ID EPHB6_HUMAN Reviewed; 1021 AA. AC O15197; A4D2I7; A8CDT5; D3DXD3; Q2TB23; Q2TB24; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 4. DT 13-FEB-2019, entry version 196. DE RecName: Full=Ephrin type-B receptor 6; DE AltName: Full=HEP; DE AltName: Full=Tyrosine-protein kinase-defective receptor EPH-6; DE Flags: Precursor; GN Name=EPHB6; 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 1), AND TISSUE SPECIFICITY. RX PubMed=9207182; DOI=10.1006/bbrc.1997.6812; RA Matsuoka H., Iwata N., Ito M., Shimoyama M., Nagata A., Chihara K., RA Takai S., Matsui T.; RT "Expression of a kinase-defective Eph-like receptor in the normal RT human brain."; RL Biochem. Biophys. Res. Commun. 235:487-492(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-122; ARG-282; RP ALA-324 AND GLN-499. RG SeattleSNPs variation discovery resource; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-1021 (ISOFORM 3). RX PubMed=18425388; RA Jin M., Komohara Y., Shichijo S., Harada M., Yamanaka R., Miyamoto S., RA Nikawa J., Itoh K., Yamada A.; RT "Identification of EphB6 variant-derived epitope peptides recognized RT by cytotoxic T-lymphocytes from HLA-A24+ malignant glioma patients."; RL Oncol. Rep. 19:1277-1283(2008). RN [8] RP PROTEIN SEQUENCE OF 32-46. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [9] RP INTERACTION WITH CBL AND EPHB1, AND PHOSPHORYLATION. RX PubMed=11713248; DOI=10.1074/jbc.M108011200; RA Freywald A., Sharfe N., Roifman C.M.; RT "The kinase-null EphB6 receptor undergoes transphosphorylation in a RT complex with EphB1."; RL J. Biol. Chem. 277:3823-3828(2002). RN [10] RP FUNCTION. RX PubMed=12517763; DOI=10.1074/jbc.M208179200; RA Freywald A., Sharfe N., Rashotte C., Grunberger T., Roifman C.M.; RT "The EphB6 receptor inhibits JNK activation in T lymphocytes and RT modulates T cell receptor-mediated responses."; RL J. Biol. Chem. 278:10150-10156(2003). RN [11] RP FUNCTION, INTERACTION WITH FYN, AND PHOSPHORYLATION. RX PubMed=15955811; DOI=10.1074/jbc.M500010200; RA Matsuoka H., Obama H., Kelly M.L., Matsui T., Nakamoto M.; RT "Biphasic functions of the kinase-defective Ephb6 receptor in cell RT adhesion and migration."; RL J. Biol. Chem. 280:29355-29363(2005). RN [12] RP TISSUE SPECIFICITY. RX PubMed=18754880; DOI=10.1111/j.1349-7006.2008.00866.x; RA Jin M., Komohara Y., Shichijo S., Yamanaka R., Nikawa J., Itoh K., RA Yamada A.; RT "Erythropoietin-producing hepatocyte B6 variant-derived peptides with RT the ability to induce glioma-reactive cytotoxic T lymphocytes in human RT leukocyte antigen-A2+ glioma patients."; RL Cancer Sci. 99:1656-1662(2008). RN [13] RP TISSUE SPECIFICITY. RX PubMed=19234485; DOI=10.1038/onc.2009.18; RA Fox B.P., Kandpal R.P.; RT "EphB6 receptor significantly alters invasiveness and other phenotypic RT characteristics of human breast carcinoma cells."; RL Oncogene 28:1706-1713(2009). RN [14] RP VARIANTS [LARGE SCALE ANALYSIS] ASN-360; PRO-603; GLN-719 AND GLY-930. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANTS [LARGE SCALE ANALYSIS] SER-122; THR-170; VAL-221; HIS-282; RP GLN-309; ALA-324; LEU-332; VAL-662; SER-743; HIS-813; LYS-875 AND RP VAL-993. 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: Kinase-defective receptor for members of the ephrin-B CC family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion CC and migration by exerting both positive and negative effects upon CC stimulation with ephrin-B2. Inhibits JNK activation, T-cell CC receptor-induced IL-2 secretion and CD25 expression upon CC stimulation with ephrin-B2. {ECO:0000269|PubMed:12517763, CC ECO:0000269|PubMed:15955811}. CC -!