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Protein

Ephrin-A2

Gene

EFNA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: GO_Central

GO - Biological processi

  1. axon guidance Source: GO_Central
  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
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_228063. EPHA-mediated growth cone collapse.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
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. extracellular region Source: Reactome
  3. neuromuscular junction Source: Ensembl
  4. perikaryon Source: Ensembl
  5. plasma membrane Source: GO_Central
Complete GO annotation...

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 ↔ 114PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 163PROSITE-ProRule annotation1 Publication
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

BgeeiO43921.
CleanExiHS_EFNA2.
ExpressionAtlasiO43921. baseline and differential.
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 – 405Combined sources
Beta strandi51 – 533Combined sources
Beta strandi59 – 635Combined sources
Beta strandi68 – 725Combined sources
Helixi83 – 853Combined sources
Beta strandi89 – 946Combined sources
Helixi96 – 1016Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi147 – 1537Combined sources
Beta strandi165 – 1706Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015107.
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

        10         20         30         40         50
MAPAQRPLLP LLLLLLPLPP PPFARAEDAA RANSDRYAVY WNRSNPRFHA
60 70 80 90 100
GAGDDGGGYT VEVSINDYLD IYCPHYGAPL PPAERMEHYV LYMVNGEGHA
110 120 130 140 150
SCDHRQRGFK RWECNRPAAP GGPLKFSEKF QLFTPFSLGF EFRPGHEYYY
160 170 180 190 200
ISATPPNAVD RPCLRLKVYV RPTNETLYEA PEPIFTSNNS CSSPGGCRLF
210
LSTIPVLWTL LGS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL1795109.

PTM databases

PhosphoSiteiO43921.

Proteomic databases

PaxDbiO43921.
PRIDEiO43921.

Protocols and materials databases

DNASUi1943.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1943.
GeneCardsiGC19P001286.
HGNCiHGNC:3222. EFNA2.
HPAiCAB005178.
MIMi602756. gene.
neXtProtiNX_O43921.
PharmGKBiPA27657.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252953.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiO43921.
KOiK05462.
OMAiCSSPGGC.
OrthoDBiEOG70W3FD.
PhylomeDBiO43921.

Enzyme and pathway databases

ReactomeiREACT_228063. EPHA-mediated growth cone collapse.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
SignaLinkiO43921.

Miscellaneous databases

ChiTaRSiEFNA2. human.
EvolutionaryTraceiO43921.
GeneWikiiEFNA2.
GenomeRNAii1943.
NextBioi7871.
PMAP-CutDBO43921.
PROiO43921.
SOURCEiSearch...

Gene expression databases

BgeeiO43921.
CleanExiHS_EFNA2.
ExpressionAtlasiO43921. baseline and differential.
GenevestigatoriO43921.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 116 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

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 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.