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Q03145

- EPHA2_MOUSE

UniProt

Q03145 - EPHA2_MOUSE

Protein

Ephrin type-A receptor 2

Gene

Epha2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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 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 sitei647 – 6471ATPPROSITE-ProRule annotation
    Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi620 – 6289ATPPROSITE-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: MGI
    4. blood vessel development Source: MGI
    5. bone remodeling Source: UniProtKB
    6. branching involved in mammary gland duct morphogenesis Source: UniProtKB
    7. cell adhesion Source: UniProtKB-KW
    8. cell chemotaxis Source: UniProtKB
    9. cell migration Source: UniProtKB
    10. ephrin receptor signaling pathway Source: UniProtKB
    11. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    12. keratinocyte differentiation Source: Ensembl
    13. lens fiber cell morphogenesis Source: UniProtKB
    14. mammary gland epithelial cell proliferation Source: UniProtKB
    15. negative regulation of protein kinase B signaling Source: UniProtKB
    16. neural tube development Source: MGI
    17. neuron differentiation Source: MGI
    18. notochord cell development Source: MGI
    19. notochord formation Source: MGI
    20. notochord morphogenesis Source: MGI
    21. osteoblast differentiation Source: UniProtKB
    22. osteoclast differentiation Source: UniProtKB
    23. peptidyl-tyrosine phosphorylation Source: GOC
    24. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    25. post-anal tail morphogenesis Source: MGI
    26. protein kinase B signaling Source: UniProtKB
    27. regulation of angiogenesis Source: UniProtKB
    28. regulation of blood vessel endothelial cell migration Source: UniProtKB
    29. regulation of cell adhesion mediated by integrin Source: UniProtKB
    30. regulation of ERK1 and ERK2 cascade Source: Ensembl
    31. regulation of lamellipodium assembly Source: UniProtKB
    32. response to growth factor Source: UniProtKB
    33. skeletal system development Source: MGI
    34. vasculogenesis Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell adhesion, Differentiation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    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
    Tyrosine-protein kinase receptor MPK-5
    Tyrosine-protein kinase receptor SEK-2
    Gene namesi
    Name:Epha2
    Synonyms:Eck, Myk2, Sek2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:95278. Epha2.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionruffle membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionlamellipodium membrane By similarity; Single-pass type I membrane protein By similarity. Cell junctionfocal adhesion By similarity
    Note: Present at regions of cell-cell contacts but also at the leading edge of migrating cells.By similarity

    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. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable, fertile but exhibit aberrant development of tail vertebra and susceptibility to carcinogenesis.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi589 – 5891Y → E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-595. 2 Publications
    Mutagenesisi589 – 5891Y → F: Inhibits EFNA1-induced vascular assembly and kinase activity. 2 Publications
    Mutagenesisi595 – 5951Y → E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-589. 2 Publications
    Mutagenesisi595 – 5951Y → F: Inhibits EFNA1-induced vascular assembly and abolishes kinase activity. 2 Publications
    Mutagenesisi736 – 7361Y → F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. No significant effect on kinase activity. Loss of binding to PI3-kinase p85 subunit. 1 Publication
    Mutagenesisi740 – 7401D → N: Loss of kinase activity and binding to VAV3. 1 Publication
    Mutagenesisi773 – 7731Y → F: No significant effect on kinase activity. Significant reduction in phosphorylation. 1 Publication
    Mutagenesisi931 – 9311Y → F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. Inhibits kinase activity. Loss of binding to VAV3 and PI3-kinase p85 subunit. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 977952Ephrin type-A receptor 2PRO_0000016801Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 ↔ 187By similarity
    Disulfide bondi104 ↔ 114By similarity
    Modified residuei152 – 1521PhosphoserineBy similarity
    Modified residuei374 – 3741PhosphoserineBy similarity
    Glycosylationi408 – 4081N-linked (GlcNAc...)3 Publications
    Glycosylationi436 – 4361N-linked (GlcNAc...)3 Publications
    Modified residuei571 – 5711PhosphoserineBy similarity
    Modified residuei580 – 5801PhosphoserineBy similarity
    Modified residuei588 – 5881PhosphothreonineBy similarity
    Modified residuei589 – 5891Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei594 – 5941PhosphothreonineBy similarity
    Modified residuei595 – 5951Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei629 – 6291PhosphotyrosineBy similarity
    Modified residuei648 – 6481PhosphothreonineBy similarity
    Modified residuei736 – 7361Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei772 – 7721PhosphothreonineBy similarity
    Modified residuei773 – 7731Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei791 – 7911PhosphoserineBy similarity
    Modified residuei792 – 7921PhosphotyrosineBy similarity
    Modified residuei870 – 8701PhosphoserineBy similarity
    Modified residuei881 – 8811PhosphoserineBy similarity
    Modified residuei893 – 8931PhosphoserineBy similarity
    Modified residuei898 – 8981PhosphoserineBy similarity
    Modified residuei899 – 8991PhosphothreonineBy similarity
    Modified residuei900 – 9001PhosphoserineBy similarity
    Modified residuei902 – 9021PhosphoserineBy similarity
    Modified residuei911 – 9111PhosphoserineBy similarity
    Modified residuei922 – 9221Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei931 – 9311PhosphotyrosineBy similarity
    Modified residuei961 – 9611PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylates. Phosphorylated at Ser-898 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. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-589 and Tyr-595 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-736 and Tyr-931 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-931 by PTPRF prevents the interaction of EPHA2 with NCK1. Dephosphorylated by ACP1.2 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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ03145.
    PRIDEiQ03145.

