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Protein

Ephrin-B2

Gene

EFNB2

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. 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
(Microbial infection) Acts as a receptor for Hendra virus and Nipah virus.4 Publications

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • animal organ morphogenesis Source: Ensembl
  • axon guidance Source: GO_Central
  • cell adhesion Source: UniProtKB
  • cell-cell signaling Source: ProtInc
  • cell migration involved in sprouting angiogenesis Source: UniProtKB
  • ephrin receptor signaling pathway Source: UniProtKB
  • lymph vessel development Source: Ensembl
  • negative regulation of keratinocyte proliferation Source: Ensembl
  • nephric duct morphogenesis Source: Ensembl
  • positive regulation of aorta morphogenesis Source: Ensembl
  • positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • regulation of chemotaxis Source: UniProtKB
  • T cell costimulation Source: Ensembl
  • venous blood vessel morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Host-virus interaction, Neurogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125266-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52799.
SIGNORiP52799.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B2
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 5
Short name:
LERK-5
HTK ligand
Short name:
HTK-L
Gene namesi
Name:EFNB2
Synonyms:EPLG5, HTKL, LERK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3227. EFNB2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 229ExtracellularSequence analysisAdd BLAST202
Transmembranei230 – 250HelicalSequence analysisAdd BLAST21
Topological domaini251 – 333CytoplasmicSequence analysisAdd BLAST83

GO - Cellular componenti

  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121 – 122LW → YM: Complete loss of Nipah protein G binding. 1 Publication2

Organism-specific databases

DisGeNETi1948.
OpenTargetsiENSG00000125266.
PharmGKBiPA27662.

Polymorphism and mutation databases

BioMutaiEFNB2.
DMDMi1706673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000000839228 – 333Ephrin-B2Add BLAST306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi36N-linked (GlcNAc...)Sequence analysis2 Publications1
Disulfide bondi62 ↔ 101Combined sources5 Publications
Disulfide bondi89 ↔ 153Combined sources5 Publications
Glycosylationi139N-linked (GlcNAc...)Sequence analysis1
Modified residuei260PhosphoserineBy similarity1
Modified residuei274PhosphothreonineBy similarity1
Modified residuei277Omega-N-methylarginineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiP52799.
MaxQBiP52799.
PaxDbiP52799.
PeptideAtlasiP52799.
PRIDEiP52799.

PTM databases

iPTMnetiP52799.
PhosphoSitePlusiP52799.

Expressioni

Tissue specificityi

Lung and kidney.

Gene expression databases

BgeeiENSG00000125266.
CleanExiHS_EFNB2.
GenevisibleiP52799. HS.

Organism-specific databases

HPAiCAB009368.
HPA008999.

Interactioni

Subunit structurei

Interacts with PDZRN3 (By similarity). Binds to the receptor tyrosine kinases EPHA4, EPHB4 and EPHA3.By similarity3 Publications
(Microbial infection) Interacts with Hendra virus and Nipah virus G protein (PubMed:16007075, PubMed:16477309, PubMed:17376907, PubMed:15998730).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK2O436397EBI-7532268,EBI-713635

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108268. 62 interactors.
DIPiDIP-46378N.
IntActiP52799. 3 interactors.
MINTiMINT-3019741.
STRINGi9606.ENSP00000245323.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 34Combined sources7
Turni44 – 46Combined sources3
Beta strandi47 – 50Combined sources4
Beta strandi57 – 62Combined sources6
Beta strandi65 – 68Combined sources4
Beta strandi75 – 81Combined sources7
Helixi83 – 87Combined sources5
Beta strandi98 – 101Combined sources4
Turni103 – 105Combined sources3
Beta strandi108 – 113Combined sources6
Beta strandi119 – 122Combined sources4
Beta strandi130 – 135Combined sources6
Helixi142 – 144Combined sources3
Beta strandi145 – 149Combined sources5
Helixi151 – 155Combined sources5
Beta strandi159 – 164Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLEX-ray2.05B28-165[»]
2I85NMR-A25-166[»]
2VSKX-ray3.30B/D28-165[»]
2VSMX-ray1.80B28-165[»]
2WO2X-ray2.45B27-167[»]
3GXUX-ray2.50B27-169[»]
4UF7X-ray1.70C/E27-167[»]
ProteinModelPortaliP52799.
SMRiP52799.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 164Ephrin RBDPROSITE-ProRule annotationAdd BLAST137

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi331 – 333PDZ-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.
InParanoidiP52799.
KOiK05463.
OMAiGSTRHND.
OrthoDBiEOG091G0BPC.
PhylomeDBiP52799.

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.