- SUBUNIT: Interacts with CBL and EPHB1. Interacts with FYN; this CC interaction takes place in a ligand-independent manner. CC {ECO:0000269|PubMed:11713248, ECO:0000269|PubMed:15955811}. CC -!- INTERACTION: CC Q0VD86:INCA1; NbExp=5; IntAct=EBI-10182490, EBI-6509505; CC Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-10182490, EBI-740897; CC Q7Z3S9:NOTCH2NLA; NbExp=3; IntAct=EBI-10182490, EBI-945833; CC Q04864:REL; NbExp=3; IntAct=EBI-10182490, EBI-307352; CC P15884:TCF4; NbExp=3; IntAct=EBI-10182490, EBI-533224; CC Q9HCM9:TRIM39; NbExp=3; IntAct=EBI-10182490, EBI-739510; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O15197-1; Sequence=Displayed; CC Name=2; CC IsoId=O15197-2; Sequence=VSP_037496; CC Name=3; Synonyms=EphB6v; CC IsoId=O15197-3; Sequence=VSP_037497, VSP_037498; CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in non invasive CC breast carcinoma cell lines (at protein level). Strong expression CC in brain and pancreas, and weak expression in other tissues, such CC as heart, placenta, lung, liver, skeletal muscle and kidney. CC Expressed in breast non invasive tumors but not in metastatic CC lesions. Isoform 3 is expressed in cell lines of glioblastomas, CC anaplastic astrocytomas, gliosarcomas and astrocytomas. Isoform 3 CC is not detected in normal tissues. {ECO:0000269|PubMed:18754880, CC ECO:0000269|PubMed:19234485, ECO:0000269|PubMed:9207182}. CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive. Its extracellular domain is capable of promoting cell CC adhesion and migration in response to low concentrations of CC ephrin-B2, but its cytoplasmic domain is essential for cell CC repulsion and inhibition of migration induced by high CC concentrations of ephrin-B2. CC -!- PTM: Ligand-binding increases phosphorylation on tyrosine CC residues. Phosphorylation on tyrosine residues is mediated by CC transphosphorylation by the catalytically active EPHB1 in a CC ligand-independent manner. Tyrosine phosphorylation of the CC receptor may act as a switch on the functional transition from CC cell adhesion/attraction to de-adhesion/repulsion. CC {ECO:0000269|PubMed:11713248, ECO:0000269|PubMed:15955811}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD03058.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAI10608.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAP20939.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAA21560.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=EAL23775.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAW51902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/ephb6/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/EPHB6ID40471ch7q34.html"; 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; D83492; BAA21560.1; ALT_INIT; mRNA. DR EMBL; AY280502; AAP20939.1; ALT_INIT; Genomic_DNA. DR EMBL; AF107256; AAD03058.1; ALT_INIT; Genomic_DNA. DR EMBL; AC104597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236959; EAL23775.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471198; EAW51900.1; -; Genomic_DNA. DR EMBL; CH471198; EAW51901.1; -; Genomic_DNA. DR EMBL; CH471198; EAW51902.