EGFR_MOUSE
ID EGFR_MOUSE Reviewed; 1210 AA.
AC Q01279;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Epidermal growth factor receptor {ECO:0000305};
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=Egfr {ECO:0000312|MGI:MGI:95294};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1408137;
RA Avivi A., Skorecki K., Yayon A., Givol D.;
RT "Promoter region of the murine fibroblast growth factor receptor 2
RT (bek/KGFR) gene.";
RL Oncogene 7:1957-1962(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ, and CD-1; TISSUE=Decidua, and Liver;
RX PubMed=7678348; DOI=10.1073/pnas.90.1.55;
RA Paria B.C., Das S.K., Andrews G.K., Dey S.K.;
RT "Expression of the epidermal growth factor receptor gene is regulated in
RT mouse blastocysts during delayed implantation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:55-59(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Hibbs M.L.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B6/C3; TISSUE=Liver;
RX PubMed=8125255; DOI=10.1101/gad.8.4.399;
RA Luetteke N.C., Phillips H.K., Qiu T.H., Copeland N.G., Earp H.S.,
RA Jenkins N.A., Lee D.C.;
RT "The mouse waved-2 phenotype results from a point mutation in the EGF
RT receptor tyrosine kinase.";
RL Genes Dev. 8:399-413(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-714.
RC TISSUE=Brain;
RX PubMed=2030916;
RA Avivi A., Lax I., Ullrich A., Schlessinger J., Givol D., Morse B.;
RT "Comparison of EGF receptor sequences as a guide to study the ligand
RT binding site.";
RL Oncogene 6:673-676(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 969-1117.
RC STRAIN=C3H/HeJ;
RA Eisinger D.P., Serrero G.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION IN CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF EPS8, AND
RP INTERACTION WITH EPS8.
RX PubMed=8404850; DOI=10.1002/j.1460-2075.1993.tb06058.x;
RA Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T., Wong W.T.,
RA di Fiore P.P.;
RT "Eps8, a substrate for the epidermal growth factor receptor kinase,
RT enhances EGF-dependent mitogenic signals.";
RL EMBO J. 12:3799-3808(1993).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=7630400; DOI=10.1038/376337a0;
RA Miettinen P.J., Berger J.E., Meneses J., Phung Y., Pedersen R.A., Werb Z.,
RA Derynck R.;
RT "Epithelial immaturity and multiorgan failure in mice lacking epidermal
RT growth factor receptor.";
RL Nature 376:337-341(1995).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=7618084; DOI=10.1126/science.7618084;
RA Threadgill D.W., Dlugosz A.A., Hansen L.A., Tennenbaum T., Lichti U.,
RA Yee D., LaMantia C., Mourton T., Herrup K., Harris R.C.;
RT "Targeted disruption of mouse EGF receptor: effect of genetic background on
RT mutant phenotype.";
RL Science 269:230-234(1995).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=7618085; DOI=10.1126/science.7618085;
RA Sibilia M., Wagner E.F.;
RT "Strain-dependent epithelial defects in mice lacking the EGF receptor.";
RL Science 269:234-238(1995).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF EPS15, ACTIVITY REGULATION, AND ENDOCYTOSIS.
RX PubMed=10953014; DOI=10.1083/jcb.150.4.905;
RA Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.;
RT "Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but
RT not constitutive, endocytosis.";
RL J. Cell Biol. 150:905-912(2000).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [13]
RP INTERACTION WITH STX19.
RX PubMed=16420529; DOI=10.1111/j.1600-0854.2005.00378.x;
RA Wang Y., Foo L.Y., Guo K., Gan B.Q., Zeng Q., Hong W., Tang B.L.;
RT "Syntaxin 9 is enriched in skin hair follicle epithelium and interacts with
RT the epidermal growth factor receptor.";
RL Traffic 7:216-226(2006).
RN [14]
RP INTERACTION WITH PIKFYVE.
RX PubMed=17909029; DOI=10.1158/0008-5472.can-07-1333;
RA Kim J., Jahng W.J., Di Vizio D., Lee J.S., Jhaveri R., Rubin M.A.,
RA Shisheva A., Freeman M.R.;
RT "The phosphoinositide kinase PIKfyve mediates epidermal growth factor
RT receptor trafficking to the nucleus.";
RL Cancer Res. 67:9229-9237(2007).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [18]
RP FUNCTION.
RX PubMed=20639532; DOI=10.1093/nar/gkq634;
RA Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
RT "A novel role of CPEB3 in regulating EGFR gene transcription via
RT association with Stat5b in neurons.";
RL Nucleic Acids Res. 38:7446-7457(2010).