P52799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVRRDSVWK YCWGVLMVLC RTAISKSIVL EPIYWNSSNS KFLPGQGLVL
60 70 80 90 100
YPQIGDKLDI ICPKVDSKTV GQYEYYKVYM VDKDQADRCT IKKENTPLLN
110 120 130 140 150
CAKPDQDIKF TIKFQEFSPN LWGLEFQKNK DYYIISTSNG SLEGLDNQEG
160 170 180 190 200
GVCQTRAMKI LMKVGQDASS AGSTRNKDPT RRPELEAGTN GRSSTTSPFV
210 220 230 240 250
KPNPGSSTDG NSAGHSGNNI LGSEVALFAG IASGCIIFIV IIITLVVLLL
260 270 280 290 300
KYRRRHRKHS PQHTTTLSLS TLATPKRSGN NNGSEPSDII IPLRTADSVF
310 320 330
CPHYEKVSGD YGHPVYIVQE MPPQSPANIY YKV
Length:333
Mass (Da):36,923
Last modified:October 1, 1996 - v1
Checksum:i6D9932A632626AEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16797 mRNA. Translation: AAA99707.1.
L38734 mRNA. Translation: AAC41752.1.
U81262 mRNA. Translation: AAD03786.1.
AL138689 Genomic DNA. Translation: CAI39907.1.
BC069342 mRNA. Translation: AAH69342.1.
BC074856 mRNA. Translation: AAH74856.1.
BC074857 mRNA. Translation: AAH74857.1.
BC105955 mRNA. Translation: AAI05956.1.
BC105956 mRNA. Translation: AAI05957.1.
BC105957 mRNA. Translation: AAI05958.1.
CCDSiCCDS9507.1.
PIRiI84743.
RefSeqiNP_004084.1. NM_004093.3.
UniGeneiHs.149239.

Genome annotation databases

EnsembliENST00000245323; ENSP00000245323; ENSG00000125266.
GeneIDi1948.
KEGGihsa:1948.
UCSCiuc001vqi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16797 mRNA. Translation: AAA99707.1.
L38734 mRNA. Translation: AAC41752.1.
U81262 mRNA. Translation: AAD03786.1.
AL138689 Genomic DNA. Translation: CAI39907.1.
BC069342 mRNA. Translation: AAH69342.1.
BC074856 mRNA. Translation: AAH74856.1.
BC074857 mRNA. Translation: AAH74857.1.
BC105955 mRNA. Translation: AAI05956.1.
BC105956 mRNA. Translation: AAI05957.1.
BC105957 mRNA. Translation: AAI05958.1.
CCDSiCCDS9507.1.
PIRiI84743.
RefSeqiNP_004084.1. NM_004093.3.
UniGeneiHs.149239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLEX-ray2.05B28-165[»]
2I85NMR-A25-166[»]
2VSKX-ray3.30B/D28-165[»]
2VSMX-ray1.80B28-165[»]
2WO2X-ray2.45B27-167[»]
3GXUX-ray2.50B27-169[»]
4UF7X-ray1.70C/E27-167[»]
ProteinModelPortaliP52799.
SMRiP52799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108268. 62 interactors.
DIPiDIP-46378N.
IntActiP52799. 3 interactors.
MINTiMINT-3019741.
STRINGi9606.ENSP00000245323.

PTM databases

iPTMnetiP52799.
PhosphoSitePlusiP52799.

Polymorphism and mutation databases

BioMutaiEFNB2.
DMDMi1706673.

Proteomic databases

EPDiP52799.
MaxQBiP52799.
PaxDbiP52799.
PeptideAtlasiP52799.
PRIDEiP52799.

Protocols and materials databases

DNASUi1948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245323; ENSP00000245323; ENSG00000125266.
GeneIDi1948.
KEGGihsa:1948.
UCSCiuc001vqi.4. human.

Organism-specific databases

CTDi1948.
DisGeNETi1948.
GeneCardsiEFNB2.
HGNCiHGNC:3227. EFNB2.
HPAiCAB009368.
HPA008999.
MIMi600527. gene.
neXtProtiNX_P52799.
OpenTargetsiENSG00000125266.
PharmGKBiPA27662.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000005839.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiP52799.
KOiK05463.
OMAiGSTRHND.
OrthoDBiEOG091G0BPC.
PhylomeDBiP52799.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125266-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52799.
SIGNORiP52799.

Miscellaneous databases

ChiTaRSiEFNB2. human.
EvolutionaryTraceiP52799.
GeneWikiiEFNB2.
GenomeRNAii1948.
PROiP52799.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125266.
CleanExiHS_EFNB2.
GenevisibleiP52799. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P52799
Secondary accession number(s): Q5JV56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 153 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, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.