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P29320 (EPHA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 3

EC=2.7.10.1
Alternative name(s):
EPH-like kinase 4
Short name=EK4
Short name=hEK4
HEK
Short name=Human embryo kinase
Tyrosine-protein kinase TYRO4
Tyrosine-protein kinase receptor ETK1
Short name=Eph-like tyrosine kinase 1
Gene names
Name:EPHA3
Synonyms:ETK, ETK1, HEK, TYRO4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length983 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands 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. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development. Ref.5

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling By similarity. Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Ref.5 Ref.6 Ref.7 Ref.9

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.5 Ref.9.

Isoform 2: Secreted Ref.5 Ref.9.

Tissue specificity

Widely expressed. Highest level in placenta.

Post-translational modification

Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1. Ref.5 Ref.9 Ref.10

Involvement in disease

Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: The gene represented in this entry may be involved in disease pathogenesis.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to retinoic acid

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

ephrin receptor signaling pathway

Inferred from direct assay Ref.5. Source: UniProtKB

fasciculation of motor neuron axon

Inferred from sequence or structural similarity. Source: UniProtKB

fasciculation of sensory neuron axon

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

regulation of Rho GTPase activity

Inferred from direct assay Ref.5. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from direct assay Ref.5. Source: UniProtKB

regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of focal adhesion assembly

Inferred from direct assay Ref.5. Source: UniProtKB

regulation of microtubule cytoskeleton organization

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentearly endosome

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay Ref.5Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29320-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P29320-2)

The sequence of this isoform differs from the canonical sequence as follows:
     532-539: SFSISGES → CMYYFNAV
     540-983: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.3
Chain21 – 983963Ephrin type-A receptor 3
PRO_0000016802

Regions

Topological domain21 – 541521Extracellular Potential
Transmembrane542 – 56524Helical; Potential
Topological domain566 – 983418Cytoplasmic Potential
Domain29 – 207179Eph LBD
Domain325 – 435111Fibronectin type-III 1
Domain436 – 53196Fibronectin type-III 2
Domain621 – 882262Protein kinase
Domain911 – 97565SAM
Nucleotide binding628 – 6336ATP
Nucleotide binding700 – 7067ATP
Nucleotide binding750 – 7512ATP
Motif981 – 9833PDZ-binding Potential
Compositional bias189 – 322134Cys-rich

Sites

Active site7461Proton acceptor By similarity
Binding site6531ATP

Amino acid modifications

Modified residue5961Phosphotyrosine; by autocatalysis Ref.5 Ref.10
Modified residue6021Phosphotyrosine; by autocatalysis Ref.5 Ref.10
Modified residue7011Phosphotyrosine; by autocatalysis Ref.10
Modified residue7791Phosphotyrosine; by autocatalysis Ref.5
Modified residue9371Phosphotyrosine By similarity
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence532 – 5398SFSISGES → CMYYFNAV in isoform 2.
VSP_002995
Alternative sequence540 – 983444Missing in isoform 2.
VSP_002996
Natural variant371T → K in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036086
Natural variant851N → S in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036087
Natural variant2071K → N in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.14
Corresponds to variant rs200567888 [ dbSNP | Ensembl ].
VAR_068853
Natural variant2291S → Y in a lung large cell carcinoma sample; somatic mutation. Ref.13
VAR_042126
Natural variant4491S → F in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.13
VAR_042127
Natural variant5181G → L in a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. Ref.13
VAR_042128
Natural variant5641I → V. Ref.13
Corresponds to variant rs55712516 [ dbSNP | Ensembl ].
VAR_042129
Natural variant5681C → S. Ref.13
Corresponds to variant rs56077781 [ dbSNP | Ensembl ].
VAR_042130
Natural variant5901L → P. Ref.13
Corresponds to variant rs56081642 [ dbSNP | Ensembl ].
VAR_042131
Natural variant6211I → L in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036088
Natural variant6601T → K in a lung carcinoma sample; somatic mutation. Ref.12
VAR_065831
Natural variant7661G → E in a lung adenocarcinoma sample; somatic mutation. Ref.13
VAR_042132
Natural variant7771A → G. Ref.13
Corresponds to variant rs34437982 [ dbSNP | Ensembl ].
VAR_042133
Natural variant8061D → N in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036089
Natural variant9141R → H. Ref.13
Corresponds to variant rs17801309 [ dbSNP | Ensembl ].
VAR_027919
Natural variant9241W → R. Ref.1 Ref.13
Corresponds to variant rs35124509 [ dbSNP | Ensembl ].
VAR_042134
Natural variant9331T → M in a lung carcinoma sample; somatic mutation. Ref.12
VAR_065832

Experimental info

Mutagenesis1331V → E: Loss of EFNA5-binding ability and function. Ref.6
Mutagenesis1521F → L: Loss of EFNA5-binding ability and function. Ref.6
Mutagenesis5961Y → F: 10-fold suppression of kinase activity; when associated with F-602. Full kinase activity; when associated with F-602 and F-742. Full kinase activity; when associated with F-602 and A-768. Ref.10
Mutagenesis6021Y → F: 10-fold suppression of kinase activity; when associated with F-596. Full kinase activity; when associated with F-596 and F-742. Full kinase activity; when associated with F-596 and A-768. Ref.10
Mutagenesis7421Y → F: Full kinase activity; when associated with F-596 and F-602. Ref.10
Mutagenesis7681S → A: Full kinase activity; when associated with F-596 and F-602. Ref.10
Sequence conflict9111T → S in AAA58633. Ref.1

Secondary structure

.................................................... 983
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: BE04DBF958245424

FASTA983110,131
        10         20         30         40         50         60 
MDCQLSILLL LSCSVLDSFG ELIPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE 

        70         80         90        100        110        120 
HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF 

       130        140        150        160        170        180 
NLYYMESDDD HGVKFREHQF TKIDTIAADE SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY 

       190        200        210        220        230        240 
LAFQDVGACV ALVSVRVYFK KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP 

       250        260        270        280        290        300 
RMYCSTEGEW LVPIGKCSCN AGYEERGFMC QACRPGFYKA LDGNMKCAKC PPHSSTQEDG 

       310        320        330        340        350        360 
SMNCRCENNY FRADKDPPSM ACTRPPSSPR NVISNINETS VILDWSWPLD TGGRKDVTFN 

       370        380        390        400        410        420 
IICKKCGWNI KQCEPCSPNV RFLPRQFGLT NTTVTVTDLL AHTNYTFEID AVNGVSELSS 

       430        440        450        460        470        480 
PPRQFAAVSI TTNQAAPSPV LTIKKDRTSR NSISLSWQEP EHPNGIILDY EVKYYEKQEQ 

       490        500        510        520        530        540 
ETSYTILRAR GTNVTISSLK PDTIYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGESS 

       550        560        570        580        590        600 
QVVMIAISAA VAIILLTVVI YVLIGRFCGY KSKHGADEKR LHFGNGHLKL PGLRTYVDPH 

       610        620        630        640        650        660 
TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV AIKTLKVGYT 

       670        680        690        700        710        720 
EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPVMIVTE YMENGSLDSF LRKHDAQFTV 

       730        740        750        760        770        780 
IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR NILINSNLVC KVSDFGLSRV LEDDPEAAYT 

       790        800        810        820        830        840 
TRGGKIPIRW TSPEAIAYRK FTSASDVWSY GIVLWEVMSY GERPYWEMSN QDVIKAVDEG 

       850        860        870        880        890        900 
YRLPPPMDCP AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN 

       910        920        930        940        950        960 
LLLDQSNVDI TTFRTTGDWL NGVWTAHCKE IFTGVEYSSC DTIAKISTDD MKKVGVTVVG 

       970        980 
PQKKIISSIK ALETQSKNGP VPV 

« Hide

Isoform 2 [UniParc].

Checksum: 14736950EF1153F1
Show »

FASTA53960,946

References

« Hide 'large scale' references
[1]"Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines."
Wicks I.P., Wilkinson D., Salvaris E., Boyd A.W.
Proc. Natl. Acad. Sci. U.S.A. 89:1611-1615(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-924.
[2]"Identification of a tumor-specific shared antigen derived from an Eph receptor and presented to CD4 T cells on HLA class II molecules."
Chiari R., Hames G., Stroobant V., Texier C., Maillere B., Boon T., Coulie P.G.
Cancer Res. 60:4855-4863(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Melanoma.
[3]"Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line."
Boyd A.W., Ward L.D., Wicks I.P., Simpson R.J., Salvaris E., Wilks A., Welch K., Loudovaris M., Rockman S., Busmanis I.
J. Biol. Chem. 267:3262-3267(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-29 AND 840-860, CHARACTERIZATION.
[4]"Unified nomenclature for Eph family receptors and their ligands, the ephrins."
Eph nomenclature committee
Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[5]"Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL-CELL ADHESION, EFNA5-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-596; TYR-602 AND TYR-779.
[6]"Dissecting the EphA3/Ephrin-A5 interactions using a novel functional mutagenesis screen."
Smith F.M., Vearing C., Lackmann M., Treutlein H., Himanen J., Chen K., Saul A., Nikolov D., Boyd A.W.
J. Biol. Chem. 279:9522-9531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: EPHRIN LIGAND-BINDING, OLIGOMERIZATION, MUTAGENESIS OF VAL-133 AND PHE-152, INTERACTION WITH CRK.
[7]"Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans."
Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.
Cell 123:291-304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ADAM10 AND EFNA5.
[8]"Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3."
Day B., To C., Himanen J.P., Smith F.M., Nikolov D.B., Boyd A.W., Lackmann M.
J. Biol. Chem. 280:26526-26532(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: EFNA5 LIGAND-BINDING.
[9]"PTP1B regulates Eph receptor function and trafficking."
Nievergall E., Janes P.W., Stegmayer C., Vail M.E., Haj F.G., Teng S.W., Neel B.G., Bastiaens P.I., Lackmann M.
J. Cell Biol. 191:1189-1203(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN1, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1, SUBCELLULAR LOCATION.
[10]"Autoregulation by the juxtamembrane region of the human ephrin receptor tyrosine kinase A3 (EphA3)."
Davis T.L., Walker J.R., Loppnau P., Butler-Cole C., Allali-Hassani A., Dhe-Paganon S.
Structure 16:873-884(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) OF 577-947 IN COMPLEX WITH ATP ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-596; TYR-602 AND TYR-701, MUTAGENESIS OF TYR-596; TYR-602; TYR-742 AND SER-768.
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-37; SER-85; LEU-621 AND ASN-806.
[12]"Somatic mutations of GUCY2F, EPHA3, and NTRK3 in human cancers."
Wood L.D., Calhoun E.S., Silliman N., Ptak J., Szabo S., Powell S.M., Riggins G.J., Wang T.L., Yan H., Gazdar A., Kern S.E., Pennacchio L., Kinzler K.W., Vogelstein B., Velculescu V.E.
Hum. Mutat. 27:1060-1061(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-660 AND MET-933.
[13]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-229; PHE-449; LEU-518; VAL-564; SER-568; PRO-590; GLU-766; GLY-777; HIS-914 AND ARG-924.
[14]"Mutational profiling of kinases in human tumours of pancreatic origin identifies candidate cancer genes in ductal and ampulla of vater carcinomas."
Corbo V., Ritelli R., Barbi S., Funel N., Campani D., Bardelli A., Scarpa A.
PLoS ONE 5:E12653-E12653(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-207.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83941 mRNA. Translation: AAA58633.1.
AF213459 mRNA. Translation: AAG43576.1.
AF213460 mRNA. Translation: AAG43577.1.
CCDSCCDS2922.1. [P29320-1]
CCDS46875.1. [P29320-2]
PIRA38224.
RefSeqNP_005224.2. NM_005233.5. [P29320-1]
NP_872585.1. NM_182644.2. [P29320-2]
UniGeneHs.123642.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSFX-ray1.77A577-947[»]
2QO2X-ray1.60A577-947[»]
2QO7X-ray1.60A577-947[»]
2QO9X-ray1.55A577-947[»]
2QOBX-ray1.65A609-947[»]
2QOCX-ray1.25A609-947[»]
2QODX-ray1.15A577-947[»]
2QOFX-ray1.20A577-947[»]
2QOIX-ray1.25A577-947[»]
2QOKX-ray1.20A577-947[»]
2QOLX-ray1.07A577-947[»]
2QONX-ray1.79A577-947[»]
2QOOX-ray1.25A577-947[»]
2QOQX-ray1.60A577-947[»]
3DZQX-ray1.75A609-947[»]
3FXXX-ray1.70A577-947[»]
3FY2X-ray1.80A577-947[»]
4G2FX-ray1.70A609-947[»]
4GK2X-ray2.20A609-947[»]
4GK3X-ray1.90A609-947[»]
4GK4X-ray2.10A609-947[»]
ProteinModelPortalP29320.
SMRP29320. Positions 26-529, 613-906, 909-975.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108356. 14 interactions.
DIPDIP-40307N.
IntActP29320. 5 interactions.
MINTMINT-7145005.
STRING9606.ENSP00000337451.

Chemistry

BindingDBP29320.
ChEMBLCHEMBL2363043.
GuidetoPHARMACOLOGY1823.

PTM databases

PhosphoSiteP29320.

Polymorphism databases

DMDM116241351.

Proteomic databases

MaxQBP29320.
PaxDbP29320.
PRIDEP29320.

Protocols and materials databases

DNASU2042.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336596; ENSP00000337451; ENSG00000044524. [P29320-1]
ENST00000452448; ENSP00000399926; ENSG00000044524. [P29320-2]
GeneID2042.
KEGGhsa:2042.
UCSCuc003dqx.1. human. [P29320-2]
uc003dqy.3. human. [P29320-1]

Organism-specific databases

CTD2042.
GeneCardsGC03P089239.
HGNCHGNC:3387. EPHA3.
HPACAB010462.
MIM114500. phenotype.
179611. gene.
neXtProtNX_P29320.
PharmGKBPA27819.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP29320.
KOK05104.
OMADMKKVGV.
OrthoDBEOG7VTDM6.
PhylomeDBP29320.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP29320.

Gene expression databases

ArrayExpressP29320.
BgeeP29320.
CleanExHS_EPHA3.
GenevestigatorP29320.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29320.
GeneWikiEPH_receptor_A3.
GenomeRNAi2042.
NextBio8295.
PROP29320.
SOURCESearch...

Entry information

Entry nameEPHA3_HUMAN
AccessionPrimary (citable) accession number: P29320
Secondary accession number(s): Q9H2V3, Q9H2V4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM