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Database: UniProt
Entry: A0A1D5NWM4_CHICK
LinkDB: A0A1D5NWM4_CHICK
Original site: A0A1D5NWM4_CHICK 
ID   A0A1D5NWM4_CHICK        Unreviewed;      1200 AA.
AC   A0A1D5NWM4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   11-DEC-2019, entry version 23.
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:ENSGALP00000044764};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000044764, ECO:0000313|Proteomes:UP000000539};
RN   [1] {ECO:0000313|Ensembl:ENSGALP00000044764, ECO:0000313|Proteomes:UP000000539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000044764,
RC   ECO:0000313|Proteomes:UP000000539};
RX   PubMed=15592404; DOI=10.1038/nature03154;
RG   International Chicken Genome Sequencing Consortium;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2] {ECO:0000313|Ensembl:ENSGALP00000044764}
RP   IDENTIFICATION.
RC   STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000044764};
RG   Ensembl;
RL   Submitted (OCT-2016) to UniProtKB.
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|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; AADN05000735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9031.ENSGALP00000029065; -.
DR   Ensembl; ENSGALT00000062155; ENSGALP00000044764; ENSGALG00000031529.
DR   GeneTree; ENSGT00940000158232; -.
DR   OrthoDB; 81952at2759; -.
DR   Reactome; R-GGA-1227986; Signaling by ERBB2.
DR   Reactome; R-GGA-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-GGA-1306955; GRB7 events in ERBB2 signaling.
DR   Reactome; R-GGA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-GGA-1963640; GRB2 events in ERBB2 signaling.
DR   Reactome; R-GGA-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-GGA-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-GGA-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-GGA-8863795; Downregulation of ERBB2 signaling.
DR   Proteomes; UP000000539; Chromosome 27.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase 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; IBA:GO_Central.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; 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:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
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:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; 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:0046777; P:protein autophosphorylation; 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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00064; FU; 3.
DR   Gene3D; 3.80.20.20; -; 2.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000619-2,
KW   ECO:0000256|SAAS:SAAS00245980}; Kinase {ECO:0000256|SAAS:SAAS00594439};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00244405};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW   Transferase {ECO:0000256|SAAS:SAAS00595469};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00594505}.
FT   TRANSMEM        608..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          674..941
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   NP_BIND         680..688
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   REGION          995..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1010
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1098..1112
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        799
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT   BINDING         707
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
SQ   SEQUENCE   1200 AA;  132206 MW;  9AF1F97AB4A77033 CRC64;
     MKLLQPSSPE SHYETLRHLY QGCQVVQGNL ELTYLPPGAD TAFLQDIKEV QGYVLIAENH
     VSAVGLQGLR IIRGTQLFQE RYALAVLGNV GLRQLGMRQL TEILKGGVHI EGNPQLCFQE
     TILWADIFHR HNELRSETRV ESTRSRTCPD CRALCAEGHC WGESPQDCQT LTNSICHGCP
     RCKGTKPTDC CHEQCAAGCT GPKHSDCLAC LNFNRSGICE LHCPPLVIYN SDTFESVPNR
     DGRYTFGASC VSQCPYNYLA TEVGSCTLVC PQNSQEVTVN NVQKCEKCSK PCPEVCYGLG
     VDFLKGVRAV NASNIRHFAG CTKIFGSLAF LPETFAGDPS TNTAPLDPQL LSVFESLEEL
     TGYLYIAAWP PGMDDLGVFQ NLRVIRGRVL HNGAYSLTLQ DLAVRALGLR ALQEISSGMV
     LIHHNPQLCF LQKVPWDSIF RHPRQHLFQT HNKAPEQCES DGLVCFHLCA HGHCWGPGPT
     QCVSCERFLR GQECVASCNL LDGATREHAN GTRCLPCHPE CQPQNGTETC FGSDADQCVA
     CAHYKDGQQC VRRCPSGVKV DASFVPIWKY PDEEGVCQLC PTNCTHSCTI RDEDGCPVDQ
     KPSQVTSIIA GVVGALLVVV LLLITVVCVK RRRQQERKHT MRRLLQETEL VEPLTPSGAL
     PNQAQMRILK ETELKKVKVL GSGAFGTVYK GIWIPDGESV KIPVAIKVLR ENTSPKANKE
     ILDEAYVMAG VGSPYVSRLL GICLTSTVQL VTQLMPYGCL LDYVRENKDR IGSQDLLNWC
     VQIAKGMSYL EEVRLVHRDL AARNVLVKSP NHVKITDFGL ARLLDIDETE YHADGGKVPI
     KWMALESILR RRFTHQSDVW SYGVTVWELM TFGAKPYDGI PAREIPDLLE KGERLPQPPI
     CTIDVYMIMV KCWMIDSECR PKFRELVTEF SRMARDPQRF VVIQNDTIGL PSSMDSTFYR
     ALLEEEDMDD LVDAEEYLVP HQGFFSAETS TAYRSRISST RSTAETPADT TEGEESAAFP
     FPPQSLVEGP ECPVPEALEV DGGAKGALPS PPATRYSEDP TALPGDESEG LDPEGFATPG
     AHATMPEYVN QAGERPSPPR HPCAPPSPPD KPKGHQGKNG LIKDTKHPFL GPFGRAVENP
     EYLAPPGLPA PTAFSQAFDN PYYWNQDPPK AGSPEGGPSS TPAAENPEYL GLAEPEDVAV
//
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