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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

  • ephrin receptor binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000099617-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiO43921.
SIGNORiO43921.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3222. EFNA2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi1943.
OpenTargetsiENSG00000099617.
PharmGKBiPA27657.

Chemistry databases

ChEMBLiCHEMBL1795109.

Polymorphism and mutation databases

BioMutaiEFNA2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000000836125 – 188Ephrin-A2Add BLAST164
PropeptideiPRO_0000008362189 – 213Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi73 ↔ 114PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 163PROSITE-ProRule annotation1 Publication
Glycosylationi174N-linked (GlcNAc...)Sequence analysis1
Lipidationi188GPI-anchor amidated asparagineSequence analysis1
Glycosylationi188N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiO43921.
PeptideAtlasiO43921.
PRIDEiO43921.

PTM databases

iPTMnetiO43921.
PhosphoSitePlusiO43921.

Miscellaneous databases

PMAP-CutDBO43921.

Expressioni

Gene expression databases

BgeeiENSG00000099617.
CleanExiHS_EFNA2.
GenevisibleiO43921. HS.

Organism-specific databases

HPAiCAB005178.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • ephrin receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi108263. 4 interactors.
DIPiDIP-48293N.
IntActiO43921. 2 interactors.
MINTiMINT-7013470.
STRINGi9606.ENSP00000215368.

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 40Combined sources5
Beta strandi51 – 53Combined sources3
Beta strandi59 – 63Combined sources5
Beta strandi68 – 72Combined sources5
Helixi83 – 85Combined sources3
Beta strandi89 – 94Combined sources6
Helixi96 – 101Combined sources6
Beta strandi107 – 114Combined sources8
Beta strandi125 – 129Combined sources5
Beta strandi147 – 153Combined sources7
Beta strandi165 – 170Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO43921.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 174Ephrin RBDPROSITE-ProRule annotationAdd BLAST141

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

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiO43921.
KOiK05462.
OMAiGSCQLFL.
OrthoDBiEOG091G0LOO.
PhylomeDBiO43921.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti6R → A in CAA07435 (PubMed:9826538).Curated1
Sequence conflicti25 – 26RA → PP in CAA07435 (PubMed:9826538).Curated2
Sequence conflicti29 – 30AA → RR in CAA07435 (PubMed:9826538).Curated2

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.3. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WO3X-ray2.35B33-173[»]
ProteinModelPortaliO43921.
SMRiO43921.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108263. 4 interactors.
DIPiDIP-48293N.
IntActiO43921. 2 interactors.
MINTiMINT-7013470.
STRINGi9606.ENSP00000215368.

Chemistry databases

ChEMBLiCHEMBL1795109.

PTM databases

iPTMnetiO43921.
PhosphoSitePlusiO43921.

Polymorphism and mutation databases

BioMutaiEFNA2.

Proteomic databases

PaxDbiO43921.
PeptideAtlasiO43921.
PRIDEiO43921.

Protocols and materials databases

DNASUi1943.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215368; ENSP00000215368; ENSG00000099617.
GeneIDi1943.
KEGGihsa:1943.
UCSCiuc002lry.3. human.

Organism-specific databases

CTDi1943.
DisGeNETi1943.
GeneCardsiEFNA2.
HGNCiHGNC:3222. EFNA2.
HPAiCAB005178.
MIMi602756. gene.
neXtProtiNX_O43921.
OpenTargetsiENSG00000099617.
PharmGKBiPA27657.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiO43921.
KOiK05462.
OMAiGSCQLFL.
OrthoDBiEOG091G0LOO.
PhylomeDBiO43921.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000099617-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiO43921.
SIGNORiO43921.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000099617.
CleanExiHS_EFNA2.
GenevisibleiO43921. HS.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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...

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: November 2, 2016
This is version 131 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

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 one 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.