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Epidermal growth factor receptor (EC 2.7.10.1)

 EGFR_MACMU              Reviewed;        1210 AA.
P55245; F6YXS7; G7ML99; H9FAB2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 2.
12-SEP-2018, entry version 150.
RecName: Full=Epidermal growth factor receptor;
EC=2.7.10.1;
Flags: Precursor;
Name=EGFR;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17573;
PubMed=17431167; DOI=10.1126/science.1139247;
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.;
"Evolutionary and biomedical insights from the rhesus macaque
genome.";
Science 316:222-234(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=22002653; DOI=10.1038/nbt.1992;
Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N.,
Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P.,
Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T.,
Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D.,
Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X.,
Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J.,
Wang X., Wang J.;
"Genome sequencing and comparison of two nonhuman primate animal
models, the cynomolgus and Chinese rhesus macaques.";
Nat. Biotechnol. 29:1019-1023(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1210.
TISSUE=Caudate nucleus;
Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.;
"De novo assembly of the rhesus macaque transcriptome from NextGen
mRNA sequences.";
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 893-977, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Hypothalamus;
PubMed=7545971;
Ma Y.J., Costa M.E., Ojeda S.R.;
"Developmental expression of the genes encoding transforming growth
factor alpha and its receptor in the hypothalamus of female rhesus
macaques.";
Neuroendocrinology 60:346-359(1994).
-!- FUNCTION: 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, AREG, 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 (By
similarity). Plays a role in enhancing learning and memory
performance (By similarity). {ECO:0000250|UniProtKB:P00533,
ECO:0000250|UniProtKB:Q01279}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ACTIVITY REGULATION: 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.
-!- SUBUNIT: 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 ELOC- and ELOB-
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 GAREM1. 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). Interacts with RNF115 and RNF126.
Interacts with GPRC5A (via its transmembrane domain). Interacts
with FAM83B; positively regulates EGFR inducing its
autophosphorylation in absence of stimulation by EGF. Interacts
with LAPTM4B; positively correlates with EGFR activation.
Interacts with STX19. {ECO:0000250|UniProtKB:P00533,
ECO:0000250|UniProtKB:Q01279}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus
membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane
{ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P00533}. Endosome
{ECO:0000250|UniProtKB:P00533}. Endosome membrane
{ECO:0000250|UniProtKB:P00533}. Nucleus
{ECO:0000250|UniProtKB:P00533}. 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). {ECO:0000250|UniProtKB:P00533}.
-!- TISSUE SPECIFICITY: Hypothalamus. {ECO:0000269|PubMed:7545971}.
-!- DEVELOPMENTAL STAGE: 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).
{ECO:0000269|PubMed:7545971}.
-!- PTM: Phosphorylated on Tyr residues in response to EGF.
Phosphorylation at Ser-695 is partial and occurs only if Thr-693
is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1
inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by
PTPRJ prevents endocytosis and stabilizes the receptor at the
plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by
methylation at Arg-1199 and enhances interaction with PTPN6.
Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3.
Dephosphorylated by PTPN1 and PTPN2.
{ECO:0000250|UniProtKB:P00533}.
-!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
which does not affect tyrosine kinase activity or signaling
capacity but may play a role in lysosomal targeting (By
similarity). Polyubiquitin linkage is mainly through 'Lys-63', but
linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs.
Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by
RNF115 and RNF126 (By similarity). {ECO:0000250|UniProtKB:P00533,
ECO:0000250|UniProtKB:Q01279}.
-!- PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation
inhibits internalization after ligand binding, and increases the
persistence of tyrosine-phosphorylated EGFR at the cell membrane.
Palmitoylation increases the amplitude and duration of EGFR
signaling. {ECO:0000250|UniProtKB:P00533}.
-!- PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates
phosphorylation at Tyr-1197. {ECO:0000250|UniProtKB:P00533}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; JH286850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CM001255; EHH17303.1; -; Genomic_DNA.
EMBL; JU327815; AFE71571.1; -; mRNA.
EMBL; S75916; AAB33095.1; -; mRNA.
