EFNB1_HUMAN
ID EFNB1_HUMAN Reviewed; 346 AA.
AC P98172; D3DVU0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Ephrin-B1;
DE AltName: Full=EFL-3;
DE AltName: Full=ELK ligand;
DE Short=ELK-L;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 2;
DE Short=LERK-2;
DE Contains:
DE RecName: Full=Ephrin-B1 C-terminal fragment {ECO:0000303|PubMed:16930449};
DE Short=Ephrin-B1 CTF {ECO:0000303|PubMed:16930449};
DE Contains:
DE RecName: Full=Ephrin-B1 intracellular domain {ECO:0000303|PubMed:16930449};
DE Short=Ephrin-B1 ICD {ECO:0000303|PubMed:16930449};
DE Flags: Precursor;
GN Name=EFNB1; Synonyms=EFL3, EPLG2, LERK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Placenta;
RX PubMed=8070404; DOI=10.1002/j.1460-2075.1994.tb06685.x;
RA Beckmann M.P., Cerretti D.P., Baum P., Vanden Bos T., James L., Farrah T.,
RA Kozlosky C., Hollingsworth T., Shilling H., Maraskovsky E., Fletcher F.A.,
RA Lhotak V., Pawson T., Lyman S.D.;
RT "Molecular characterization of a family of ligands for eph-related tyrosine
RT kinase receptors.";
RL EMBO J. 13:3757-3762(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=7973638; DOI=10.1126/science.7973638;
RA Davis S., Gale N.W., Aldrich T.H., Maisonpierre P.C., Lhotak V., Pawson T.,
RA Goldfarb M., Yancopoulos G.D.;
RT "Ligands for EPH-related receptor tyrosine kinases that require membrane
RT attachment or clustering for activity.";
RL Science 266:816-819(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fletcher F.A., Huebner K., Shaffer L.G., Monaco A., Mueller U.,
RA Kozlosky C., Druck T., Simoneaux D.K., Fairweather N., Chelly J.,
RA Cerretti D.P., Belmont J.W., Beckmann M.P., Lyman S.D.;
RT "Assignment of the human Elk ligand gene, EPLG2, to chromosome region
RT Xq12.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GRIP1 AND GRIP2.
RC TISSUE=Fetal brain;
RX PubMed=10197531; DOI=10.1016/s0896-6273(00)80706-0;
RA Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H.,
RA Klein R.;
RT "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
RT membrane microdomains.";
RL Neuron 22:511-524(1999).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, NUCLEAR LOCALIZATION
RP SIGNAL, AND MUTAGENESIS OF 260-VAL--THR-273 AND 344-TYR--VAL-346.
RX PubMed=16930449; DOI=10.1186/1750-1326-1-2;
RA Tomita T., Tanaka S., Morohashi Y., Iwatsubo T.;
RT "Presenilin-dependent intramembrane cleavage of ephrin-B1.";
RL Mol. Neurodegener. 1:2-2(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP INTERACTION WITH TLE1.
RX PubMed=21429299; DOI=10.5483/bmbrep.2011.44.3.199;
RA Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.;
RT "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4.";
RL BMB Rep. 44:199-204(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANTS CFNS LEU-54 AND ILE-111.
RX PubMed=15124102; DOI=10.1086/421532;
RA Wieland I., Jakubiczka S., Muschke P., Cohen M., Thiele H., Gerlach K.L.,
RA Adams R.H., Wieacker P.;
RT "Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome.";
RL Am. J. Hum. Genet. 74:1209-1215(2004).
RN [16]
RP VARIANTS CFNS THR-62; SER-98; PRO-115; HIS-119; THR-119; SER-151; VAL-151;
RP PRO-155; ILE-158 AND VAL-158, AND VARIANT HIS-154.
RX PubMed=15166289; DOI=10.1073/pnas.0402819101;
RA Twigg S.R.F., Kan R., Babbs C., Bochukova E.G., Robertson S.P., Wall S.A.,
RA Morriss-Kay G.M., Wilkie A.O.M.;
RT "Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation,
RT cause craniofrontonasal syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8652-8657(2004).
