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Database: UniProt
Entry: P54760
LinkDB: P54760
Original site: P54760 
ID   EPHB4_HUMAN             Reviewed;         987 AA.
AC   P54760; Q9BTA5; Q9BXP0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   03-SEP-2014, entry version 163.
DE   RecName: Full=Ephrin type-B receptor 4;
DE            EC=2.7.10.1;
DE   AltName: Full=Hepatoma transmembrane kinase;
DE   AltName: Full=Tyrosine-protein kinase TYRO11;
DE   Flags: Precursor;
GN   Name=EPHB4; Synonyms=HTK, MYK1, TYRO11;
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], SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=8188704;
RA   Bennett B.D., Wang Z., Kuang W.J., Wang A., Groopman J.E.,
RA   Goeddel D.V., Scadden D.T.;
RT   "Cloning and characterization of HTK, a novel transmembrane tyrosine
RT   kinase of the EPH subfamily.";
RL   J. Biol. Chem. 269:14211-14218(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA   Miller W., Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-987.
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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   [5]
RP   FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, AND FUNCTION IN
RP   CELL MIGRATION.
RX   PubMed=12734395; DOI=10.1242/jcs.00426;
RA   Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G.;
RT   "Forward EphB4 signaling in endothelial cells controls cellular
RT   repulsion and segregation from ephrinB2 positive cells.";
RL   J. Cell Sci. 116:2461-2470(2003).
RN   [6]
RP   FUNCTION IN POSTNATAL AND TUMOR ANGIOGENESIS.
RX   PubMed=16424904; DOI=10.1038/sj.emboj.7600949;
RA   Erber R., Eichelsbacher U., Powajbo V., Korn T., Djonov V., Lin J.,
RA   Hammes H.P., Grobholz R., Ullrich A., Vajkoczy P.;
RT   "EphB4 controls blood vascular morphogenesis during postnatal
RT   angiogenesis.";
RL   EMBO J. 25:628-641(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-976, AND
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; THR-976 AND
RP   TYR-987, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 17-196 IN COMPLEX WITH
RP   EFNB2, MUTAGENESIS OF LEU-95, AND DISULFIDE BOND.
RX   PubMed=16867992; DOI=10.1074/jbc.M605766200;
RA   Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R.,
RA   Han G.W., Seifert J.M., Widmer H., Auer M., Kuhn P.;
RT   "Structural and biophysical characterization of the EphB4*ephrinB2
RT   protein-protein interaction and receptor specificity.";
RL   J. Biol. Chem. 281:28185-28192(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 17-196 IN COMPLEX WITH
RP   ANTAGONISTIC PEPTIDE, AND DISULFIDE BOND.
RX   PubMed=16472751; DOI=10.1016/j.str.2005.11.011;
RA   Chrencik J.E., Brooun A., Recht M.I., Kraus M.L., Koolpe M.,
RA   Kolatkar A.R., Bruce R.H., Martiny-Baron G., Widmer H., Pasquale E.B.,
RA   Kuhn P.;
RT   "Structure and thermodynamic characterization of the EphB4/Ephrin-B2
RT   antagonist peptide complex reveals the determinants for receptor
RT   specificity.";
RL   Structure 14:321-330(2006).
RN   [14]
RP   STRUCTURE BY NMR OF 434-529.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the second FN3 domain from human ephrin type-B
RT   receptor 4.";
RL   Submitted (JUL-2007) to the PDB data bank.
RN   [15]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-67; ILE-113; LEU-346; VAL-371;
RP   GLU-576; HIS-678; THR-882; TRP-889 AND ASP-890.
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. Together with its cognate ligand/functional ligand
CC       EFNB2 plays a central role in heart morphogenesis and angiogenesis
CC       through regulation of cell adhesion and cell migration. EPHB4-
CC       mediated forward signaling controls cellular repulsion and
CC       segregation form EFNB2-expressing cells. Plays also a role in
CC       postnatal blood vessel remodeling, morphogenesis and permeability
CC       and is thus important in the context of tumor angiogenesis.
