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UniProtKB - P29320 (EPHA3_HUMAN)

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Protein

Ephrin type-A receptor 3

Gene

EPHA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
View the complete GO annotation on QuickGO ...

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
  • negative regulation of endocytosis Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of protein localization to plasma membrane Source: UniProtKB
  • 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
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processCell adhesion
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000044524.10
HGNCiHGNC:3387 EPHA3
MIMi179611 gene
neXtProtiNX_P29320

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

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

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...) asparagineSequence analysis1
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi493N-linked (GlcNAc...) asparagineSequence 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
ProteomicsDBi54536
54537 [P29320-2]

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, 28 interactors
DIPiDIP-40307N
IntActiP29320, 9 interactors
MINTiP29320
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

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

CDDicd10481 EphR_LBD_A3, 1 hit
cd00063 FN3, 2 hits
Gene3Di2.60.120.260, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936 Eph_TM
IPR034266 EphA3_rcpt_lig-bd
IPR001090 Ephrin_rcpt_lig-bd_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR008979 Galactose-bd-like_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001660 SAM
IPR013761 SAM/pointed_sf
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
PfamiView protein in Pfam
PF14575 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
PIRSFiPIRSF000666 TyrPK_ephrin_receptor, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00615 EPH_lbd, 1 hit
SM01411 Ephrin_rec_like, 1 hit
SM00060 FN3, 2 hits
SM00454 SAM, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF49265 SSF49265, 1 hit
SSF49785 SSF49785, 1 hit
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits
PROSITEiView protein in PROSITE
PS01186 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

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 dbSNP:rs200567888Ensembl.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 → V1 PublicationCorresponds to variant dbSNP:rs55712516Ensembl.1
Natural variantiVAR_042130568C → S1 PublicationCorresponds to variant dbSNP:rs56077781Ensembl.1
Natural variantiVAR_042131590L → P1 PublicationCorresponds to variant dbSNP:rs56081642Ensembl.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 → G1 PublicationCorresponds to variant dbSNP:rs34437982Ensembl.1
Natural variantiVAR_036089806D → N in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_027919914R → H1 PublicationCorresponds to variant dbSNP:rs17801309Ensembl.1
Natural variantiVAR_042134924W → R2 PublicationsCorresponds to variant dbSNP:rs35124509Ensembl.1
Natural variantiVAR_065832933T → M in a lung carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs372594677Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiEPHA3_HUMAN
AccessioniPrimary (citable) accession number: P29320
Secondary accession number(s): Q9H2V3, Q9H2V4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 17, 2006
Last modified: June 20, 2018
This is version 196 of the entry and version 2 of the sequence. See 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

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