ID EPHB2_HUMAN Reviewed; 1055 AA. AC P29323; O43477; Q5T0U6; Q5T0U7; Q5T0U8; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 5. DT 22-JAN-2014, entry version 174. DE RecName: Full=Ephrin type-B receptor 2; DE EC=2.7.10.1; DE AltName: Full=Developmentally-regulated Eph-related tyrosine kinase; DE AltName: Full=ELK-related tyrosine kinase; DE AltName: Full=EPH tyrosine kinase 3; DE AltName: Full=EPH-like kinase 5; DE Short=EK5; DE Short=hEK5; DE AltName: Full=Renal carcinoma antigen NY-REN-47; DE AltName: Full=Tyrosine-protein kinase TYRO5; DE AltName: Full=Tyrosine-protein kinase receptor EPH-3; DE Flags: Precursor; GN Name=EPHB2; Synonyms=DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8033077; RA Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y., RA Naito Y., Yamada K., Sugimura H., Kino I.; RT "Overexpression of ERK, an EPH family receptor protein tyrosine RT kinase, in various human tumors."; RL Cancer Res. 54:3645-3650(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Fetal brain; RX PubMed=8589679; DOI=10.1093/hmg/4.11.2033; RA Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A., RA Sulman E.P., Brodeur G.M., Pleasure D.E.; RT "Molecular characterization and chromosomal localization of DRT RT (EPHT3): a developmentally regulated human protein-tyrosine kinase RT gene of the EPH family."; RL Hum. Mol. Genet. 4:2033-2045(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=9696046; DOI=10.1038/sj.onc.1201960; RA Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.; RT "A variant transcript encoding an isoform of the human protein RT tyrosine kinase EPHB2 is generated by alternative splicing and RT alternative use of polyadenylation signals."; RL Oncogene 17:521-526(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=7898931; RA Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., RA Basu R., Welcher A.A.; RT "cDNA cloning and tissue distribution of five human EPH-like receptor RT protein-tyrosine kinases."; RL Oncogene 10:897-905(1995). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2). RC TISSUE=Fetal brain; RX PubMed=7601466; DOI=10.1016/0888-7543(95)80224-A; RA Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N., RA Nomura N., Yamamoto T., Hori T.-A.; RT "Identification of the human ERK gene as a putative receptor tyrosine RT kinase and its chromosomal localization to 1p36.1: a comparative RT mapping of human, mouse, and rat chromosomes."; RL Genomics 26:382-384(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2). RC TISSUE=Gastric carcinoma; RX PubMed=7688222; DOI=10.1006/bbrc.1993.1878; RA Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.; RT "Identification of protein-tyrosine kinase genes preferentially RT expressed in embryo stomach and gastric cancer."; RL Biochem. Biophys. Res. Commun. 194:698-705(1993). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712. RX PubMed=1648701; RA Chan J., Watt V.M.; RT "eek and erk, new members of the eph subclass of receptor protein- RT tyrosine kinases."; RL Oncogene 6:1057-1061(1991). RN [9] RP NOMENCLATURE. RX PubMed=9267020; RG Eph nomenclature committee; RT "Unified nomenclature for Eph family receptors and their ligands, the RT ephrins."; RL Cell 90:403-404(1997). RN [10] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), AND RP MASS SPECTROMETRY. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT). RX PubMed=9933164; DOI=10.1126/science.283.5403.833; RA Thanos C.D., Goodwill K.E., Bowie J.U.; RT "Oligomeric structure of the human EphB2 receptor SAM domain."; RL Science 283:833-836(1999). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN RP COMPLEX WITH ANTAGONISTIC PEPTIDE, AND DISULFIDE BOND. RX PubMed=17897949; DOI=10.1074/jbc.M706340200; RA Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K., RA Abagyan R., Widmer H., Pasquale E.B., Kuhn P.; RT "Three-dimensional structure of the EphB2 receptor in complex with an RT antagonistic peptide reveals a novel mode of inhibition."; RL J. Biol. Chem. 282:36505-36513(2007). RN [15] RP VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, AND RP FUNCTION AS A TUMOR SUPPRESSOR. RX PubMed=15300251; DOI=10.1038/ng1408; RA Huusko P., Ponciano-Jackson D., Wolf M., Kiefer J.A., Azorsa D.O., RA Tuzmen S., Weaver D., Robbins C., Moses T., Allinen M., Hautaniemi S., RA Chen Y., Elkahloun A., Basik M., Bova G.S., Bubendorf L., Lugli A., RA Sauter G., Schleutker J., Ozcelik H., Elowe S., Pawson T., Trent J.M., RA Carpten J.D., Kallioniemi O.