RN [17]
RP VARIANTS CFNS ARG-27; LEU-54; SER-119; HIS-119; ALA-137; PHE-138; SER-151;
RP SER-153; TYR-153 AND ARG-182.
RX PubMed=15959873; DOI=10.1002/humu.20193;
RA Wieland I., Reardon W., Jakubiczka S., Franco B., Kress W.,
RA Vincent-Delorme C., Thierry P., Edwards M., Koenig R., Rusu C.,
RA Schweiger S., Thompson E., Tinschert S., Stewart F., Wieacker P.;
RT "Twenty-six novel EFNB1 mutations in familial and sporadic
RT craniofrontonasal syndrome (CFNS).";
RL Hum. Mutat. 26:113-118(2005).
CC -!- FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family
CC of receptor tyrosine kinases which are crucial for migration, repulsion
CC and adhesion during neuronal, vascular and epithelial development
CC (PubMed:8070404, PubMed:7973638). Binding to Eph receptors residing on
CC adjacent cells leads to contact-dependent bidirectional signaling into
CC neighboring cells (PubMed:8070404, PubMed:7973638). Shows high affinity
CC for the receptor tyrosine kinase EPHB1/ELK (PubMed:8070404,
CC PubMed:7973638). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds
CC to, and induces collapse of, commissural axons/growth cones in vitro
CC (By similarity). May play a role in constraining the orientation of
CC longitudinally projecting axons (By similarity).
CC {ECO:0000250|UniProtKB:P52795, ECO:0000269|PubMed:7973638,
CC ECO:0000269|PubMed:8070404}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via
CC PDZ domain 6) (PubMed:10197531). Interacts with TLE1 (PubMed:21429299).
CC The intracellular domain peptide interacts with ZHX2; the interaction
CC enhances ZHX2 transcriptional repression activity (By similarity).
CC {ECO:0000250|UniProtKB:P52795, ECO:0000269|PubMed:10197531,
CC ECO:0000269|PubMed:21429299}.
CC -!- INTERACTION:
CC P98172; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-538287, EBI-12109402;
CC P98172; P04626: ERBB2; NbExp=11; IntAct=EBI-538287, EBI-641062;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10197531,
CC ECO:0000269|PubMed:7973638}; Single-pass type I membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:10197531}. Note=May
CC recruit GRIP1 and GRIP2 to membrane raft domains.
CC {ECO:0000269|PubMed:10197531}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-B1 C-terminal fragment]: Cell membrane
CC {ECO:0000269|PubMed:16930449}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-B1 intracellular domain]: Nucleus
CC {ECO:0000269|PubMed:16930449}. Note=Colocalizes with ZHX2 in the
CC nucleus. {ECO:0000250|UniProtKB:P52795}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:8070404, PubMed:7973638).
CC Detected in both neuronal and non-neuronal tissues (PubMed:8070404,
CC PubMed:7973638). Seems to have particularly strong expression in
CC retina, sciatic nerve, heart and spinal cord (PubMed:7973638).
CC {ECO:0000269|PubMed:7973638, ECO:0000269|PubMed:8070404}.
CC -!- INDUCTION: Up-regulated in response to TNF.
CC {ECO:0000269|PubMed:8070404}.
CC -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC domain. {ECO:0000269|PubMed:7973638}.
CC -!- PTM: Proteolytically processed. The ectodomain is cleaved, probably by
CC a metalloprotease, to produce a membrane-tethered C-terminal fragment.
CC This fragment is then further processed by the gamma-secretase complex
CC to yield a soluble intracellular domain peptide which can translocate
CC to the nucleus. The intracellular domain peptide is highly labile
CC suggesting that it is targeted for degradation by the proteasome.
CC {ECO:0000269|PubMed:16930449}.
