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Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3)

 EPHB2_HUMAN             Reviewed;        1055 AA.
P29323; O43477; Q5T0U6; Q5T0U7; Q5T0U8;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 5.
10-OCT-2018, entry version 223.
RecName: Full=Ephrin type-B receptor 2;
EC=2.7.10.1;
AltName: Full=Developmentally-regulated Eph-related tyrosine kinase;
AltName: Full=ELK-related tyrosine kinase;
AltName: Full=EPH tyrosine kinase 3;
AltName: Full=EPH-like kinase 5;
Short=EK5;
Short=hEK5;
AltName: Full=Renal carcinoma antigen NY-REN-47;
AltName: Full=Tyrosine-protein kinase TYRO5;
AltName: Full=Tyrosine-protein kinase receptor EPH-3;
Flags: Precursor;
Name=EPHB2; Synonyms=DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8033077;
Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y.,
Naito Y., Yamada K., Sugimura H., Kino I.;
"Overexpression of ERK, an EPH family receptor protein tyrosine
kinase, in various human tumors.";
Cancer Res. 54:3645-3650(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fetal brain;
PubMed=8589679; DOI=10.1093/hmg/4.11.2033;
Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A.,
Sulman E.P., Brodeur G.M., Pleasure D.E.;
"Molecular characterization and chromosomal localization of DRT
(EPHT3): a developmentally regulated human protein-tyrosine kinase
gene of the EPH family.";
Hum. Mol. Genet. 4:2033-2045(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=9696046; DOI=10.1038/sj.onc.1201960;
Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.;
"A variant transcript encoding an isoform of the human protein
tyrosine kinase EPHB2 is generated by alternative splicing and
alternative use of polyadenylation signals.";
Oncogene 17:521-526(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2).
TISSUE=Brain;
PubMed=7898931;
Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M.,
Basu R., Welcher A.A.;
"cDNA cloning and tissue distribution of five human EPH-like receptor
protein-tyrosine kinases.";
Oncogene 10:897-905(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2).
TISSUE=Fetal brain;
PubMed=7601466; DOI=10.1016/0888-7543(95)80224-A;
Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N.,
Nomura N., Yamamoto T., Hori T.-A.;
"Identification of the human ERK gene as a putative receptor tyrosine
kinase and its chromosomal localization to 1p36.1: a comparative
mapping of human, mouse, and rat chromosomes.";
Genomics 26:382-384(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2).
TISSUE=Gastric carcinoma;
PubMed=7688222; DOI=10.1006/bbrc.1993.1878;
Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.;
"Identification of protein-tyrosine kinase genes preferentially
expressed in embryo stomach and gastric cancer.";
Biochem. Biophys. Res. Commun. 194:698-705(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712.
PubMed=1648701;
Chan J., Watt V.M.;
"eek and erk, new members of the eph subclass of receptor protein-
tyrosine kinases.";
Oncogene 6:1057-1061(1991).
[9]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[10]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT).
PubMed=9933164; DOI=10.1126/science.283.5403.833;
Thanos C.D., Goodwill K.E., Bowie J.U.;
"Oligomeric structure of the human EphB2 receptor SAM domain.";
Science 283:833-836(1999).
[14]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN
COMPLEX WITH ANTAGONISTIC PEPTIDE, AND DISULFIDE BOND.
PubMed=17897949; DOI=10.1074/jbc.M706340200;
Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K.,
Abagyan R., Widmer H., Pasquale E.B., Kuhn P.;
"Three-dimensional structure of the EphB2 receptor in complex with an
antagonistic peptide reveals a novel mode of inhibition.";
J. Biol. Chem. 282:36505-36513(2007).
[15]
VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, AND
FUNCTION AS A TUMOR SUPPRESSOR.
PubMed=15300251; DOI=10.1038/ng1408;
Huusko P., Ponciano-Jackson D., Wolf M., Kiefer J.A., Azorsa D.O.,
Tuzmen S., Weaver D., Robbins C., Moses T., Allinen M., Hautaniemi S.,
Chen Y., Elkahloun A., Basik M., Bova G.S., Bubendorf L., Lugli A.,
Sauter G., Schleutker J., Ozcelik H., Elowe S., Pawson T., Trent J.M.,
Carpten J.D., Kallioniemi O.-P., Mousses S.;
"Nonsense-mediated decay microarray analysis identifies mutations of
EPHB2 in human prostate cancer.";
Nat. Genet. 36:979-983(2004).
[16]
VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883.
