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P52799

- EFNB2_HUMAN

UniProt

P52799 - EFNB2_HUMAN

Protein

Ephrin-B2

Gene

EFNB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. axon guidance Source: RefGenome
    3. cell adhesion Source: UniProtKB
    4. cell-cell signaling Source: ProtInc
    5. cell migration involved in sprouting angiogenesis Source: UniProtKB
    6. ephrin receptor signaling pathway Source: UniProtKB
    7. lymph vessel development Source: Ensembl
    8. negative regulation of keratinocyte proliferation Source: Ensembl
    9. organ morphogenesis Source: Ensembl
    10. positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
    11. regulation of chemotaxis Source: UniProtKB
    12. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Angiogenesis, Differentiation, Host-virus interaction, Neurogenesis

    Enzyme and pathway databases

    SignaLinkiP52799.

    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
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:3227. EFNB2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi121 – 1222LW → YM: Complete loss of Nipah protein G binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA27662.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 333306Ephrin-B2PRO_0000008392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi62 ↔ 101
    Disulfide bondi89 ↔ 153
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP52799.
    PaxDbiP52799.
    PeptideAtlasiP52799.
    PRIDEiP52799.

    PTM databases

    PhosphoSiteiP52799.

    Expressioni

    Tissue specificityi

    Lung and kidney.

    Gene expression databases

    ArrayExpressiP52799.
    BgeeiP52799.
    CleanExiHS_EFNB2.
    GenevestigatoriP52799.

    Organism-specific databases

    HPAiCAB009368.
    HPA008999.

    Interactioni

    Subunit structurei

    Interacts with PDZRN3 By similarity. Binds to the receptor tyrosine kinases EPHA4, EPHB4 and EPHA3. Binds to Hendra virus and Nipah virus G protein.By similarity5 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi108268. 4 interactions.
    DIPiDIP-46378N.
    IntActiP52799. 1 interaction.
    MINTiMINT-3019741.
    STRINGi9606.ENSP00000245323.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 367
    Turni44 – 463
    Beta strandi47 – 504
    Beta strandi57 – 626
    Beta strandi65 – 684
    Beta strandi75 – 817
    Helixi83 – 886
    Beta strandi98 – 1014
    Turni103 – 1053
    Beta strandi108 – 1169
    Beta strandi130 – 1356
    Helixi142 – 1443
    Beta strandi145 – 1495
    Helixi151 – 1555
    Beta strandi159 – 1646

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP52799.
    SMRiP52799. Positions 25-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52799.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 229202ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini251 – 33383CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei230 – 25021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 164137Ephrin RBDPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi331 – 3333PDZ-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

    eggNOGiNOG261641.
    HOGENOMiHOG000220931.
    HOVERGENiHBG051448.
    InParanoidiP52799.
    KOiK05463.
    OMAiGSTRHND.
    OrthoDBiEOG7288S5.
    PhylomeDBiP52799.

    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.

    P52799-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVRRDSVWK YCWGVLMVLC RTAISKSIVL EPIYWNSSNS KFLPGQGLVL    50
    YPQIGDKLDI ICPKVDSKTV GQYEYYKVYM VDKDQADRCT IKKENTPLLN 100
    CAKPDQDIKF TIKFQEFSPN LWGLEFQKNK DYYIISTSNG SLEGLDNQEG 150
    GVCQTRAMKI LMKVGQDASS AGSTRNKDPT RRPELEAGTN GRSSTTSPFV 200
    KPNPGSSTDG NSAGHSGNNI LGSEVALFAG IASGCIIFIV IIITLVVLLL 250
    KYRRRHRKHS PQHTTTLSLS TLATPKRSGN NNGSEPSDII IPLRTADSVF 300
    CPHYEKVSGD YGHPVYIVQE MPPQSPANIY YKV 333
    Length:333
    Mass (Da):36,923
    Last modified:October 1, 1996 - v1
    Checksum:i6D9932A632626AEA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi1706673.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9507.1.
    PIRi I84743.
    RefSeqi NP_004084.1. NM_004093.3.
    UniGenei Hs.149239.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HLE X-ray 2.05 B 28-165 [» ]
    2I85 NMR - A 25-166 [» ]
    2VSK X-ray 3.30 B/D 28-165 [» ]
    2VSM X-ray 1.80 B 28-165 [» ]
    2WO2 X-ray 2.45 B 27-167 [» ]
    3GXU X-ray 2.50 B 27-169 [» ]
    ProteinModelPortali P52799.
    SMRi P52799. Positions 25-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108268. 4 interactions.
    DIPi DIP-46378N.
    IntActi P52799. 1 interaction.
    MINTi MINT-3019741.
    STRINGi 9606.ENSP00000245323.