-P., Mousses S.; RT "Nonsense-mediated decay microarray analysis identifies mutations of RT EPHB2 in human prostate cancer."; RL Nat. Genet. 36:979-983(2004). RN [16] RP VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883. RX PubMed=16155194; DOI=10.1136/jmg.2005.035790; RA Kittles R.A., Baffoe-Bonnie A.B., Moses T.Y., Robbins C.M., RA Ahaghotu C., Huusko P., Pettaway C., Vijayakumar S., Bennett J., RA Hoke G., Mason T., Weinrich S., Trent J.M., Collins F.S., Mousses S., RA Bailey-Wilson J., Furbert-Harris P., Dunston G., Powell I.J., RA Carpten J.D.; RT "A common nonsense mutation in EphB2 is associated with prostate RT cancer risk in African American men with a positive family history."; RL J. Med. Genet. 43:507-511(2006). RN [17] RP VARIANTS [LARGE SCALE ANALYSIS] SER-279; GLY-289; VAL-361; ASN-678 AND RP TRP-844. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously CC transmembrane ephrin-B family ligands residing on adjacent cells, CC leading to contact-dependent bidirectional signaling into CC neighboring cells. The signaling pathway downstream of the CC receptor is referred to as forward signaling while the signaling CC pathway downstream of the ephrin ligand is referred to as reverse CC signaling. Functions in axon guidance during development. Involved CC in the guidance of commissural axons, that form a major CC interhemispheric connection between the 2 temporal lobes of the CC cerebral cortex. Also involved in guidance of contralateral inner CC ear efferent growth cones at the midline and of retinal ganglion CC cell axons to the optic disk. Beside axon guidance, also regulates CC dendritic spines development and maturation and stimulates the CC formation of excitatory synapses. Upon activation by EFNB1, CC abolishes the ARHGEF15-mediated negative regulation on excitatory CC synapse formation. Controls other aspects of development including CC angiogenesis, palate development and in inner ear development CC through regulation of endolymph production. Forward and reverse CC signaling through the EFNB2/EPHB2 complex regulate movement and CC adhesion of cells that tubularize the urethra and septate the CC cloaca. May function as a tumor suppressor. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The CC heterotetramer is composed of an ephrin dimer and a receptor CC dimer. Oligomerization is probably required to induce biological CC responses (By similarity). Interacts (via PDZ-binding motif) with CC GRIP1 and PICK1 (via PDZ domain) (By similarity). Interacts with CC ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and CC degradation by the proteasome. Interacts with AQP1; involved in CC endolymph production in the inner ear. CC -!- INTERACTION: CC P49790:NUP153; NbExp=2; IntAct=EBI-1059294, EBI-286779; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Cell projection, axon (By similarity). Cell projection, CC dendrite (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=EPHB2v, Long; CC IsoId=P29323-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P29323-2; Sequence=VSP_003016, VSP_003017; CC Note=Contains a phosphoserine at position 983; CC Name=3; CC IsoId=P29323-3; Sequence=VSP_015713, VSP_003016, VSP_003017; CC Note=No experimental confirmation available. Contains a CC phosphoserine at position 984; CC -!- TISSUE SPECIFICITY: Brain, heart, lung, kidney, placenta, CC pancreas, liver and skeletal muscle. Preferentially expressed in CC fetal brain. CC -!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy CC originating in tissues of the prostate. Most prostate cancers are CC adenocarcinomas that develop in the acini of the prostatic ducts. CC Other rare histopathologic types of prostate cancer that occur in CC approximately 5% of patients include small cell carcinoma, CC mucinous carcinoma, prostatic ductal carcinoma, transitional cell CC carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid CC cystic carcinoma (basaloid), signet-ring cell carcinoma and CC neuroendocrine carcinoma. Note=The gene represented in this entry CC may be involved in disease pathogenesis. EPHB2 mutations have been CC found in a prostate cancer cell line derived from a brain CC metastasis. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Ephrin receptor subfamily. CC -!- SIMILARITY: Contains 1 Eph LBD (Eph ligand-binding) domain. CC -!