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P29317

- EPHA2_HUMAN

UniProt

P29317 - EPHA2_HUMAN

Protein

Ephrin type-A receptor 2

Gene

EPHA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A 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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.7 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei646 – 6461ATPPROSITE-ProRule annotation
    Active sitei739 – 7391Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi619 – 6279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ephrin receptor activity Source: InterPro
    3. protein binding Source: UniProtKB
    4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of Rac GTPase activity Source: UniProtKB
    2. angiogenesis Source: UniProtKB-KW
    3. axial mesoderm formation Source: Ensembl
    4. bone remodeling Source: UniProtKB
    5. branching involved in mammary gland duct morphogenesis Source: UniProtKB
    6. cell adhesion Source: UniProtKB-KW
    7. cell chemotaxis Source: UniProtKB
    8. cell migration Source: UniProtKB
    9. ephrin receptor signaling pathway Source: UniProtKB
    10. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    11. keratinocyte differentiation Source: UniProtKB
    12. lens fiber cell morphogenesis Source: UniProtKB
    13. mammary gland epithelial cell proliferation Source: UniProtKB
    14. multicellular organismal development Source: ProtInc
    15. negative regulation of protein kinase B signaling Source: UniProtKB
    16. neural tube development Source: Ensembl
    17. neuron differentiation Source: Ensembl
    18. notochord cell development Source: Ensembl
    19. notochord formation Source: Ensembl
    20. osteoblast differentiation Source: UniProtKB
    21. osteoclast differentiation Source: UniProtKB
    22. peptidyl-tyrosine phosphorylation Source: GOC
    23. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    24. post-anal tail morphogenesis Source: Ensembl
    25. protein kinase B signaling Source: UniProtKB
    26. regulation of angiogenesis Source: UniProtKB
    27. regulation of blood vessel endothelial cell migration Source: UniProtKB
    28. regulation of cell adhesion mediated by integrin Source: UniProtKB
    29. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    30. regulation of lamellipodium assembly Source: UniProtKB
    31. response to growth factor Source: UniProtKB
    32. skeletal system development Source: Ensembl
    33. vasculogenesis Source: Ensembl
    34. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell adhesion, Differentiation, Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP29317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 2 (EC:2.7.10.1)
    Alternative name(s):
    Epithelial cell kinase
    Tyrosine-protein kinase receptor ECK
    Gene namesi
    Name:EPHA2
    Synonyms:ECK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3386. EPHA2.

    Subcellular locationi

    GO - Cellular componenti

    1. focal adhesion Source: UniProtKB
    2. integral component of plasma membrane Source: UniProtKB
    3. lamellipodium membrane Source: UniProtKB-SubCell
    4. leading edge membrane Source: UniProtKB
    5. plasma membrane Source: UniProtKB
    6. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 6, multiple types (CTRCT6) [MIM:116600]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT6 includes posterior polar and age-related cortical cataracts, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. Age-related cortical cataract is a developmental punctate opacity restricted to the cortex. The cataract is white or cerulean, increases in number with age, but rarely affects vision.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti721 – 7211R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 Publication
    Corresponds to variant rs116506614 [ dbSNP | Ensembl ].
    VAR_062532
    Natural varianti940 – 9401T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
    VAR_058907
    Natural varianti948 – 9481G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
    VAR_058908
    Overexpressed in several cancer types and promotes malignancy.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031R → E: Significantly reduced response to EFNA1. 1 Publication
    Mutagenesisi646 – 6461K → M: Loss of kinase activity. 1 Publication
    Mutagenesisi739 – 7391D → N: Increases serum-induced chemotaxis. Loss of EFNA1-dependent regulation of cell migration. 1 Publication
    Mutagenesisi897 – 8971S → A or D: Loss of serum-induced phosphorylation by PKB. Loss of serum-induced chemotaxis. 1 Publication

