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Database: UniProt
Entry: A0A2K6EBS0_MACNE
LinkDB: A0A2K6EBS0_MACNE
Original site: A0A2K6EBS0_MACNE 
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
//
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