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).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in placenta but also
CC       detected in kidney, liver, lung, pancreas, skeletal muscle and
CC       heart. Expressed in primitive and myeloid, but not lymphoid,
CC       hematopoietic cells. Also observed in cell lines derived from
CC       liver, breast, colon, lung, melanocyte and cervix.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal heart, lung, liver and to
CC       a lower extent in brain. Not expressed in adult brain.
CC   -!- PTM: Phosphorylated; autophosphorylation is stimulated by EFNB2.
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.
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DR   EMBL; U07695; AAA20598.1; -; mRNA.
DR   EMBL; AF312032; AAK21010.1; -; Genomic_DNA.
DR   EMBL; BC004264; AAH04264.1; -; mRNA.
DR   CCDS; CCDS5706.1; -.
DR   PIR; A54092; A54092.
DR   RefSeq; NP_004435.3; NM_004444.4.
DR   UniGene; Hs.437008; -.
DR   PDB; 2BBA; X-ray; 1.65 A; A=17-196.
DR   PDB; 2E7H; NMR; -; A=434-529.
DR   PDB; 2HLE; X-ray; 2.05 A; A=17-196.
DR   PDB; 2QKQ; X-ray; 2.10 A; A/B=896-977.
DR   PDB; 2VWU; X-ray; 2.00 A; A=598-887.
DR   PDB; 2VWV; X-ray; 1.90 A; A=598-899.
DR   PDB; 2VWW; X-ray; 1.90 A; A=598-899.
DR   PDB; 2VWX; X-ray; 1.65 A; A=598-899.
DR   PDB; 2VWY; X-ray; 1.65 A; A=598-899.
DR   PDB; 2VWZ; X-ray; 1.65 A; A=598-899.
DR   PDB; 2VX0; X-ray; 2.10 A; A=598-899.
DR   PDB; 2VX1; X-ray; 1.65 A; A=598-899.
DR   PDB; 2X9F; X-ray; 1.75 A; A=598-899.
DR   PDB; 2XVD; X-ray; 1.70 A; A=598-899.
DR   PDB; 2YN8; X-ray; 2.11 A; A/B=598-892.
DR   PDB; 3ZEW; X-ray; 2.50 A; A/B=598-892.
DR   PDB; 4AW5; X-ray; 2.33 A; A=605-890.
DR   PDB; 4BB4; X-ray; 1.65 A; A=598-899.
DR   PDBsum; 2BBA; -.
DR   PDBsum; 2E7H; -.
DR   PDBsum; 2HLE; -.
DR   PDBsum; 2QKQ; -.
DR   PDBsum; 2VWU; -.
DR   PDBsum; 2VWV; -.
DR   PDBsum; 2VWW; -.
DR   PDBsum; 2VWX; -.
DR   PDBsum; 2VWY; -.
DR   PDBsum; 2VWZ; -.
DR   PDBsum; 2VX0; -.
DR   PDBsum; 2VX1; -.
DR   PDBsum; 2X9F; -.
DR   PDBsum; 2XVD; -.
DR   PDBsum; 2YN8; -.
DR   PDBsum; 3ZEW; -.
DR   PDBsum; 4AW5; -.
DR   PDBsum; 4BB4; -.
DR   ProteinModelPortal; P54760; -.
DR   SMR; P54760; 15-529, 608-973.
DR   BioGrid; 108364; 4.
DR   IntAct; P54760; 2.
DR   STRING; 9606.ENSP00000350896; -.
DR   BindingDB; P54760; -.
DR   ChEMBL; CHEMBL5147; -.
DR   GuidetoPHARMACOLOGY; 1833; -.
DR   PhosphoSite; P54760; -.
DR   DMDM; 19860819; -.
DR   DOSAC-COBS-2DPAGE; P54760; -.
DR   MaxQB; P54760; -.
DR   PaxDb; P54760; -.
