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P06494

- ERBB2_RAT

UniProt

P06494 - ERBB2_RAT

Protein

Receptor tyrosine-protein kinase erbB-2

Gene

Erbb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization By similarity.By similarity
    In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth By similarity.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei755 – 7551ATPPROSITE-ProRule annotation
    Active sitei847 – 8471Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi728 – 7369ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. glycoprotein binding Source: RGD
    4. Hsp90 protein binding Source: RGD
    5. protein binding Source: RGD
    6. protein heterodimerization activity Source: RGD
    7. protein tyrosine kinase activity Source: RGD
    8. receptor signaling protein tyrosine kinase activity Source: InterPro
    9. RNA polymerase I core binding Source: UniProtKB
    10. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC
    11. ubiquitin protein ligase binding Source: RGD

    GO - Biological processi

    1. central nervous system development Source: RGD
    2. estrus Source: RGD
    3. glial cell differentiation Source: RGD
    4. liver development Source: RGD
    5. mammary gland involution Source: RGD
    6. negative regulation of apoptotic process Source: RGD
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. peripheral nervous system development Source: RGD
    9. positive regulation of cell growth Source: UniProtKB
    10. positive regulation of cell proliferation Source: RGD
    11. positive regulation of MAPK cascade Source: RGD
    12. positive regulation of phosphatidylinositol 3-kinase signaling Source: RGD
    13. positive regulation of Ras protein signal transduction Source: RGD
    14. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
    16. positive regulation of translation Source: UniProtKB
    17. protein autophosphorylation Source: RGD
    18. regulation of cell differentiation Source: RGD
    19. regulation of cell proliferation Source: RGD
    20. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    21. regulation of microtubule-based process Source: UniProtKB
    22. response to axon injury Source: RGD
    23. response to drug Source: RGD
    24. response to progesterone Source: RGD
    25. skeletal muscle tissue development Source: RGD
    26. sympathetic nervous system development Source: RGD
    27. tongue development Source: RGD
    28. transcription, DNA-templated Source: UniProtKB-KW
    29. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Activator, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor tyrosine-protein kinase erbB-2 (EC:2.7.10.1)
    Alternative name(s):
    Epidermal growth factor receptor-related protein
    Proto-oncogene Neu
    Proto-oncogene c-ErbB-2
    p185erbB2
    p185neu
    CD_antigen: CD340
    Gene namesi
    Name:Erbb2
    Synonyms:Neu
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2561. Erbb2.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasmperinuclear region By similarity. Nucleus 1 Publication

    GO - Cellular componenti

    1. apical plasma membrane Source: RGD
    2. basal plasma membrane Source: RGD
    3. basolateral plasma membrane Source: RGD
    4. integral component of membrane Source: UniProtKB-KW
    5. lateral loop Source: RGD
    6. membrane raft Source: RGD
    7. microvillus Source: RGD
    8. nucleus Source: RGD
    9. perinuclear region of cytoplasm Source: RGD
    10. plasma membrane Source: Reactome
    11. postsynaptic membrane Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 12571235Receptor tyrosine-protein kinase erbB-2PRO_0000016671Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 53By similarity
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi163 ↔ 193By similarity
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi196 ↔ 205By similarity
    Disulfide bondi200 ↔ 213By similarity
    Disulfide bondi221 ↔ 228By similarity
    Disulfide bondi225 ↔ 236By similarity
    Disulfide bondi237 ↔ 245By similarity
    Disulfide bondi241 ↔ 253By similarity
    Disulfide bondi256 ↔ 265By similarity
    Glycosylationi260 – 2601N-linked (GlcNAc...)1 Publication
    Disulfide bondi269 ↔ 296By similarity
    Disulfide bondi300 ↔ 312By similarity
    Disulfide bondi316 ↔ 332By similarity
    Disulfide bondi335 ↔ 339By similarity
    Disulfide bondi343 ↔ 368By similarity
    Disulfide bondi476 ↔ 506By similarity
    Disulfide bondi513 ↔ 522By similarity
    Disulfide bondi517 ↔ 530By similarity
    Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi533 ↔ 542By similarity
    Disulfide bondi546 ↔ 562By similarity
    Disulfide bondi565 ↔ 578By similarity
    Disulfide bondi569 ↔ 586By similarity
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi589 ↔ 598By similarity
    Disulfide bondi602 ↔ 625By similarity
    Disulfide bondi628 ↔ 636By similarity
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi632 ↔ 644By similarity
    Modified residuei1056 – 10561PhosphoserineBy similarity
    Modified residuei1109 – 11091PhosphoserineBy similarity
    Modified residuei1141 – 11411Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1198 – 11981PhosphotyrosineSequence Analysis
    Modified residuei1250 – 12501Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Signaling via SEMA4C promotes phosphorylation at Tyr-1250 By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP06494.
    PRIDEiP06494.

    PTM databases

    PhosphoSiteiP06494.