CC -!- DISEASE: Craniofrontonasal syndrome (CFNS) [MIM:304110]: X-linked
CC inherited syndrome characterized by hypertelorism, coronal synostosis
CC with brachycephaly, downslanting palpebral fissures, clefting of the
CC nasal tip, joint anomalies, longitudinally grooved fingernails and
CC other digital anomalies. {ECO:0000269|PubMed:15124102,
CC ECO:0000269|PubMed:15166289, ECO:0000269|PubMed:15959873}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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; U09304; AAA53093.1; -; mRNA.
DR EMBL; L37361; AAA52369.1; -; mRNA.
DR EMBL; U09303; AAB41127.1; -; mRNA.
DR EMBL; AL136092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05370.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05371.1; -; Genomic_DNA.
DR EMBL; BC016649; AAH16649.1; -; mRNA.
DR EMBL; BC052979; AAH52979.1; -; mRNA.
DR CCDS; CCDS14391.1; -.
DR PIR; S46993; S46993.
DR RefSeq; NP_004420.1; NM_004429.4.
DR PDB; 6THG; X-ray; 4.07 A; C/D/F/H/J=29-167.
DR PDBsum; 6THG; -.
DR AlphaFoldDB; P98172; -.
DR SMR; P98172; -.
DR BioGRID; 108267; 256.
DR CORUM; P98172; -.
DR IntAct; P98172; 43.
DR MINT; P98172; -.
DR STRING; 9606.ENSP00000204961; -.
DR GlyGen; P98172; 1 site.
DR iPTMnet; P98172; -.
DR PhosphoSitePlus; P98172; -.
DR BioMuta; EFNB1; -.
DR DMDM; 1706668; -.
DR EPD; P98172; -.
DR jPOST; P98172; -.
DR MassIVE; P98172; -.
DR MaxQB; P98172; -.
DR PaxDb; P98172; -.
DR PeptideAtlas; P98172; -.
DR PRIDE; P98172; -.
DR ProteomicsDB; 57806; -.
DR Antibodypedia; 43761; 589 antibodies from 36 providers.
DR DNASU; 1947; -.
DR Ensembl; ENST00000204961.5; ENSP00000204961.4; ENSG00000090776.6.
DR GeneID; 1947; -.
DR KEGG; hsa:1947; -.
DR MANE-Select; ENST00000204961.5; ENSP00000204961.4; NM_004429.5; NP_004420.1.
DR UCSC; uc004dxd.5; human.
DR CTD; 1947; -.
DR DisGeNET; 1947; -.
DR GeneCards; EFNB1; -.
DR HGNC; HGNC:3226; EFNB1.
DR HPA; ENSG00000090776; Low tissue specificity.
DR MalaCards; EFNB1; -.
DR MIM; 300035; gene.
DR MIM; 304110; phenotype.
DR neXtProt; NX_P98172; -.
DR OpenTargets; ENSG00000090776; -.
DR Orphanet; 1520; Craniofrontonasal dysplasia.
DR PharmGKB; PA27661; -.
DR VEuPathDB; HostDB:ENSG00000090776; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000160128; -.
DR HOGENOM; CLU_072080_0_0_1; -.
DR InParanoid; P98172; -.
DR OMA; CNKPQQE; -.
DR OrthoDB; 903831at2759; -.
DR PhylomeDB; P98172; -.
DR PathwayCommons; P98172; -.
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 SignaLink; P98172; -.
DR SIGNOR; P98172; -.
DR BioGRID-ORCS; 1947; 13 hits in 710 CRISPR screens.
DR ChiTaRS; EFNB1; human.
DR GeneWiki; EFNB1; -.
DR GenomeRNAi; 1947; -.
DR Pharos; P98172; Tbio.
DR PRO; PR:P98172; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P98172; protein.
DR Bgee; ENSG00000090776; Expressed in ventricular zone and 124 other tissues.
