Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q60750

- EPHA1_MOUSE

UniProt

Q60750 - EPHA1_MOUSE

Protein

Ephrin type-A receptor 1

Gene

Epha1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.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 sitei657 – 6571ATPPROSITE-ProRule annotation
    Active sitei750 – 7501Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi631 – 6399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of Rho GTPase activity Source: UniProtKB
    2. angiogenesis Source: UniProtKB-KW
    3. cell surface receptor signaling pathway Source: UniProtKB
    4. negative regulation of cell migration Source: UniProtKB
    5. negative regulation of protein kinase activity Source: UniProtKB
    6. peptidyl-tyrosine phosphorylation Source: UniProtKB
    7. positive regulation of angiogenesis Source: UniProtKB
    8. positive regulation of cell-matrix adhesion Source: UniProtKB
    9. positive regulation of cell migration Source: UniProtKB
    10. positive regulation of cell proliferation Source: UniProtKB
    11. positive regulation of stress fiber assembly Source: UniProtKB
    12. protein autophosphorylation Source: UniProtKB
    13. regulation of Rac GTPase activity Source: UniProtKB
    14. substrate adhesion-dependent cell spreading Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 1 (EC:2.7.10.1)
    Short name:
    mEpha1
    Alternative name(s):
    Embryonic stem cell kinase
    Tyrosine-protein kinase receptor ESK
    Gene namesi
    Name:Epha1
    Synonyms:Esk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:107381. Epha1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display a partially-penetrant uterovaginal and tail development defects. The uterovaginal defect is due to a defect in apoptosis during development.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 977951Ephrin type-A receptor 1By similarityPRO_0000016799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Modified residuei600 – 6001Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei606 – 6061Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei782 – 7821Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei907 – 9071PhosphoserineBy similarity
    Modified residuei911 – 9111PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1 By similarity.By similarity
    Ubiquitinated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ60750.
    PRIDEiQ60750.

    PTM databases

    PhosphoSiteiQ60750.

    Expressioni

    Tissue specificityi

    Preferentially expressed in epithelial cells including skin, kidney, liver and thymus.2 Publications

    Gene expression databases

    BgeeiQ60750.
    CleanExiMM_EPHA1.
    GenevestigatoriQ60750.

    Interactioni

    Subunit structurei

    Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration. Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199468. 1 interaction.
    IntActiQ60750. 4 interactions.
    MINTiMINT-7013408.

    Structurei

    Secondary structure

    1
    977
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi456 – 4605
    Beta strandi463 – 4675
    Beta strandi481 – 4877
    Beta strandi492 – 50615
    Beta strandi512 – 5209
    Beta strandi522 – 5243
    Beta strandi532 – 5354

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X5ANMR-A446-539[»]
    ProteinModelPortaliQ60750.
    SMRiQ60750. Positions 25-539, 600-909, 912-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60750.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 548522ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini570 – 977408CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei549 – 56921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 210183Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini333 – 446114Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini448 – 53992Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 885261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini914 – 97764SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 330139Cys-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.
    InParanoidiQ60750.
    KOiK05102.
    OMAiQAYEDPA.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiQ60750.
    TreeFamiTF315363.

    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. 1 hit.
    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.

