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P06494

- ERBB2_RAT

UniProt

P06494 - ERBB2_RAT

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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

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 heterodimerization activity Source: RGD
  6. protein tyrosine kinase activity Source: RGD
  7. receptor signaling protein tyrosine kinase activity Source: InterPro
  8. RNA polymerase I core binding Source: UniProtKB
  9. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC
  10. 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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP06494.
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

        10         20         30         40         50
MELAAWCRWG FLLALLPPGI AGTQVCTGTD MKLRLPASPE THLDMLRHLY
60 70 80 90 100
QGCQVVQGNL ELTYVPANAS LSFLQDIQEV QGYMLIAHNQ VKRVPLQRLR
110 120 130 140 150
IVRGTQLFED KYALAVLDNR DPQDNVAAST PGRTPEGLRE LQLRSLTEIL
160 170 180 190 200
KGGVLIRGNP QLCYQDMVLW KDVFRKNNQL APVDIDTNRS RACPPCAPAC
210 220 230 240 250
KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ CAAGCTGPKH
260 270 280 290 300
SDCLACLHFN HSGICELHCP ALVTYNTDTF ESMHNPEGRY TFGASCVTTC
310 320 330 340 350
PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA RVCYGLGMEH
360 370 380 390 400
LRGARAITSD NVQEFDGCKK IFGSLAFLPE SFDGDPSSGI APLRPEQLQV
410 420 430 440 450
FETLEEITGY LYISAWPDSL RDLSVFQNLR IIRGRILHDG AYSLTLQGLG
460 470 480 490 500
IHSLGLRSLR ELGSGLALIH RNAHLCFVHT VPWDQLFRNP HQALLHSGNR
510 520 530 540 550
PEEDLCVSSG LVCNSLCAHG HCWGPGPTQC VNCSHFLRGQ ECVEECRVWK
560 570 580 590 600
GLPREYVSDK RCLPCHPECQ PQNSSETCFG SEADQCAACA HYKDSSSCVA
610 620 630 640 650
RCPSGVKPDL SYMPIWKYPD EEGICQPCPI NCTHSCVDLD ERGCPAEQRA
660 670 680 690 700
SPVTFIIATV VGVLLFLILV VVVGILIKRR RQKIRKYTMR RLLQETELVE
710 720 730 740 750
PLTPSGAMPN QAQMRILKET ELRKVKVLGS GAFGTVYKGI WIPDGENVKI
760 770 780 790 800
PVAIKVLREN TSPKANKEIL DEAYVMAGVG SPYVSRLLGI CLTSTVQLVT
810 820 830 840 850
QLMPYGCLLD HVREHRGRLG SQDLLNWCVQ IAKGMSYLED VRLVHRDLAA
860 870 880 890 900
RNVLVKSPNH VKITDFGLAR LLDIDETEYH ADGGKVPIKW MALESILRRR
910 920 930 940 950
FTHQSDVWSY GVTVWELMTF GAKPYDGIPA REIPDLLEKG ERLPQPPICT
960 970 980 990 1000
IDVYMIMVKC WMIDSECRPR FRELVSEFSR MARDPQRFVV IQNEDLGPSS
1010 1020 1030 1040 1050
PMDSTFYRSL LEDDDMGDLV DAEEYLVPQQ GFFSPDPTPG TGSTAHRRHR
1060 1070 1080 1090 1100
SSSTRSGGGE LTLGLEPSEE GPPRSPLAPS EGAGSDVFDG DLAMGVTKGL
1110 1120 1130 1140 1150
QSLSPHDLSP LQRYSEDPTL PLPPETDGYV APLACSPQPE YVNQSEVQPQ
1160 1170 1180 1190 1200
PPLTPEGPLP PVRPAGATLE RPKTLSPGKN GVVKDVFAFG GAVENPEYLV
1210 1220 1230 1240 1250
PREGTASPPH PSPAFSPAFD NLYYWDQNSS EQGPPPSNFE GTPTAENPEY

LGLDVPV
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.
InParanoidi P06494.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 160 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

Dasty 3