    Expressioni

    Gene expression databases

    GenevestigatoriP06494.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1198. Interacts with PRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr-1250) with MEMO1. Interacts with MUC1. Interacts (when phosphorylated on Tyr-1141) with GRB7 (via SH2 domain). Interacts (when phosphorylated on Tyr-1250) with ERBB2IP Interacts with SRC, KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA94, MYOC and ACTB By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-132326.

    Structurei

    Secondary structure

    1
    1257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 273
    Helixi39 – 5012
    Beta strandi54 – 6310
    Helixi72 – 743
    Beta strandi79 – 824
    Beta strandi84 – 885
    Turni109 – 1113
    Beta strandi112 – 1176
    Beta strandi153 – 1586
    Helixi170 – 1734
    Helixi176 – 1783
    Beta strandi183 – 1853
    Beta strandi201 – 2033
    Beta strandi205 – 2095
    Beta strandi228 – 2325
    Helixi233 – 2353
    Beta strandi241 – 2433
    Beta strandi245 – 2495
    Beta strandi252 – 26110
    Beta strandi264 – 2685
    Beta strandi272 – 2743
    Beta strandi290 – 2923
    Beta strandi295 – 2995
    Beta strandi310 – 3156
    Beta strandi320 – 3245
    Beta strandi330 – 3345
    Helixi349 – 3513
    Turni359 – 3613
    Helixi362 – 3654
    Beta strandi369 – 3779
    Helixi379 – 3835
    Turni386 – 3894
    Helixi395 – 4017
    Beta strandi406 – 4094
    Beta strandi411 – 4144
    Helixi424 – 4263
    Turni439 – 4413
    Beta strandi442 – 4487
    Beta strandi464 – 4707
    Helixi483 – 4864
    Beta strandi494 – 4996
    Turni507 – 5104
    Helixi518 – 5203
    Beta strandi522 – 5265
    Beta strandi530 – 5389
    Beta strandi541 – 5444
    Beta strandi547 – 5537
    Beta strandi558 – 5614
    Beta strandi573 – 5753
    Beta strandi577 – 5826
    Helixi583 – 5853
    Beta strandi586 – 5949
    Beta strandi597 – 6015
    Beta strandi604 – 6063
    Beta strandi615 – 6195
    Beta strandi623 – 6275
    Helixi650 – 66920
    Helixi670 – 6745
    Helixi675 – 6795

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IIJNMR-A647-681[»]
    1N8YX-ray2.40C23-631[»]
    2J1Hmodel-A/B649-681[»]
    ProteinModelPortaliP06494.
    SMRiP06494. Positions 23-631, 647-1027.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06494.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 654632ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini678 – 1257580CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei655 – 67723HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini722 – 989268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni678 – 69114Nuclear localization signalBy similarityAdd
    BLAST
    Regioni678 – 69114Required for interaction with KPNB1 and EEA1By similarityAdd
    BLAST
    Regioni1197 – 11993Interaction with PIK3C2BBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi159 – 369211Cys-richAdd
    BLAST
    Compositional biasi473 – 646174Cys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000230982.
    HOVERGENiHBG000490.
    PhylomeDBiP06494.

    Family and domain databases

    Gene3Di3.80.20.20. 2 hits.
    InterProiIPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
    [Graphical view]
    PfamiPF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00261. FU. 4 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06494-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELAAWCRWG FLLALLPPGI AGTQVCTGTD MKLRLPASPE THLDMLRHLY     50
    QGCQVVQGNL ELTYVPANAS LSFLQDIQEV QGYMLIAHNQ VKRVPLQRLR 100
    IVRGTQLFED KYALAVLDNR DPQDNVAAST PGRTPEGLRE LQLRSLTEIL 150
    KGGVLIRGNP QLCYQDMVLW KDVFRKNNQL APVDIDTNRS RACPPCAPAC 200
    KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ CAAGCTGPKH 250
    SDCLACLHFN HSGICELHCP ALVTYNTDTF ESMHNPEGRY TFGASCVTTC 300
    PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA RVCYGLGMEH 350
    LRGARAITSD NVQEFDGCKK IFGSLAFLPE SFDGDPSSGI APLRPEQLQV 400
    FETLEEITGY LYISAWPDSL RDLSVFQNLR IIRGRILHDG AYSLTLQGLG 450
    IHSLGLRSLR ELGSGLALIH RNAHLCFVHT VPWDQLFRNP HQALLHSGNR 500
    PEEDLCVSSG LVCNSLCAHG HCWGPGPTQC VNCSHFLRGQ ECVEECRVWK 550
    GLPREYVSDK RCLPCHPECQ PQNSSETCFG SEADQCAACA HYKDSSSCVA 600
    RCPSGVKPDL SYMPIWKYPD EEGICQPCPI NCTHSCVDLD ERGCPAEQRA 650
    SPVTFIIATV VGVLLFLILV VVVGILIKRR RQKIRKYTMR RLLQETELVE 700
    PLTPSGAMPN QAQMRILKET ELRKVKVLGS GAFGTVYKGI WIPDGENVKI 750
    PVAIKVLREN TSPKANKEIL DEAYVMAGVG SPYVSRLLGI CLTSTVQLVT 800
    QLMPYGCLLD HVREHRGRLG SQDLLNWCVQ IAKGMSYLED VRLVHRDLAA 850
    RNVLVKSPNH VKITDFGLAR LLDIDETEYH ADGGKVPIKW MALESILRRR 900
    FTHQSDVWSY GVTVWELMTF GAKPYDGIPA REIPDLLEKG ERLPQPPICT 950
    IDVYMIMVKC WMIDSECRPR FRELVSEFSR MARDPQRFVV IQNEDLGPSS 1000
    PMDSTFYRSL LEDDDMGDLV DAEEYLVPQQ GFFSPDPTPG TGSTAHRRHR 1050
    SSSTRSGGGE LTLGLEPSEE GPPRSPLAPS EGAGSDVFDG DLAMGVTKGL 1100
    QSLSPHDLSP LQRYSEDPTL PLPPETDGYV APLACSPQPE YVNQSEVQPQ 1150
    PPLTPEGPLP PVRPAGATLE RPKTLSPGKN GVVKDVFAFG GAVENPEYLV 1200
    PREGTASPPH PSPAFSPAFD NLYYWDQNSS EQGPPPSNFE GTPTAENPEY 1250
    LGLDVPV 1257
    Length:1,257
    Mass (Da):138,832
    Last modified:December 15, 1998 - v3
    Checksum:i6129264583011402
    GO

