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Protein

Receptor tyrosine-protein kinase erbB-2

Gene

Erbb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 sitei754 – 7541ATPPROSITE-ProRule annotation
Active sitei846 – 8461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi727 – 7359ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell surface receptor signaling pathway Source: MGI
  • heart development Source: MGI
  • motor neuron axon guidance Source: MGI
  • myelination Source: MGI
  • negative regulation of immature T cell proliferation in thymus Source: MGI
  • nervous system development Source: MGI
  • neuromuscular junction development Source: MGI
  • oligodendrocyte differentiation Source: MGI
  • peptidyl-tyrosine phosphorylation Source: MGI
  • peripheral nervous system development Source: MGI
  • phosphatidylinositol 3-kinase signaling Source: MGI
  • positive regulation of cell adhesion Source: MGI
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of GTPase activity Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
  • signal transduction Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL
  • wound healing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_285824. GRB7 events in ERBB2 signaling.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_323938. Downregulation of ERBB2:ERBB3 signaling.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor tyrosine-protein kinase erbB-2 (EC:2.7.10.1)
Alternative name(s):
Proto-oncogene Neu
Proto-oncogene c-ErbB-2
p185erbB2
CD_antigen: CD340
Gene namesi
Name:Erbb2
Synonyms:Kiaa3023, Neu
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95410. Erbb2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 653631ExtracellularSequence AnalysisAdd
BLAST
Transmembranei654 – 67421HelicalSequence AnalysisAdd
BLAST
Topological domaini675 – 1256582CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle Source: MGI
  • endosome membrane Source: MGI
  • integral component of membrane Source: UniProtKB
  • myelin sheath Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 12561234Receptor tyrosine-protein kinase erbB-2PRO_0000042181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 53By similarity
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi125 – 1251N-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...)Sequence Analysis
Disulfide bondi269 ↔ 296By similarity
Disulfide bondi300 ↔ 312By similarity
Disulfide bondi316 ↔ 332By similarity
Disulfide bondi335 ↔ 339By similarity
Disulfide bondi343 ↔ 368By similarity
Disulfide bondi476 ↔ 505By similarity
Disulfide bondi512 ↔ 521By similarity
Disulfide bondi516 ↔ 529By similarity
Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi532 ↔ 541By similarity
Disulfide bondi545 ↔ 561By similarity
Disulfide bondi564 ↔ 577By similarity
Disulfide bondi568 ↔ 585By similarity
Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi588 ↔ 597By similarity
Disulfide bondi601 ↔ 624By similarity
Disulfide bondi627 ↔ 635By similarity
Glycosylationi630 – 6301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi631 ↔ 643By similarity
Modified residuei1055 – 10551PhosphoserineBy similarity
Modified residuei1108 – 11081PhosphoserineBy similarity
Modified residuei1140 – 11401Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1197 – 11971PhosphotyrosineSequence Analysis
Modified residuei1249 – 12491Phosphotyrosine; 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-1249 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP70424.
PaxDbiP70424.
PRIDEiP70424.

PTM databases

PhosphoSiteiP70424.

Expressioni

Tissue specificityi

Expressed predominantly in uterine epithelial cells. In the muscle, expression localizes to the synaptic sites of muscle fibers.

Developmental stagei

On days 1-4 of pregnancy, ERBB2 is detected primarily in epithelial cells, the day 1 uterus showing the highest accumulation. On day 5, the epithelium and the decidualizing stromal cells around the implanting blastocyst exhibit accumulation of this receptor. On days 6-8, the expression persists in the epithelium at both the implantation and interimplantation sites in addition to modest levels in the secondary decidual zone. On days 7 and 8, accumulation is also prominent in the trophoblastic giant cells.

Gene expression databases

BgeeiP70424.
ExpressionAtlasiP70424. baseline and differential.
GenevisibleiP70424. MM.

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-1197. Interacts with PRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr-1249) with MEMO1. Interacts with MUC1. Interacts (when phosphorylated on Tyr-1140) with GRB7 (via SH2 domain). Interacts (when phosphorylated on Tyr-1249) with ERBB2IP. Interacts with KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA94 and ACTB (By similarity). Interacts with SRC and MYOC.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Erbb3Q615262EBI-2945468,EBI-931878
Stat3P422274EBI-2945468,EBI-602878

Protein-protein interaction databases

BioGridi199496. 7 interactions.
DIPiDIP-40912N.
IntActiP70424. 4 interactions.
MINTiMINT-138121.
STRINGi10090.ENSMUSP00000053897.