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi116600. phenotype.
    Orphaneti98993. Posterior polar cataract.
    98994. Total congenital cataract.
    PharmGKBiPA27818.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 976953Ephrin type-A receptor 2PRO_0000016800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi70 ↔ 188
    Disulfide bondi105 ↔ 115
    Modified residuei153 – 1531Phosphoserine
    Modified residuei373 – 3731Phosphoserine
    Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...)1 Publication
    Modified residuei570 – 5701Phosphoserine3 Publications
    Modified residuei575 – 5751Phosphotyrosine
    Modified residuei579 – 5791Phosphoserine1 Publication
    Modified residuei587 – 5871Phosphothreonine
    Modified residuei588 – 5881Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei593 – 5931Phosphothreonine
    Modified residuei594 – 5941Phosphotyrosine; by autocatalysis
    Modified residuei628 – 6281Phosphotyrosine1 Publication
    Modified residuei647 – 6471Phosphothreonine2 Publications
    Modified residuei735 – 7351Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei771 – 7711Phosphothreonine
    Modified residuei772 – 7721Phosphotyrosine; by autocatalysis
    Modified residuei790 – 7901Phosphoserine
    Modified residuei791 – 7911Phosphotyrosine
    Modified residuei869 – 8691Phosphoserine1 Publication
    Modified residuei880 – 8801Phosphoserine
    Modified residuei892 – 8921Phosphoserine1 Publication
    Modified residuei897 – 8971Phosphoserine; by PKB1 Publication
    Modified residuei898 – 8981Phosphothreonine
    Modified residuei899 – 8991Phosphoserine
    Modified residuei901 – 9011Phosphoserine1 Publication
    Modified residuei910 – 9101Phosphoserine
    Modified residuei921 – 9211Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei930 – 9301Phosphotyrosine1 Publication
    Modified residuei960 – 9601Phosphotyrosine

    Post-translational modificationi

    Autophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Dephosphorylated by ACP1.7 Publications
    Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP29317.
    PaxDbiP29317.
    PRIDEiP29317.

    PTM databases

    PhosphoSiteiP29317.

    Expressioni

    Tissue specificityi

    Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.1 Publication

    Inductioni

    Up-regulated by UV irradiation via a TP53-independent, MAPK-dependent mechanism.1 Publication

    Gene expression databases

    ArrayExpressiP29317.
    BgeeiP29317.
    CleanExiHS_EPHA2.
    GenevestigatoriP29317.

    Organism-specific databases

    HPAiCAB010464.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration By similarity. Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts (via SAM domain) with ANKS1A (via SAM domain). Interacts with human herpes virus 8/HHV-8 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction triggers EPHA2 phosphorylation and endocytosis, allowing virus entry. Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EFNA1P208277EBI-702104,EBI-715194
    EPHA7Q153753EBI-702104,EBI-1383428
    HSP90AB1P082382EBI-702104,EBI-352572
    PTK2Q053973EBI-702104,EBI-702142

    Protein-protein interaction databases

    BioGridi108288. 36 interactions.
    DIPiDIP-96N.
    IntActiP29317. 16 interactions.
    MINTiMINT-3972729.
    STRINGi9606.ENSP00000351209.