PubMed=16155194; DOI=10.1136/jmg.2005.035790;
Kittles R.A., Baffoe-Bonnie A.B., Moses T.Y., Robbins C.M.,
Ahaghotu C., Huusko P., Pettaway C., Vijayakumar S., Bennett J.,
Hoke G., Mason T., Weinrich S., Trent J.M., Collins F.S., Mousses S.,
Bailey-Wilson J., Furbert-Harris P., Dunston G., Powell I.J.,
Carpten J.D.;
"A common nonsense mutation in EphB2 is associated with prostate
cancer risk in African American men with a positive family history.";
J. Med. Genet. 43:507-511(2006).
[17]
VARIANTS [LARGE SCALE ANALYSIS] SER-279; GLY-289; VAL-361; ASN-678 AND
TRP-844.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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:15300251}.
-!- 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:17897949}.
-!- INTERACTION:
P49790:NUP153; NbExp=2; IntAct=EBI-1059294, EBI-286779;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell projection, axon {ECO:0000250}. Cell projection,
dendrite {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=EPHB2v, Long;
IsoId=P29323-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P29323-2; Sequence=VSP_003016, VSP_003017;
Note=Contains a phosphoserine at position 983.
{ECO:0000244|PubMed:19369195};
Name=3;
IsoId=P29323-3; Sequence=VSP_015713, VSP_003016, VSP_003017;
Note=No experimental confirmation available. Contains a
phosphoserine at position 984. {ECO:0000244|PubMed:19369195};
-!- TISSUE SPECIFICITY: Brain, heart, lung, kidney, placenta,
pancreas, liver and skeletal muscle. Preferentially expressed in
fetal brain.
-!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy
originating in tissues of the prostate. Most prostate cancers are
adenocarcinomas that develop in the acini of the prostatic ducts.
Other rare histopathologic types of prostate cancer that occur in
approximately 5% of patients include small cell carcinoma,
mucinous carcinoma, prostatic ductal carcinoma, transitional cell
carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid
cystic carcinoma (basaloid), signet-ring cell carcinoma and
neuroendocrine carcinoma. {ECO:0000269|PubMed:15300251,
ECO:0000269|PubMed:16155194}. Note=The gene represented in this
entry may be involved in disease pathogenesis. EPHB2 mutations
have been found in a prostate cancer cell line derived from a
brain metastasis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; D31661; BAA06506.1; -; mRNA.
EMBL; L41939; AAA99310.1; -; mRNA.
EMBL; AF025304; AAB94602.1; -; mRNA.
EMBL; AL035704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL158086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L36643; AAA74244.1; -; mRNA.
EMBL; D37827; BAA07073.1; -; mRNA.
EMBL; D14717; BAA03537.1; -; mRNA.
EMBL; X59292; CAA41981.1; -; Genomic_DNA.
CCDS; CCDS229.2; -. [P29323-2]
CCDS; CCDS230.1; -. [P29323-3]
CCDS; CCDS81279.1; -. [P29323-1]
PIR; A57174; A57174.
PIR; I78842; I78842.
RefSeq; NP_001296122.1; NM_001309193.1. [P29323-1]
RefSeq; NP_004433.2; NM_004442.7. [P29323-3]
RefSeq; NP_059145.2; NM_017449.4. [P29323-2]
UniGene; Hs.380705; -.
UniGene; Hs.523329; -.
PDB; 1B4F; X-ray; 1.95 A; A/B/C/D/E/F/G/H=908-985.
PDB; 1F0M; X-ray; 2.20 A; A=908-985.
PDB; 2QBX; X-ray; 2.30 A; A/B=20-196.
PDB; 3ZFM; X-ray; 2.27 A; A=604-898.
PDBsum; 1B4F; -.
PDBsum; 1F0M; -.
PDBsum; 2QBX; -.
PDBsum; 3ZFM; -.
ProteinModelPortal; P29323; -.
SMR; P29323; -.
BioGrid; 108362; 23.
DIP; DIP-1162N; -.
IntAct; P29323; 4.
MINT; P29323; -.
STRING; 9606.ENSP00000363763; -.
BindingDB; P29323; -.
ChEMBL; CHEMBL3290; -.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
GuidetoPHARMACOLOGY; 1831; -.
iPTMnet; P29323; -.
PhosphoSitePlus; P29323; -.
SwissPalm; P29323; -.
BioMuta; EPHB2; -.
DMDM; 76803654; -.
EPD; P29323; -.
MaxQB; P29323; -.
PaxDb; P29323; -.
PeptideAtlas; P29323; -.
PRIDE; P29323; -.
ProteomicsDB; 54540; -.
ProteomicsDB; 54541; -. [P29323-2]
ProteomicsDB; 54542; -. [P29323-3]
DNASU; 2048; -.
Ensembl; ENST00000374630; ENSP00000363761; ENSG00000133216. [P29323-2]
Ensembl; ENST00000374632; ENSP00000363763; ENSG00000133216. [P29323-3]
Ensembl; ENST00000400191; ENSP00000383053; ENSG00000133216. [P29323-1]
GeneID; 2048; -.
