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P55245

- EGFR_MACMU

UniProt

P55245 - EGFR_MACMU

Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (22 Jan 2014)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.

    Catalytic activityi

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

    Enzyme regulationi

    Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei745 – 7451ATPPROSITE-ProRule annotation
    Active sitei837 – 8371Proton acceptorPROSITE-ProRule annotation
    Binding sitei855 – 8551ATPPROSITE-ProRule annotation
    Sitei1016 – 10161Important for interaction with PIK3C2BBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi718 – 7269ATPPROSITE-ProRule annotation
    Nucleotide bindingi790 – 7912ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. epidermal growth factor-activated receptor activity Source: Ensembl
    4. nitric-oxide synthase regulator activity Source: Ensembl
    5. protein tyrosine kinase activity Source: UniProtKB
    6. receptor signaling protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    1. cell morphogenesis Source: Ensembl
    2. cell proliferation Source: Ensembl
    3. cellular response to epidermal growth factor stimulus Source: UniProtKB
    4. cellular response to estradiol stimulus Source: UniProtKB
    5. cerebral cortex cell migration Source: Ensembl
    6. digestive tract morphogenesis Source: Ensembl
    7. embryonic placenta development Source: Ensembl
    8. epidermal growth factor receptor signaling pathway Source: UniProtKB
    9. hair follicle development Source: Ensembl
    10. learning or memory Source: UniProtKB
    11. morphogenesis of an epithelial fold Source: Ensembl
    12. negative regulation of apoptotic process Source: Ensembl
    13. negative regulation of protein catabolic process Source: Ensembl
    14. positive regulation of catenin import into nucleus Source: Ensembl
    15. positive regulation of cell migration Source: Ensembl
    16. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    17. positive regulation of DNA repair Source: Ensembl
    18. positive regulation of DNA replication Source: Ensembl
    19. positive regulation of epithelial cell proliferation Source: Ensembl
    20. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    21. positive regulation of fibroblast proliferation Source: Ensembl
    22. positive regulation of MAP kinase activity Source: Ensembl
    23. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    24. positive regulation of protein kinase B signaling Source: Ensembl
    25. positive regulation of protein phosphorylation Source: UniProtKB
    26. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    27. protein autophosphorylation Source: Ensembl
    28. regulation of nitric-oxide synthase activity Source: Ensembl
    29. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    30. response to UV-A Source: Ensembl
    31. salivary gland morphogenesis Source: Ensembl
    32. single organismal cell-cell adhesion Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor (EC:2.7.10.1)
    Gene namesi
    Name:EGFR
    OrganismiMacaca mulatta (Rhesus macaque)
    Taxonomic identifieri9544 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
    ProteomesiUP000006718: Unplaced

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity. Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity. Nucleus membrane By similarity; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane By similarity. Nucleus By similarity
    Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) By similarity.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. endocytic vesicle Source: Ensembl
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. endosome Source: UniProtKB
    5. endosome membrane Source: UniProtKB-SubCell
    6. Golgi membrane Source: UniProtKB-SubCell
    7. integral component of membrane Source: UniProtKB-KW
    8. membrane raft Source: Ensembl
    9. nuclear membrane Source: UniProtKB-SubCell
    10. nucleus Source: UniProtKB
    11. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 12101186Epidermal growth factor receptorPRO_0000160254Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 58By similarity
    Glycosylationi73 – 731N-linked (GlcNAc...); atypicalBy similarity
    Glycosylationi128 – 1281N-linked (GlcNAc...)By similarity
    Disulfide bondi157 ↔ 187By similarity
    Glycosylationi175 – 1751N-linked (GlcNAc...)By similarity
    Disulfide bondi190 ↔ 199By similarity
    Disulfide bondi194 ↔ 207By similarity
    Glycosylationi196 – 1961N-linked (GlcNAc...)By similarity
    Disulfide bondi215 ↔ 223By similarity
    Disulfide bondi219 ↔ 231By similarity
    Modified residuei229 – 2291PhosphoserineBy similarity
    Disulfide bondi232 ↔ 240By similarity
    Disulfide bondi236 ↔ 248By similarity
    Disulfide bondi251 ↔ 260By similarity
    Disulfide bondi264 ↔ 291By similarity
    Disulfide bondi295 ↔ 307By similarity
    Disulfide bondi311 ↔ 326By similarity
    Disulfide bondi329 ↔ 333By similarity
    Disulfide bondi337 ↔ 362By similarity
    Glycosylationi352 – 3521N-linked (GlcNAc...)By similarity
    Glycosylationi361 – 3611N-linked (GlcNAc...)By similarity
    Glycosylationi413 – 4131N-linked (GlcNAc...)By similarity
    Glycosylationi444 – 4441N-linked (GlcNAc...)By similarity
    Disulfide bondi470 ↔ 499By similarity
    Disulfide bondi506 ↔ 515By similarity
    Disulfide bondi510 ↔ 523By similarity
    Disulfide bondi526 ↔ 535By similarity
    Glycosylationi528 – 5281N-linked (GlcNAc...)By similarity
    Disulfide bondi539 ↔ 555By similarity
    Disulfide bondi558 ↔ 571By similarity
    Disulfide bondi562 ↔ 579By similarity
    Glycosylationi568 – 5681N-linked (GlcNAc...)By similarity
    Disulfide bondi582 ↔ 591By similarity
    Disulfide bondi595 ↔ 617By similarity
    Glycosylationi603 – 6031N-linked (GlcNAc...)By similarity
    Disulfide bondi620 ↔ 628By similarity
    Disulfide bondi624 ↔ 636By similarity
    Modified residuei678 – 6781Phosphothreonine; by PKC and PKD/PRKD1By similarity
    Modified residuei693 – 6931Phosphothreonine; by PKD/PRKD1By similarity
    Modified residuei695 – 6951PhosphoserineBy similarity
    Cross-linki716 – 716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki737 – 737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki754 – 754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki867 – 867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki929 – 929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki970 – 970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei991 – 9911PhosphoserineBy similarity
    Modified residuei995 – 9951PhosphoserineBy similarity
    Modified residuei998 – 9981Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1016 – 10161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1026 – 10261PhosphoserineBy similarity
    Modified residuei1039 – 10391PhosphoserineBy similarity
    Modified residuei1041 – 10411PhosphothreonineBy similarity
    Modified residuei1042 – 10421PhosphoserineBy similarity
    Modified residuei1064 – 10641PhosphoserineBy similarity
    Modified residuei1070 – 10701PhosphoserineBy similarity
    Modified residuei1071 – 10711PhosphoserineBy similarity
    Modified residuei1081 – 10811PhosphoserineBy similarity
    Modified residuei1092 – 10921Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1110 – 11101Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1166 – 11661PhosphoserineBy similarity
    Modified residuei1172 – 11721Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1197 – 11971Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1199 – 11991Omega-N-methylated arginineBy similarity

