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Protein

Ephrin-B2

Gene

EFNB2

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

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • 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
  • negative regulation of neuron projection development Source: ARUK-UCL
  • positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of neuron death Source: ARUK-UCL
  • regulation of chemotaxis Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Host cell receptor for virus entry, Receptor
Biological processAngiogenesis, Differentiation, Host-virus interaction, Neurogenesis

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000125266.6
HGNCiHGNC:3227 EFNB2
MIMi600527 gene
neXtProtiNX_P52799

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 domaini28 – 229ExtracellularSequence analysisAdd BLAST202
Transmembranei230 – 250HelicalSequence analysisAdd BLAST21
Topological domaini251 – 333CytoplasmicSequence analysisAdd BLAST83

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...) asparagineSequence analysis2 Publications1
Disulfide bondi62 ↔ 101Combined sources5 Publications
Disulfide bondi89 ↔ 153Combined sources5 Publications
Glycosylationi139N-linked (GlcNAc...) asparagineSequence 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
ProteomicsDBi56538

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

Show more details

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108268, 68 interactors
DIPiDIP-46378N
IntActiP52799, 9 interactors
MINTiP52799
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

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00390000005839
HOGENOMiHOG000220931
HOVERGENiHBG051448
InParanoidiP52799
KOiK05463
OMAiNCARPDQ
OrthoDBiEOG091G0BPC
PhylomeDBiP52799

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.

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 No translation available.
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
ENST00000646441; ENSP00000493716; ENSG00000125266
GeneIDi1948
KEGGihsa:1948
UCSCiuc001vqi.4 human

Similar proteinsi

Entry informationi

Entry nameiEFNB2_HUMAN
AccessioniPrimary (citable) accession number: P52799
Secondary accession number(s): Q5JV56
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 18, 2018
This is version 167 of the entry and version 1 of the sequence. See 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

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