ERBB2_MOUSE
ID ERBB2_MOUSE Reviewed; 1256 AA.
AC P70424; Q61525; Q6ZPE0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Receptor tyrosine-protein kinase erbB-2;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene Neu;
DE AltName: Full=Proto-oncogene c-ErbB-2;
DE AltName: Full=p185erbB2;
DE AltName: CD_antigen=CD340;
DE Flags: Precursor;
GN Name=Erbb2; Synonyms=Kiaa3023, Neu;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 786-934.
RC STRAIN=CD-1; TISSUE=Uterus;
RX PubMed=9048643; DOI=10.1210/endo.138.3.4991;
RA Lim J., Dey S.K., Das S.K.;
RT "Differential expression of the erbB2 gene in the periimplantation mouse
RT uterus: potential mediator of signaling by epidermal growth factor-like
RT growth factors.";
RL Endocrinology 138:1328-1337(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1012-1107.
RX PubMed=7589796; DOI=10.1006/dbio.1995.0012;
RA Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R.;
RT "Synapse-associated expression of an acetylcholine receptor-inducing
RT protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in
RT developing mammalian muscle.";
RL Dev. Biol. 172:158-169(1995).
RN [4]
RP FUNCTION, AND INTERACTION WITH SRC.
RX PubMed=7542762;
RA Muthuswamy S.K., Muller W.J.;
RT "Direct and specific interaction of c-Src with Neu is involved in signaling
RT by the epidermal growth factor receptor.";
RL Oncogene 11:271-279(1995).
RN [5]
RP INTERACTION WITH PRKCABP.
RX PubMed=11278603; DOI=10.1074/jbc.m010032200;
RA Jaulin-Bastard F., Saito H., Le Bivic A., Ollendorff V., Marchetto S.,
RA Birnbaum D., Borg J.-P.;
RT "The ERBB2/HER2 receptor differentially interacts with ERBIN and PICK1 PSD-
RT 95/DLG/ZO-1 domain proteins.";
RL J. Biol. Chem. 276:15256-15263(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 [7]
RP INTERACTION WITH MYOC.
RX PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA Tomarev S.I.;
RT "Myocilin mediates myelination in the peripheral nervous system through
RT ErbB2/3 signaling.";
RL J. Biol. Chem. 288:26357-26371(2013).
CC -!- FUNCTION: Protein tyrosine kinase that is part of several cell surface
CC receptor complexes, but that apparently needs a coreceptor for ligand
CC binding. Essential component of a neuregulin-receptor complex, although
CC neuregulins do not interact with it alone. GP30 is a potential ligand
CC for this receptor. Regulates outgrowth and stabilization of peripheral
CC microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1
CC signaling pathway elicits the phosphorylation and thus the inhibition
CC of GSK3B at cell membrane. This prevents the phosphorylation of APC and
CC CLASP2, allowing its association with the cell membrane. In turn,
CC membrane-bound APC allows the localization of MACF1 to the cell
CC membrane, which is required for microtubule capture and stabilization
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: In the nucleus is involved in transcriptional regulation.
CC Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter
CC and activates its transcription. Implicated in transcriptional
CC activation of CDKN1A; the function involves STAT3 and SRC. Involved in
CC the transcription of rRNA genes by RNA Pol I and enhances protein
CC synthesis and cell growth (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a
CC complex with EGFR and either PIK3C2A or PIK3C2B. May interact with
CC PIK3C2B when phosphorylated on Tyr-1197. Interacts with PLXNB1.
CC Interacts (when phosphorylated on Tyr-1249) with MEMO1. Interacts with
CC MUC1. Interacts (when phosphorylated on Tyr-1140) with GRB7 (via SH2
CC domain). Interacts (when phosphorylated on Tyr-1249) with ERBIN.
CC Interacts with KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA194 and ACTB.
CC Interacts (preferentially with the tyrosine phosphorylated form) with
CC CPNE3; this interaction occurs at the cell membrane and is increased in
CC a growth factor heregulin-dependent manner. Interacts with HSP90AA1 and
CC HSP90AB1 in an ATP-dependent manner; the interaction suppresses ERBB2
CC kinase activity (By similarity). Interacts with SRC (PubMed:7542762).