- SIMILARITY: Contains 2 fibronectin type-III domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D31661; BAA06506.1; -; mRNA. DR EMBL; L41939; AAA99310.1; -; mRNA. DR EMBL; AF025304; AAB94602.1; -; mRNA. DR EMBL; AL035704; CAI22645.1; -; Genomic_DNA. DR EMBL; AL158086; CAI22645.1; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI22645.1; JOINED; Genomic_DNA. DR EMBL; AL035704; CAI22646.1; -; Genomic_DNA. DR EMBL; AL158086; CAI22646.1; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI22646.1; JOINED; Genomic_DNA. DR EMBL; AL035704; CAI22647.2; -; Genomic_DNA. DR EMBL; AL158086; CAI22647.2; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI22647.2; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI22897.1; -; Genomic_DNA. DR EMBL; AL035704; CAI22897.1; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI22897.1; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI22898.1; -; Genomic_DNA. DR EMBL; AL512444; CAI22898.1; JOINED; Genomic_DNA. DR EMBL; AL035704; CAI22898.1; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI22899.2; -; Genomic_DNA. DR EMBL; AL035704; CAI22899.2; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI22899.2; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI16428.1; -; Genomic_DNA. DR EMBL; AL035704; CAI16428.1; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI16428.1; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI16429.1; -; Genomic_DNA. DR EMBL; AL035704; CAI16429.1; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI16429.1; JOINED; Genomic_DNA. DR EMBL; AL512444; CAI16430.2; -; Genomic_DNA. DR EMBL; AL035704; CAI16430.2; JOINED; Genomic_DNA. DR EMBL; AL158086; CAI16430.2; JOINED; Genomic_DNA. DR EMBL; L36643; AAA74244.1; -; mRNA. DR EMBL; D37827; BAA07073.1; -; mRNA. DR EMBL; D14717; BAA03537.1; -; mRNA. DR EMBL; X59292; CAA41981.1; -; Genomic_DNA. DR PIR; A57174; A57174. DR PIR; I78842; I78842. DR RefSeq; NP_004433.2; NM_004442.6. DR RefSeq; NP_059145.2; NM_017449.3. DR RefSeq; XP_005245832.1; XM_005245775.1. DR UniGene; Hs.523329; -. DR PDB; 1B4F; X-ray; 1.95 A; A/B/C/D/E/F/G/H=910-985. DR PDB; 1F0M; X-ray; 2.20 A; A=910-985. DR PDB; 2QBX; X-ray; 2.30 A; A/B=20-196. DR PDBsum; 1B4F; -. DR PDBsum; 1F0M; -. DR PDBsum; 2QBX; -. DR ProteinModelPortal; P29323; -. DR SMR; P29323; 20-531, 575-985. DR DIP; DIP-1162N; -. DR IntAct; P29323; 3. DR MINT; MINT-5005955; -. DR STRING; 9606.ENSP00000363763; -. DR BindingDB; P29323; -. DR ChEMBL; CHEMBL3290; -. DR GuidetoPHARMACOLOGY; 1831; -. DR PhosphoSite; P29323; -. DR DMDM; 76803654; -. DR PaxDb; P29323; -. DR PRIDE; P29323; -. DR DNASU; 2048; -. DR Ensembl; ENST00000374630; ENSP00000363761; ENSG00000133216. DR Ensembl; ENST00000374632; ENSP00000363763; ENSG00000133216. DR Ensembl; ENST00000400191; ENSP00000383053; ENSG00000133216. DR GeneID; 2048; -. DR KEGG; hsa:2048; -. DR UCSC; uc009vqj.1; human. DR CTD; 2048; -. DR GeneCards; GC01P023037; -. DR H-InvDB; HIX0028518; -. DR HGNC; HGNC:3393; EPHB2. DR HPA; CAB013647; -. DR MIM; 176807; phenotype. DR MIM; 600997; gene. DR MIM; 603688; phenotype. DR neXtProt; NX_P29323; -. DR Orphanet; 1331; Familial prostate cancer. DR PharmGKB; PA27825; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000233856; -. DR HOVERGEN; HBG062180; -. DR InParanoid; P29323; -. DR KO; K05111; -. DR OMA; IVCNRRR; -. DR OrthoDB; EOG7VTDM6; -. DR PhylomeDB; P29323; -. DR BRENDA; 2.7.10.1; 2681. DR Reactome; REACT_111045; Developmental Biology. DR SignaLink; P29323; -. DR ChiTaRS; EPHB2; human. DR EvolutionaryTrace; P29323; -. DR GeneWiki; EPH_receptor_B2; -. DR GenomeRNAi; 2048; -. DR NextBio; 8325; -. DR PRO; PR:P29323; -. DR ArrayExpress; P29323; -. DR Bgee; P29323; -. DR CleanEx; HS_EPHB2; -. DR Genevestigator; P29323; -. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl. DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB. DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB. DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB. DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl. DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl. DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB. DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB. DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl. DR GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl. DR GO; GO:0060021; P:palate development; ISS:UniProtKB. DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB. DR GO; GO:0050878; P:regulation of body fluid levels; ISS:UniProtKB. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl. DR GO; GO:0001655; P:urogenital system development; ISS:UniProtKB. DR Gene3D; 1.10.150.50; -; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR027936; Eph_TM. DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom. DR InterPro; IPR003961; Fibronectin_type3. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR009030; Growth_fac_rcpt_N_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed. DR InterPro; IPR021129; SAM_type1. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt. DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS. DR Pfam; PF14575; EphA2_TM; 1. DR Pfam; PF01404; Ephrin_lbd; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07699; GCC2_GCC3; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF00536; SAM_1; 1. DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00615; EPH_lbd; 1. DR SMART; SM00060; FN3; 2. DR SMART; SM00454; SAM; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF47769; SSF47769; 1. DR SUPFAM; SSF49265; SSF49265; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF57184; SSF57184; 2. DR PROSITE; PS51550; EPH_LBD; 1. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1. DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Cell projection; Complete proteome; Developmental protein; KW Disease mutation; Disulfide bond; Glycoprotein; Kinase; Membrane; KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Repeat; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tumor suppressor; KW Tyrosine-protein kinase. FT SIGNAL 1 18 Potential. FT CHAIN 19 1055 Ephrin type-B receptor 2. FT /FTId=PRO_0000016827. FT TOPO_DOM 19 543 Extracellular (Potential). FT TRANSMEM 544 564 Helical; (Potential). FT TOPO_DOM 565 1055 Cytoplasmic (Potential). FT DOMAIN 20 202 Eph LBD. FT DOMAIN 324 434 Fibronectin type-III 1. FT DOMAIN 435 530 Fibronectin type-III 2. FT DOMAIN 621 884 Protein kinase. FT DOMAIN 913 977 SAM. FT NP_BIND 627 635 ATP (By similarity). FT MOTIF 984 986 PDZ-binding (in isoform 2) (Potential). FT COMPBIAS 184 324 Cys-rich. FT ACT_SITE 746 746 Proton acceptor (By similarity). FT BINDING 653 653 ATP (By similarity). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). FT CARBOHYD 336 336 N-linked (GlcNAc...) (Potential). FT CARBOHYD 428 428 N-linked (GlcNAc...) (Potential). FT CARBOHYD 482 482 N-linked (GlcNAc...) (Potential). FT DISULFID 62 184 FT DISULFID 97 107 FT VAR_SEQ 568 568 R -> RR (in isoform 3). FT /FTId=VSP_015713. FT VAR_SEQ 986 986 G -> V (in isoform 2 and isoform 3). FT /FTId=VSP_003016. FT VAR_SEQ 987 1055 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_003017. FT VARIANT 199 199 R -> H (in prostate cancer). FT /FTId=VAR_032853. FT VARIANT 279 279 A -> S (in prostate cancer; FT dbSNP:rs35882952). FT /FTId=VAR_032854. FT VARIANT 289 289 C -> G. FT /FTId=VAR_042172. FT VARIANT 361 361 I -> V (in dbSNP:rs56180036). FT /FTId=VAR_042173. FT VARIANT 650 650 V -> A (in prostate cancer; FT dbSNP:rs142173175). FT /FTId=VAR_032855. FT VARIANT 678 678 D -> N (in dbSNP:rs28936395). FT /FTId=VAR_042174. FT VARIANT 679 679 H -> N (in prostate cancer). FT /FTId=VAR_032856. FT VARIANT 844 844 R -> W (in dbSNP:rs55826626). FT /FTId=VAR_042175. FT VARIANT 883 883 M -> V (in prostate cancer). FT /FTId=VAR_032857. FT VARIANT 909 909 I -> M (in prostate cancer). FT /FTId=VAR_032858. FT CONFLICT 1 20 MALRRLGAALLLLPLLAAVE -> MWVPVLALPVCTYA FT (in Ref. 1; BAA06506). FT CONFLICT 154 154 G -> D (in Ref. 1; BAA06506). FT CONFLICT 476 476 K -> KQ (in Ref. 1; BAA06506). FT CONFLICT 495 496 Missing (in Ref. 5; AAA74244). FT CONFLICT 532 532 E -> D (in Ref. 1; BAA06506). FT CONFLICT 589 589 M -> I (in Ref. 5; AAA74244). FT CONFLICT 671 671 A -> R (in Ref. 7; BAA03537). FT CONFLICT 788 788 I -> F (in Ref. 5; AAA74244). FT CONFLICT 853 853 S -> A (in Ref. 1; BAA06506, 6; BAA07073 FT and 7; BAA03537). FT CONFLICT 923 923 E -> K (in Ref. 1; BAA06506, 6; BAA07073 FT and 7; BAA03537). FT CONFLICT 958 958 V -> L (in Ref. 2; AAA99310). FT STRAND 21 25 FT HELIX 26 28 FT STRAND 36 39 FT STRAND 44 49 FT STRAND 55 61 FT STRAND 66 68 FT STRAND 71 74 FT STRAND 84 94 FT HELIX 97 99 FT STRAND 111 120 FT STRAND 130 132 FT STRAND 135 141 FT STRAND 148 152 FT STRAND 155 166 FT STRAND 171 183 FT STRAND 185 194 FT HELIX 918 924 FT HELIX 928 930 FT HELIX 931 936 FT HELIX 942 945 FT HELIX 950 955 FT HELIX 961 982 SQ 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 //