PIR; I78540; I78540.
RefSeq; XP_014988922.1; XM_015133436.1.
UniGene; Mmu.3397; -.
SMR; P55245; -.
STRING; 9544.ENSMMUP00000029471; -.
PRIDE; P55245; -.
GeneID; 613027; -.
KEGG; mcc:613027; -.
CTD; 1956; -.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
HOGENOM; HOG000230982; -.
InParanoid; P55245; -.
KO; K04361; -.
TreeFam; TF106002; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
CDD; cd00064; FU; 3.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 4.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
Isopeptide bond; Kinase; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 24 {ECO:0000250|UniProtKB:P00533}.
CHAIN 25 1210 Epidermal growth factor receptor.
/FTId=PRO_0000160254.
TOPO_DOM 25 645 Extracellular. {ECO:0000255}.
TRANSMEM 646 668 Helical. {ECO:0000255}.
TOPO_DOM 669 1210 Cytoplasmic. {ECO:0000255}.
REPEAT 75 300 Approximate.
REPEAT 390 600 Approximate.
DOMAIN 712 979 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 718 726 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 790 791 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 688 704 Important for dimerization,
phosphorylation and activation.
{ECO:0000250}.
ACT_SITE 837 837 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 745 745 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 855 855 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1016 1016 Important for interaction with PIK3C2B.
{ECO:0000250}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 678 678 Phosphothreonine; by PKC and PKD/PRKD1.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 693 693 Phosphothreonine; by PKD/PRKD1.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 998 998 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1016 1016 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1026 1026 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1041 1041 Phosphothreonine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1069 1069 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1070 1070 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1071 1071 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1081 1081 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1092 1092 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1110 1110 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1172 1172 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1197 1197 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1199 1199 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1199 1199 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
LIPID 1049 1049 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P00533}.
LIPID 1146 1146 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P00533}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 31 58 {ECO:0000250|UniProtKB:P00533}.
DISULFID 157 187 {ECO:0000250|UniProtKB:P00533}.
DISULFID 190 199 {ECO:0000250|UniProtKB:P00533}.
DISULFID 194 207 {ECO:0000250|UniProtKB:P00533}.
DISULFID 215 223 {ECO:0000250|UniProtKB:P00533}.
DISULFID 219 231 {ECO:0000250|UniProtKB:P00533}.
DISULFID 232 240 {ECO:0000250|UniProtKB:P00533}.
DISULFID 236 248 {ECO:0000250|UniProtKB:P00533}.
DISULFID 251 260 {ECO:0000250|UniProtKB:P00533}.
DISULFID 264 291 {ECO:0000250|UniProtKB:P00533}.
DISULFID 295 307 {ECO:0000250|UniProtKB:P00533}.
DISULFID 311 326 {ECO:0000250|UniProtKB:P00533}.
DISULFID 329 333 {ECO:0000250|UniProtKB:P00533}.
DISULFID 337 362 {ECO:0000250|UniProtKB:P00533}.
DISULFID 470 499 {ECO:0000250|UniProtKB:P00533}.
DISULFID 506 515 {ECO:0000250|UniProtKB:P00533}.
DISULFID 510 523 {ECO:0000250|UniProtKB:P00533}.
DISULFID 526 535 {ECO:0000250|UniProtKB:P00533}.
DISULFID 539 555 {ECO:0000250|UniProtKB:P00533}.
DISULFID 558 571 {ECO:0000250|UniProtKB:P00533}.
DISULFID 562 579 {ECO:0000250|UniProtKB:P00533}.
DISULFID 582 591 {ECO:0000250|UniProtKB:P00533}.
DISULFID 595 617 {ECO:0000250|UniProtKB:P00533}.
DISULFID 620 628 {ECO:0000250|UniProtKB:P00533}.
DISULFID 624 636 {ECO:0000250|UniProtKB:P00533}.
CROSSLNK 716 716 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 737 737 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 754 754 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 867 867 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 929 929 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 970 970 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CONFLICT 541 541 V -> I (in Ref. 2; EHH17303).
{ECO:0000305}.
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


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