ID A0A2K6EBS0_MACNE Unreviewed; 963 AA.
AC A0A2K6EBS0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Receptor tyrosine-protein kinase erbB-2 {ECO:0000256|ARBA:ARBA00040669};
DE AltName: Full=Proto-oncogene c-ErbB-2 {ECO:0000256|ARBA:ARBA00041969};
DE AltName: Full=p185erbB2 {ECO:0000256|ARBA:ARBA00042465};
GN Name=ERBB2 {ECO:0000313|Ensembl:ENSMNEP00000045616.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000045616.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000045616.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A2K6EBS0; -.
DR Ensembl; ENSMNET00000070129.1; ENSMNEP00000045616.1; ENSMNEG00000045300.1.
DR GeneTree; ENSGT00940000158232; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000045300; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProt.
DR GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR CDD; cd00064; FU; 2.
DR CDD; cd05109; PTKc_HER2; 1.
DR Gene3D; 6.10.250.2930; -; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR044912; Egfr_JX_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 PANTHER; PTHR24416:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 1.
DR Pfam; PF21314; TM_ErbB1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
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 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..963
FT /note="Receptor tyrosine-protein kinase erbB-2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014318610"
FT TRANSMEM 359..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..695
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 742..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 963 AA; 106063 MW; 50D4C7842576908E CRC64;
MELAAWCRWG LLLALLPPGA AGTQDNYLST DVGSCTLVCP LHNQEVTAED GTQRCEKCSK
PCARVCYGLG MEHLREVRAV TSANIQEFAG CKKIFGSLAF LPESFDGDPA SNTAPLQPEQ
LRVFETLEEI TGYLYISAWP DSLPDLSVLQ NLQVIRGRIL HNGAYSLTLQ GLGISWLGLR
SLRELGSGLA LIHHNTRLCF VHTVPWDQLF RNPHQALLHT ANRPEDECVG EGLACHQLCA
RGHCWGPGPT QCVNCSQFLR GQECVEECRV LQGLPREYVN ARHCLPCHPE CQPQNGSVTC
FGPEADQCVA CAHYKDPPFC VARCPSGVKP DLSYMPIWKF PDEEGTCQPC PINCTHSPLT
SIISAVVGIL LVVVLGVVFG ILIKRRQQKI RKYTMRRLLQ ETELVEPLTP SGAMPNQAQM
RILKETELRK VKVLGSGAFG TVYKGIWIPD GENVKIPVAI KVLRENTSPK ANKEILDEAY
VMAGVGSPYV SRLLGICLTS TVQLVTQLMP YGCLLDHVRE NRGRLGSQDL LNWCMQIAKG
MSYLEDVRLV HRDLAARNVL VKSPNHVKIT DFGLARLLDI DETEYHADGG KVPIKWMALE
SILRRRFTHQ SDVWSYGVTV WELMTFGAKP YDGIPAREIP DLLEKGERLP QPPICTIDVY
MIMVKCWMID SECRPRFREL VSEFSRMARD PQRFVVIQNE DLGPASPLDS TFYRSLLEDD
DMGDLVDAEE YLVPQQGFFC PDPAPGTGGM VHHRHRSSST RSGGGDLTLG LEPSEEEAPR
SPRAPSEGTG SDVFDGDLGM GAAKGLQSLP AHDPSPLQRY SEDPTVPLPS ETDGYVAPLT
CSPQPEYVNQ PDVRPQPPSP QEGPLSPARP TGATLERPKT LSPGKNGVVK DVFAFGGAVE
NPEYLAPRGG AAPQPHLPPA FSPAFDNLYY WDQDPSERGA PPSTFKGTPT AENPEYLGLD
VPV
//