DR Genevisible; P98172; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR CDD; cd10426; Ephrin-B_Ectodomain; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034255; Ephrin-B_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Craniosynostosis; Developmental protein;
KW Differentiation; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 28..346
FT /note="Ephrin-B1"
FT /id="PRO_0000008387"
FT CHAIN 218..346
FT /note="Ephrin-B1 C-terminal fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445791"
FT CHAIN 260..346
FT /note="Ephrin-B1 intracellular domain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445792"
FT TOPO_DOM 28..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..164
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 169..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..294
FT /note="Interaction with ZHX2"
FT /evidence="ECO:0000250|UniProtKB:P52795"
FT MOTIF 260..273
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16930449"
FT MOTIF 344..346
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 170..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 89..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT VARIANT 27
FT /note="P -> R (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023127"
FT VARIANT 54
FT /note="P -> L (in CFNS; dbSNP:rs104894801)"
FT /evidence="ECO:0000269|PubMed:15124102,
FT ECO:0000269|PubMed:15959873"
FT /id="VAR_023128"
FT VARIANT 62
FT /note="I -> T (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023129"
FT VARIANT 98
FT /note="L -> S (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023130"
FT VARIANT 111
FT /note="T -> I (in CFNS; dbSNP:rs104894796)"
FT /evidence="ECO:0000269|PubMed:15124102"
FT /id="VAR_023131"
FT VARIANT 115
FT /note="Q -> P (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023132"
FT VARIANT 119
FT /note="P -> H (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289,
FT ECO:0000269|PubMed:15959873"
FT /id="VAR_023133"
FT VARIANT 119
FT /note="P -> S (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023134"
FT VARIANT 119
FT /note="P -> T (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023135"
FT VARIANT 137
FT /note="T -> A (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023136"
FT VARIANT 138
FT /note="S -> F (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023137"
FT VARIANT 151
FT /note="G -> S (in CFNS; dbSNP:rs28936069)"
FT /evidence="ECO:0000269|PubMed:15166289,
FT ECO:0000269|PubMed:15959873"
FT /id="VAR_023138"
FT VARIANT 151
FT /note="G -> V (in CFNS; dbSNP:rs28936070)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023139"
FT VARIANT 153
FT /note="C -> S (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023140"
FT VARIANT 153
FT /note="C -> Y (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023141"
FT VARIANT 154
FT /note="R -> H (in dbSNP:rs146636295)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023142"
FT VARIANT 155
FT /note="T -> P (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023143"
FT VARIANT 158
FT /note="M -> I (in CFNS; dbSNP:rs28935170)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023144"
FT VARIANT 158
FT /note="M -> V (in CFNS; dbSNP:rs28936071)"
FT /evidence="ECO:0000269|PubMed:15166289"
FT /id="VAR_023145"
FT VARIANT 172
FT /note="T -> M (in dbSNP:rs7889678)"
FT /id="VAR_059256"
FT VARIANT 182
FT /note="S -> R (in CFNS)"
FT /evidence="ECO:0000269|PubMed:15959873"
FT /id="VAR_023146"
FT VARIANT 189
FT /note="V -> A (in dbSNP:rs16989105)"
FT /id="VAR_023147"
FT MUTAGEN 260..273
FT /note="Missing: The intracellular domain peptide fails to
FT localize to the nucleus."
FT /evidence="ECO:0000269|PubMed:16930449"
FT MUTAGEN 344..346
FT /note="Missing: No effect on gamma-secretase mediated
FT proteolysis of the C-terminal fragment."
FT /evidence="ECO:0000269|PubMed:16930449"
SQ SEQUENCE 346 AA; 38007 MW; 473DD2F1A5BF89DE CRC64;
MARPGQRWLG KWLVAMVVWA LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL
DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNRPEQEIRF TIKFQEFSPN
YMGLEFKKHH DYYITSTSNG SLEGLENREG GVCRTRTMKI IMKVGQDPNA VTPEQLTTSR
PSKEADNTVK MATQAPGSRG SLGDSDGKHE TVNQEEKSGP GASGGSSGDP DGFFNSKVAL
FAAVGAGCVI FLLIIIFLTV LLLKLRKRHR KHTQQRAAAL SLSTLASPKG GSGTAGTEPS
DIIIPLRTTE NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