RN [19]
RP UBIQUITINATION BY RNF115 AND RNF126, AND INTERACTION WITH RNF115 AND
RP RNF126.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
RN [20]
RP INTERACTION WITH GPRC5A.
RX PubMed=25744720; DOI=10.1158/0008-5472.can-14-2005;
RA Zhong S., Yin H., Liao Y., Yao F., Li Q., Zhang J., Jiao H., Zhao Y.,
RA Xu D., Liu S., Song H., Gao Y., Liu J., Ma L., Pang Z., Yang R., Ding C.,
RA Sun B., Lin X., Ye X., Guo W., Han B., Zhou B.P., Chin Y.E., Deng J.;
RT "Lung tumor suppressor GPRC5A binds EGFR and restrains its effector
RT signaling.";
RL Cancer Res. 75:1801-1814(2015).
CC -!- FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family
CC and activating several signaling cascades to convert extracellular cues
CC into appropriate cellular responses (PubMed:8404850). Known ligands
CC include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin,
CC epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers
CC receptor homo- and/or heterodimerization and autophosphorylation on key
CC cytoplasmic residues. The phosphorylated receptor recruits adapter
CC proteins like GRB2 which in turn activates complex downstream signaling
CC cascades. Activates at least 4 major downstream signaling cascades
CC including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs
CC modules. May also activate the NF-kappa-B signaling cascade. Also
CC directly phosphorylates other proteins like RGS16, activating its
CC GTPase activity and probably coupling the EGF receptor signaling to the
CC G protein-coupled receptor signaling. Also phosphorylates MUC1 and
CC increases its interaction with SRC and CTNNB1/beta-catenin (By
CC similarity). Positively regulates cell migration via interaction with
CC CCDC88A/GIV which retains EGFR at the cell membrane following ligand
CC stimulation, promoting EGFR signaling which triggers cell migration (By
CC similarity). Plays a role in enhancing learning and memory performance
CC (PubMed:20639532). {ECO:0000250|UniProtKB:P00533,
CC ECO:0000269|PubMed:10953014, ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:8404850}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Endocytosis and inhibition of the activated EGFR
CC by phosphatases like PTPRJ and PTPRK constitute immediate regulatory
CC mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR
CC endocytosis and activity. Moreover, inducible feedback inhibitors
CC including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative
CC regulatory mechanisms for the EGFR signaling.
CC {ECO:0000269|PubMed:10953014}.
CC -!- SUBUNIT: Binding of the ligand triggers homo- and/or heterodimerization
CC of the receptor triggering its autophosphorylation. Heterodimer with
CC ERBB2. Forms a complex with CCDC88A/GIV (via SH2-like region) and GNAI3
CC which leads to enhanced EGFR signaling and triggering of cell
CC migration; binding of CCDC88A requires autophosphorylation of the EGFR
CC C-terminal region, and ligand stimulation is required for recruitment
CC of GNAI3 to the complex (By similarity). Interacts with ERRFI1;
CC inhibits dimerization of the kinase domain and autophosphorylation.
CC Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts
CC with GRB2; an adapter protein coupling the receptor to downstream
CC signaling pathways. Interacts with GAB2; involved in signaling
CC downstream of EGFR. Interacts with STAT3; mediates EGFR downstream
CC signaling in cell proliferation. Interacts with RIPK1; involved in NF-
CC kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and
CC CBLC; involved in EGFR ubiquitination and regulation. Interacts with
CC SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated
CC ubiquitination and proteasomal degradation. Interacts with PRMT5;
CC methylates EGFR and enhances interaction with PTPN6. Interacts
CC (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of
CC MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-
CC dependent nuclear transport of EGFR by retrograde trafficking from the
CC Golgi to the ER. Interacts with TNK2; this interaction is dependent on
CC EGF stimulation and kinase activity of EGFR. Interacts with PCNA;
CC positively regulates PCNA. Interacts with PELP1. Interacts with MUC1.
CC Interacts with AP2M1. Interacts with FER. Interacts (via SH2 domains)
CC with GRB2, NCK1 and NCK2. Interacts with EPS8; mediates EPS8
CC phosphorylation. Interacts with ATXN2. Interacts with GAREM1. Interacts
CC (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may
CC regulate EGFR internalization after EGF stimulation. Interacts with
CC GPER1; the interaction occurs in an estrogen-dependent manner.
CC Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via
CC zinc fingers). Interacts with RNF115 and RNF126. Interacts with GPRC5A
CC (via its transmembrane domain) (PubMed:25744720). Interacts with
CC FAM83B; positively regulates EGFR inducing its autophosphorylation in
CC absence of stimulation by EGF (By similarity). Interacts with LAPTM4B;
CC positively correlates with EGFR activation (By similarity). Interacts
CC with STX19 (PubMed:16420529). Interacts with CD44 (By similarity).