    Sequence cautioni

    The sequence AAH61863.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA27059.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451S → G in AAH61863. (PubMed:15489334)Curated
    Sequence conflicti505 – 5095LCVSS → CGLE in AAH61863. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti661 – 6611V → E in oncogenic NEU.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03362 mRNA. Translation: CAA27059.1. Different initiation.
    BC061863 mRNA. Translation: AAH61863.1. Different initiation.
    PIRiA24562. TVRTNU.
    UniGeneiRn.93966.

    Genome annotation databases

    UCSCiRGD:2561. rat.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03362 mRNA. Translation: CAA27059.1 . Different initiation.
    BC061863 mRNA. Translation: AAH61863.1 . Different initiation.
    PIRi A24562. TVRTNU.
    UniGenei Rn.93966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IIJ NMR - A 647-681 [» ]
    1N8Y X-ray 2.40 C 23-631 [» ]
    2J1H model - A/B 649-681 [» ]
    ProteinModelPortali P06494.
    SMRi P06494. Positions 23-631, 647-1027.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-132326.

    Chemistry

    BindingDBi P06494.
    ChEMBLi CHEMBL3848.

    PTM databases

    PhosphoSitei P06494.

    Proteomic databases

    PaxDbi P06494.
    PRIDEi P06494.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2561. rat.

    Organism-specific databases

    RGDi 2561. Erbb2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230982.
    HOVERGENi HBG000490.
    PhylomeDBi P06494.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.

    Miscellaneous databases

    EvolutionaryTracei P06494.
    PROi P06494.

    Gene expression databases

    Genevestigatori P06494.

    Family and domain databases

    Gene3Di 3.80.20.20. 2 hits.
    InterProi IPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
    [Graphical view ]
    Pfami PF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00261. FU. 4 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The neu oncogene encodes an epidermal growth factor receptor-related protein."
      Bargmann C.I., Hung M.-C., Weinberg R.A.
      Nature 319:226-230(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Neuroblastoma.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    3. "Direct DNA sequencing of the rat neu oncogene transmembrane domain reveals no mutation in urinary bladder carcinomas induced by N-butyl-N-(4-hydroxybutyl)nitrosamine, N-[4-(5-nitro-2-furyl)-2-thiazolyl]formamide or N-methyl-N-nitrosourea."
      Masui T., Mann A.M., Macatee T.L., Garland E.M., Okamura T., Smith R.A., Cohen S.M.
      Carcinogenesis 12:1975-1978(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 634-699.
    4. "An extended family of protein-tyrosine kinase genes differentially expressed in the vertebrate nervous system."
      Lai C., Lemke G.
      Neuron 6:691-704(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 852-905.
      Tissue: Sciatic nerve.
    5. "Nuclear localization of p185neu tyrosine kinase and its association with transcriptional transactivation."
      Xie Y., Hung M.C.
      Biochem. Biophys. Res. Commun. 203:1589-1598(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Three dimensional structure of the transmembrane region of the proto-oncogenic and oncogenic forms of the neu protein."
      Gullick W.J., Bottomley A.C., Lofts F.J., Doak D.G., Mulvey D., Newman R., Crumpton M.J., Sternberg M.J.E., Campbell I.D.
      EMBO J. 11:43-48(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 650-668.
    7. "Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab."
      Cho H.-S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B., Denney D.W. Jr., Leahy D.J.
      Nature 421:756-760(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-631 IN COMPLEX WITH THE ANTIBODY HERCEPTIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-260.

    Entry informationi

    Entry nameiERBB2_RAT
    AccessioniPrimary (citable) accession number: P06494
    Secondary accession number(s): Q6P732
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

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