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Ephrin type-B receptor 1 (EC 2.7.10.1)

 EPHB1_MOUSE             Reviewed;         984 AA.
Q8CBF3; B1B1C2; Q3UY27; Q6PG23; Q8CBE2;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 139.
RecName: Full=Ephrin type-B receptor 1;
EC=2.7.10.1;
Flags: Precursor;
Name=Ephb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH NCK1.
TISSUE=Kidney;
PubMed=9430661; DOI=10.1074/jbc.273.3.1303;
Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.;
"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation
to c-Jun kinase.";
J. Biol. Chem. 273:1303-1308(1998).
[5]
INTERACTION WITH PICK1.
PubMed=9883737; DOI=10.1016/S0896-6273(00)80663-7;
Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
"PDZ proteins bind, cluster, and synaptically colocalize with Eph
receptors and their ephrin ligands.";
Neuron 21:1453-1463(1998).
[6]
INTERACTION WITH GRB7.
PubMed=12223469; DOI=10.1074/jbc.M203165200;
Han D.C., Shen T.L., Miao H., Wang B., Guan J.L.;
"EphB1 associates with Grb7 and regulates cell migration.";
J. Biol. Chem. 277:45655-45661(2002).
[7]
INTERACTION WITH GRB2; SHC1 AND SRC.
PubMed=12925710; DOI=10.1083/jcb.200302073;
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
chemotaxis.";
J. Cell Biol. 162:661-671(2003).
[8]
FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY
SYNAPSE FORMATION, AND SUBCELLULAR LOCATION.
PubMed=14691139; DOI=10.1083/jcb.200306033;
Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.;
"Multiple EphB receptor tyrosine kinases shape dendritic spines in the
hippocampus.";
J. Cell Biol. 163:1313-1326(2003).
[9]
DISRUPTION PHENOTYPE, FUNCTION IN RETINAL GLANGLION CELL AXON
GUIDANCE, AND DEVELOPMENTAL STAGE.
PubMed=12971893; DOI=10.1016/j.neuron.2003.08.017;
Williams S.E., Mann F., Erskine L., Sakurai T., Wei S., Rossi D.J.,
Gale N.W., Holt C.E., Mason C.A., Henkemeyer M.;
"Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic
chiasm.";
Neuron 39:919-935(2003).
[10]
FUNCTION IN NEUROGENESIS, IDENTIFICATION OF EFNB3 AS LIGAND, AND
TISSUE SPECIFICITY.
PubMed=18057206; DOI=10.1523/JNEUROSCI.4158-07.2007;
Chumley M.J., Catchpole T., Silvany R.E., Kernie S.G., Henkemeyer M.;
"EphB receptors regulate stem/progenitor cell proliferation,
migration, and polarity during hippocampal neurogenesis.";
J. Neurosci. 27:13481-13490(2007).
[11]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=18524895; DOI=10.1523/JNEUROSCI.0632-08.2008;
Lee R., Petros T.J., Mason C.A.;
"Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2
through inducing expression of the guidance receptor EphB1.";
J. Neurosci. 28:5910-5919(2008).
[12]
DISRUPTION PHENOTYPE.
PubMed=19025592; DOI=10.1186/1744-8069-4-60;
Han Y., Song X.S., Liu W.T., Henkemeyer M., Song X.J.;
"Targeted mutation of EphB1 receptor prevents development of
neuropathic hyperalgesia and physical dependence on morphine in
mice.";
Mol. Pain 4:60-60(2008).
[13]
UBIQUITINATION BY CBL, AND INTERACTION WITH CBL.
PubMed=18034775; DOI=10.1111/j.1600-0854.2007.00679.x;
Fasen K., Cerretti D.P., Huynh-Do U.;
"Ligand binding induces Cbl-dependent EphB1 receptor degradation
through the lysosomal pathway.";
Traffic 9:251-266(2008).
