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Protein

Ephrin-B2

Gene

Efnb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.1 Publication

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • signaling receptor binding Source: MGI

GO - Biological processi

  • animal organ morphogenesis Source: MGI
  • axon guidance Source: GO_Central
  • blood vessel morphogenesis Source: MGI
  • cell adhesion Source: UniProtKB
  • cell migration Source: GO_Central
  • cell migration involved in sprouting angiogenesis Source: UniProtKB
  • ephrin receptor signaling pathway Source: UniProtKB
  • lymph vessel development Source: MGI
  • negative regulation of keratinocyte proliferation Source: MGI
  • negative regulation of neuron projection development Source: MGI
  • nephric duct morphogenesis Source: MGI
  • positive regulation of aorta morphogenesis Source: MGI
  • positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of neuron death Source: MGI
  • regulation of chemotaxis Source: UniProtKB
  • T cell costimulation Source: MGI
  • venous blood vessel morphogenesis Source: MGI

Keywordsi

Molecular functionDevelopmental protein
Biological processAngiogenesis, Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-2682334 EPH-Ephrin signaling
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-3928664 Ephrin signaling
R-MMU-3928665 EPH-ephrin mediated repulsion of cells

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B2
Alternative name(s):
ELF-2
EPH-related receptor tyrosine kinase ligand 5
Short name:
LERK-5
HTK ligand
Short name:
HTK-L
Gene namesi
Name:Efnb2
Synonyms:Elf2, Epl5, Eplg5, Htkl, Lerk5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105097 Efnb2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 232ExtracellularSequence analysisAdd BLAST204
Transmembranei233 – 253HelicalSequence analysisAdd BLAST21
Topological domaini254 – 336CytoplasmicSequence analysisAdd BLAST83

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000839329 – 336Ephrin-B2Add BLAST308

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi65 ↔ 104Combined sources2 Publications
Disulfide bondi92 ↔ 156Combined sources2 Publications
Glycosylationi142N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei263PhosphoserineCombined sources1
Modified residuei277PhosphothreonineCombined sources1
Modified residuei280Omega-N-methylarginineCombined sources1

Post-translational modificationi

Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP52800
PeptideAtlasiP52800
PRIDEiP52800

PTM databases

iPTMnetiP52800
PhosphoSitePlusiP52800

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 disk (PubMed:7651410, PubMed:10704386). Expressed in myogenic progenitor cells (PubMed:27446912).3 Publications

Developmental stagei

Expressed in the floor plate throughout the period of commissural axon pathfinding (PubMed:7651410, PubMed:10704386). In myogenic progenitor cells, highly expressed during early development (E11.5) and progressively repressed as developments proceeds (PubMed:27446912).3 Publications

Gene expression databases

BgeeiENSMUSG00000001300
CleanExiMM_EFNB2
MM_ELF2
ExpressionAtlasiP52800 baseline and differential
GenevisibleiP52800 MM

Interactioni

Subunit structurei

Interacts with PDZRN3. Binds to the ephrin receptor EPHA3, EPHA4 and EPHB4 (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • signaling receptor binding Source: MGI

Protein-protein interaction databases

BioGridi199395, 1 interactor
DIPiDIP-29208N
IntActiP52800, 17 interactors
MINTiP52800
STRINGi10090.ENSMUSP00000001319

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni47 – 49Combined sources3
Beta strandi50 – 53Combined sources4
Beta strandi60 – 64Combined sources5
Beta strandi70 – 72Combined sources3
Beta strandi78 – 84Combined sources7
Helixi86 – 91Combined sources6
Beta strandi101 – 104Combined sources4
Beta strandi112 – 116Combined sources5
Beta strandi133 – 138Combined sources6
Helixi145 – 147Combined sources3
Helixi154 – 158Combined sources5
Beta strandi162 – 167Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IKOX-ray1.92P30-207[»]
1KGYX-ray2.70E/F/G/H31-168[»]
ProteinModelPortaliP52800
SMRiP52800
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52800

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 167Ephrin RBDPROSITE-ProRule annotationAdd BLAST137

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi334 – 336PDZ-bindingSequence analysis3

Sequence similaritiesi

Belongs to the ephrin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00390000005839
HOGENOMiHOG000220931
HOVERGENiHBG051448
InParanoidiP52800
KOiK05463
OMAiNCARPDQ
OrthoDBiEOG091G0BPC

Family and domain databases

CDDicd10426 Ephrin-B_Ectodomain, 1 hit
Gene3Di2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034255 Ephrin-B_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD
PANTHERiPTHR11304 PTHR11304, 1 hit
PfamiView protein in Pfam
PF00812 Ephrin, 1 hit
PRINTSiPR01347 EPHRIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
PROSITEiView protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P52800-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMARSRRDS VWKYCWGLLM VLCRTAISRS IVLEPIYWNS SNSKFLPGQG
60 70 80 90 100
LVLYPQIGDK LDIICPKVDS KTVGQYEYYK VYMVDKDQAD RCTIKKENTP
110 120 130 140 150
LLNCARPDQD VKFTIKFQEF SPNLWGLEFQ KNKDYYIIST SNGSLEGLDN
160 170 180 190 200
QEGGVCQTRA MKILMKVGQD ASSAGSARNH GPTRRPELEA GTNGRSSTTS
210 220 230 240 250
PFVKPNPGSS TDGNSAGHSG NNLLGSEVAL FAGIASGCII FIVIIITLVV
260 270 280 290 300
LLLKYRRRHR KHSPQHTTTL SLSTLATPKR GGNNNGSEPS DVIIPLRTAD
310 320 330
SVFCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
Length:336
Mass (Da):37,202
Last modified:October 1, 1996 - v1
Checksum:iD08894996E399554
GO

Sequence cautioni

The sequence AAC42052 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti177A → T in AAA99708 (PubMed:8559144).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16819 mRNA Translation: AAA99708.1
L38847 mRNA Translation: AAC42052.1 Different initiation.
U30244 mRNA Translation: AAA82934.1
BC057009 mRNA Translation: AAH57009.1
CCDSiCCDS22090.1
PIRiI49766
RefSeqiNP_034241.2, NM_010111.5
UniGeneiMm.209813

Genome annotation databases

EnsembliENSMUST00000001319; ENSMUSP00000001319; ENSMUSG00000001300
GeneIDi13642
KEGGimmu:13642
UCSCiuc009kue.1 mouse

Similar proteinsi

Entry informationi

Entry nameiEFNB2_MOUSE
AccessioniPrimary (citable) accession number: P52800
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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