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   27-MAR-2024, entry version 226.
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). Interacts with
CC       SH3BGRL (By similarity). {ECO:0000250|UniProtKB:P04626,
CC       ECO:0000269|PubMed:11278603, ECO:0000269|PubMed:23897819,
CC       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       Cell projection, ruffle 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. Internalized from the cell membrane in response to EGF
CC       stimulation. {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};
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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   GlyCosmos; P70424; 7 sites, No reported glycans.
DR   GlyGen; P70424; 7 sites.
DR   iPTMnet; P70424; -.
DR   PhosphoSitePlus; P70424; -.
DR   jPOST; P70424; -.
DR   MaxQB; P70424; -.
DR   PaxDb; 10090-ENSMUSP00000053897; -.
DR   PeptideAtlas; P70424; -.
DR   ProteomicsDB; 275937; -.
DR   Pumba; P70424; -.
DR   Antibodypedia; 740; 7266 antibodies from 62 providers.
DR   DNASU; 13866; -.
DR   Ensembl; ENSMUST00000058295.6; ENSMUSP00000053897.6; ENSMUSG00000062312.6.
DR   GeneID; 13866; -.
DR   KEGG; mmu:13866; -.
DR   UCSC; uc007lgi.1; mouse.
DR   AGR; MGI:95410; -.
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; 1614410at2759; -.
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-1306955; GRB7 events in ERBB2 signaling.
DR   Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 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 79 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 204 other cell types or tissues.
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:0043219; C:lateral loop; ISO:MGI.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005902; C:microvillus; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005654; C:nucleoplasm; ISO: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:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0002116; C:semaphorin receptor complex; IMP:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015026; F:coreceptor activity; IMP:BHF-UCL.
DR   GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:MGI.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; 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:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR   GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
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:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0035025; P:positive regulation of Rho protein signal transduction; IMP:BHF-UCL.
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: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:0014044; P:Schwann cell development; IMP:MGI.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:BHF-UCL.
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   CDD; cd05109; PTKc_HER2; 1.
DR   CDD; cd12094; TM_ErbB2; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 4.10.1140.10; membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor like domain; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR049328; TM_ErbB1.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
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   Pfam; PF21314; TM_ErbB1; 1.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; P70424; MM.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Cell membrane; Cell projection; Cytoplasm;
KW   Disulfide bond; Endosome; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW   Signal; Transcription; Transcription regulation; Transferase;
KW   Transmembrane; Transmembrane helix; 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         878
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04626"
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
//