    Post-translational modificationi

    Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-955', but linkage through 'Lys-940', 'Lys-903' and 'Lys-921' also occur. Deubiquitinated by OTUD7B, preventing degradation By similarity.By similarity
    Phosphorylated. Autophosphorylates. Dephosphorylated by PTPN1 and PTPN2 By similarity.By similarity
    Methylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Expressioni

    Tissue specificityi

    Hypothalamus.

    Developmental stagei

    Levels in the medial basal hypothalamus and preoptic area are elevated during neonatal life (1 week-6 months), decrease during juvenile development (8-18 months) and markedly increase during the expected time of puberty (30-36 months).

    Interactioni

    Subunit structurei

    Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with ATX2. Interacts with GAREM. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers) By similarity.By similarity

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 645621ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini669 – 1210542CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei646 – 66823HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati75 – 300226ApproximateAdd
    BLAST
    Repeati390 – 600211ApproximateAdd
    BLAST
    Domaini712 – 979268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni688 – 70417Important for dimerization, phosphorylation and activationBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000230982.
    InParanoidiP55245.
    TreeFamiTF106002.

    Family and domain databases

    Gene3Di3.80.20.20. 2 hits.
    InterProiIPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
    [Graphical view]
    PfamiPF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00261. FU. 4 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P55245-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS     50
    LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP 100
    LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF 150
    SNNPALCNVE SIQWRDIVSS EFLSNMSMDF QNHLGSCQKC DPSCPNGSCW 200
    GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV 250
    CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 300
    VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDTLS 350
    INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE 400
    ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL 450
    RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSSQKTKI ISNRGENSCK 500
    ATGQVCHALC SPEGCWGPEP RDCVSCQNVS RGRECVDKCN VLEGEPREFV 550
    ENSECIQCHP ECLPQVMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 600
    GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCARNG PKIPSIATGM 650
    VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN 700
    QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA 750
    TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD 800
    YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH 850
    VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 900
    GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC 950
    WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA 1000
    LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI 1050
    DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR 1100
    PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST 1150
    FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 1200
    APQSSEFIGA 1210
    Length:1,210
    Mass (Da):134,350
    Last modified:January 22, 2014 - v2
    Checksum:iE114E9CEE96D64CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti541 – 5411V → I in EHH17303. (PubMed:22002653)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JH286850 Genomic DNA. No translation available.
    CM001255 Genomic DNA. Translation: EHH17303.1.
    JU327815 mRNA. Translation: AFE71571.1.
    S75916 mRNA. Translation: AAB33095.1.
    PIRiI78540.
    UniGeneiMmu.3397.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JH286850 Genomic DNA. No translation available.
    CM001255 Genomic DNA. Translation: EHH17303.1 .
    JU327815 mRNA. Translation: AFE71571.1 .
    S75916 mRNA. Translation: AAB33095.1 .
    PIRi I78540.
    UniGenei Mmu.3397.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P55245.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230982.
    InParanoidi P55245.
    TreeFami TF106002.

    Family and domain databases

    Gene3Di 3.80.20.20. 2 hits.
    InterProi IPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
    [Graphical view ]
    Pfami PF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00261. FU. 4 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evolutionary and biomedical insights from the rhesus macaque genome."
      Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., Makova K.D., Miller W., Milosavljevic A.
      , Palermo R.E., Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., Zwieg A.S.
      Science 316:222-234(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 17573.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "De novo assembly of the rhesus macaque transcriptome from NextGen mRNA sequences."
      Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.
      Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1210.
      Tissue: Caudate nucleus.
    4. "Developmental expression of the genes encoding transforming growth factor alpha and its receptor in the hypothalamus of female rhesus macaques."
      Ma Y.J., Costa M.E., Ojeda S.R.
      Neuroendocrinology 60:346-359(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 893-977.
      Tissue: Hypothalamus.

    Entry informationi

    Entry nameiEGFR_MACMU
    AccessioniPrimary (citable) accession number: P55245
    Secondary accession number(s): F6YXS7, G7ML99, H9FAB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 22, 2014
    Last modified: October 1, 2014
    This is version 119 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

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