KEGG; hsa:2048; -.
UCSC; uc001bge.4; human. [P29323-1]
CTD; 2048; -.
DisGeNET; 2048; -.
EuPathDB; HostDB:ENSG00000133216.16; -.
GeneCards; EPHB2; -.
H-InvDB; HIX0028518; -.
HGNC; HGNC:3393; EPHB2.
HPA; CAB013647; -.
HPA; HPA071200; -.
MalaCards; EPHB2; -.
MIM; 176807; phenotype.
MIM; 600997; gene.
MIM; 603688; phenotype.
neXtProt; NX_P29323; -.
OpenTargets; ENSG00000133216; -.
Orphanet; 1331; Familial prostate cancer.
PharmGKB; PA27825; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P29323; -.
KO; K05111; -.
OMA; VCRGCPS; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P29323; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-373760; L1CAM interactions.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P29323; -.
SIGNOR; P29323; -.
ChiTaRS; EPHB2; human.
EvolutionaryTrace; P29323; -.
GeneWiki; EPH_receptor_B2; -.
GenomeRNAi; 2048; -.
PRO; PR:P29323; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000133216; Expressed in 185 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_EPHB2; -.
ExpressionAtlas; P29323; baseline and differential.
Genevisible; P29323; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0044877; F:protein-containing complex binding; ISS:ARUK-UCL.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051389; P:inactivation of MAPKK activity; ISS:ARUK-UCL.
GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
GO; GO:0007612; P:learning; ISS:ARUK-UCL.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL.
GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ARUK-UCL.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:ARUK-UCL.
GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
GO; GO:0106028; P:neuron projection retraction; IEA:Ensembl.
GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:ARUK-UCL.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:ARUK-UCL.
GO; GO:0097104; P:postsynaptic membrane assembly; IEA:Ensembl.
GO; GO:0050878; P:regulation of body fluid levels; ISS:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:ARUK-UCL.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
GO; GO:0001655; P:urogenital system development; ISS: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;
Disease mutation; Disulfide bond; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tumor suppressor;
Tyrosine-protein kinase.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1055 Ephrin type-B receptor 2.
/FTId=PRO_0000016827.
TOPO_DOM 19 543 Extracellular. {ECO:0000255}.
TRANSMEM 544 564 Helical. {ECO:0000255}.
TOPO_DOM 565 1055 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 (in isoform 2).
{ECO:0000255}.
COMPBIAS 184 324 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 653 653 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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:0000255}.
DISULFID 62 184 {ECO:0000269|PubMed:17897949}.
DISULFID 97 107 {ECO:0000269|PubMed:17897949}.
VAR_SEQ 568 568 R -> RR (in isoform 3).
{ECO:0000303|PubMed:8589679}.
/FTId=VSP_015713.
VAR_SEQ 986 986 G -> V (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:7601466,
ECO:0000303|PubMed:7688222,
ECO:0000303|PubMed:7898931,
ECO:0000303|PubMed:8033077,
ECO:0000303|PubMed:8589679}.
/FTId=VSP_003016.
VAR_SEQ 987 1055 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:7601466,
ECO:0000303|PubMed:7688222,
ECO:0000303|PubMed:7898931,
ECO:0000303|PubMed:8033077,
ECO:0000303|PubMed:8589679}.
/FTId=VSP_003017.
VARIANT 199 199 R -> H (in prostate cancer;
dbSNP:rs201754821).
{ECO:0000269|PubMed:15300251}.
/FTId=VAR_032853.
VARIANT 279 279 A -> S (in prostate cancer;
dbSNP:rs35882952).
{ECO:0000269|PubMed:15300251,
ECO:0000269|PubMed:16155194,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_032854.
VARIANT 289 289 C -> G. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042172.
VARIANT 361 361 I -> V (in dbSNP:rs56180036).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042173.
VARIANT 650 650 V -> A (in prostate cancer;
dbSNP:rs142173175).
{ECO:0000269|PubMed:16155194}.
/FTId=VAR_032855.
VARIANT 678 678 D -> N (in dbSNP:rs28936395).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042174.
VARIANT 679 679 H -> N (in prostate cancer).
{ECO:0000269|PubMed:15300251}.
/FTId=VAR_032856.
VARIANT 844 844 R -> W (in dbSNP:rs55826626).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042175.
VARIANT 883 883 M -> V (in prostate cancer;
dbSNP:rs372653137).
{ECO:0000269|PubMed:16155194}.
/FTId=VAR_032857.
VARIANT 909 909 I -> M (in prostate cancer).
{ECO:0000269|PubMed:15300251}.
/FTId=VAR_032858.
CONFLICT 1 20 MALRRLGAALLLLPLLAAVE -> MWVPVLALPVCTYA
(in Ref. 1; BAA06506). {ECO:0000305}.
