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Protein

Ephrin-B3

Gene

EFNB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • transmembrane-ephrin receptor activity Source: ProtInc

GO - Biological processi

  • adult walking behavior Source: Ensembl
  • axon choice point recognition Source: Ensembl
  • axon guidance Source: GO_Central
  • cell-cell signaling Source: ProtInc
  • ephrin receptor signaling pathway Source: MGI
  • nervous system development Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Host-virus interaction, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_263952. EPHB-mediated forward signaling.
REACT_264047. Ephrin signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
SignaLinkiQ15768.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B3
Alternative name(s):
EPH-related receptor transmembrane ligand ELK-L3
EPH-related receptor tyrosine kinase ligand 8
Short name:
LERK-8
Gene namesi
Name:EFNB3
Synonyms:EPLG8, LERK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3228. EFNB3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 226199ExtracellularSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Topological domaini248 – 34093CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1252LW → YM: Complete loss of Nipah protein G binding. 1 Publication

Organism-specific databases

PharmGKBiPA27663.

Polymorphism and mutation databases

BioMutaiEFNB3.
DMDMi2494367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 340313Ephrin-B3PRO_0000008395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 104PROSITE-ProRule annotation
Disulfide bondi92 ↔ 156PROSITE-ProRule annotation
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Modified residuei274 – 2741Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ15768.
PRIDEiQ15768.

PTM databases

PhosphoSiteiQ15768.

Miscellaneous databases

PMAP-CutDBQ15768.

Expressioni

Tissue specificityi

Highly expressed in brain; expressed in embryonic floor plate, roof plate and hindbrain segments.

Gene expression databases

BgeeiQ15768.
CleanExiHS_EFNB3.
GenevisibleiQ15768. HS.

Organism-specific databases

HPAiHPA001623.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2. Binds to Nipah virus G protein.2 Publications

Protein-protein interaction databases

BioGridi108269. 12 interactions.
DIPiDIP-59196N.
IntActiQ15768. 4 interactions.
STRINGi9606.ENSP00000226091.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKFX-ray4.65C/D27-169[»]
ProteinModelPortaliQ15768.
SMRiQ15768. Positions 29-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 167140Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi338 – 3403PDZ-bindingSequence Analysis

Sequence similaritiesi

Belongs to the ephrin family.PROSITE-ProRule annotation
Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG268537.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiQ15768.
KOiK05463.
OMAiSSPSYEF.
OrthoDBiEOG7288S5.
PhylomeDBiQ15768.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15768-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPPHSGPGG VRVGALLLLG VLGLVSGLSL EPVYWNSANK RFQAEGGYVL
60 70 80 90 100
YPQIGDRLDL LCPRARPPGP HSSPNYEFYK LYLVGGAQGR RCEAPPAPNL
110 120 130 140 150
LLTCDRPDLD LRFTIKFQEY SPNLWGHEFR SHHDYYIIAT SDGTREGLES
160 170 180 190 200
LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP VSEMPMERDR GAAHSLEPGK
210 220 230 240 250
ENLPGDPTSN ATSRGAEGPL PPPSMPAVAG AAGGLALLLL GVAGAGGAMC
260 270 280 290 300
WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
310 320 330 340
GAADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV
Length:340
Mass (Da):35,835
Last modified:November 1, 1996 - v1
Checksum:iEDFF2A23C2FDE79F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661R → Q.
VAR_002356

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57001 mRNA. Translation: AAB05170.1.
U66406 mRNA. Translation: AAC51203.1.
U62775 mRNA. Translation: AAC50707.1.
AK314841 mRNA. Translation: BAG37359.1.
CH471108 Genomic DNA. Translation: EAW90133.1.
CH471108 Genomic DNA. Translation: EAW90135.1.
BC022499 mRNA. Translation: AAH22499.1.
BC042944 mRNA. Translation: AAH42944.1.
CCDSiCCDS11120.1.
RefSeqiNP_001397.1. NM_001406.3.
UniGeneiHs.26988.

Genome annotation databases

EnsembliENST00000226091; ENSP00000226091; ENSG00000108947.
GeneIDi1949.
KEGGihsa:1949.
UCSCiuc002gis.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57001 mRNA. Translation: AAB05170.1.
U66406 mRNA. Translation: AAC51203.1.
U62775 mRNA. Translation: AAC50707.1.
AK314841 mRNA. Translation: BAG37359.1.
CH471108 Genomic DNA. Translation: EAW90133.1.
CH471108 Genomic DNA. Translation: EAW90135.1.
BC022499 mRNA. Translation: AAH22499.1.
BC042944 mRNA. Translation: AAH42944.1.
CCDSiCCDS11120.1.
RefSeqiNP_001397.1. NM_001406.3.
UniGeneiHs.26988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKFX-ray4.65C/D27-169[»]
ProteinModelPortaliQ15768.
SMRiQ15768. Positions 29-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108269. 12 interactions.
DIPiDIP-59196N.
IntActiQ15768. 4 interactions.
STRINGi9606.ENSP00000226091.

PTM databases

PhosphoSiteiQ15768.

Polymorphism and mutation databases

BioMutaiEFNB3.
DMDMi2494367.

Proteomic databases

PaxDbiQ15768.
PRIDEiQ15768.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226091; ENSP00000226091; ENSG00000108947.
GeneIDi1949.
KEGGihsa:1949.
UCSCiuc002gis.3. human.

Organism-specific databases

CTDi1949.
GeneCardsiGC17P007608.
HGNCiHGNC:3228. EFNB3.
HPAiHPA001623.
MIMi602297. gene.
neXtProtiNX_Q15768.
PharmGKBiPA27663.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG268537.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiQ15768.
KOiK05463.
OMAiSSPSYEF.
OrthoDBiEOG7288S5.
PhylomeDBiQ15768.

Enzyme and pathway databases

ReactomeiREACT_263952. EPHB-mediated forward signaling.
REACT_264047. Ephrin signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
SignaLinkiQ15768.

Miscellaneous databases

ChiTaRSiEFNB3. human.
GeneWikiiEFNB3.
GenomeRNAii1949.
NextBioi7899.
PMAP-CutDBQ15768.
PROiQ15768.
SOURCEiSearch...

Gene expression databases

BgeeiQ15768.
CleanExiHS_EFNB3.
GenevisibleiQ15768. HS.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cerretti D.P.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA cloning, chromosomal localization, and expression pattern of EPLG8, a new member of the EPLG gene family encoding ligands of EPH-related protein-tyrosine kinase receptors."
    Tang X.X., Pleasure D.E., Ikegaki N.
    Genomics 41:17-24(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments."
    Gale N.W., Flenniken A., Compton D.C., Jenkins N.A., Copeland N.G., Gilbert D.J., Davis S., Wilkinson D.G., Yancopoulos G.D.
    Oncogene 13:1343-1352(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain cortex.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-42.
  8. "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains."
    Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.
    Neuron 22:511-524(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRIP1 AND GRIP2.
    Tissue: Fetal brain.
  9. "Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus."
    Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W., Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.
    PLoS Pathog. 2:78-86(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NIPAH VIRUS PROTEIN G, MUTAGENESIS OF 124-LEU-TRP-125.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEFNB3_HUMAN
AccessioniPrimary (citable) accession number: Q15768
Secondary accession number(s): B2RBW2
, D3DTQ6, O00680, Q8TBH7, Q92875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.