CC Interacts with PGRMC1; the interaction requires PGRMC1 homodimerization
CC (By similarity). Interacts with PIKFYVE (PubMed:17909029). Interacts
CC with NEU3. Interacts with TRAF4. {ECO:0000250|UniProtKB:P00533,
CC ECO:0000269|PubMed:16420529, ECO:0000269|PubMed:17909029,
CC ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:25744720,
CC ECO:0000269|PubMed:8404850}.
CC -!- INTERACTION:
CC Q01279; P22682: Cbl; NbExp=2; IntAct=EBI-6296235, EBI-640919;
CC Q01279; P32883: Kras; NbExp=3; IntAct=EBI-6296235, EBI-644267;
CC Q01279; Q15109: AGER; Xeno; NbExp=2; IntAct=EBI-6296235, EBI-1646426;
CC Q01279; P01133: EGF; Xeno; NbExp=3; IntAct=EBI-6296235, EBI-640857;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00533};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P00533}. Endosome
CC {ECO:0000250|UniProtKB:P00533}. Endosome membrane
CC {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}.
CC Note=In response to EGF, translocated from the cell membrane to the
CC nucleus via Golgi and ER. Endocytosed upon activation by ligand.
CC Colocalized with GPER1 in the nucleus of estrogen agonist-induced
CC cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}.
CC -!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
CC which does not affect tyrosine kinase activity or signaling capacity
CC but may play a role in lysosomal targeting. Polyubiquitin linkage is
CC mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and
CC 'Lys-29' also occurs. Deubiquitinated by OTUD7B, preventing degradation
CC (By similarity). Ubiquitinated by RNF115 and RNF126.
CC {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:23418353}.
CC -!- PTM: Phosphorylated on Tyr residues in response to EGF. Phosphorylation
CC at Ser-697 is partial and occurs only if Thr-695 is phosphorylated.
CC Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced
CC MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis
CC and stabilizes the receptor at the plasma membrane. Autophosphorylation
CC at Tyr-1199 is stimulated by methylation at Arg-1199 and enhances
CC interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110
CC recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.
CC {ECO:0000250|UniProtKB:P00533}.
CC -!- PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits
CC internalization after ligand binding, and increases the persistence of
CC tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation
CC increases the amplitude and duration of EGFR signaling.
CC {ECO:0000250|UniProtKB:P00533}.
CC -!- PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates
CC phosphorylation at Tyr-1197. {ECO:0000250|UniProtKB:P00533}.
CC -!- DISRUPTION PHENOTYPE: Mice are growth retarded and die at different
CC stages of development depending on their genetic background. Embryonic
CC death is due to placental defects. Mice surviving until birth or later
CC display brain, bone, heart and various epithelial development defects
CC in several organs, including skin, lung and gastrointestinal tract.
CC {ECO:0000269|PubMed:7618084, ECO:0000269|PubMed:7618085,
CC ECO:0000269|PubMed:7630400}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X78987; CAA55587.1; -; mRNA.
DR EMBL; U03425; AAA17899.1; -; mRNA.
DR EMBL; X59698; CAA42219.1; -; mRNA.
DR EMBL; L06864; AAA53029.1; -; mRNA.
DR EMBL; Z12608; CAA78249.1; -; mRNA.
DR CCDS; CCDS24443.1; -.
DR PIR; A53183; A53183.
DR RefSeq; NP_997538.1; NM_207655.2.
DR AlphaFoldDB; Q01279; -.
DR BMRB; Q01279; -.
DR SMR; Q01279; -.
DR BioGRID; 199402; 44.
DR CORUM; Q01279; -.
DR DIP; DIP-5763N; -.
DR IntAct; Q01279; 14.
DR MINT; Q01279; -.
DR STRING; 10090.ENSMUSP00000020329; -.
DR BindingDB; Q01279; -.
DR ChEMBL; CHEMBL3608; -.
DR GlyConnect; 2297; 1 N-Linked glycan (1 site).
DR GlyGen; Q01279; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q01279; -.
DR PhosphoSitePlus; Q01279; -.
DR SwissPalm; Q01279; -.
DR CPTAC; non-CPTAC-3383; -.
DR jPOST; Q01279; -.
DR PaxDb; Q01279; -.
DR PeptideAtlas; Q01279; -.
DR PRIDE; Q01279; -.
DR ProteomicsDB; 277563; -.
DR ABCD; Q01279; 1 sequenced antibody.
DR Antibodypedia; 718; 10079 antibodies from 64 providers.
DR DNASU; 13649; -.
DR Ensembl; ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
DR GeneID; 13649; -.