[14]
FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
transmembrane ephrin-B family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. Cognate/functional ephrin ligands for this receptor
include EFNB1, EFNB2 and EFNB3. During nervous system development,
regulates retinal axon guidance redirecting ipsilaterally
ventrotemporal retinal ganglion cells axons at the optic chiasm
midline. This probably requires repulsive interaction with EFNB2.
In the adult nervous system together with EFNB3, regulates
chemotaxis, proliferation and polarity of the hippocampus neural
progenitors. In addition to its role in axon guidance plays also
an important redundant role with other ephrin-B receptors in
development and maturation of dendritic spines and synapse
formation. May also regulate angiogenesis. More generally, may
play a role in targeted cell migration and adhesion. Upon
activation by EFNB1 and probably other ephrin-B ligands activates
the MAPK/ERK and the JNK signaling cascades to regulate cell
migration and adhesion respectively. Involved in the maintenance
of the pool of satellite cells (muscle stem cells) by promoting
their self-renewal and reducing their activation and
differentiation (PubMed:27446912). {ECO:0000269|PubMed:12971893,
ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:18057206,
ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:27446912}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Heterotetramer upon binding of the ligand. The
heterotetramer is composed of an ephrin dimer and a receptor
dimer. Oligomerization is probably required to induce biological
responses (By similarity). Interacts with EPHB6;
transphosphorylates EPHB6 to form an active signaling complex (By
similarity). Interacts with PICK1. Interacts (through Tyr-594)
with NCK1 (via SH2 domain); activates the JUN cascade to regulate
cell adhesion. The ligand-activated form interacts (through Tyr-
928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated
form interacts (residues within the catalytic domain) with GRB2
(via SH2 domain). Interacts with GRB2, SHC1 and SRC; activates the
MAPK/ERK cascade to regulate cell migration. Interacts with CBL;
regulates receptor degradation through ubiquitination. Interacts
with ACP1. {ECO:0000250|UniProtKB:P54762,
ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:12925710,
ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:9430661,
ECO:0000269|PubMed:9883737}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P54762}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P54762}. Early endosome membrane
{ECO:0000250|UniProtKB:P54762}. Cell projection, dendrite
{ECO:0000269|PubMed:14691139}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CBF3-1; Sequence=Displayed;
Name=2;
IsoId=Q8CBF3-2; Sequence=VSP_021595;
-!- TISSUE SPECIFICITY: Expressed in neural stem and progenitor cells
in the dentate gyrus (PubMed:18057206). Expressed in myogenic
progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:18057206,
ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: Expressed in growth cones of ventrotemporal
(uncrossed) retinal ganglion cells that give rise to ipsilateral
projections (at protein level) (PubMed:12971893, PubMed:18524895).
In myogenic progenitor cells, initially expressed early during
myogenic development (E11.5), down-regulated during the fetal
stage (lower levels at E17.5) to be re-expressed in postnatal
satellite cells (PubMed:27446912). {ECO:0000269|PubMed:12971893,
ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:27446912}.
-!- PTM: Phosphorylated. Autophosphorylation is stimulated by the
ligand EFNB1. Required for interaction with SH2 domain-containing
interactors, for activation of the MAPK/ERK and JUN signaling
cascades and for ubiquitination by CBL (By similarity).
{ECO:0000250|UniProtKB:P54762}.
-!- PTM: Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-
ubiquitination by CBL is regulated by SRC and leads to lysosomal
degradation. {ECO:0000269|PubMed:18034775}.
-!- DISRUPTION PHENOTYPE: Mice development is apparently normal.
However, they display a dramatic reduction of ipsilateral retinal
projection. Mice do not develop neuropathic algesia and physical
dependence to morphine. {ECO:0000269|PubMed:12971893,
ECO:0000269|PubMed:19025592}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AK036148; BAC29320.1; -; mRNA.
EMBL; AK036211; BAC29348.1; -; mRNA.
EMBL; AK135018; BAE22386.1; -; mRNA.
EMBL; CT025594; CAM23741.1; -; Genomic_DNA.
