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Protein

Ephrin-B2

Gene

Efnb2

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 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
  • 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
  • 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
  • regulation of chemotaxis Source: UniProtKB
  • T cell costimulation Source: MGI
  • venous blood vessel morphogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105097. Efnb2.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • focal adhesion Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
Complete GO annotation...

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...)1 Publication1
Disulfide bondi65 ↔ 104Combined sources2 Publications
Disulfide bondi92 ↔ 156Combined sources2 Publications
Glycosylationi142N-linked (GlcNAc...)Sequence 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.

Developmental stagei

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

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

WithEntry#Exp.IntActNotes
Epha4Q031372EBI-1032676,EBI-1539152
SRCP129312EBI-1032676,EBI-621482From a different organism.

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi199395. 1 interactor.
DIPiDIP-29208N.
IntActiP52800. 4 interactors.
MINTiMINT-1959060.
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
Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP52800.
KOiK05463.
OMAiGSTRHND.
OrthoDBiEOG091G0BPC.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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.

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi199395. 1 interactor.
DIPiDIP-29208N.
IntActiP52800. 4 interactors.
MINTiMINT-1959060.
STRINGi10090.ENSMUSP00000001319.

PTM databases

iPTMnetiP52800.
PhosphoSitePlusiP52800.

Proteomic databases

PaxDbiP52800.
PeptideAtlasiP52800.
PRIDEiP52800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1948.
MGIiMGI:105097. Efnb2.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP52800.
KOiK05463.
OMAiGSTRHND.
OrthoDBiEOG091G0BPC.

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.

Miscellaneous databases

EvolutionaryTraceiP52800.
PROiP52800.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001300.
CleanExiMM_EFNB2.
MM_ELF2.
ExpressionAtlasiP52800. baseline and differential.
GenevisibleiP52800. MM.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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...

Entry informationi

Entry nameiEFNB2_MOUSE
AccessioniPrimary (citable) accession number: P52800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 144 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

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

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 one 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.