    PTM databases

    PhosphoSiteiQ03145.

    Expressioni

    Tissue specificityi

    Expressed in the lung, intestine and liver.1 Publication

    Developmental stagei

    First detected in gastrulation stage embryos (6.5-7.5 dpc) in ectodermal cells adjacent to the distal region of the primitive streak. By the neural plate stage (approximately 7.5 dpc), EPHA2 expression becomes restricted to the extreme distal end or node of the primitive streak. After the beginning of somitogenesis (approximately 8.0 dpc), expression persists in the node as this structure regresses toward the caudal end of the embryo. In addition, beginning at the mid head fold stage (approximately 7.75 dpc), we observe that EPHA2 exhibits a dynamic and spatially restricted expression pattern in the prospective hindbrain region. EPHA2 transcripts are initially detected in a 5-cell wide strip of mesodermal cells underlying prospective rhombomere 4 (R4). Subsequently at the beginning of somitogenesis, expression is observed in prospective R4. At the 4-8-somite stage, EPHA2 transcripts are observed in R4, mesenchymal cells underlying R4, and surface ectoderm in the vicinity of the developing second branchial arch. By the 10-somite stage, expression in these cells is down-regulated. Additionally, at the 5-8-somite stage, EPHA2 transcripts are detected initially in the lateral mesenchyme immediately underlying the surface ectoderm adjacent to R5 and R6, and subsequently in surface ectoderm overlying the developing third branchial arch.4 Publications

    Gene expression databases

    BgeeiQ03145.
    CleanExiMM_EPHA2.
    GenevestigatoriQ03145.

    Interactioni

    Subunit structurei

    Homodimer. 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 with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion. 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. Interacts with ANKS1A.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Epha4Q031373EBI-529701,EBI-1539152

    Protein-protein interaction databases

    BioGridi199469. 2 interactions.
    DIPiDIP-829N.
    IntActiQ03145. 4 interactions.
    MINTiMINT-3388286.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03145.
    SMRiQ03145. Positions 24-529, 603-971.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 538513ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini560 – 977418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei539 – 55921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 205179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 433105Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 53092Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini614 – 876263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini905 – 96965SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 205205Mediates interaction with CLDN4By similarityAdd
    BLAST
    Regioni607 – 907301Mediates interaction with ARHGEF16By similarityAdd
    BLAST
    Regioni887 – 97791Negatively regulates interaction with ARHGEF16By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi975 – 9773PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi187 – 326140Cys-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.
    GeneTreeiENSGT00740000115081.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiQ3UNI2.
    KOiK05103.
    OMAiLVPIGQC.
    OrthoDBiEOG7VTDM6.
    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.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q03145-1 [UniParc]FASTAAdd to Basket

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    MELRAVGFCL ALLWGCALAA AAAQGKEVVL LDFAAMKGEL GWLTHPYGKG    50
    WDLMQNIMDD MPIYMYSVCN VVSGDQDNWL RTNWVYREEA ERIFIELKFT 100
    VRDCNSFPGG ASSCKETFNL YYAESDVDYG TNFQKRQFTK IDTIAPDEIT 150
    VSSDFEARNV KLNVEERMVG PLTRKGFYLA FQDIGACVAL LSVRVYYKKC 200
    PEMLQSLARF PETIAVAVSD TQPLATVAGT CVDHAVVPYG GEGPLMHCTV 250
    DGEWLVPIGQ CLCQEGYEKV EDACRACSPG FFKSEASESP CLECPEHTLP 300
    STEGATSCQC EEGYFRAPED PLSMSCTRPP SAPNYLTAIG MGAKVELRWT 350
    APKDTGGRQD IVYSVTCEQC WPESGECGPC EASVRYSEPP HALTRTSVTV 400
    SDLEPHMNYT FAVEARNGVS GLVTSRSFRT ASVSINQTEP PKVRLEDRST 450
    TSLSVTWSIP VSQQSRVWKY EVTYRKKGDA NSYNVRRTEG FSVTLDDLAP 500
    DTTYLVQVQA LTQEGQGAGS KVHEFQTLST EGSANMAVIG GVAVGVVLLL 550
    VLAGVGLFIH RRRRNLRARQ SSEDVRFSKS EQLKPLKTYV DPHTYEDPNQ 600
    AVLKFTTEIH PSCVARQKVI GAGEFGEVYK GTLKASSGKK EIPVAIKTLK 650
    AGYTEKQRVD FLSEASIMGQ FSHHNIIRLE GVVSKYKPMM IITEYMENGA 700
    LDKFLREKDG EFSVLQLVGM LRGIASGMKY LANMNYVHRD LAARNILVNS 750
    NLVCKVSDFG LSRVLEDDPE ATYTTSGGKI PIRWTAPEAI SYRKFTSASD 800
    VWSYGIVMWE VMTYGERPYW ELSNHEVMKA INDGFRLPTP MDCPSAIYQL 850
    MMQCWQQERS RRPKFADIVS ILDKLIRAPD SLKTLADFDP RVSIRLPSTS 900
    GSEGVPFRTV SEWLESIKMQ QYTEHFMVAG YTAIEKVVQM SNEDIKRIGV 950
    RLPGHQKRIA YSLLGLKDQV NTVGIPI 977
    Length:977
    Mass (Da):108,852
    Last modified:July 27, 2011 - v3
    Checksum:i66338CE7EF2DEE02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → T in CAA55135. (PubMed:8183555)Curated
    Sequence conflicti112 – 1132SS → HA in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti189 – 1891A → R in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti209 – 2091R → C in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti244 – 2441P → A in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti258 – 2603IGQ → SE in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti291 – 2911C → S in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti339 – 3402IG → C in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti371 – 3722WP → CA in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti383 – 3831S → T in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti457 – 4571W → R in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti485 – 4851V → G in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti511 – 5111L → W in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti534 – 5341A → R in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti678 – 6781R → P in CAA55135. (PubMed:8183555)Curated
    Sequence conflicti681 – 6811G → A in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti819 – 8202YW → LL in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti878 – 8781A → R in AAA82113. (PubMed:7918100)Curated
    Sequence conflicti919 – 9202MQ → IE in AAA82113. (PubMed:7918100)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78339 mRNA. Translation: CAA55135.1.
    U07634 mRNA. Translation: AAA82113.1.
    AK137704 mRNA. Translation: BAE23470.1.
    AK144202 mRNA. Translation: BAE25765.1.
    AL607087, AL670285 Genomic DNA. Translation: CAM17000.1.
    AL670285, AL607087 Genomic DNA. Translation: CAM20402.1.
    CH466615 Genomic DNA. Translation: EDL13361.1.
    BC140960 mRNA. Translation: AAI40961.1.
    X76010 mRNA. Translation: CAA53597.1.
    X57243 mRNA. Translation: CAA40519.1.
    CCDSiCCDS18869.1.
    PIRiI48759.
    I48974.
    S49004.
    RefSeqiNP_034269.2. NM_010139.3.
    UniGeneiMm.2581.

    Genome annotation databases

    EnsembliENSMUST00000006614; ENSMUSP00000006614; ENSMUSG00000006445.
    GeneIDi13836.
    KEGGimmu:13836.
    UCSCiuc008voc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78339 mRNA. Translation: CAA55135.1 .
    U07634 mRNA. Translation: AAA82113.1 .
    AK137704 mRNA. Translation: BAE23470.1 .
    AK144202 mRNA. Translation: BAE25765.1 .
    AL607087 , AL670285 Genomic DNA. Translation: CAM17000.1 .
    AL670285 , AL607087 Genomic DNA. Translation: CAM20402.1 .
    CH466615 Genomic DNA. Translation: EDL13361.1 .
    BC140960 mRNA. Translation: AAI40961.1 .
    X76010 mRNA. Translation: CAA53597.1 .
    X57243 mRNA. Translation: CAA40519.1 .
    CCDSi CCDS18869.1.
    PIRi I48759.
    I48974.
    S49004.
    RefSeqi NP_034269.2. NM_010139.3.
    UniGenei Mm.2581.

    3D structure databases

    ProteinModelPortali Q03145.
    SMRi Q03145. Positions 24-529, 603-971.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199469. 2 interactions.
    DIPi DIP-829N.
    IntActi Q03145. 4 interactions.
    MINTi MINT-3388286.

