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Reviewed, UniProtKB/Swiss-Prot O43921 (EFNA2_HUMAN)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ephrin-A2
Alternative name(s):
    EPH-related receptor tyrosine kinase ligand 6
      Short name=LERK-6
    HEK7-ligand
      Short name=HEK7-L
Gene names
Name: EFNA2
Synonyms: EPLG6, LERK6
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Subunit structure

Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Sequence similarities

Belongs to the ephrin family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
Gene Ontology (GO)
   Biological processcell-cell signaling Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionephrin receptor binding Ref.2

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 188164Ephrin-A2
PRO_0000008361
Propeptide189 – 21325Removed in mature form Potential
PRO_0000008362

Amino acid modifications

Lipidation1881GPI-anchor amidated asparagine Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Disulfide bond73 ↔ 114 By similarity

Experimental info

Sequence conflict61R → A in CAA07435. Ref.2
Sequence conflict25 – 262RA → PP in CAA07435. Ref.2
Sequence conflict29 – 302AA → RR in CAA07435. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O43921-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 33C9FB1A8168B2D0

FASTA21323,878
        10         20         30         40         50         60 
MAPAQRPLLP LLLLLLPLPP PPFARAEDAA RANSDRYAVY WNRSNPRFHA GAGDDGGGYT 

        70         80         90        100        110        120 
VEVSINDYLD IYCPHYGAPL PPAERMEHYV LYMVNGEGHA SCDHRQRGFK RWECNRPAAP 

       130        140        150        160        170        180 
GGPLKFSEKF QLFTPFSLGF EFRPGHEYYY ISATPPNAVD RPCLRLKVYV RPTNETLYEA 

       190        200        210 
PEPIFTSNNS CSSPGGCRLF LSTIPVLWTL LGS 

« Hide

References

« Hide 'large scale' references
[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: 9465306] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, chromosal 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: 9826538] [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. expand/collapse author list , 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: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

U92896, U92893, U92894 Genomic DNA. Translation: AAC39577.1.
AJ007292 mRNA. Translation: CAA07435.1.
AC004258 Genomic DNA. Translation: AAC04896.1.
IPIIPI00015159.
PIRJE0322.
RefSeqNP_001396.2.
UniGeneHs.532655

3D structure databases

HSSPHSSP built from PDB template 1KGY based on UniProtKB P52800.
ModBaseSearch...

Proteomic databases

PRIDEO43921.

Genome annotation databases

EnsemblENSG00000099617. Homo sapiens. [Contig view]
GeneID1943.
KEGGhsa:1943.

Organism-specific databases

GeneCardsGC19P001237.
H-InvDBHIX0040152.
HGNCHGNC:3222. EFNA2.
HPACAB005178.
MIM602756. gene.
PharmGKBPA27657.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO43921.
HOVERGENO43921.
OMAO43921. NNSCSSL.

Enzyme and pathway databases

Pathway_Interaction_DBepha_fwdpathway. EPHA forward signaling.

Gene expression databases

ArrayExpressO43921.
BgeeO43921.
CleanExHS_EFNA2.
GermOnlineENSG00000099617. Homo sapiens.

Family and domain databases

InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 1 hit.
PANTHERPTHR11304. Ephrin. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01299. EPHRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio7871.
PMAP-CutDBO43921.
SOURCESearch...

Entry information

Entry nameEFNA2_HUMAN
AccessionPrimary (citable) accession number: O43921
Secondary accession number(s): O76020
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents