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Protein

Ephrin type-A receptor 3

Gene

EPHA3

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

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei653ATP1
Active sitei746Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi628 – 633ATP6
Nucleotide bindingi700 – 706ATP7
Nucleotide bindingi750 – 751ATP2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • GPI-linked ephrin receptor activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cell migration Source: UniProtKB
  • cellular response to retinoic acid Source: BHF-UCL
  • ephrin receptor signaling pathway Source: UniProtKB
  • fasciculation of motor neuron axon Source: UniProtKB
  • fasciculation of sensory neuron axon Source: UniProtKB
  • positive regulation of neuron projection development Source: BHF-UCL
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of epithelial to mesenchymal transition Source: UniProtKB
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00578-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP29320.
SIGNORiP29320.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EPHA3
Synonyms:ETK, ETK1, HEK, TYRO4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3387. EPHA3.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 541ExtracellularSequence analysisAdd BLAST521
Transmembranei542 – 565HelicalSequence analysisAdd BLAST24
Topological domaini566 – 983CytoplasmicSequence analysisAdd BLAST418

GO - Cellular componenti

  • early endosome Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Colorectal cancer (CRC)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:114500

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi133V → E: Loss of EFNA5-binding ability and function. 1 Publication1
Mutagenesisi152F → L: Loss of EFNA5-binding ability and function. 1 Publication1
Mutagenesisi596Y → 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. 1 Publication1
Mutagenesisi602Y → 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. 1 Publication1
Mutagenesisi742Y → F: Full kinase activity; when associated with F-596 and F-602. 1 Publication1
Mutagenesisi768S → A: Full kinase activity; when associated with F-596 and F-602. 1 Publication1

Organism-specific databases

DisGeNETi2042.
MIMi114500. phenotype.
OpenTargetsiENSG00000044524.
PharmGKBiPA27819.

Chemistry databases

ChEMBLiCHEMBL4954.
GuidetoPHARMACOLOGYi1823.

Polymorphism and mutation databases

BioMutaiEPHA3.
DMDMi116241351.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000001680221 – 983Ephrin type-A receptor 3Add BLAST963

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi232N-linked (GlcNAc...)Sequence analysis1
Glycosylationi337N-linked (GlcNAc...)Sequence analysis1
Glycosylationi391N-linked (GlcNAc...)Sequence analysis1
Glycosylationi404N-linked (GlcNAc...)Sequence analysis1
Glycosylationi493N-linked (GlcNAc...)Sequence analysis1
Modified residuei596Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei602Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei701Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei779Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei937PhosphotyrosineBy similarity1

Post-translational modificationi

Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP29320.
PaxDbiP29320.
PeptideAtlasiP29320.
PRIDEiP29320.

PTM databases

iPTMnetiP29320.
PhosphoSitePlusiP29320.

Expressioni

Tissue specificityi

Widely expressed. Highest level in placenta.

Gene expression databases

BgeeiENSG00000044524.
CleanExiHS_EPHA3.
ExpressionAtlasiP29320. baseline and differential.
GenevisibleiP29320. HS.

Organism-specific databases

HPAiCAB010462.

Interactioni

Subunit structurei

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.By similarity5 Publications

Protein-protein interaction databases

BioGridi108356. 21 interactors.
DIPiDIP-40307N.
IntActiP29320. 5 interactors.
MINTiMINT-7145005.
STRINGi9606.ENSP00000337451.

Chemistry databases

BindingDBiP29320.

Structurei

Secondary structure

1983
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Turni38 – 41Combined sources4
Beta strandi45 – 48Combined sources4
Beta strandi51 – 58Combined sources8
Beta strandi64 – 71Combined sources8
Beta strandi75 – 77Combined sources3
Beta strandi80 – 83Combined sources4
Beta strandi96 – 104Combined sources9
Helixi106 – 108Combined sources3
Beta strandi117 – 128Combined sources12
Beta strandi130 – 132Combined sources3
Helixi137 – 139Combined sources3
Beta strandi141 – 147Combined sources7
Helixi154 – 159Combined sources6
Beta strandi165 – 170Combined sources6
Beta strandi176 – 200Combined sources25
Turni610 – 612Combined sources3
Helixi618 – 620Combined sources3
Beta strandi621 – 629Combined sources9
Beta strandi631 – 641Combined sources11
Beta strandi647 – 654Combined sources8
Helixi661 – 674Combined sources14
Beta strandi685 – 689Combined sources5
Beta strandi691 – 694Combined sources4
Beta strandi696 – 700Combined sources5
Helixi707 – 712Combined sources6
Turni713 – 716Combined sources4
Helixi720 – 739Combined sources20
Helixi749 – 751Combined sources3
Beta strandi752 – 754Combined sources3
Beta strandi760 – 762Combined sources3
Helixi765 – 768Combined sources4
Helixi788 – 790Combined sources3
Helixi793 – 798Combined sources6
Helixi803 – 818Combined sources16
Turni819 – 821Combined sources3
Turni824 – 827Combined sources4
Helixi830 – 838Combined sources9
Helixi851 – 860Combined sources10
Helixi865 – 867Combined sources3
Helixi871 – 883Combined sources13
Helixi885 – 889Combined sources5
Beta strandi890 – 892Combined sources3
Beta strandi898 – 903Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4L0PX-ray2.26A29-201[»]
4P4CX-ray1.60A609-947[»]
4P5QX-ray1.35A606-947[»]
4P5ZX-ray2.00A606-947[»]
4TWNX-ray1.71A609-947[»]
4TWOX-ray2.05A609-947[»]
ProteinModelPortaliP29320.
SMRiP29320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 207Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini325 – 435Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini436 – 531Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini621 – 882Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini911 – 975SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi981 – 983PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi189 – 322Cys-richAdd BLAST134

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP29320.
KOiK05104.
OMAiSHGWEEI.
OrthoDBiEOG091G00W0.
PhylomeDBiP29320.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29320-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDCQLSILLL LSCSVLDSFG ELIPQPSNEV NLLDSKTIQG ELGWISYPSH
60 70 80 90 100
GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK
110 120 130 140 150
FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFREHQF TKIDTIAADE
160 170 180 190 200
SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK
210 220 230 240 250
KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW
260 270 280 290 300
LVPIGKCSCN AGYEERGFMC QACRPGFYKA LDGNMKCAKC PPHSSTQEDG
310 320 330 340 350
SMNCRCENNY FRADKDPPSM ACTRPPSSPR NVISNINETS VILDWSWPLD
360 370 380 390 400
TGGRKDVTFN IICKKCGWNI KQCEPCSPNV RFLPRQFGLT NTTVTVTDLL
410 420 430 440 450
AHTNYTFEID AVNGVSELSS PPRQFAAVSI TTNQAAPSPV LTIKKDRTSR
460 470 480 490 500
NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK
510 520 530 540 550
PDTIYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGESS QVVMIAISAA
560 570 580 590 600
VAIILLTVVI YVLIGRFCGY KSKHGADEKR LHFGNGHLKL PGLRTYVDPH
610 620 630 640 650
TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV
660 670 680 690 700
AIKTLKVGYT EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPVMIVTE
710 720 730 740 750
YMENGSLDSF LRKHDAQFTV IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR
760 770 780 790 800
NILINSNLVC KVSDFGLSRV LEDDPEAAYT TRGGKIPIRW TSPEAIAYRK
810 820 830 840 850
FTSASDVWSY GIVLWEVMSY GERPYWEMSN QDVIKAVDEG YRLPPPMDCP
860 870 880 890 900
AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN
910 920 930 940 950
LLLDQSNVDI TTFRTTGDWL NGVWTAHCKE IFTGVEYSSC DTIAKISTDD
960 970 980
MKKVGVTVVG PQKKIISSIK ALETQSKNGP VPV
Length:983
Mass (Da):110,131
Last modified:October 17, 2006 - v2
Checksum:iBE04DBF958245424
GO
Isoform 2 (identifier: P29320-2) [UniParc]FASTAAdd to basket