    PTM databases

    PhosphoSitei Q03145.

    Proteomic databases

    PaxDbi Q03145.
    PRIDEi Q03145.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006614 ; ENSMUSP00000006614 ; ENSMUSG00000006445 .
    GeneIDi 13836.
    KEGGi mmu:13836.
    UCSCi uc008voc.2. mouse.

    Organism-specific databases

    CTDi 1969.
    MGIi MGI:95278. Epha2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115081.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi Q3UNI2.
    KOi K05103.
    OMAi LVPIGQC.
    OrthoDBi EOG7VTDM6.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    NextBioi 284656.
    PROi Q03145.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q03145.
    CleanExi MM_EPHA2.
    Genevestigatori Q03145.

    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 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. "The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development."
      Ganju P., Shigemoto K., Brennan J., Entwistle A., Reith A.D.
      Oncogene 9:1613-1624(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
    2. "The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development."
      Ruiz J.C., Robertson E.J.
      Mech. Dev. 46:87-100(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Vagina.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain.
    7. "Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain."
      Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P.
      Mech. Dev. 47:3-17(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-977, DEVELOPMENTAL STAGE.
      Strain: C57BL/6.
      Tissue: Embryo.
    8. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
      Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
      Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 742-799.
      Tissue: Embryonic brain.
    9. "Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase."
      Pandey A., Duan H., Dixit V.M.
      J. Biol. Chem. 270:19201-19204(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA.
      Tissue: Embryonic brain.
    10. "Involvement of EphA2 in the formation of the tail notochord via interaction with ephrinA1."
      Naruse-Nakajima C., Asano M., Iwakura Y.
      Mech. Dev. 102:95-105(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    11. "EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation."
      Brantley-Sieders D.M., Caughron J., Hicks D., Pozzi A., Ruiz J.C., Chen J.
      J. Cell Sci. 117:2037-2049(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, DISRUPTION PHENOTYPE.
    12. "Disruption of EphA2 receptor tyrosine kinase leads to increased susceptibility to carcinogenesis in mouse skin."
      Guo H., Miao H., Gerber L., Singh J., Denning M.F., Gilliam A.C., Wang B.
      Cancer Res. 66:7050-7058(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION, DISRUPTION PHENOTYPE.
    13. "Essential role of Vav family guanine nucleotide exchange factors in EphA receptor-mediated angiogenesis."
      Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W., Chen J.
      Mol. Cell. Biol. 26:4830-4842(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, INTERACTION WITH VAV2 AND VAV3, MUTAGENESIS OF TYR-589; TYR-595 AND ASP-740.
    14. "Identification and functional analysis of phosphorylated tyrosine residues within EphA2 receptor tyrosine kinase."
      Fang W.B., Brantley-Sieders D.M., Hwang Y., Ham A.-J.L., Chen J.
      J. Biol. Chem. 283:16017-16026(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH VAV2; VAV3 AND PI3-KINASE P85 SUBUNIT, PHOSPHORYLATION AT TYR-589; TYR-595; TYR-736 AND TYR-773, MUTAGENESIS OF TYR-589; TYR-595; TYR-736; TYR-773 AND TYR-931.
    15. "Loss of ephrin-A5 function disrupts lens fiber cell packing and leads to cataract."
      Cooper M.A., Son A.I., Komlos D., Sun Y., Kleiman N.J., Zhou R.
      Proc. Natl. Acad. Sci. U.S.A. 105:16620-16625(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LENS FIBER CELLS MORPHOGENESIS.
    16. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-595 AND TYR-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    17. "Bidirectional signaling through ephrinA2-EphA2 enhances osteoclastogenesis and suppresses osteoblastogenesis."
      Irie N., Takada Y., Watanabe Y., Matsuzaki Y., Naruse C., Asano M., Iwakura Y., Suda T., Matsuo K.
      J. Biol. Chem. 284:14637-14644(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BONE IN REMODELING.
    18. "Regulation of mammary gland branching morphogenesis by EphA2 receptor tyrosine kinase."
      Vaught D., Chen J., Brantley-Sieders D.M.
      Mol. Biol. Cell 20:2572-2581(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAMMARY GLAND DEVELOPMENT.
    19. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
      Tissue: Myoblast.
    20. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
    21. "The SAM domains of Anks family proteins are critically involved in modulating the degradation of EphA receptors."
      Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.
      Mol. Cell. Biol. 30:1582-1592(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH ANKS1A.

    Entry informationi

    Entry nameiEPHA2_MOUSE
    AccessioniPrimary (citable) accession number: Q03145
    Secondary accession number(s): Q3UNI2, Q60633, Q62212
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3