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471198; EAW51903.1; -; Genomic_DNA. DR EMBL; BC051028; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC110606; AAI10607.1; -; mRNA. DR EMBL; BC110607; AAI10608.2; ALT_INIT; mRNA. DR EMBL; EU054308; ABV55388.1; -; mRNA. DR PIR; JC5526; JC5526. DR RefSeq; NP_001267724.2; NM_001280795.2. DR RefSeq; NP_004436.4; NM_004445.5. DR UniGene; Hs.380089; -. DR ProteinModelPortal; O15197; -. DR SMR; O15197; -. DR BioGrid; 108365; 17. DR IntAct; O15197; 22. DR MINT; O15197; -. DR STRING; 9606.ENSP00000376684; -. DR BindingDB; O15197; -. DR ChEMBL; CHEMBL5836; -. DR iPTMnet; O15197; -. DR PhosphoSitePlus; O15197; -. DR BioMuta; EPHB6; -. DR jPOST; O15197; -. DR PaxDb; O15197; -. DR PeptideAtlas; O15197; -. DR PRIDE; O15197; -. DR ProteomicsDB; 48502; -. DR ProteomicsDB; 48503; -. [O15197-2] DR ProteomicsDB; 48504; -. [O15197-3] DR Ensembl; ENST00000392957; ENSP00000376684; ENSG00000106123. DR Ensembl; ENST00000442129; ENSP00000410789; ENSG00000106123. DR GeneID; 2051; -. DR KEGG; hsa:2051; -. DR CTD; 2051; -. DR DisGeNET; 2051; -. DR GeneCards; EPHB6; -. DR HGNC; HGNC:3396; EPHB6. DR HPA; HPA035784; -. DR MIM; 602757; gene. DR neXtProt; NX_O15197; -. DR PharmGKB; PA27828; -. DR eggNOG; KOG0196; Eukaryota. DR eggNOG; COG0515; LUCA. DR HOGENOM; HOG000233856; -. DR HOVERGEN; HBG062180; -. DR InParanoid; O15197; -. DR KO; K05114; -. DR OrthoDB; 933071at2759; -. DR PhylomeDB; O15197; -. DR TreeFam; TF314013; -. DR Reactome; R-HSA-2682334; EPH-Ephrin signaling. DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling. DR Reactome; R-HSA-3928664; Ephrin signaling. DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells. DR ChiTaRS; EPHB6; human. DR GeneWiki; EPHB6; -. DR GenomeRNAi; 2051; -. DR PRO; PR:O15197; -. DR Proteomes; UP000005640; Unplaced. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005003; F:ephrin receptor activity; TAS:ProtInc. DR GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd00063; FN3; 2. 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; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like. 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; PF07699; Ephrin_rec_like; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF07647; SAM_2; 1. DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00615; EPH_lbd; 1. DR SMART; SM01411; Ephrin_rec_like; 1. DR SMART; SM00060; FN3; 2. DR SMART; SM00454; SAM; 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; 1. DR PROSITE; PS51550; EPH_LBD; 1. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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 Alternative splicing; ATP-binding; Complete proteome; KW Direct protein sequencing; Glycoprotein; Membrane; Nucleotide-binding; KW Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 31 {ECO:0000269|PubMed:15340161}. FT CHAIN 32 1021 Ephrin type-B receptor 6. FT /FTId=PRO_0000016837. FT TOPO_DOM 32 594 Extracellular. {ECO:0000255}. FT TRANSMEM 595 615 Helical. {ECO:0000255}. FT TOPO_DOM 616 1021 Cytoplasmic. {ECO:0000255}. FT DOMAIN 33 237 Eph LBD. {ECO:0000255|PROSITE- FT ProRule:PRU00883}. FT DOMAIN 369 486 Fibronectin type-III 1. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 487 582 Fibronectin type-III 2. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 670 919 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 948 1012 SAM. {ECO:0000255|PROSITE- FT ProRule:PRU00184}. FT NP_BIND 676 684 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOTIF 1019 1021 PDZ-binding. {ECO:0000255}. FT COMPBIAS 166 176 Poly-Ser. FT COMPBIAS 219 366 Cys-rich. FT COMPBIAS 881 884 Poly-Pro. FT CARBOHYD 480 480 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 16 292 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_037496. FT VAR_SEQ 487 540 VPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYD FT QAEDESHSFTLTS -> GELFSLAFRIPCLRSFEPPSLLLI FT SSLVHPCRPPLKADPAPRDSYPHNNFPFAL (in FT isoform 3). FT {ECO:0000303|PubMed:18425388}. FT /FTId=VSP_037497. FT VAR_SEQ 541 1021 Missing (in isoform 3). FT {ECO:0000303|PubMed:18425388}. FT /FTId=VSP_037498. FT VARIANT 122 122 G -> S (in dbSNP:rs8177173). FT {ECO:0000269|PubMed:17344846, FT ECO:0000269|Ref.2}. FT /FTId=VAR_019139. FT VARIANT 170 170 S -> T. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042190. FT VARIANT 221 221 A -> V. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042191. FT VARIANT 282 282 P -> H. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042192. FT VARIANT 282 282 P -> R (in dbSNP:rs8177143). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_019140. FT VARIANT 309 309 R -> Q (in dbSNP:rs55728646). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042193. FT VARIANT 324 324 S -> A (in dbSNP:rs8177146). FT {ECO:0000269|PubMed:17344846, FT ECO:0000269|Ref.2}. FT /FTId=VAR_019141. FT VARIANT 332 332 S -> L (in dbSNP:rs35189999). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042194. FT VARIANT 360 360 D -> N (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036091. FT VARIANT 499 499 R -> Q (in dbSNP:rs8177175). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_019142. FT VARIANT 603 603 A -> P (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036092. FT VARIANT 662 662 A -> V (in dbSNP:rs35984674). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042195. FT VARIANT 719 719 R -> Q (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036093. FT VARIANT 743 743 P -> S (in an ovarian mucinous carcinoma FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042196. FT VARIANT 813 813 R -> H. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042197. FT VARIANT 875 875 E -> K (in a glioblastoma multiforme FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042198. FT VARIANT 930 930 D -> G (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036094. FT VARIANT 993 993 I -> V. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042199. SQ SEQUENCE 1021 AA; 110700 MW; BF1D4D9BE34358A5 CRC64; MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT YPPGGWDEVS VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA QRAHIRLHFS VRACSSLGVS GGTCRETFTL YYRQAEEPDS PDSVSSWHLK RWTKVDTIAA DESFPSSSSS SSSSSSAAWA VGPHGAGQRA GLQLNVKERS FGPLTQRGFY VAFQDTGACL ALVAVRLFSY TCPAVLRSFA SFPETQASGA GGASLVAAVG TCVAHAEPEE DGVGGQAGGS PPRLHCNGEG KWMVAVGGCR CQPGYQPARG DKACQACPRG LYKSSAGNAP CSPCPARSHA PNPAAPVCPC LEGFYRASSD PPEAPCTGPP SAPQELWFEV QGSALMLHWR LPRELGGRGD LLFNVVCKEC EGRQEPASGG GGTCHRCRDE VHFDPRQRGL TESRVLVGGL RAHVPYILEV QAVNGVSELS PDPPQAAAIN VSTSHEVPSA VPVVHQVSRA SNSITVSWPQ PDQTNGNILD YQLRYYDQAE DESHSFTLTS ETNTATVTQL SPGHIYGFQV RARTAAGHGP YGGKVYFQTL PQGELSSQLP ERLSLVIGSI LGALAFLLLA AITVLAVVFQ RKRRGTGYTE QLQQYSSPGL GVKYYIDPST YEDPCQAIRE LAREVDPAYI KIEEVIGTGS FGEVRQGRLQ PRGRREQTVA IQALWAGGAE SLQMTFLGRA AVLGQFQHPN ILRLEGVVTK SRPLMVLTEF MELGPLDSFL RQREGQFSSL QLVAMQRGVA AAMQYLSSFA FVHRSLSAHS VLVNSHLVCK VARLGHSPQG PSCLLRWAAP EVIAHGKHTT SSDVWSFGIL MWEVMSYGER PYWDMSEQEV LNAIEQEFRL PPPPGCPPGL HLLMLDTWQK DRARRPHFDQ LVAAFDKMIR KPDTLQAGGD PGERPSQALL TPVALDFPCL DSPQAWLSAI GLECYQDNFS KFGLCTFSDV AQLSLEDLPA LGITLAGHQK KLLHHIQLLQ QHLRQQGSVE V //