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Protein

Ephrin-B1

Gene

Efnb1

Organism
Mus musculus (Mouse)
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. Binds to the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. 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.1 Publication

GO - Molecular functioni

  • ephrin receptor binding Source: MGI

GO - Biological processi

  • axon guidance Source: MGI
  • embryonic pattern specification Source: MGI
  • ephrin receptor signaling pathway Source: GO_Central
  • neural crest cell migration Source: MGI
  • positive regulation of T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_278281. Ephrin signaling.
REACT_292566. EPH-Ephrin signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B1
Alternative name(s):
CEK5 receptor ligand
Short name:
CEK5-L
ELK ligand
Short name:
ELK-L
EPH-related receptor tyrosine kinase ligand 2
Short name:
LERK-2
Stimulated by retinoic acid gene 1 protein
Gene namesi
Name:Efnb1
Synonyms:Epl2, Eplg2, Lerk2, Stra1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:102708. Efnb1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 236212ExtracellularSequence AnalysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence AnalysisAdd
BLAST
Topological domaini258 – 34588CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 345321Ephrin-B1PRO_0000008388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 101PROSITE-ProRule annotation
Disulfide bondi89 ↔ 153PROSITE-ProRule annotation
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Modified residuei286 – 2861PhosphoserineBy similarity

Post-translational modificationi

Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP52795.
PaxDbiP52795.
PRIDEiP52795.

PTM databases

PhosphoSiteiP52795.

Expressioni

Tissue specificityi

Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disc.

Developmental stagei

Expressed in the floor plate throughout the period of commissural axon pathfinding.

Gene expression databases

BgeeiP52795.
CleanExiMM_EFNB1.
ExpressionAtlasiP52795. baseline and differential.
GenevestigatoriP52795.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2. Interacts with TLE1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Psen1P497692EBI-8107507,EBI-990067
SdcbpO089923EBI-8107507,EBI-538265

Protein-protein interaction databases

BioGridi199394. 4 interactions.
DIPiDIP-29206N.
IntActiP52795. 5 interactions.
MINTiMINT-1793539.
STRINGi10090.ENSMUSP00000050716.

Structurei

3D structure databases

ProteinModelPortaliP52795.
SMRiP52795. Positions 32-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 164135Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi343 – 3453PDZ-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

eggNOGiNOG262190.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP52795.
KOiK05463.
OMAiPDSFFNS.
OrthoDBiEOG7288S5.
PhylomeDBiP52795.

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.

P52795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARPGQRWLS KWLVAMVVLT LCRLATPLAK NLEPVSWSSL NPKFLSGKGL
60 70 80 90 100
VIYPKIGDKL DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT
110 120 130 140 150
CNKPHQEIRF TIKFQEFSPN YMGLEFKKYH DYYITSTSNG SLEGLENREG
160 170 180 190 200
GVCRTRTMKI VMKVGQDPNA VTPEQLTTSR PSKESDNTVK TATQAPGRGS
210 220 230 240 250
QGDSDGKHET VNQEEKSGPG AGGGGSGDSD SFFNSKVALF AAVGAGCVIF
260 270 280 290 300
LLIIIFLTVL LLKLRKRHRK HTQQRAAALS LSTLASPKGG SGTAGTEPSD
310 320 330 340
IIIPLRTTEN NYCPHYEKVS GDYGHPVYIV QEMPPQSPAN IYYKV
Length:345
Mass (Da):37,859
Last modified:October 1, 1996 - v1
Checksum:i8C96FD3DC5CBC405
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901S → T in AAA53231 (PubMed:7649373).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07602
, U07598, U07599, U07600 Genomic DNA. Translation: AAC53247.1.
Z48781 mRNA. Translation: CAA88695.1.
U12983 mRNA. Translation: AAA53231.1.
BC006797 mRNA. Translation: AAH06797.1.
BC021656 mRNA. Translation: AAH21656.1.
CCDSiCCDS30298.1.
PIRiI48780.
RefSeqiNP_034240.1. NM_010110.4.
UniGeneiMm.3374.

Genome annotation databases

EnsembliENSMUST00000052839; ENSMUSP00000050716; ENSMUSG00000031217.
GeneIDi13641.
KEGGimmu:13641.
UCSCiuc009tvi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07602
, U07598, U07599, U07600 Genomic DNA. Translation: AAC53247.1.
Z48781 mRNA. Translation: CAA88695.1.
U12983 mRNA. Translation: AAA53231.1.
BC006797 mRNA. Translation: AAH06797.1.
BC021656 mRNA. Translation: AAH21656.1.
CCDSiCCDS30298.1.
PIRiI48780.
RefSeqiNP_034240.1. NM_010110.4.
UniGeneiMm.3374.

3D structure databases

ProteinModelPortaliP52795.
SMRiP52795. Positions 32-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199394. 4 interactions.
DIPiDIP-29206N.
IntActiP52795. 5 interactions.
MINTiMINT-1793539.
STRINGi10090.ENSMUSP00000050716.

PTM databases

PhosphoSiteiP52795.

Proteomic databases

MaxQBiP52795.
PaxDbiP52795.
PRIDEiP52795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052839; ENSMUSP00000050716; ENSMUSG00000031217.
GeneIDi13641.
KEGGimmu:13641.
UCSCiuc009tvi.1. mouse.

Organism-specific databases

CTDi1947.
MGIiMGI:102708. Efnb1.

Phylogenomic databases

eggNOGiNOG262190.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP52795.
KOiK05463.
OMAiPDSFFNS.
OrthoDBiEOG7288S5.
PhylomeDBiP52795.

Enzyme and pathway databases

ReactomeiREACT_278281. Ephrin signaling.
REACT_292566. EPH-Ephrin signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

NextBioi284342.
PROiP52795.
SOURCEiSearch...

Gene expression databases

BgeeiP52795.
CleanExiMM_EFNB1.
ExpressionAtlasiP52795. baseline and differential.
GenevestigatoriP52795.

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. "Genomic organization and chromosomal localization of mouse Eplg2, a gene encoding a binding protein for the receptor tyrosine kinase elk."
    Fletcher F.A., Renshaw B., Hollingsworth T., Baum P., Lyman S.D., Jenkins N.A., Gilbert D.J., Copeland N.G., Davison B.L.
    Genomics 24:127-132(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  2. "Efficient cloning of cDNAs of retinoic acid-responsive genes in P19 embryonal carcinoma cells and characterization of a novel mouse gene, Stra1 (mouse LERK-2/Eplg2)."
    Bouillet P., Oulad-Abdelghani M., Vicaire S., Garnier J.-M., Schuhbaur B., Dolle P., Chambon P.
    Dev. Biol. 170:420-433(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "cDNA cloning and characterization of a ligand for the Cek5 receptor protein-tyrosine kinase."
    Shao H., Lou L., Pandey A., Pasquale E.B., Dixit V.M.
    J. Biol. Chem. 269:26606-26609(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. "Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
    Imondi R., Wideman C., Kaprielian Z.
    Development 127:1397-1410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  7. "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4."
    Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.
    BMB Rep. 44:199-204(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLE1.

Entry informationi

Entry nameiEFNB1_MOUSE
AccessioniPrimary (citable) accession number: P52795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 27, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.