    PTM databases

    PhosphoSitei P52799.

    Polymorphism databases

    DMDMi 1706673.

    Proteomic databases

    MaxQBi P52799.
    PaxDbi P52799.
    PeptideAtlasi P52799.
    PRIDEi P52799.

    Protocols and materials databases

    DNASUi 1948.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245323 ; ENSP00000245323 ; ENSG00000125266 .
    GeneIDi 1948.
    KEGGi hsa:1948.
    UCSCi uc001vqi.3. human.

    Organism-specific databases

    CTDi 1948.
    GeneCardsi GC13M107142.
    HGNCi HGNC:3227. EFNB2.
    HPAi CAB009368.
    HPA008999.
    MIMi 600527. gene.
    neXtProti NX_P52799.
    PharmGKBi PA27662.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261641.
    HOGENOMi HOG000220931.
    HOVERGENi HBG051448.
    InParanoidi P52799.
    KOi K05463.
    OMAi GSTRHND.
    OrthoDBi EOG7288S5.
    PhylomeDBi P52799.

    Enzyme and pathway databases

    SignaLinki P52799.

    Miscellaneous databases

    EvolutionaryTracei P52799.
    GeneWikii EFNB2.
    GenomeRNAii 1948.
    NextBioi 7895.
    PROi P52799.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52799.
    Bgeei P52799.
    CleanExi HS_EFNB2.
    Genevestigatori P52799.

    Family and domain databases

    Gene3Di 2.60.40.420. 1 hit.
    InterProi IPR008972. Cupredoxin.
    IPR001799. Ephrin.
    IPR019765. Ephrin_CS.
    [Graphical view ]
    PANTHERi PTHR11304. PTHR11304. 1 hit.
    Pfami PF00812. Ephrin. 1 hit.
    [Graphical view ]
    PRINTSi PR01347. EPHRIN.
    ProDomi PD002533. Ephrin. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF49503. SSF49503. 1 hit.
    PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
    PS51551. EPHRIN_RBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk."
      Bennett B.D., Zeigler F.C., Gu Q., Fendly B., Goddard A.D., Gillett N., Matthews W.
      Proc. Natl. Acad. Sci. U.S.A. 92:1866-1870(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas."
      Vogt T., Stolz W., Welsh J., Jung B., Kerbel R.S., Kobayashi H., Landthaler M., McClelland M.
      Clin. Cancer Res. 4:791-797(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Lung.
    6. "Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells."
      Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G.
      J. Cell Sci. 116:2461-2470(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    7. "EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus."
      Negrete O.A., Levroney E.L., Aguilar H.C., Bertolotti-Ciarlet A., Nazarian R., Tajyar S., Lee B.
      Nature 436:401-405(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIPAH VIRUS PROTEIN G.
    8. "Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus."
      Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W., Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.
      PLoS Pathog. 2:78-86(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIPAH VIRUS PROTEIN G, MUTAGENESIS OF 121-LEU-TRP-122.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity."
      Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R., Han G.W., Seifert J.M., Widmer H., Auer M., Kuhn P.
      J. Biol. Chem. 281:28185-28192(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 28-165 IN COMPLEX WITH EPHB4, DISULFIDE BONDS.
    11. "Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2."
      Bowden T.A., Aricescu A.R., Gilbert R.J., Grimes J.M., Jones E.Y., Stuart D.I.
      Nat. Struct. Mol. Biol. 15:567-572(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-165 IN COMPLEXES WITH NIPAH VIRUS AND HENDRA VIRUS GLYCOPROTEINS.
    12. "Structural plasticity of EPH receptor A4 facilitates cross-class ephrin signaling."
      Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.
      Structure 17:1386-1397(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 27-167 IN COMPLEX WITH EPHA4, DISULFIDE BONDS.
    13. "Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity."
      Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.
      J. Biol. Chem. 285:644-654(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-169 IN COMPLEX WITH EPHA4.

    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: October 1, 2014
    This is version 132 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

    External Data

    Dasty 3