CC Interacts with MYOC (PubMed:23897819). Interacts with PRKCABP
CC (PubMed:11278603). Interacts with SORL1; this interaction regulates
CC ERBB2 subcellular distribution by promoting its recycling after
CC internalization from endosomes back to the plasma membrane, hence
CC stimulates ERBB2-mediated signaling (By similarity).
CC {ECO:0000250|UniProtKB:P04626, ECO:0000269|PubMed:11278603,
CC ECO:0000269|PubMed:23897819, ECO:0000269|PubMed:7542762}.
CC -!- INTERACTION:
CC P70424; P18762: Adrb2; NbExp=3; IntAct=EBI-2945468, EBI-491143;
CC P70424; Q61526: Erbb3; NbExp=2; IntAct=EBI-2945468, EBI-931878;
CC P70424; P42227: Stat3; NbExp=4; IntAct=EBI-2945468, EBI-602878;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04626};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}.
CC Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:P04626}. Nucleus
CC {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus
CC requires endocytosis, probably endosomal sorting and is mediated by
CC importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde
CC vesicles. {ECO:0000250|UniProtKB:P04626}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in uterine epithelial
CC cells. In the muscle, expression localizes to the synaptic sites of
CC muscle fibers.
CC -!- DEVELOPMENTAL STAGE: On days 1-4 of pregnancy, ERBB2 is detected
CC primarily in epithelial cells, the day 1 uterus showing the highest
CC accumulation. On day 5, the epithelium and the decidualizing stromal
CC cells around the implanting blastocyst exhibit accumulation of this
CC receptor. On days 6-8, the expression persists in the epithelium at
CC both the implantation and interimplantation sites in addition to modest
CC levels in the secondary decidual zone. On days 7 and 8, accumulation is
CC also prominent in the trophoblastic giant cells.
CC -!- PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one
CC subunit of the dimeric receptor phosphorylates tyrosine residues on the
CC other subunit. Ligand-binding increases phosphorylation on tyrosine
CC residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1249.
CC Dephosphorylated by PTPN12. {ECO:0000250|UniProtKB:P04626}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98297.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK129487; BAC98297.1; ALT_INIT; mRNA.
DR EMBL; U71126; AAB17380.1; -; mRNA.
DR EMBL; L47239; AAA93532.1; -; mRNA.
DR CCDS; CCDS25349.1; -.
DR RefSeq; NP_001003817.1; NM_001003817.1.
DR AlphaFoldDB; P70424; -.
DR SMR; P70424; -.
DR BioGRID; 199496; 9.
DR DIP; DIP-40912N; -.
DR IntAct; P70424; 6.
DR MINT; P70424; -.
DR STRING; 10090.ENSMUSP00000053897; -.
DR ChEMBL; CHEMBL2311234; -.
DR GlyGen; P70424; 7 sites.
DR iPTMnet; P70424; -.
DR PhosphoSitePlus; P70424; -.
DR jPOST; P70424; -.
DR MaxQB; P70424; -.
DR PaxDb; P70424; -.
DR PeptideAtlas; P70424; -.
DR PRIDE; P70424; -.
DR ProteomicsDB; 275937; -.
DR Antibodypedia; 740; 6121 antibodies from 61 providers.
DR DNASU; 13866; -.
DR Ensembl; ENSMUST00000058295; ENSMUSP00000053897; ENSMUSG00000062312.
DR GeneID; 13866; -.
DR KEGG; mmu:13866; -.
DR UCSC; uc007lgi.1; mouse.
DR CTD; 2064; -.
DR MGI; MGI:95410; Erbb2.
DR VEuPathDB; HostDB:ENSMUSG00000062312; -.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000158232; -.
DR HOGENOM; CLU_003384_1_1_1; -.
DR InParanoid; P70424; -.
DR OMA; YVSDRHC; -.
DR OrthoDB; 81952at2759; -.
DR PhylomeDB; P70424; -.
DR TreeFam; TF106002; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-1227986; Signaling by ERBB2.
DR Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
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-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-MMU-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR BioGRID-ORCS; 13866; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Erbb2; mouse.
DR PRO; PR:P70424; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P70424; protein.
DR Bgee; ENSMUSG00000062312; Expressed in dorsal pancreas and 202 other tissues.
DR Genevisible; P70424; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0038143; C:ERBB3:ERBB2 complex; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043219; C:lateral loop; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:BHF-UCL.
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:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IDA:MGI.
DR GO; GO:0038135; P:ERBB2-ERBB4 signaling pathway; IDA:MGI.
