ID F7CBG7_CALJA Unreviewed; 1255 AA.
AC F7CBG7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000619};
GN Name=ERBB2 {ECO:0000313|EMBL:JAB15173.1,
GN ECO:0000313|Ensembl:ENSCJAP00000001808.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001808.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000001808.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB15173.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB43535.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB23621.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB15173.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB39883.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000001808.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037619}.
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:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR EMBL; GAMS01007963; JAB15173.1; -; mRNA.
DR EMBL; GAMR01010311; JAB23621.1; -; mRNA.
DR EMBL; GAMQ01001968; JAB39883.1; -; mRNA.
DR EMBL; GAMP01009220; JAB43535.1; -; mRNA.
DR RefSeq; XP_002806904.1; XM_002806858.3.
DR STRING; 9483.ENSCJAP00000001808; -.
DR Ensembl; ENSCJAT00000001919.5; ENSCJAP00000001808.3; ENSCJAG00000008874.5.
DR GeneID; 100391332; -.
DR KEGG; cjc:100391332; -.
DR CTD; 2064; -.
DR GeneTree; ENSGT00940000158232; -.
DR OMA; YVSDRHC; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF106002; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000008874; Expressed in kidney and 6 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0038143; C:ERBB3:ERBB2 complex; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002116; C:semaphorin receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; IEA:Ensembl.
DR GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0001042; F:RNA polymerase I core binding; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IEA:Ensembl.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IEA:Ensembl.
DR GO; GO:0038135; P:ERBB2-ERBB4 signaling pathway; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0032886; P:regulation of microtubule-based process; IEA:Ensembl.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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; 3.
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.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000619};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000619}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1255
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041117085"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 720..987
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1034..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 845
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 726..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 753
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1255 AA; 138225 MW; 0139419BE01DD04D CRC64;
MELAAWCRWG LLFALLPPGA AGTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL
ELTYLPANAS LSFLQDIQEV QGYVLIAHNQ VRQVPLQRLR IVRGTQLFED NYALAVLDNG
DPLDNTTPVT GASPGGLREL QLRSLTEILK GGVWIQRNPQ LCYQDMVLWK DIFHKNNQLA
LTLIDTNRSR ACHPCSPACK GSRCWGESSE DCQSLTRTVC AGGCARCKGP LPTDCCHEQC
AAGCTGPKHS DCLACLHFNH SGICELHCPA LVTYNTDTFE SMPNPEGRYT FGASCVTACP
YNYLSTDVGS CTLVCPLHNQ EVTAEDGTQR CEKCSKPCAR VCYGLGMEHL REVRAVTSAN
IQEFAGCKKI FGSLAFLPES FDGDPASNTV PLQPEQLQVF ETLEEITGYL YISAWPDSLP
DLSVFQNLQV IRGRILHNGA YLLTLQGLGI SWLGLRSLRE LGSGLALIHH NARLCFVHTV
PWDNLFRNPH QALLHTANRP EHECVGKDLA CHPLCARGHC WGPGPTQCVN CSQFLRGQEC
VEECRVLQGL PREYVNARHC LPCHPECQPQ NGSVTCSGPE ADQCVACAHY KDSPFCVARC
PSGVKPDLSY MPIWKFPDEE GTCQPCPINC THSCVDLDDK GCPAEQRASP LTSIISAVVG
ILLFMVLGLL LGILMKRRQQ KIRKYTMRRL LQETELVEPL TPSGAMPNQA QMRILKETEL
RKVKVLGSGA FGTVYKGIWI PDGENVKIPV AIKVLRENTS PKANKEILDE AYVMAGVGSP
YVSRLLGICL TSTVQLVTQL MPYGCLLDHV REHRGRLGSQ DLLNWCVQIA KGMSYLEDVR
LVHRDLAARN VLVKSPNHVK ITDFGLARLL DIDETEYHAD GGKVPIKWMA LESILRRRFT
HQSDVWSYGV TVWELMTFGA KPYDGIPARE IPDLLEKGER LPQPPICTID VYMIMVKCWM
IDSECRPRFR ELVSEFSRMA RDPQRFVVIQ NEDLGPASPL DSTFYRSLLE DDDMEDLVDA
EEYLVPQQGF FCPDPAPGAG GMAHHRHRSS STRSGSGDLM LGLEPSEEEA PRSPLAPSEG
AGSDVFDGDL GMGAAKGLQS LPPHDPSPLQ RYSEDPTVPL PSETDGYVAP PTCSPQPEYV
NQPDVRPQPS LPQEGPLPPA RPAGATLERP KTLSPGKNGV VKDVFAFGSA VENPEYLAPR
GGAAPQPHPP PAFSPAFDNL YYWDQDPSER GAPPSTFEGT PTAENPEYLG LDVPV
//
