ECO:0000244|PDB:1JPA}.
HELIX 887 890 {ECO:0000244|PDB:1JPA}.
SEQUENCE 986 AA; 109899 MW; 92DB5234F18758A7 CRC64;
MAVRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ
VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF
DLATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RNGFYLAFQD
YGGCMSLIAV RVFYRKCPRI IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY
CNGDGEWLVP IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA
TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS GGREDLVYNI
ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA HTQYTFEIQA VNGVTDQSPF
SPQFASVNIT TNQAAPSAVS IMHQVSRTVD SITLSWSQPD QPNGVILDYE LQYYEKELSE
YNATAIKSPT NTVTVQGLKA GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIKEK
LPLIVGSSAA GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF
TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV AIKTLKSGYT
EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE FMENGSLDSF LRQNDGQFTV
IQLVGMLRGI AAGMKYLADM NYVHRDLAAR NILVNSNLVC KVSDFGLSRF LEDDTSDPTY
TSALGGKIPI RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE
QDYRLPPPMD CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI
NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM EDILRVGVTL
AGHQKKILNS IQVMRAQMNQ IQSVEV


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