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P06494

- ERBB2_RAT

UniProt

P06494 - ERBB2_RAT

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Protein

Receptor tyrosine-protein kinase erbB-2

Gene
Erbb2, Neu
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.1 Publication
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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei755 – 7551ATP By similarity
Active sitei847 – 8471Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi728 – 7369ATP By similarity

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 654632Extracellular Reviewed predictionAdd
BLAST
Transmembranei655 – 67723Helical; Reviewed predictionAdd
BLAST
Topological domaini678 – 1257580Cytoplasmic Reviewed predictionAdd
BLAST

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 – 2222 Reviewed predictionAdd
BLAST
Chaini23 – 12571235Receptor tyrosine-protein kinase erbB-2PRO_0000016671Add
BLAST

Amino acid modifications

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

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.

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.

Miscellaneous databases

EvolutionaryTraceiP06494.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini722 – 989268Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni678 – 69114Nuclear localization signal By similarityAdd
BLAST
Regioni678 – 69114Required for interaction with KPNB1 and EEA1 By similarityAdd
BLAST
Regioni1197 – 11993Interaction with PIK3C2B By similarity

Compositional bias

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

Sequence similaritiesi

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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451S → G in AAH61863. 1 Publication
Sequence conflicti505 – 5095LCVSS → CGLE in AAH61863. 1 Publication

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

« 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: June 11, 2014
This is version 158 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

Similar proteinsi