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P29320

- EPHA3_HUMAN

UniProt

P29320 - EPHA3_HUMAN

Protein

Ephrin type-A receptor 3

Gene

EPHA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei653 – 6531ATP
    Active sitei746 – 7461Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi628 – 6336ATP
    Nucleotide bindingi700 – 7067ATP
    Nucleotide bindingi750 – 7512ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GPI-linked ephrin receptor activity Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell migration Source: UniProtKB
    3. cellular response to retinoic acid Source: BHF-UCL
    4. ephrin receptor signaling pathway Source: UniProtKB
    5. fasciculation of motor neuron axon Source: UniProtKB
    6. fasciculation of sensory neuron axon Source: UniProtKB
    7. positive regulation of neuron projection development Source: BHF-UCL
    8. regulation of actin cytoskeleton organization Source: UniProtKB
    9. regulation of epithelial to mesenchymal transition Source: UniProtKB
    10. regulation of focal adhesion assembly Source: UniProtKB
    11. regulation of microtubule cytoskeleton organization Source: UniProtKB
    12. regulation of Rho GTPase activity Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP29320.

    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
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3387. EPHA3.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331V → E: Loss of EFNA5-binding ability and function. 1 Publication
    Mutagenesisi152 – 1521F → L: Loss of EFNA5-binding ability and function. 1 Publication
    Mutagenesisi596 – 5961Y → 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 Publication
    Mutagenesisi602 – 6021Y → 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 Publication
    Mutagenesisi742 – 7421Y → F: Full kinase activity; when associated with F-596 and F-602. 1 Publication
    Mutagenesisi768 – 7681S → A: Full kinase activity; when associated with F-596 and F-602. 1 Publication

    Organism-specific databases

    MIMi114500. phenotype.
    PharmGKBiPA27819.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 983963Ephrin type-A receptor 3PRO_0000016802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
    Modified residuei596 – 5961Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei602 – 6021Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei701 – 7011Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei779 – 7791Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei937 – 9371PhosphotyrosineBy similarity

    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.
    PRIDEiP29320.

    PTM databases

    PhosphoSiteiP29320.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest level in placenta.

    Gene expression databases

    ArrayExpressiP29320.
    BgeeiP29320.
    CleanExiHS_EPHA3.
    GenevestigatoriP29320.

    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. 14 interactions.
    DIPiDIP-40307N.
    IntActiP29320. 5 interactions.
    MINTiMINT-7145005.
    STRINGi9606.ENSP00000337451.

    Structurei

    Secondary structure

    1
    983
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni610 – 6123
    Helixi618 – 6203
    Beta strandi621 – 6299
    Beta strandi631 – 64111
    Beta strandi647 – 6548
    Helixi661 – 67414
    Beta strandi685 – 6895
    Beta strandi691 – 6944
    Beta strandi696 – 7005
    Helixi707 – 7126
    Turni713 – 7164
    Helixi720 – 73920
    Helixi749 – 7513
    Beta strandi752 – 7543
    Beta strandi760 – 7623
    Helixi765 – 7673
    Helixi788 – 7903
    Helixi793 – 7986
    Helixi803 – 81816
    Turni819 – 8213
    Turni824 – 8274
    Helixi830 – 8389
    Helixi851 – 86010
    Helixi865 – 8673
    Helixi871 – 88313
    Helixi885 – 8895
    Beta strandi890 – 8923
    Beta strandi898 – 9036

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP29320.
    SMRiP29320. Positions 26-529, 613-906, 909-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29320.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 541521ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini566 – 983418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei542 – 56524HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 207179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini325 – 435111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini436 – 53196Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini621 – 882262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini911 – 97565SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi981 – 9833PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi189 – 322134Cys-richAdd
    BLAST

    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

    eggNOGiCOG0515.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiP29320.
    KOiK05104.
    OMAiDMKKVGV.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP29320.
    TreeFamiTF315608.

    Family and domain databases

    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. 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]
    PfamiPF14575. 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]
    PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00615. EPH_lbd. 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. Align

    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

    MDCQLSILLL LSCSVLDSFG ELIPQPSNEV NLLDSKTIQG ELGWISYPSH    50
    GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK 100
    FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFREHQF TKIDTIAADE 150
    SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK 200
    KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW 250
    LVPIGKCSCN AGYEERGFMC QACRPGFYKA LDGNMKCAKC PPHSSTQEDG 300
    SMNCRCENNY FRADKDPPSM ACTRPPSSPR NVISNINETS VILDWSWPLD 350
    TGGRKDVTFN IICKKCGWNI KQCEPCSPNV RFLPRQFGLT NTTVTVTDLL 400
    AHTNYTFEID AVNGVSELSS PPRQFAAVSI TTNQAAPSPV LTIKKDRTSR 450
    NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK 500
    PDTIYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGESS QVVMIAISAA 550
    VAIILLTVVI YVLIGRFCGY KSKHGADEKR LHFGNGHLKL PGLRTYVDPH 600
    TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV 650
    AIKTLKVGYT EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPVMIVTE 700
    YMENGSLDSF LRKHDAQFTV IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR 750
    NILINSNLVC KVSDFGLSRV LEDDPEAAYT TRGGKIPIRW TSPEAIAYRK 800
    FTSASDVWSY GIVLWEVMSY GERPYWEMSN QDVIKAVDEG YRLPPPMDCP 850
    AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN 900
    LLLDQSNVDI TTFRTTGDWL NGVWTAHCKE IFTGVEYSSC DTIAKISTDD 950
    MKKVGVTVVG PQKKIISSIK ALETQSKNGP VPV 983
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti911 – 9111T → S in AAA58633. (PubMed:1311845)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371T → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036086
    Natural varianti85 – 851N → S in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036087
    Natural varianti207 – 2071K → N in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication
    Corresponds to variant rs200567888 [ dbSNP | Ensembl ].
    VAR_068853
    Natural varianti229 – 2291S → Y in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042126
    Natural varianti449 – 4491S → F in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_042127
    Natural varianti518 – 5181G → L in a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. 1 Publication
    VAR_042128
    Natural varianti564 – 5641I → V.1 Publication
    Corresponds to variant rs55712516 [ dbSNP | Ensembl ].
    VAR_042129
    Natural varianti568 – 5681C → S.1 Publication
    Corresponds to variant rs56077781 [ dbSNP | Ensembl ].
    VAR_042130
    Natural varianti590 – 5901L → P.1 Publication
    Corresponds to variant rs56081642 [ dbSNP | Ensembl ].
    VAR_042131
    Natural varianti621 – 6211I → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036088
    Natural varianti660 – 6601T → K in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_065831
    Natural varianti766 – 7661G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042132
    Natural varianti777 – 7771A → G.1 Publication
    Corresponds to variant rs34437982 [ dbSNP | Ensembl ].
    VAR_042133
    Natural varianti806 – 8061D → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036089
    Natural varianti914 – 9141R → H.1 Publication
    Corresponds to variant rs17801309 [ dbSNP | Ensembl ].
    VAR_027919
    Natural varianti924 – 9241W → R.2 Publications
    Corresponds to variant rs35124509 [ dbSNP | Ensembl ].
    VAR_042134
    Natural varianti933 – 9331T → M in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_065832

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei532 – 5398SFSISGES → CMYYFNAV in isoform 2. 1 PublicationVSP_002995
    Alternative sequencei540 – 983444Missing in isoform 2. 1 PublicationVSP_002996Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.1. human. [P29320-2]
    uc003dqy.3. human. [P29320-1]

    Polymorphism databases

    DMDMi116241351.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83941 mRNA. Translation: AAA58633.1 .
    AF213459 mRNA. Translation: AAG43576.1 .
    AF213460 mRNA. Translation: AAG43577.1 .
    CCDSi CCDS2922.1. [P29320-1 ]
    CCDS46875.1. [P29320-2 ]
    PIRi A38224.
    RefSeqi NP_005224.2. NM_005233.5. [P29320-1 ]
    NP_872585.1. NM_182644.2. [P29320-2 ]
    UniGenei Hs.123642.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GSF X-ray 1.77 A 577-947 [» ]
    2QO2 X-ray 1.60 A 577-947 [» ]
    2QO7 X-ray 1.60 A 577-947 [» ]
    2QO9 X-ray 1.55 A 577-947 [» ]
    2QOB X-ray 1.65 A 609-947 [» ]
    2QOC X-ray 1.25 A 609-947 [» ]
    2QOD X-ray 1.15 A 577-947 [» ]
    2QOF X-ray 1.20 A 577-947 [» ]
    2QOI X-ray 1.25 A 577-947 [» ]
    2QOK X-ray 1.20 A 577-947 [» ]
    2QOL X-ray 1.07 A 577-947 [» ]
    2QON X-ray 1.79 A 577-947 [» ]
    2QOO X-ray 1.25 A 577-947 [» ]
    2QOQ X-ray 1.60 A 577-947 [» ]
    3DZQ X-ray 1.75 A 609-947 [» ]
    3FXX X-ray 1.70 A 577-947 [» ]
    3FY2 X-ray 1.80 A 577-947 [» ]
    4G2F X-ray 1.70 A 609-947 [» ]
    4GK2 X-ray 2.20 A 609-947 [» ]
    4GK3 X-ray 1.90 A 609-947 [» ]
    4GK4 X-ray 2.10 A 609-947 [» ]
    4L0P X-ray 2.26 A 29-201 [» ]
    ProteinModelPortali P29320.
    SMRi P29320. Positions 26-529, 613-906, 909-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108356. 14 interactions.
    DIPi DIP-40307N.
    IntActi P29320. 5 interactions.
    MINTi MINT-7145005.
    STRINGi 9606.ENSP00000337451.

    Chemistry

    BindingDBi P29320.
    ChEMBLi CHEMBL2363043.
    GuidetoPHARMACOLOGYi 1823.

    PTM databases

    PhosphoSitei P29320.

    Polymorphism databases

    DMDMi 116241351.

    Proteomic databases

    MaxQBi P29320.
    PaxDbi P29320.
    PRIDEi P29320.

    Protocols and materials databases

    DNASUi 2042.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336596 ; ENSP00000337451 ; ENSG00000044524 . [P29320-1 ]
    ENST00000452448 ; ENSP00000399926 ; ENSG00000044524 . [P29320-2 ]
    GeneIDi 2042.
    KEGGi hsa:2042.
    UCSCi uc003dqx.1. human. [P29320-2 ]
    uc003dqy.3. human. [P29320-1 ]

    Organism-specific databases

    CTDi 2042.
    GeneCardsi GC03P089239.
    HGNCi HGNC:3387. EPHA3.
    HPAi CAB010462.
    MIMi 114500. phenotype.
    179611. gene.
    neXtProti NX_P29320.
    PharmGKBi PA27819.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P29320.
    KOi K05104.
    OMAi DMKKVGV.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P29320.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P29320.

    Miscellaneous databases

    EvolutionaryTracei P29320.
    GeneWikii EPH_receptor_A3.
    GenomeRNAii 2042.
    NextBioi 8295.
    PROi P29320.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29320.
    Bgeei P29320.
    CleanExi HS_EPHA3.
    Genevestigatori P29320.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProi IPR027936. 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 ]
    Pfami PF14575. 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 ]
    PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-37; SER-85; LEU-621 AND ASN-806.
    12. 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.
      , 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.

    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: October 1, 2014
    This is version 167 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

    External Data

    Dasty 3