EPHB1_MOUSE
ID EPHB1_MOUSE Reviewed; 984 AA.
AC Q8CBF3; B1B1C2; Q3UY27; Q6PG23; Q8CBE2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ephrin type-B receptor 1;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=Ephb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH NCK1.
RC TISSUE=Kidney;
RX PubMed=9430661; DOI=10.1074/jbc.273.3.1303;
RA Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.;
RT "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to
RT c-Jun kinase.";
RL J. Biol. Chem. 273:1303-1308(1998).
RN [5]
RP INTERACTION WITH PICK1.
RX PubMed=9883737; DOI=10.1016/s0896-6273(00)80663-7;
RA Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
RA Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
RT "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors
RT and their ephrin ligands.";
RL Neuron 21:1453-1463(1998).
RN [6]
RP INTERACTION WITH GRB7.
RX PubMed=12223469; DOI=10.1074/jbc.m203165200;
RA Han D.C., Shen T.L., Miao H., Wang B., Guan J.L.;
RT "EphB1 associates with Grb7 and regulates cell migration.";
RL J. Biol. Chem. 277:45655-45661(2002).
RN [7]
RP INTERACTION WITH GRB2; SHC1 AND SRC.
RX PubMed=12925710; DOI=10.1083/jcb.200302073;
RA Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
RT "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
RT chemotaxis.";
RL J. Cell Biol. 162:661-671(2003).
RN [8]
RP FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE
RP FORMATION, AND SUBCELLULAR LOCATION.
RX PubMed=14691139; DOI=10.1083/jcb.200306033;
RA Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.;
RT "Multiple EphB receptor tyrosine kinases shape dendritic spines in the
RT hippocampus.";
RL J. Cell Biol. 163:1313-1326(2003).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION IN RETINAL GLANGLION CELL AXON GUIDANCE, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12971893; DOI=10.1016/j.neuron.2003.08.017;
RA Williams S.E., Mann F., Erskine L., Sakurai T., Wei S., Rossi D.J.,
RA Gale N.W., Holt C.E., Mason C.A., Henkemeyer M.;
RT "Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm.";
RL Neuron 39:919-935(2003).
RN [10]
RP FUNCTION IN NEUROGENESIS, IDENTIFICATION OF EFNB3 AS LIGAND, AND TISSUE
RP SPECIFICITY.
RX PubMed=18057206; DOI=10.1523/jneurosci.4158-07.2007;
RA Chumley M.J., Catchpole T., Silvany R.E., Kernie S.G., Henkemeyer M.;
RT "EphB receptors regulate stem/progenitor cell proliferation, migration, and
RT polarity during hippocampal neurogenesis.";
RL J. Neurosci. 27:13481-13490(2007).
RN [11]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18524895; DOI=10.1523/jneurosci.0632-08.2008;
RA Lee R., Petros T.J., Mason C.A.;
RT "Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2 through
RT inducing expression of the guidance receptor EphB1.";
RL J. Neurosci. 28:5910-5919(2008).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=19025592; DOI=10.1186/1744-8069-4-60;
RA Han Y., Song X.S., Liu W.T., Henkemeyer M., Song X.J.;
RT "Targeted mutation of EphB1 receptor prevents development of neuropathic
RT hyperalgesia and physical dependence on morphine in mice.";
RL Mol. Pain 4:60-60(2008).
RN [13]
RP UBIQUITINATION BY CBL, AND INTERACTION WITH CBL.
RX PubMed=18034775; DOI=10.1111/j.1600-0854.2007.00679.x;
RA Fasen K., Cerretti D.P., Huynh-Do U.;
RT "Ligand binding induces Cbl-dependent EphB1 receptor degradation through
RT the lysosomal pathway.";
RL Traffic 9:251-266(2008).