DR KEGG; mmu:13649; -.
DR UCSC; uc007ibo.1; mouse.
DR CTD; 1956; -.
DR MGI; MGI:95294; Egfr.
DR VEuPathDB; HostDB:ENSMUSG00000020122; -.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000155450; -.
DR HOGENOM; CLU_003384_0_1_1; -.
DR InParanoid; Q01279; -.
DR OMA; CYVGNIR; -.
DR OrthoDB; 81952at2759; -.
DR PhylomeDB; Q01279; -.
DR TreeFam; TF106002; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-1227986; Signaling by ERBB2.
DR Reactome; R-MMU-1236394; Signaling by ERBB4.
DR Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-177929; Signaling by EGFR.
DR Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
DR Reactome; R-MMU-180292; GAB1 signalosome.
DR Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-MMU-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR BioGRID-ORCS; 13649; 2 hits in 113 CRISPR screens.
DR ChiTaRS; Egfr; mouse.
DR PRO; PR:Q01279; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q01279; protein.
DR Bgee; ENSMUSG00000020122; Expressed in left lobe of liver and 292 other tissues.
DR ExpressionAtlas; Q01279; baseline and differential.
DR Genevisible; Q01279; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0097489; C:multivesicular body, internal vesicle lumen; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0048408; F:epidermal growth factor binding; IDA:MGI.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IGI:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:Ensembl.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1905208; P:negative regulation of cardiocyte differentiation; ISO:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; ISO:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:MGI.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
DR GO; GO:0033594; P:response to hydroxyisoflavone; IEA:Ensembl.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0070141; P:response to UV-A; ISO:MGI.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0043586; P:tongue development; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; -; 2.
DR Gene3D; 6.10.250.2930; -; 1.
DR InterPro; IPR044912; Egfr_JX_dom.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
KW Hydroxylation; Isopeptide bond; Kinase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CHAIN 25..1210
FT /note="Epidermal growth factor receptor"
FT /id="PRO_0000016666"
FT TOPO_DOM 25..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..300
FT /note="Approximate"
FT REPEAT 390..600
FT /note="Approximate"
FT DOMAIN 714..981
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 690..706
FT /note="Important for dimerization, phosphorylation and
FT activation"
FT /evidence="ECO:0000250"
FT REGION 1113..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 839
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 720..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 792..793
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1018
FT /note="Important for interaction with PIK3C2B"
FT /evidence="ECO:0000250"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 680
FT /note="Phosphothreonine; by PKC and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 695
FT /note="Phosphothreonine; by PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 747
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1000
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1018
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1043
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1069
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1092
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1110
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1172
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1199
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT LIPID 1051
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT LIPID 1146
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..58
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 157..187
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 190..199
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 194..207
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 215..223
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 219..231
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 232..240
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 236..248
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 251..260
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 264..291
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 295..307
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 311..326
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 329..333
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 337..362
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 470..499
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 506..515
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 510..523
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 526..535
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 539..555
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 558..571
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 562..579
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 582..591
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 595..617
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 620..628
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 624..636
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 718
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 756
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 869
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 931
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CONFLICT 539
FT /note="C -> W (in Ref. 5; CAA42219)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="L -> F (in Ref. 4; AAA17899)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116..1117
FT /note="HP -> DR (in Ref. 6; CAA78249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1210 AA; 134853 MW; 690E20D46DF2D2F5 CRC64;
MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS LQRMYNNCEV
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN ALYENTYALA
ILSNYGTNRT GLRELPMRNL QEILIGAVRF SNNPILCNMD TIQWRDIVQN VFMSNMSMDL
QSHPSSCPKC DPSCPNGSCW GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC
TGPRESDCLV CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS INATNIKHFK
YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE ITGFLLIQAW PDNWTDLHAF
ENLEIIRGRT KQHGQFSLAV VGLNITSLGL RSLKEISDGD VIISGNRNLC YANTINWKKL
FGTPNQKTKI MNNRAEKDCK AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN
ILEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM
GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT GIVGGLLFIV
VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA PNQAHLRILK ETEFKKIKVL
GSGAFGTVYK GLWIPEGEKV KIPVAIKELR EATSPKANKE ILDEAYVMAS VDNPHVCRLL
GICLTSTVQL ITQLMPYGCL LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL
AARNVLVKTP QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW
SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV KCWMIDADSR
PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY RALMDEEDME DVVDADEYLI
PQQGFFNSPS TSRTPLLSSL SATSNNSTVA CINRNGSCRV KEDAFLQRYS SDPTGAVTED
NIDDAFLPVP EYVNQSVPKR PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN
TAQPTCLSSG FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV
APPSSEFIGA
