EGFR_MACMU
ID EGFR_MACMU Reviewed; 1210 AA.
AC P55245; F6YXS7; G7ML99; H9FAB2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Epidermal growth factor receptor;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=EGFR;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573;
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1210.
RC TISSUE=Caudate nucleus;
RA Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.;
RT "De novo assembly of the rhesus macaque transcriptome from NextGen mRNA
RT sequences.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 893-977, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Hypothalamus;
RX PubMed=7545971; DOI=10.1159/000126769;
RA Ma Y.J., Costa M.E., Ojeda S.R.;
RT "Developmental expression of the genes encoding transforming growth factor
RT alpha and its receptor in the hypothalamus of female rhesus macaques.";
RL Neuroendocrinology 60:346-359(1994).
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. Known ligands include EGF,
CC TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG
CC and HBEGF/heparin-binding EGF. Ligand binding triggers receptor
CC 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 (By similarity). {ECO:0000250|UniProtKB:P00533,
CC ECO:0000250|UniProtKB:Q01279}.
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 -!- 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 regions) and
CC GNAI3 which leads to enhanced EGFR signaling and triggering of cell
CC migration; binding to CCDC88A requires autophosphorylation of the EGFR
CC C-terminal region, and ligand stimulation is required for recruitment
CC of GNAI3 to the complex. Interacts with ERRFI1; inhibits dimerization
CC of the kinase domain and autophosphorylation. Part of a complex with
CC ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter
CC protein coupling the receptor to downstream signaling pathways.
CC Interacts with GAB2; involved in signaling downstream of EGFR.
CC Interacts with STAT3; mediates EGFR downstream signaling in cell
CC proliferation. Interacts with RIPK1; involved in NF-kappa-B activation.
CC Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in
CC EGFR ubiquitination and regulation. Interacts with SOCS5; regulates
CC EGFR degradation through ELOC- and ELOB-mediated ubiquitination and
CC proteasomal degradation. Interacts with PRMT5; methylates EGFR and
CC enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6;
CC inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1;
CC essential for regulation of EGF-dependent nuclear transport of EGFR by
CC retrograde trafficking from the Golgi to the ER. Interacts with TNK2;
CC this interaction is dependent on EGF stimulation and kinase activity of
CC EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with
CC PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER.
CC May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via
CC SH2 domains) with GRB2, NCK1 and NCK2. Interacts with ATXN2. Interacts
CC with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the
CC interaction is direct and may regulate EGFR internalization after EGF
CC stimulation. Interacts with GPER1; the interaction occurs in an
CC estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase
CC domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126.
CC Interacts with GPRC5A (via its transmembrane domain). Interacts with
CC FAM83B; positively regulates EGFR inducing its autophosphorylation in
CC absence of stimulation by EGF. Interacts with LAPTM4B; positively
CC correlates with EGFR activation. Interacts with STX19. Interacts with
CC CD44. Interacts with PGRMC1; the interaction requires PGRMC1
CC homodimerization. Interacts with PIKFYVE. Interacts with NEU3.
CC Interacts with TRAF4. {ECO:0000250|UniProtKB:P00533}.
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 -!- TISSUE SPECIFICITY: Hypothalamus. {ECO:0000269|PubMed:7545971}.
CC -!- DEVELOPMENTAL STAGE: Levels in the medial basal hypothalamus and
CC preoptic area are elevated during neonatal life (1 week-6 months),
CC decrease during juvenile development (8-18 months) and markedly
CC increase during the expected time of puberty (30-36 months).
CC {ECO:0000269|PubMed:7545971}.
CC -!- PTM: Phosphorylated on Tyr residues in response to EGF. Phosphorylation
CC at Ser-695 is partial and occurs only if Thr-693 is phosphorylated.
CC Phosphorylation at Thr-678 and Thr-693 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-1197 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: 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 (By similarity).
CC Polyubiquitin linkage is mainly through 'Lys-63', but linkage through
CC 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B
CC prevents degradation. Ubiquitinated by RNF115 and RNF126 (By
CC similarity). {ECO:0000250|UniProtKB:P00533,
CC ECO:0000250|UniProtKB:Q01279}.
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 -!- 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; JH286850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM001255; EHH17303.1; -; Genomic_DNA.
DR EMBL; JU327815; AFE71571.1; -; mRNA.
DR EMBL; S75916; AAB33095.1; -; mRNA.
DR PIR; I78540; I78540.
DR RefSeq; XP_014988922.1; XM_015133436.1.
DR AlphaFoldDB; P55245; -.
DR BMRB; P55245; -.
DR SMR; P55245; -.
DR STRING; 9544.ENSMMUP00000029471; -.
DR GeneID; 613027; -.
DR KEGG; mcc:613027; -.
DR CTD; 1956; -.
DR eggNOG; KOG1025; Eukaryota.
DR HOGENOM; CLU_003384_0_1_1; -.
DR InParanoid; P55245; -.
DR OrthoDB; 81952at2759; -.
DR TreeFam; TF106002; -.
DR Proteomes; UP000006718; Unplaced.
DR Proteomes; UP000013456; Chromosome 3.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IEA:UniProtKB-SubCell.
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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0048408; F:epidermal growth factor binding; IBA:GO_Central.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; -; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Hydroxylation; Isopeptide bond;
KW Kinase; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Nucleus;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW 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_0000160254"
FT TOPO_DOM 25..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..300
FT /note="Approximate"
FT REPEAT 390..600
FT /note="Approximate"
FT DOMAIN 712..979
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 688..704
FT /note="Important for dimerization, phosphorylation and
FT activation"
FT /evidence="ECO:0000250"
FT REGION 1097..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 718..726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 790..791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1016
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 678
FT /note="Phosphothreonine; by PKC and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 693
FT /note="Phosphothreonine; by PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 745
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 998
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1016
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1041
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1064
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 1081
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; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 1199
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT LIPID 1049
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:0000250"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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 716
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 867
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CROSSLNK 970
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CONFLICT 541
FT /note="V -> I (in Ref. 2; EHH17303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1210 AA; 134350 MW; E114E9CEE96D64CC CRC64;
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA
VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS EFLSNMSMDF
QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC
TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDTLS INATNIKHFK
NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF
ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL
FGTSSQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCQNVS RGRECVDKCN
VLEGEPREFV ENSECIQCHP ECLPQVMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCARNG PKIPSIATGM VGALLLLLVV
ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS
GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI
CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA
RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK
FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ
QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED
SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN
TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV
APQSSEFIGA