    Structurei

    Secondary structure

    1
    976
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 336
    Helixi34 – 363
    Turni37 – 404
    Beta strandi44 – 5714
    Beta strandi59 – 624
    Beta strandi64 – 696
    Beta strandi73 – 764
    Beta strandi79 – 824
    Beta strandi92 – 10312
    Helixi105 – 1073
    Beta strandi108 – 1103
    Turni112 – 1143
    Beta strandi119 – 12810
    Helixi136 – 1383
    Beta strandi139 – 1457
    Beta strandi148 – 1514
    Helixi153 – 1575
    Beta strandi161 – 17010
    Beta strandi175 – 18713
    Beta strandi189 – 19911
    Beta strandi204 – 2063
    Beta strandi209 – 2113
    Beta strandi218 – 2214
    Beta strandi224 – 2274
    Beta strandi238 – 2403
    Beta strandi244 – 2474
    Beta strandi253 – 2575
    Beta strandi266 – 2694
    Beta strandi272 – 2754
    Beta strandi286 – 2883
    Beta strandi295 – 2984
    Beta strandi335 – 3384
    Beta strandi343 – 3486
    Beta strandi361 – 3699
    Beta strandi376 – 3783
    Beta strandi384 – 3874
    Beta strandi389 – 3924
    Beta strandi394 – 4007
    Beta strandi407 – 4159
    Helixi419 – 4213
    Beta strandi427 – 4337
    Beta strandi441 – 4466
    Beta strandi453 – 4575
    Turni460 – 4656
    Beta strandi467 – 4759
    Beta strandi483 – 49311
    Beta strandi502 – 5109
    Beta strandi522 – 5254
    Helixi536 – 55621
    Beta strandi557 – 5615
    Helixi597 – 6004
    Turni601 – 6044
    Helixi610 – 6123
    Beta strandi613 – 6219
    Beta strandi623 – 63210
    Beta strandi641 – 6477
    Helixi654 – 66714
    Beta strandi678 – 6825
    Beta strandi684 – 6874
    Beta strandi689 – 6935
    Helixi700 – 7067
    Turni707 – 7093
    Helixi713 – 73220
    Helixi742 – 7443
    Beta strandi745 – 7473
    Beta strandi753 – 7553
    Helixi781 – 7833
    Helixi786 – 7916
    Helixi796 – 81116
    Turni817 – 8204
    Helixi823 – 8319
    Helixi844 – 85310
    Helixi858 – 8603
    Helixi864 – 87310
    Helixi878 – 8825
    Helixi909 – 9157
    Helixi919 – 9213
    Helixi922 – 9276
    Helixi933 – 9375
    Helixi941 – 9466
    Helixi952 – 96413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MQBX-ray2.30A/B596-900[»]
    2E8NNMR-A902-976[»]
    2K9YNMR-A/B523-563[»]
    2KSONMR-A908-972[»]
    2X10X-ray3.00A27-534[»]
    2X11X-ray4.83A27-534[»]
    3C8XX-ray1.95A23-202[»]
    3CZUX-ray2.65A23-202[»]
    3FL7X-ray2.50A23-531[»]
    3HEIX-ray2.00A/C/E/G/I/K/M/O28-201[»]
    3HPNX-ray2.52A/B/C/D/E/F28-201[»]
    3KKAX-ray2.40C/D/E903-971[»]
    3MBWX-ray2.81A23-326[»]
    3MX0X-ray3.51A/C27-435[»]
    3SKJX-ray2.50E/F23-202[»]
    4P2KX-ray1.50A590-876[»]
    4PDOX-ray2.10A/B590-876[»]
    4TRLX-ray2.45A590-876[»]
    ProteinModelPortaliP29317.
    SMRiP29317. Positions 25-528, 555-970.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29317.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 537514ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini559 – 976418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei538 – 55821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 206179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 432105Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 52992Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini613 – 875263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini904 – 96865SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 206206Mediates interaction with CLDN4Add
    BLAST
    Regioni606 – 906301Mediates interaction with ARHGEF16 and ELMO2Add
    BLAST
    Regioni886 – 97691Negatively regulates interaction with ARHGEF16Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi974 – 9763PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi188 – 325138Cys-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.
    InParanoidiP29317.
    KOiK05103.
    OMAiLVPIGQC.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP29317.
    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.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    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.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 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.
    PROSITEiPS51550. 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: P29317-1) [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

    MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK    50
    GWDLMQNIMN DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF 100
    TVRDCNSFPG GASSCKETFN LYYAESDLDY GTNFQKRLFT KIDTIAPDEI 150
    TVSSDFEARH VKLNVEERSV GPLTRKGFYL AFQDIGACVA LLSVRVYYKK 200
    CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG EEPRMHCAVD 250
    GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS 300
    PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP 350
    PQDSGGREDI VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS 400
    DLEPHMNYTF TVEARNGVSG LVTSRSFRTA SVSINQTEPP KVRLEGRSTT 450
    SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN SYNVRRTEGF SVTLDDLAPD 500
    TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG VAVGVVLLLV 550
    LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA 600
    VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA 650
    GYTEKQRVDF LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL 700
    DKFLREKDGE FSVLQLVGML RGIAAGMKYL ANMNYVHRDL AARNILVNSN 750
    LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP IRWTAPEAIS YRKFTSASDV 800
    WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM DCPSAIYQLM 850
    MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG 900
    SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR 950
    LPGHQKRIAY SLLGLKDQVN TVGIPI 976
    Length:976
    Mass (Da):108,266
    Last modified:May 5, 2009 - v2
    Checksum:i845D7E1BBCCAACCC
    GO
    Isoform 2 (identifier: P29317-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         477-497: GDSNSYNVRRTEGFSVTLDDL → VTPRGAGLALAGPTAGDRLVT
         498-976: Missing.

    Show »
    Length:497
    Mass (Da):54,305
    Checksum:iEB5CEB75AE01F814
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 996IFIELK → NNFELN in AAA53375. (PubMed:2174105)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991K → N.
    Corresponds to variant rs1058372 [ dbSNP | Ensembl ].
    VAR_055989
    Natural varianti391 – 3911G → R.1 Publication
    Corresponds to variant rs34192549 [ dbSNP | Ensembl ].
    VAR_042121
    Natural varianti511 – 5111T → M.1 Publication
    Corresponds to variant rs55747232 [ dbSNP | Ensembl ].
    VAR_042122
    Natural varianti568 – 5681R → H.1 Publication
    Corresponds to variant rs56198600 [ dbSNP | Ensembl ].
    VAR_042123
    Natural varianti631 – 6311M → T.
    Corresponds to variant rs34021505 [ dbSNP | Ensembl ].
    VAR_055990
    Natural varianti721 – 7211R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 Publication
    Corresponds to variant rs116506614 [ dbSNP | Ensembl ].
    VAR_062532
    Natural varianti777 – 7771G → S in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042124
    Natural varianti876 – 8761R → H.1 Publication
    Corresponds to variant rs35903225 [ dbSNP | Ensembl ].
    VAR_042125
    Natural varianti940 – 9401T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
    VAR_058907
    Natural varianti948 – 9481G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
    VAR_058908

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei477 – 49721GDSNS…TLDDL → VTPRGAGLALAGPTAGDRLV T in isoform 2. 1 PublicationVSP_056014Add
    BLAST
    Alternative sequencei498 – 976479Missing in isoform 2. 1 PublicationVSP_056015Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59371 mRNA. Translation: AAA53375.1.
    EU826606 mRNA. Translation: ACF47642.1.
    AL451042 Genomic DNA. Translation: CAH71943.1.
    CH471167 Genomic DNA. Translation: EAW51769.1.
    BC037166 mRNA. Translation: AAH37166.1.
    CCDSiCCDS169.1.
    PIRiA36355.
    RefSeqiNP_004422.2. NM_004431.3.
    UniGeneiHs.171596.

    Genome annotation databases

    EnsembliENST00000358432; ENSP00000351209; ENSG00000142627.
    GeneIDi1969.
    KEGGihsa:1969.
    UCSCiuc001aya.2. human.

    Polymorphism databases

    DMDMi229462861.

    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
    M59371 mRNA. Translation: AAA53375.1 .
    EU826606 mRNA. Translation: ACF47642.1 .
    AL451042 Genomic DNA. Translation: CAH71943.1 .
    CH471167 Genomic DNA. Translation: EAW51769.1 .
    BC037166 mRNA. Translation: AAH37166.1 .
    CCDSi CCDS169.1.
    PIRi A36355.
    RefSeqi NP_004422.2. NM_004431.3.
    UniGenei Hs.171596.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MQB X-ray 2.30 A/B 596-900 [» ]
    2E8N NMR - A 902-976 [» ]
    2K9Y NMR - A/B 523-563 [» ]
    2KSO NMR - A 908-972 [» ]
    2X10 X-ray 3.00 A 27-534 [» ]
    2X11 X-ray 4.83 A 27-534 [» ]
    3C8X X-ray 1.95 A 23-202 [» ]
    3CZU X-ray 2.65 A 23-202 [» ]
    3FL7 X-ray 2.50 A 23-531 [» ]
    3HEI X-ray 2.00 A/C/E/G/I/K/M/O 28-201 [» ]
    3HPN X-ray 2.52 A/B/C/D/E/F 28-201 [» ]
    3KKA X-ray 2.40 C/D/E 903-971 [» ]
    3MBW X-ray 2.81 A 23-326 [» ]
    3MX0 X-ray 3.51 A/C 27-435 [» ]
    3SKJ X-ray 2.50 E/F 23-202 [» ]
    4P2K X-ray 1.50 A 590-876 [» ]
    4PDO X-ray 2.10 A/B 590-876 [» ]
    4TRL X-ray 2.45 A 590-876 [» ]
    ProteinModelPortali P29317.
    SMRi P29317. Positions 25-528, 555-970.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108288. 36 interactions.
    DIPi DIP-96N.
    IntActi P29317. 16 interactions.
    MINTi MINT-3972729.
    STRINGi 9606.ENSP00000351209.

    Chemistry

    BindingDBi P29317.
    ChEMBLi CHEMBL2068.
    DrugBanki DB01254. Dasatinib.
    GuidetoPHARMACOLOGYi 1822.

    PTM databases

    PhosphoSitei P29317.

    Polymorphism databases

    DMDMi 229462861.

    Proteomic databases

    MaxQBi P29317.
    PaxDbi P29317.
    PRIDEi P29317.

    Protocols and materials databases

    DNASUi 1969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358432 ; ENSP00000351209 ; ENSG00000142627 .
    GeneIDi 1969.
    KEGGi hsa:1969.
    UCSCi uc001aya.2. human.

    Organism-specific databases

    CTDi 1969.
    GeneCardsi GC01M016450.
    HGNCi HGNC:3386. EPHA2.
    HPAi CAB010464.
    MIMi 116600. phenotype.
    176946. gene.
    neXtProti NX_P29317.
    Orphaneti 98993. Posterior polar cataract.
    98994. Total congenital cataract.
    PharmGKBi PA27818.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P29317.
    KOi K05103.
    OMAi LVPIGQC.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P29317.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P29317.

    Miscellaneous databases

    EvolutionaryTracei P29317.
    GeneWikii EPH_receptor_A2.
    GenomeRNAii 1969.
    NextBioi 7983.
    PROi P29317.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29317.
    Bgeei P29317.
    CleanExi HS_EPHA2.
    Genevestigatori P29317.