RN [14]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
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 neighboring
CC cells. The signaling pathway downstream of the receptor is referred to
CC as forward signaling while the signaling pathway downstream of the
CC ephrin ligand is referred to as reverse signaling. Cognate/functional
CC ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During
CC nervous system development, regulates retinal axon guidance redirecting
CC ipsilaterally ventrotemporal retinal ganglion cells axons at the optic
CC chiasm midline. This probably requires repulsive interaction with
CC EFNB2. In the adult nervous system together with EFNB3, regulates
CC chemotaxis, proliferation and polarity of the hippocampus neural
CC progenitors. In addition to its role in axon guidance also plays an
CC important redundant role with other ephrin-B receptors in development
CC and maturation of dendritic spines and synapse formation. May also
CC regulate angiogenesis. More generally, may play a role in targeted cell
CC migration and adhesion. Upon activation by EFNB1 and probably other
CC ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades
CC to regulate cell migration and adhesion respectively. Involved in the
CC maintenance of the pool of satellite cells (muscle stem cells) by
CC promoting their self-renewal and reducing their activation and
CC differentiation (PubMed:27446912). {ECO:0000269|PubMed:12971893,
CC ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:18057206,
CC ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:27446912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity).
CC Interacts with EPHB6; transphosphorylates EPHB6 to form an active
CC signaling complex (By similarity). Interacts with PICK1. Interacts
CC (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade
CC to regulate cell adhesion. The ligand-activated form interacts (through
CC Tyr-928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated
CC form interacts (residues within the catalytic domain) with GRB2 (via
CC SH2 domain). Interacts with GRB2, SHC1 and SRC; activates the MAPK/ERK
CC cascade to regulate cell migration. Interacts with CBL; regulates
CC receptor degradation through ubiquitination. Interacts with ACP1.
CC {ECO:0000250|UniProtKB:P54762, ECO:0000269|PubMed:12223469,
CC ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:18034775,
CC ECO:0000269|PubMed:9430661, ECO:0000269|PubMed:9883737}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54762};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54762}.
CC Early endosome membrane {ECO:0000250|UniProtKB:P54762}. Cell
CC projection, dendrite {ECO:0000269|PubMed:14691139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CBF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBF3-2; Sequence=VSP_021595;
CC -!- TISSUE SPECIFICITY: Expressed in neural stem and progenitor cells in
CC the dentate gyrus (PubMed:18057206). Expressed in myogenic progenitor
CC cells (PubMed:27446912). {ECO:0000269|PubMed:18057206,
CC ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Expressed in growth cones of ventrotemporal
CC (uncrossed) retinal ganglion cells that give rise to ipsilateral
CC projections (at protein level) (PubMed:12971893, PubMed:18524895). In
CC myogenic progenitor cells, initially expressed early during myogenic
CC development (11.5 dpc), down-regulated during the fetal stage (lower
CC levels at 17.5 dpc) to be re-expressed in postnatal satellite cells
CC (PubMed:27446912). {ECO:0000269|PubMed:12971893,
CC ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:27446912}.
CC -!- PTM: Phosphorylated. Autophosphorylation is stimulated by the ligand
CC EFNB1. Required for interaction with SH2 domain-containing interactors,
CC for activation of the MAPK/ERK and JUN signaling cascades and for
CC ubiquitination by CBL (By similarity). {ECO:0000250|UniProtKB:P54762}.
CC -!- PTM: Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-
CC ubiquitination by CBL is regulated by SRC and leads to lysosomal
CC degradation. {ECO:0000269|PubMed:18034775}.
CC -!- DISRUPTION PHENOTYPE: Mice development is apparently normal. However,
CC they display a dramatic reduction of ipsilateral retinal projection.
CC Mice do not develop neuropathic algesia and physical dependence to
CC morphine. {ECO:0000269|PubMed:12971893, ECO:0000269|PubMed:19025592}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AK036148; BAC29320.1; -; mRNA.
DR EMBL; AK036211; BAC29348.1; -; mRNA.
DR EMBL; AK135018; BAE22386.1; -; mRNA.
DR EMBL; AC109247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057301; AAH57301.1; -; mRNA.
