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O43921

- EFNA2_HUMAN

UniProt

O43921 - EFNA2_HUMAN

Protein

Ephrin-A2

Gene

EFNA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Cell surface GPI-bound 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. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis By similarity.By similarity

    GO - Molecular functioni

    1. ephrin receptor binding Source: RefGenome

    GO - Biological processi

    1. axon guidance Source: RefGenome
    2. bone remodeling Source: UniProtKB
    3. cell-cell signaling Source: ProtInc
    4. ephrin receptor signaling pathway Source: UniProtKB
    5. olfactory bulb development Source: Ensembl
    6. osteoclast differentiation Source: UniProtKB

    Enzyme and pathway databases

    SignaLinkiO43921.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin-A2
    Alternative name(s):
    EPH-related receptor tyrosine kinase ligand 6
    Short name:
    LERK-6
    HEK7 ligand
    Short name:
    HEK7-L
    Gene namesi
    Name:EFNA2
    Synonyms:EPLG6, LERK6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3222. EFNA2.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. neuromuscular junction Source: Ensembl
    3. perikaryon Source: Ensembl
    4. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27657.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 188164Ephrin-A2PRO_0000008361Add
    BLAST
    Propeptidei189 – 21325Removed in mature formSequence AnalysisPRO_0000008362Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi73 ↔ 1141 PublicationPROSITE-ProRule annotation
    Disulfide bondi102 ↔ 1631 PublicationPROSITE-ProRule annotation
    Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
    Lipidationi188 – 1881GPI-anchor amidated asparagineSequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiO43921.
    PRIDEiO43921.

    PTM databases

    PhosphoSiteiO43921.

    Miscellaneous databases

    PMAP-CutDBO43921.

    Expressioni

    Gene expression databases

    ArrayExpressiO43921.
    BgeeiO43921.
    CleanExiHS_EFNA2.
    GenevestigatoriO43921.

    Organism-specific databases

    HPAiCAB005178.

    Interactioni

    Subunit structurei

    Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5. Interacts with EPHA8; activates EPHA8.1 Publication

    Protein-protein interaction databases

    BioGridi108263. 5 interactions.
    DIPiDIP-48293N.
    IntActiO43921. 2 interactions.
    MINTiMINT-7013470.
    STRINGi9606.ENSP00000215368.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 405
    Beta strandi51 – 533
    Beta strandi59 – 635
    Beta strandi68 – 725
    Helixi83 – 853
    Beta strandi89 – 946
    Helixi96 – 1016
    Beta strandi107 – 1148
    Beta strandi125 – 1295
    Beta strandi147 – 1537
    Beta strandi165 – 1706

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WO3X-ray2.35B33-173[»]
    ProteinModelPortaliO43921.
    SMRiO43921. Positions 33-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43921.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 174141Ephrin RBDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ephrin family.PROSITE-ProRule annotation
    Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG252953.
    HOGENOMiHOG000234373.
    HOVERGENiHBG051447.
    InParanoidiO43921.
    KOiK05462.
    OMAiCSSPGGC.
    OrthoDBiEOG70W3FD.
    PhylomeDBiO43921.

    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.

    O43921-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPAQRPLLP LLLLLLPLPP PPFARAEDAA RANSDRYAVY WNRSNPRFHA    50
    GAGDDGGGYT VEVSINDYLD IYCPHYGAPL PPAERMEHYV LYMVNGEGHA 100
    SCDHRQRGFK RWECNRPAAP GGPLKFSEKF QLFTPFSLGF EFRPGHEYYY 150
    ISATPPNAVD RPCLRLKVYV RPTNETLYEA PEPIFTSNNS CSSPGGCRLF 200
    LSTIPVLWTL LGS 213
    Length:213
    Mass (Da):23,878
    Last modified:June 1, 1998 - v1
    Checksum:i33C9FB1A8168B2D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → A in CAA07435. (PubMed:9826538)Curated
    Sequence conflicti25 – 262RA → PP in CAA07435. (PubMed:9826538)Curated
    Sequence conflicti29 – 302AA → RR in CAA07435. (PubMed:9826538)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92896, U92893, U92894 Genomic DNA. Translation: AAC39577.1.
    AJ007292 mRNA. Translation: CAA07435.1.
    AC004258 Genomic DNA. Translation: AAC04896.1.
    CCDSiCCDS12061.1.
    PIRiJE0322.
    RefSeqiNP_001396.2. NM_001405.3.
    UniGeneiHs.741510.

    Genome annotation databases

    EnsembliENST00000215368; ENSP00000215368; ENSG00000099617.
    GeneIDi1943.
    KEGGihsa:1943.
    UCSCiuc002lry.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92896 , U92893 , U92894 Genomic DNA. Translation: AAC39577.1 .
    AJ007292 mRNA. Translation: CAA07435.1 .
    AC004258 Genomic DNA. Translation: AAC04896.1 .
    CCDSi CCDS12061.1.
    PIRi JE0322.
    RefSeqi NP_001396.2. NM_001405.3.
    UniGenei Hs.741510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WO3 X-ray 2.35 B 33-173 [» ]
    ProteinModelPortali O43921.
    SMRi O43921. Positions 33-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108263. 5 interactions.
    DIPi DIP-48293N.
    IntActi O43921. 2 interactions.
    MINTi MINT-7013470.
    STRINGi 9606.ENSP00000215368.

    Chemistry

    ChEMBLi CHEMBL1795109.

    PTM databases

    PhosphoSitei O43921.

    Proteomic databases

    PaxDbi O43921.
    PRIDEi O43921.

    Protocols and materials databases

    DNASUi 1943.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215368 ; ENSP00000215368 ; ENSG00000099617 .
    GeneIDi 1943.
    KEGGi hsa:1943.
    UCSCi uc002lry.2. human.

    Organism-specific databases

    CTDi 1943.
    GeneCardsi GC19P001286.
    HGNCi HGNC:3222. EFNA2.
    HPAi CAB005178.
    MIMi 602756. gene.
    neXtProti NX_O43921.
    PharmGKBi PA27657.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252953.
    HOGENOMi HOG000234373.
    HOVERGENi HBG051447.
    InParanoidi O43921.
    KOi K05462.
    OMAi CSSPGGC.
    OrthoDBi EOG70W3FD.
    PhylomeDBi O43921.

    Enzyme and pathway databases

    SignaLinki O43921.

    Miscellaneous databases

    EvolutionaryTracei O43921.
    GeneWikii EFNA2.
    GenomeRNAii 1943.
    NextBioi 7871.
    PMAP-CutDB O43921.
    PROi O43921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43921.
    Bgeei O43921.
    CleanExi HS_EFNA2.
    Genevestigatori O43921.

    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. "Characterization of the genes for mouse LERK-3/Ephrin-A3 (Epl3), mouse LERK-4/Ephrin-A4 (Epl4), and human LERK-6/Ephrin-A2 (EPLG6): conservation of intron/exon structure."
      Cerretti D.P., Nelson N.
      Genomics 47:131-135(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning, chromosomal mapping, and tissue expression of the gene encoding the human Eph-family kinase ligand ephrin-A2."
      Aasheim H.-C., Pedeutour F., Grosgeorge J., Logtenberg T.
      Biochem. Biophys. Res. Commun. 252:378-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 (2.35 ANGSTROMS) OF 33-177 IN COMPLEX WITH EPHA4, DISULFIDE BONDS, SUBUNIT.

    Entry informationi

    Entry nameiEFNA2_HUMAN
    AccessioniPrimary (citable) accession number: O43921
    Secondary accession number(s): O76020
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 111 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 19
      Human chromosome 19: 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