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

Show »
Length:539
Mass (Da):60,946
Checksum:i14736950EF1153F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti911T → S in AAA58633 (PubMed:1311845).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03608637T → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_03608785N → S in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_068853207K → N in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs200567888dbSNPEnsembl.1
Natural variantiVAR_042126229S → Y in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042127449S → F in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042128518G → L in a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_042129564I → V.1 PublicationCorresponds to variant rs55712516dbSNPEnsembl.1
Natural variantiVAR_042130568C → S.1 PublicationCorresponds to variant rs56077781dbSNPEnsembl.1
Natural variantiVAR_042131590L → P.1 PublicationCorresponds to variant rs56081642dbSNPEnsembl.1
Natural variantiVAR_036088621I → L in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_065831660T → K in a lung carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042132766G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042133777A → G.1 PublicationCorresponds to variant rs34437982dbSNPEnsembl.1
Natural variantiVAR_036089806D → N in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_027919914R → H.1 PublicationCorresponds to variant rs17801309dbSNPEnsembl.1
Natural variantiVAR_042134924W → R.2 PublicationsCorresponds to variant rs35124509dbSNPEnsembl.1
Natural variantiVAR_065832933T → M in a lung carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs372594677dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002995532 – 539SFSISGES → CMYYFNAV in isoform 2. 1 Publication8
Alternative sequenceiVSP_002996540 – 983Missing in isoform 2. 1 PublicationAdd BLAST444

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83941 mRNA. Translation: AAA58633.1.
AF213459 mRNA. Translation: AAG43576.1.
AF213460 mRNA. Translation: AAG43577.1.
CCDSiCCDS2922.1. [P29320-1]
CCDS46875.1. [P29320-2]
PIRiA38224.
RefSeqiNP_005224.2. NM_005233.5. [P29320-1]
NP_872585.1. NM_182644.2. [P29320-2]
UniGeneiHs.123642.

Genome annotation databases

EnsembliENST00000336596; ENSP00000337451; ENSG00000044524. [P29320-1]
ENST00000452448; ENSP00000399926; ENSG00000044524. [P29320-2]
GeneIDi2042.
KEGGihsa:2042.
UCSCiuc003dqx.2. human. [P29320-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83941 mRNA. Translation: AAA58633.1.
AF213459 mRNA. Translation: AAG43576.1.
AF213460 mRNA. Translation: AAG43577.1.
CCDSiCCDS2922.1. [P29320-1]
CCDS46875.1. [P29320-2]
PIRiA38224.
RefSeqiNP_005224.2. NM_005233.5. [P29320-1]
NP_872585.1. NM_182644.2. [P29320-2]
UniGeneiHs.123642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4L0PX-ray2.26A29-201[»]
4P4CX-ray1.60A609-947[»]
4P5QX-ray1.35A606-947[»]
4P5ZX-ray2.00A606-947[»]
4TWNX-ray1.71A609-947[»]
4TWOX-ray2.05A609-947[»]
ProteinModelPortaliP29320.
SMRiP29320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108356. 21 interactors.
DIPiDIP-40307N.
IntActiP29320. 5 interactors.
MINTiMINT-7145005.
STRINGi9606.ENSP00000337451.

Chemistry databases

BindingDBiP29320.
ChEMBLiCHEMBL4954.
GuidetoPHARMACOLOGYi1823.

PTM databases

iPTMnetiP29320.
PhosphoSitePlusiP29320.

Polymorphism and mutation databases

BioMutaiEPHA3.
DMDMi116241351.

Proteomic databases

MaxQBiP29320.
PaxDbiP29320.
PeptideAtlasiP29320.
PRIDEiP29320.

Protocols and materials databases

DNASUi2042.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336596; ENSP00000337451; ENSG00000044524. [P29320-1]
ENST00000452448; ENSP00000399926; ENSG00000044524. [P29320-2]
GeneIDi2042.
KEGGihsa:2042.
UCSCiuc003dqx.2. human. [P29320-1]

Organism-specific databases

CTDi2042.
DisGeNETi2042.
GeneCardsiEPHA3.
HGNCiHGNC:3387. EPHA3.
HPAiCAB010462.
MIMi114500. phenotype.
179611. gene.
neXtProtiNX_P29320.
OpenTargetsiENSG00000044524.
PharmGKBiPA27819.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP29320.
KOiK05104.
OMAiSHGWEEI.
OrthoDBiEOG091G00W0.
PhylomeDBiP29320.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS00578-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP29320.
SIGNORiP29320.

Miscellaneous databases

EvolutionaryTraceiP29320.
GeneWikiiEPH_receptor_A3.
GenomeRNAii2042.
PROiP29320.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000044524.
CleanExiHS_EPHA3.
ExpressionAtlasiP29320. baseline and differential.
GenevisibleiP29320. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHA3_HUMAN
AccessioniPrimary (citable) accession number: P29320
Secondary accession number(s): Q9H2V3, Q9H2V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 187 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.