    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.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    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.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 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 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. "cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases."
      Lindberg R.A., Hunter T.
      Mol. Cell. Biol. 10:6316-6324(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
      Tissue: Epithelium.
    2. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreas.
    6. "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.
    7. "Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
      Miao H., Burnett E., Kinch M., Simon E., Wang B.
      Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INTEGRIN-MEDIATED CELL ADHESION, FUNCTION IN CELL MIGRATION, PHOSPHORYLATION, INTERACTION WITH PTK2/FAK1 AND PTPN11, SUBCELLULAR LOCATION.
    8. "EphA2 overexpression causes tumorigenesis of mammary epithelial cells."
      Zelinski D.P., Zantek N.D., Stewart J.C., Irizarry A.R., Kinch M.S.
      Cancer Res. 61:2301-2306(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ONCOGENICITY.
    9. "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation."
      Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.
      J. Biol. Chem. 277:39274-39279(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACP1, DEPHOSPHORYLATION BY ACP1.
    10. "EphA2 phosphorylates the cytoplasmic tail of Claudin-4 and mediates paracellular permeability."
      Tanaka M., Kamata R., Sakai R.
      J. Biol. Chem. 280:42375-42382(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL-CELL INTERACTION, INTERACTION WITH CLDN4, MUTAGENESIS OF LYS-646.
    11. "Ephrin-A1 is a negative regulator in glioma through down-regulation of EphA2 and FAK."
      Liu D.-P., Wang Y., Koeffler H.P., Xie D.
      Int. J. Oncol. 30:865-871(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation."
      Zhuang G., Hunter S., Hwang Y., Chen J.
      J. Biol. Chem. 282:2683-2694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPPL1.
    13. "EphA2 is an essential mediator of UV radiation-induced apoptosis."
      Zhang G., Njauw C.-N., Park J.M., Naruse C., Asano M., Tsao H.
      Cancer Res. 68:1691-1696(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, INDUCTION BY UV.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-579 AND THR-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor."
      Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.
      Oncogene 27:7260-7273(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-892 AND SER-901, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "EphA2 mediates ligand-dependent inhibition and ligand-independent promotion of cell migration and invasion via a reciprocal regulatory loop with Akt."
      Miao H., Li D.Q., Mukherjee A., Guo H., Petty A., Cutter J., Basilion J.P., Sedor J., Wu J., Danielpour D., Sloan A.E., Cohen M.L., Wang B.
      Cancer Cell 16:9-20(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-739 AND SER-897, PHOSPHORYLATION AT SER-897 BY PKB.
    18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-435.
      Tissue: Liver.
    19. "Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis."
      Annamalai B., Liu X., Gopal U., Isaacs J.S.
      Mol. Cancer Res. 7:1021-1032(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY STUB1.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-628; THR-647 AND SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
      Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
      J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH ARHGEF16; DOCK4 AND ELMO2.
    22. "Ligand targeting of EphA2 enhances keratinocyte adhesion and differentiation via desmoglein 1."
      Lin S., Gordon K., Kaplan N., Getsios S.
      Mol. Biol. Cell 21:3902-3914(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KERATINOCYTE ADHESION AND DIFFERENTIATION, SUBCELLULAR LOCATION.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor."
      Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M., Leone M.
      Biochemistry 51:2136-2145(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKS1A.
    26. Cited for: INTERACTION WITH HHV-8 GLYCOPROTEIN L/GLYCOPROTEIN H.
    27. "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
      Lee H., Bennett A.M.
      Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, PHOSPHORYLATION AT TYR-930, DEPHOSPHORYLATION AT TYR-930 BY PTPRF, INTERACTION WITH NCK1.
    28. "Early insights into the function of KIAA1199, a markedly overexpressed protein in human colorectal tumors."
      Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J., Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.
      PLoS ONE 8:E69473-E69473(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEMIP.
    29. "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
      Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
      Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 596-900.
    30. "Solution structure of the C-terminal SAM-domain of EPHAA2: ephrin type-A receptor 2 precursor (EC 2.7.10.1)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 902-976.
    31. "Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex."
      Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M., Nguyen M., Rajashankar K.R., Wang B., Nikolov D.B.
      EMBO Rep. 10:722-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 28-201, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-201 IN COMPLEX WITH EFNA1, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ARG-103.
    32. "Ephrin A1 bound to the ligand binding domain of the human ephrin A2 (EPHA2) receptor protein kinase."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-202, DISULFIDE BOND.
    33. "Left-handed dimer of EPHA2 transmembrane domain helix packing diversity among receptor tyrosine kinases."
      Mayzel M.L., Bocharov E.V., Volynsky P.E., Arseniev A.S.
      Submitted (AUG-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 523-563.
    34. "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] ARG-391; MET-511; HIS-568; SER-777 AND HIS-876.
    35. "The EPHA2 gene is associated with cataracts linked to chromosome 1p."
      Shiels A., Bennett T.M., Knopf H.L.S., Maraini G., Li A., Jiao X., Hejtmancik J.F.
      Mol. Vis. 14:2042-2055(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT6 TRP-948.
    36. "Mutations of the EPHA2 receptor tyrosine kinase gene cause autosomal dominant congenital cataract."
      Zhang T., Hua R., Xiao W., Burdon K.P., Bhattacharya S.S., Craig J.E., Shang D., Zhao X., Mackey D.A., Moore A.T., Luo Y., Zhang J., Zhang X.
      Hum. Mutat. 30:E603-E611(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT6 ILE-940.
    37. Cited for: VARIANT CTRCT6 GLN-721, CHARACTERIZATION OF VARIANT CTRCT6 GLN-721.
    38. "Human cataract mutations in EPHA2 SAM domain alter receptor stability and function."
      Park J.E., Son A.I., Hua R., Wang L., Zhang X., Zhou R.
      PLoS ONE 7:E36564-E36564(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CTRCT6 ILE-940 AND CTRCT6 TRP-948.

    Entry informationi

    Entry nameiEPHA2_HUMAN
    AccessioniPrimary (citable) accession number: P29317
    Secondary accession number(s): B5A968, Q8N3Z2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 174 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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