DR CCDS; CCDS40742.1; -. [Q8CBF3-1]
DR CCDS; CCDS52901.1; -. [Q8CBF3-2]
DR RefSeq; NP_001161768.1; NM_001168296.1. [Q8CBF3-2]
DR RefSeq; NP_775623.3; NM_173447.3. [Q8CBF3-1]
DR AlphaFoldDB; Q8CBF3; -.
DR SMR; Q8CBF3; -.
DR BioGRID; 234781; 4.
DR IntAct; Q8CBF3; 1.
DR STRING; 10090.ENSMUSP00000035129; -.
DR GlyGen; Q8CBF3; 3 sites.
DR iPTMnet; Q8CBF3; -.
DR PhosphoSitePlus; Q8CBF3; -.
DR MaxQB; Q8CBF3; -.
DR PaxDb; Q8CBF3; -.
DR PeptideAtlas; Q8CBF3; -.
DR PRIDE; Q8CBF3; -.
DR ProteomicsDB; 277888; -. [Q8CBF3-1]
DR ProteomicsDB; 277889; -. [Q8CBF3-2]
DR Antibodypedia; 33398; 589 antibodies from 40 providers.
DR DNASU; 270190; -.
DR Ensembl; ENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537. [Q8CBF3-1]
DR Ensembl; ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537. [Q8CBF3-2]
DR GeneID; 270190; -.
DR KEGG; mmu:270190; -.
DR UCSC; uc009rfn.2; mouse. [Q8CBF3-1]
DR UCSC; uc012gzg.1; mouse. [Q8CBF3-2]
DR CTD; 2047; -.
DR MGI; MGI:1096337; Ephb1.
DR VEuPathDB; HostDB:ENSMUSG00000032537; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000155297; -.
DR HOGENOM; CLU_000288_141_0_1; -.
DR InParanoid; Q8CBF3; -.
DR OMA; MACKACP; -.
DR PhylomeDB; Q8CBF3; -.
DR TreeFam; TF315608; -.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 270190; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ephb1; mouse.
DR PRO; PR:Q8CBF3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CBF3; protein.
DR Bgee; ENSMUSG00000032537; Expressed in ear vesicle and 207 other tissues.
DR ExpressionAtlas; Q8CBF3; baseline and differential.
DR Genevisible; Q8CBF3; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0032433; C:filopodium tip; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI.
DR GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0021934; P:hindbrain tangential cell migration; ISO:MGI.
DR GO; GO:0001771; P:immunological synapse formation; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:1902725; P:negative regulation of satellite cell differentiation; IMP:UniProtKB.
DR GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; IMP:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
DR GO; GO:0014719; P:skeletal muscle satellite cell activation; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10476; EphR_LBD_B1; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd09551; SAM_EPH-B1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034231; EphB1_rcpt_lig-bd.
DR InterPro; IPR042819; EphB1_SAM.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; PF07714; PK_Tyr_Ser-Thr; 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; 1.
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 Alternative splicing; ATP-binding; Cell adhesion; Cell membrane;
KW Cell projection; Endosome; Glycoprotein; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..984
FT /note="Ephrin type-B receptor 1"
FT /id="PRO_0000260317"
FT TOPO_DOM 18..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..201
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 322..432
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 433..528
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 619..882
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 911..975
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 982..984
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 744
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 625..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 600
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P54753"
FT MOD_RES 928
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 588..628
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021595"
FT CONFLICT 72
FT /note="L -> Q (in Ref. 1; BAE22386)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="L -> P (in Ref. 1; BAE22386)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="K -> I (in Ref. 3; AAH57301)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="P -> Q (in Ref. 1; BAC29348)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="P -> R (in Ref. 3; AAH57301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 984 AA; 109881 MW; E967019C82AA400A CRC64;
MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV
CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV
IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY
GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC
NGDGEWMVPI GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC
KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP
QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN
SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP
LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGSPG MKIYIDPFTY
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK
QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ
LVGMLRGIAA GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS
SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD
YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGVTLAG
HQKKILSSIH SMRVQMNQSP SVMA