EMBL; AC109247; CAM23741.1; JOINED; Genomic_DNA.
EMBL; AC132684; CAM23741.1; JOINED; Genomic_DNA.
EMBL; AC156635; CAM23741.1; JOINED; Genomic_DNA.
EMBL; BC057301; AAH57301.1; -; mRNA.
CCDS; CCDS40742.1; -. [Q8CBF3-1]
CCDS; CCDS52901.1; -. [Q8CBF3-2]
RefSeq; NP_001161768.1; NM_001168296.1. [Q8CBF3-2]
RefSeq; NP_775623.3; NM_173447.3. [Q8CBF3-1]
UniGene; Mm.22897; -.
ProteinModelPortal; Q8CBF3; -.
SMR; Q8CBF3; -.
BioGrid; 234781; 3.
IntAct; Q8CBF3; 1.
STRING; 10090.ENSMUSP00000035129; -.
iPTMnet; Q8CBF3; -.
PhosphoSitePlus; Q8CBF3; -.
PaxDb; Q8CBF3; -.
PeptideAtlas; Q8CBF3; -.
PRIDE; Q8CBF3; -.
Ensembl; ENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537. [Q8CBF3-1]
Ensembl; ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537. [Q8CBF3-2]
GeneID; 270190; -.
KEGG; mmu:270190; -.
UCSC; uc009rfn.2; mouse. [Q8CBF3-1]
UCSC; uc012gzg.1; mouse. [Q8CBF3-2]
CTD; 2047; -.
MGI; MGI:1096337; Ephb1.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; Q8CBF3; -.
KO; K05110; -.
OMA; KACPAGM; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; Q8CBF3; -.
TreeFam; TF315608; -.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
ChiTaRS; Ephb1; mouse.
PRO; PR:Q8CBF3; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032537; -.
CleanEx; MM_EPHB1; -.
ExpressionAtlas; Q8CBF3; baseline and differential.
Genevisible; Q8CBF3; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0032433; C:filopodium tip; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; IDA:MGI.
GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI.
GO; GO:0021545; P:cranial nerve development; IMP:MGI.
GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB.
GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
GO; GO:0001771; P:immunological synapse formation; ISO:MGI.
GO; GO:1902725; P:negative regulation of satellite cell differentiation; IMP:UniProtKB.
GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; IMP:UniProtKB.
GO; GO:0061351; P:neural precursor cell proliferation; IMP:UniProtKB.
GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
GO; GO:0014719; P:skeletal muscle satellite cell activation; IMP:UniProtKB.
CDD; cd10476; EphR_LBD_B1; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034231; EphB1_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell adhesion; Cell membrane;
Cell projection; Complete proteome; Endosome; Glycoprotein; Kinase;
Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 984 Ephrin type-B receptor 1.
/FTId=PRO_0000260317.
TOPO_DOM 18 540 Extracellular. {ECO:0000255}.
TRANSMEM 541 563 Helical. {ECO:0000255}.
TOPO_DOM 564 984 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 201 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 322 432 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 433 528 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 619 882 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 911 975 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 625 633 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 982 984 PDZ-binding. {ECO:0000255}.
COMPBIAS 183 319 Cys-rich.
ACT_SITE 744 744 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 651 651 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 600 600 Phosphotyrosine.
{ECO:0000250|UniProtKB:P54753}.
MOD_RES 928 928 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 588 628 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021595.
CONFLICT 72 72 L -> Q (in Ref. 1; BAE22386).
{ECO:0000305}.
CONFLICT 187 187 L -> P (in Ref. 1; BAE22386).
{ECO:0000305}.
CONFLICT 194 194 K -> I (in Ref. 3; AAH57301).
{ECO:0000305}.
CONFLICT 641 641 P -> Q (in Ref. 1; BAC29348).
{ECO:0000305}.
CONFLICT 678 678 P -> R (in Ref. 3; AAH57301).
{ECO:0000305}.
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


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