    Q60750-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET    50
    GWSEVQQMLN GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL 100
    QFTVRDCKSF PGGAGPLGCK ETFNLFYMES DQDVGIQLRR PLFQKVTTVA 150
    ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR GLYLAFHNPG SCVALVSVRV 200
    FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL GSSGTPRMHC 250
    SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ 300
    HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS 350
    LRWEPPRDTG GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL 400
    TTSTVQVQGL EPYANYTFTV KSQNRVSGLD SSSPSSASLS INMGHAESLS 450
    GLSLKLVKKE PRQLELTWAG SRPRNPGGNL SYELHVLNQD EEWHQMVLEP 500
    RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV SRSLTGGEIV 550
    AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY 600
    VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD 650
    CKTVAIKTLK DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM 700
    IITEFMENGA LDAFLKERED QLAPGQLVAM LLGIASGMNC LSGHNYVHRD 750
    LAARNILVNQ NLCCKVSDFG LTRLLDDFDG TYETQGGKIP IRWTAPEAIA 800
    HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI EDGYRLPPPV 850
    DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR 900
    VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT 950
    AEDLTQMGIT LPGHQKRILC SIQGFKD 977
    Length:977
    Mass (Da):108,578
    Last modified:May 10, 2004 - v2
    Checksum:iAB78D6E6C8B2E7F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1631G → D in AAG12206. (PubMed:11519828)Curated
    Sequence conflicti422 – 4221S → P in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti504 – 5041L → R in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti521 – 5211T → A in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti590 – 5901D → G in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti636 – 6361F → Y in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti660 – 6601K → R in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti720 – 7201D → G in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti769 – 7691F → L in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti797 – 7971E → G in AAC52384. (PubMed:8552593)Curated
    Sequence conflicti817 – 8171M → T in AAG12206. (PubMed:11519828)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF131197 mRNA. Translation: AAG12206.1.
    AK028478 mRNA. Translation: BAC25971.1.
    U18084 mRNA. Translation: AAC52384.1.
    CCDSiCCDS20067.1.
    RefSeqiNP_076069.2. NM_023580.4.
    UniGeneiMm.133330.

    Genome annotation databases

    EnsembliENSMUST00000073387; ENSMUSP00000073099; ENSMUSG00000029859.
    GeneIDi13835.
    KEGGimmu:13835.
    UCSCiuc009brc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF131197 mRNA. Translation: AAG12206.1 .
    AK028478 mRNA. Translation: BAC25971.1 .
    U18084 mRNA. Translation: AAC52384.1 .
    CCDSi CCDS20067.1.
    RefSeqi NP_076069.2. NM_023580.4.
    UniGenei Mm.133330.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X5A NMR - A 446-539 [» ]
    ProteinModelPortali Q60750.
    SMRi Q60750. Positions 25-539, 600-909, 912-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199468. 1 interaction.
    IntActi Q60750. 4 interactions.
    MINTi MINT-7013408.

    PTM databases

    PhosphoSitei Q60750.

    Proteomic databases

    PaxDbi Q60750.
    PRIDEi Q60750.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073387 ; ENSMUSP00000073099 ; ENSMUSG00000029859 .
    GeneIDi 13835.
    KEGGi mmu:13835.
    UCSCi uc009brc.1. mouse.

    Organism-specific databases

    CTDi 2041.
    MGIi MGI:107381. Epha1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115081.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi Q60750.
    KOi K05102.
    OMAi QAYEDPA.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi Q60750.
    TreeFami TF315363.

    Enzyme and pathway databases

    Reactomei REACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

    Miscellaneous databases

    EvolutionaryTracei Q60750.
    NextBioi 284652.
    PROi Q60750.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q60750.
    CleanExi MM_EPHA1.
    Genevestigatori Q60750.

    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. 1 hit.
    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. "Characterization of the Epha1 receptor tyrosine kinase: expression in epithelial tissues."
      Coulthard M.G., Lickliter J.D., Subanesan N., Chen K., Webb G.C., Lowry A.J., Koblar S., Bottema C.D., Boyd A.W.
      Growth Factors 18:303-317(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, EFNA1 LIGAND-BINDING.
    2. "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: Skin.
    3. "Embryonic stem cells express multiple Eph-subfamily receptor tyrosine kinases."
      Lickliter J.D., Smith F.M., Olsson J.E., Mackwell K.L., Boyd A.W.
      Proc. Natl. Acad. Sci. U.S.A. 93:145-150(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-814.
      Strain: 129/Sv.
    4. "Generation and characterization of EphA1 receptor tyrosine kinase reporter knockout mice."
      Duffy S.L., Coulthard M.G., Spanevello M.D., Herath N.I., Yeadon T.M., McCarron J.K., Carter J.C., Tonks I.D., Kay G.F., Phillips G.E., Boyd A.W.
      Genesis 46:553-561(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS, TISSUE SPECIFICITY.
    5. "The solution structure of the second fibronectin type III domain of mouse ephrin type-A receptor 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 446-539.

    Entry informationi

    Entry nameiEPHA1_MOUSE
    AccessioniPrimary (citable) accession number: Q60750
    Secondary accession number(s): Q8CED9, Q9ESJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3