DR GO; GO:0044849; P:estrous cycle; ISO:MGI.
DR GO; GO:0010001; P:glial cell differentiation; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:BHF-UCL.
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:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0048485; P:sympathetic nervous system development; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
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 1: Evidence at protein level;
KW Activator; ATP-binding; Cell membrane; Cytoplasm; Disulfide bond; Endosome;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1256
FT /note="Receptor tyrosine-protein kinase erbB-2"
FT /id="PRO_0000042181"
FT TOPO_DOM 23..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..1256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 721..988
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 677..690
FT /note="Required for interaction with KPNB1 and EEA1"
FT /evidence="ECO:0000250"
FT REGION 1030..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1198
FT /note="Interaction with PIK3C2B"
FT /evidence="ECO:0000250"
FT REGION 1200..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 677..690
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1150..1165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 846
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 727..735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06494"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1113
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1140
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT MOD_RES 1249
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..53
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 163..193
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 196..205
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 200..213
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 221..228
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 225..236
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 237..245
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 241..253
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 256..265
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 269..296
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 300..312
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 316..332
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 335..339
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 343..368
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 476..505
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 512..521
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 516..529
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 532..541
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 545..561
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 564..577
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 568..585
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 588..597
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 601..624
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 627..635
FT /evidence="ECO:0000250|UniProtKB:P04626"
FT DISULFID 631..643
FT /evidence="ECO:0000250|UniProtKB:P04626"
SQ SEQUENCE 1256 AA; 138579 MW; 6040978428B93A28 CRC64;
MELAAWCRWG FLLALLSPGA AGTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL
ELTYLPANAS LSFLQDIQEV QGYMLIAHNR VKHVPLQRLR IVRGTQLFED KYALAVLDNR
DPLDNVTTAA PGRTPEGLRE LQLRSLTEIL KGGVLIRGNP QLCYQDMVLW KDVLRKNNQL
APVDMDTNRS RACPPCAPTC KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ
CAAGCTGPKH SDCLACLHFN HSGICELHCP ALITYNTDTF ESMLNPEGRY TFGASCVTTC
PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA GVCYGLGMEH LRGARAITSD
NIQEFAGCKK IFGSLAFLPE SFDGNPSSGV APLKPEHLQV FETLEEITGY LYISAWPESF
QDLSVFQNLR VIRGRILHDG AYSLTLQGLG IHSLGLRSLR ELGSGLALIH RNTHLCFVNT
VPWDQLFRNP HQALLHSGNR PEEACGLEGL VCNSLCARGH CWGPGPTQCV NCSQFLRGQE
CVEECRVWKG LPREYVRGKH CLPCHPECQP QNSSETCYGS EADQCEACAH YKDSSSCVAR
CPSGVKPDLS YMPIWKYPDE EGICQPCPIN CTHSCVDLDE RGCPAEQRAS PVTFIIATVV
GVLLFLIIVV VIGILIKRRR QKIRKYTMRR LLQETELVEP LTPSGAVPNQ AQMRILKETE
LRKLKVLGSG AFGTVYKGIW IPDGENVKIP VAIKVLRENT SPKANKEILD EAYVMAGVGS
PYVSRLLGIC LTSTVQLVTQ LMPYGCLLDH VREHRGRLGS QDLLNWCVQI AKGMSYLEEV
RLVHRDLAAR NVLVKSPNHV KITDFGLARL LDIDETEYHA DGGKVPIKWM ALESILRRRF
THQSDVWSYG VTVWELMTFG AKPYDGIPAR EIPDLLEKGE RLPQPPICTI DVYMIMVKCW
MIDSECRPRF RELVSEFSRM ARDPQRFVVI QNEDLGPSSP MDSTFYRSLL EDDDMGELVD
AEEYLVPQQG FFSPDPALGT GSTAHRRHRS SSARSGGGEL TLGLEPSEEE PPRSPLAPSE
GAGSDVFDGD LAVGVTKGLQ SLSPHDLSPL QRYSEDPTLP LPPETDGYVA PLACSPQPEY
VNQPEVRPQS PLTPEGPPPP IRPAGATLER PKTLSPGKNG VVKDVFAFGG AVENPEYLAP
RAGTASQPHP SPAFSPAFDN LYYWDQNSSE QGPPPSTFEG TPTAENPEYL GLDVPV