CONFLICT 154 154 G -> D (in Ref. 1; BAA06506).
{ECO:0000305}.
CONFLICT 476 476 K -> KQ (in Ref. 1; BAA06506).
{ECO:0000305}.
CONFLICT 495 496 Missing (in Ref. 5; AAA74244).
{ECO:0000305}.
CONFLICT 532 532 E -> D (in Ref. 1; BAA06506).
{ECO:0000305}.
CONFLICT 589 589 M -> I (in Ref. 5; AAA74244).
{ECO:0000305}.
CONFLICT 671 671 A -> R (in Ref. 7; BAA03537).
{ECO:0000305}.
CONFLICT 788 788 I -> F (in Ref. 5; AAA74244).
{ECO:0000305}.
CONFLICT 853 853 S -> A (in Ref. 1; BAA06506, 6; BAA07073
and 7; BAA03537). {ECO:0000305}.
CONFLICT 923 923 E -> K (in Ref. 1; BAA06506, 6; BAA07073
and 7; BAA03537). {ECO:0000305}.
CONFLICT 958 958 V -> L (in Ref. 2; AAA99310).
{ECO:0000305}.
STRAND 21 25 {ECO:0000244|PDB:2QBX}.
HELIX 26 28 {ECO:0000244|PDB:2QBX}.
STRAND 36 39 {ECO:0000244|PDB:2QBX}.
STRAND 44 49 {ECO:0000244|PDB:2QBX}.
STRAND 55 61 {ECO:0000244|PDB:2QBX}.
STRAND 66 68 {ECO:0000244|PDB:2QBX}.
STRAND 71 74 {ECO:0000244|PDB:2QBX}.
STRAND 84 94 {ECO:0000244|PDB:2QBX}.
HELIX 97 99 {ECO:0000244|PDB:2QBX}.
STRAND 111 120 {ECO:0000244|PDB:2QBX}.
STRAND 130 132 {ECO:0000244|PDB:2QBX}.
STRAND 135 141 {ECO:0000244|PDB:2QBX}.
STRAND 148 152 {ECO:0000244|PDB:2QBX}.
STRAND 155 166 {ECO:0000244|PDB:2QBX}.
STRAND 171 183 {ECO:0000244|PDB:2QBX}.
STRAND 185 194 {ECO:0000244|PDB:2QBX}.
HELIX 618 620 {ECO:0000244|PDB:3ZFM}.
STRAND 621 626 {ECO:0000244|PDB:3ZFM}.
STRAND 635 640 {ECO:0000244|PDB:3ZFM}.
STRAND 648 655 {ECO:0000244|PDB:3ZFM}.
HELIX 661 674 {ECO:0000244|PDB:3ZFM}.
STRAND 685 689 {ECO:0000244|PDB:3ZFM}.
STRAND 691 700 {ECO:0000244|PDB:3ZFM}.
HELIX 707 712 {ECO:0000244|PDB:3ZFM}.
TURN 713 716 {ECO:0000244|PDB:3ZFM}.
HELIX 720 739 {ECO:0000244|PDB:3ZFM}.
HELIX 749 751 {ECO:0000244|PDB:3ZFM}.
STRAND 752 754 {ECO:0000244|PDB:3ZFM}.
STRAND 760 762 {ECO:0000244|PDB:3ZFM}.
HELIX 790 792 {ECO:0000244|PDB:3ZFM}.
HELIX 795 800 {ECO:0000244|PDB:3ZFM}.
HELIX 805 820 {ECO:0000244|PDB:3ZFM}.
TURN 826 829 {ECO:0000244|PDB:3ZFM}.
HELIX 832 840 {ECO:0000244|PDB:3ZFM}.
HELIX 853 862 {ECO:0000244|PDB:3ZFM}.
HELIX 873 885 {ECO:0000244|PDB:3ZFM}.
HELIX 887 890 {ECO:0000244|PDB:3ZFM}.
HELIX 918 924 {ECO:0000244|PDB:1B4F}.
HELIX 928 930 {ECO:0000244|PDB:1B4F}.
HELIX 931 936 {ECO:0000244|PDB:1B4F}.
HELIX 942 945 {ECO:0000244|PDB:1B4F}.
HELIX 950 955 {ECO:0000244|PDB:1B4F}.
HELIX 961 982 {ECO:0000244|PDB:1B4F}.
SEQUENCE 1055 AA; 117493 MW; 4F8BFEDC45986483 CRC64;
MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ
VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF
DSATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD
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 AEYQTSIQEK
LPLIIGSSAA 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 IQSVEGQPLA RRPRATGRTK RCQPRDVTKK TCNSNDGKKK
GMGKKKTDPG RGREIQGIFF KEDSHKESND CSCGG


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