ID   B4DTR1_HUMAN            Unreviewed;       979 AA.
AC   B4DTR1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   13-FEB-2019, entry version 109.
DE   RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|SAAS:SAAS00593197};
DE            EC=2.7.10.1 {ECO:0000256|SAAS:SAAS00593197};
GN   Name=ERBB2 {ECO:0000313|Ensembl:ENSP00000404047};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG62073.1};
RN   [1] {ECO:0000213|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000404047, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3] {ECO:0000313|EMBL:BAG62073.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:BAG62073.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA   Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA   Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA   Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000213|PubMed:18691976}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [5] {ECO:0000213|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6] {ECO:0000213|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:ra3-RA3(2010).
RN   [7] {ECO:0000213|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:rs3-RS3(2011).
RN   [8] {ECO:0000313|Ensembl:ENSP00000404047}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [9] {ECO:0000213|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; Evidence={ECO:0000256|SAAS:SAAS01123262};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|SAAS:SAAS00941529}.
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DR   EMBL; AC079199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK300321; BAG62073.1; -; mRNA.
DR   UniGene; Hs.446352; -.
DR   Ensembl; ENST00000445658; ENSP00000404047; ENSG00000141736.
DR   UCSC; uc010wek.3; human.
DR   EuPathDB; HostDB:ENSG00000141736.13; -.
DR   HGNC; HGNC:3430; ERBB2.
DR   OpenTargets; ENSG00000141736; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   eggNOG; ENOG410XNSR; LUCA.
DR   GeneTree; ENSGT00940000158232; -.
DR   HOGENOM; HOG000230982; -.
DR   HOVERGEN; HBG000490; -.
DR   ChiTaRS; ERBB2; human.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000141736; Expressed in 212 organ(s), highest expression level in esophagus mucosa.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00064; FU; 2.
DR   Gene3D; 3.80.20.20; -; 1.
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   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
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   ATP-binding {ECO:0000256|SAAS:SAAS00461464};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Kinase {ECO:0000256|SAAS:SAAS00594505};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00461464};
KW   Proteomics identification {ECO:0000213|MaxQB:B4DTR1,
KW   ECO:0000213|PeptideAtlas:B4DTR1};
KW   Receptor {ECO:0000313|EMBL:BAG62073.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS00594505};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00594505}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    979       Receptor protein-tyrosine kinase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014085121.
FT   TRANSMEM    378    399       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      444    711       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
SQ   SEQUENCE   979 AA;  107571 MW;  F0015E7394171A14 CRC64;
     MELAALCRWG LLLALLPPGA ASTQDNYLST DVGSCTLVCP LHNQEVTAED GTQRCEKCSK
     PCARVCYGLG MEHLREVRAV TSANIQEFAG CKKIFGSLAF LPESFDGDPA SNTAPLQPEQ
     LQVFETLEEI TGYLYISAWP DSLPDLSVFQ NLQVIRGRIL HNGAYSLTLQ GLGISWLGLR
     SLRELGSGLA LIHHNTHLCF VHTVPWDQLF RNPHQALLHT ANRPEDECVG EGLACHQLCA
     RGHCWGPGPT QCVNCSQFLR GQECVEECRV LQGLPREYVN ARHCLPCHPE CQPQNGSVTC
     FGPEADQCVA CAHYKDPPFC VARCPSGVKP DLSYMPIWKF PDEEGACQPC PINCTHSCVD
     LDDKGCPAEQ RASPLTSIIS AVVGILLVVV LGVVFGILIK RRQQKIRKYT MRRLLQETEL
     VEPLTPSGAM PNQAQMRILK ETELRKVKVL GSGAFGTVYK GIWIPDGENV KIPVAIKVLR
     ENTSPKANKE ILDEAYVMAG VGSPYVSRLL GICLTSTVQL VTQLMPYGCL LDHVRENRGR
     LGSQDLLNWC MQIAKGMSYL EDVRLVHRDL AARNVLVKSP NHVKITDFGL ARLLDIDETE
     YHADGGKVPI KWMALESILR RRFTHQSDVW SYGVTVWELM TFGAKPYDGI PAREIPDLLE
     KGERLPQPPI CTIDVYMIMV KCWMIDSECR PRFRELVSEF SRMARDPQRF VVIQNEDLGP
     ASPLDSTFYR SLLEDDDMGD LVDAEEYLVP QQGFFCPDPA PGAGGMVHHR HRSSSTRSGG
     GDLTLGLEPS EEEAPRSPLA PSEGAGSDVF DGDLGMGAAK GLQSLPTHDP SPLQRYSEDP
     TVPLPSETDG YVAPLTCSPQ PEYVNQPDVR PQPPSPREGP LPAARPAGAT LERPKTLSPG
     KNGVVKDVFA FGGAVENPEY LTPQGGAAPQ PHPPPAFSPA FDNLYYWDQD PPERGAPPST
     FKGTPTAENP EYLGLDVPV
//