DR   PRIDE; P54760; -.
DR   DNASU; 2050; -.
DR   Ensembl; ENST00000358173; ENSP00000350896; ENSG00000196411.
DR   GeneID; 2050; -.
DR   KEGG; hsa:2050; -.
DR   UCSC; uc003uwm.1; human.
DR   CTD; 2050; -.
DR   GeneCards; GC07M100402; -.
DR   H-InvDB; HIX0025312; -.
DR   HGNC; HGNC:3395; EPHB4.
DR   HPA; CAB013537; -.
DR   MIM; 600011; gene.
DR   neXtProt; NX_P54760; -.
DR   PharmGKB; PA27827; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000233856; -.
DR   HOVERGEN; HBG062180; -.
DR   InParanoid; P54760; -.
DR   KO; K05113; -.
DR   OMA; TVFYFES; -.
DR   PhylomeDB; P54760; -.
DR   TreeFam; TF315608; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   SignaLink; P54760; -.
DR   ChiTaRS; EPHB4; human.
DR   EvolutionaryTrace; P54760; -.
DR   GeneWiki; EPH_receptor_B4; -.
DR   GenomeRNAi; 2050; -.
DR   NextBio; 8335; -.
DR   PRO; PR:P54760; -.
DR   ArrayExpress; P54760; -.
DR   Bgee; P54760; -.
DR   CleanEx; HS_EPHB4; -.
DR   Genevestigator; P54760; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005003; F:ephrin receptor activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:GOC.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA: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; PS01186; EGF_2; 1.
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; Angiogenesis; ATP-binding; Cell membrane;
KW   Complete proteome; Developmental protein; Disulfide bond;
KW   Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     15       Potential.
FT   CHAIN        16    987       Ephrin type-B receptor 4.
FT                                /FTId=PRO_0000016834.
FT   TOPO_DOM     16    539       Extracellular (Potential).
FT   TRANSMEM    540    560       Helical; (Potential).
FT   TOPO_DOM    561    987       Cytoplasmic (Potential).
FT   DOMAIN       17    202       Eph LBD.
FT   DOMAIN      323    432       Fibronectin type-III 1.
FT   DOMAIN      436    529       Fibronectin type-III 2.
FT   DOMAIN      615    899       Protein kinase.
FT   DOMAIN      907    971       SAM.
FT   NP_BIND     621    629       ATP (By similarity).
FT   MOTIF       985    987       PDZ-binding (Potential).
FT   COMPBIAS    184    320       Cys-rich.
FT   ACT_SITE    740    740       Proton acceptor (By similarity).
FT   BINDING     647    647       ATP (By similarity).
FT   MOD_RES     911    911       Phosphoserine.
FT   MOD_RES     976    976       Phosphothreonine.
FT   MOD_RES     987    987       Phosphotyrosine.
FT   CARBOHYD    203    203       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    335    335       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    426    426       N-linked (GlcNAc...) (Potential).
FT   DISULFID     61    184
FT   DISULFID     97    107
FT   VARIANT      67     67       P -> L (in dbSNP:rs34653459).
FT                                /FTId=VAR_042181.
FT   VARIANT     113    113       V -> I (in dbSNP:rs55866373).
FT                                /FTId=VAR_042182.
FT   VARIANT     346    346       P -> L (in a metastatic melanoma sample;
FT                                somatic mutation).
FT                                /FTId=VAR_042183.
FT   VARIANT     371    371       A -> V (in dbSNP:rs55720981).
FT                                /FTId=VAR_042184.
FT   VARIANT     576    576       D -> E (in dbSNP:rs36050247).
FT                                /FTId=VAR_042185.
FT   VARIANT     678    678       R -> H (in dbSNP:rs55692440).
FT                                /FTId=VAR_042186.
FT   VARIANT     882    882       A -> T (in dbSNP:rs34918225).
FT                                /FTId=VAR_042187.
FT   VARIANT     889    889       R -> W (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                /FTId=VAR_042188.
FT   VARIANT     890    890       E -> D (in dbSNP:rs35638378).
FT                                /FTId=VAR_042189.
FT   MUTAGEN      95     95       L->R: Reduces binding affinity for EFNB2.
FT   CONFLICT     62     62       D -> E (in Ref. 1; AAA20598).
FT   CONFLICT    308    308       Y -> D (in Ref. 1; AAA20598).
FT   CONFLICT    464    464       V -> W (in Ref. 1; AAA20598).
FT   CONFLICT    926    927       ES -> AR (in Ref. 1; AAA20598).
FT   STRAND       17     22
FT   HELIX        23     25
FT   STRAND       33     36
FT   STRAND       43     48
FT   STRAND       54     61
FT   STRAND       63     65
FT   STRAND       70     74
FT   STRAND       84     95
FT   HELIX        97     99
FT   STRAND      109    121
FT   STRAND      130    132
FT   STRAND      135    142
FT   STRAND      160    166
FT   STRAND      171    182
FT   STRAND      184    196
FT   STRAND      441    446
FT   STRAND      449    453
FT   STRAND      460    462
FT   STRAND      466    473
FT   TURN        479    481
FT   STRAND      482    496
FT   STRAND      503    510
FT   HELIX       612    614
FT   STRAND      615    623
FT   STRAND      625    634
FT   STRAND      637    639
FT   STRAND      642    649
FT   HELIX       655    668
FT   STRAND      679    683
FT   STRAND      685    694
FT   HELIX       701    707
FT   TURN        708    710
FT   HELIX       714    733
FT   HELIX       743    745
FT   STRAND      746    748
FT   STRAND      754    756
FT   HELIX       765    767
FT   HELIX       784    786
FT   HELIX       789    794
FT   HELIX       799    814
FT   TURN        815    817
FT   TURN        820    823
FT   HELIX       826    834
FT   HELIX       847    856
FT   HELIX       861    863
FT   HELIX       867    879
FT   HELIX       881    885
FT   HELIX       912    918
FT   HELIX       922    924
FT   HELIX       925    930
FT   HELIX       936    939
FT   HELIX       944    950
FT   HELIX       955    965
SQ   SEQUENCE   987 AA;  108270 MW;  11A004622F194706 CRC64;
     MELRVLLCWA SLAAALEETL LNTKLETADL KWVTFPQVDG QWEELSGLDE EQHSVRTYEV
     CDVQRAPGQA HWLRTGWVPR RGAVHVYATL RFTMLECLSL PRAGRSCKET FTVFYYESDA
     DTATALTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN VKTLRLGPLS KAGFYLAFQD
     QGACMALLSL HLFYKKCAQL TVNLTRFPET VPRELVVPVA GSCVVDAVPA PGPSPSLYCR
     EDGQWAEQPV TGCSCAPGFE AAEGNTKCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSA
     VCQCRVGYFR ARTDPRGAPC TTPPSAPRSV VSRLNGSSLH LEWSAPLESG GREDLTYALR
     CRECRPGGSC APCGGDLTFD PGPRDLVEPW VVVRGLRPDF TYTFEVTALN GVSSLATGPV
     PFEPVNVTTD REVPPAVSDI RVTRSSPSSL SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS
     SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SEGWREQLAL
     IAGTAVVGVV LVLVVIVVAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
     EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK GGYTERQRRE
     FLSEASIMGQ FEHPNIIRLE GVVTNSMPVM ILTEFMENGA LDSFLRLNDG QFTVIQLVGM
     LRGIASGMRY LAEMSYVHRD LAARNILVNS NLVCKVSDFG LSRFLEENSS DPTYTSSLGG
     KIPIRWTAPE AIAFRKFTSA SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP
     PPPDCPTSLH QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD
     QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFELVS QISAEDLLRI GVTLAGHQKK
     ILASVQHMKS QAKPGTPGGT GGPAPQY
//
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