Structurei

3D structure databases

ProteinModelPortaliP70424.
SMRiP70424. Positions 23-630, 678-1010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini721 – 988268Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni677 – 69014Required for interaction with KPNB1 and EEA1By similarityAdd
BLAST
Regioni1196 – 11983Interaction with PIK3C2BBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi677 – 69014Nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi193 – 26977Cys-richAdd
BLAST
Compositional biasi1117 – 116347Pro-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.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP70424.
KOiK05083.
OMAiACYPLCA.
OrthoDBiEOG7V49XM.
PhylomeDBiP70424.
TreeFamiTF106002.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. 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.
IPR000494. Rcpt_L-dom.
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.

P70424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELAAWCRWG FLLALLSPGA AGTQVCTGTD MKLRLPASPE THLDMLRHLY
60 70 80 90 100
QGCQVVQGNL ELTYLPANAS LSFLQDIQEV QGYMLIAHNR VKHVPLQRLR
110 120 130 140 150
IVRGTQLFED KYALAVLDNR DPLDNVTTAA PGRTPEGLRE LQLRSLTEIL
160 170 180 190 200
KGGVLIRGNP QLCYQDMVLW KDVLRKNNQL APVDMDTNRS RACPPCAPTC
210 220 230 240 250
KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ CAAGCTGPKH
260 270 280 290 300
SDCLACLHFN HSGICELHCP ALITYNTDTF ESMLNPEGRY TFGASCVTTC
310 320 330 340 350
PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA GVCYGLGMEH
360 370 380 390 400
LRGARAITSD NIQEFAGCKK IFGSLAFLPE SFDGNPSSGV APLKPEHLQV
410 420 430 440 450
FETLEEITGY LYISAWPESF QDLSVFQNLR VIRGRILHDG AYSLTLQGLG
460 470 480 490 500
IHSLGLRSLR ELGSGLALIH RNTHLCFVNT VPWDQLFRNP HQALLHSGNR
510 520 530 540 550
PEEACGLEGL VCNSLCARGH CWGPGPTQCV NCSQFLRGQE CVEECRVWKG
560 570 580 590 600
LPREYVRGKH CLPCHPECQP QNSSETCYGS EADQCEACAH YKDSSSCVAR
610 620 630 640 650
CPSGVKPDLS YMPIWKYPDE EGICQPCPIN CTHSCVDLDE RGCPAEQRAS
660 670 680 690 700
PVTFIIATVV GVLLFLIIVV VIGILIKRRR QKIRKYTMRR LLQETELVEP
710 720 730 740 750
LTPSGAVPNQ AQMRILKETE LRKLKVLGSG AFGTVYKGIW IPDGENVKIP
760 770 780 790 800
VAIKVLRENT SPKANKEILD EAYVMAGVGS PYVSRLLGIC LTSTVQLVTQ
810 820 830 840 850
LMPYGCLLDH VREHRGRLGS QDLLNWCVQI AKGMSYLEEV RLVHRDLAAR
860 870 880 890 900
NVLVKSPNHV KITDFGLARL LDIDETEYHA DGGKVPIKWM ALESILRRRF
910 920 930 940 950
THQSDVWSYG VTVWELMTFG AKPYDGIPAR EIPDLLEKGE RLPQPPICTI
960 970 980 990 1000
DVYMIMVKCW MIDSECRPRF RELVSEFSRM ARDPQRFVVI QNEDLGPSSP
1010 1020 1030 1040 1050
MDSTFYRSLL EDDDMGELVD AEEYLVPQQG FFSPDPALGT GSTAHRRHRS
1060 1070 1080 1090 1100
SSARSGGGEL TLGLEPSEEE PPRSPLAPSE GAGSDVFDGD LAVGVTKGLQ
1110 1120 1130 1140 1150
SLSPHDLSPL QRYSEDPTLP LPPETDGYVA PLACSPQPEY VNQPEVRPQS
1160 1170 1180 1190 1200
PLTPEGPPPP IRPAGATLER PKTLSPGKNG VVKDVFAFGG AVENPEYLAP
1210 1220 1230 1240 1250
RAGTASQPHP SPAFSPAFDN LYYWDQNSSE QGPPPSTFEG TPTAENPEYL

GLDVPV
Length:1,256
Mass (Da):138,579
Last modified:September 27, 2005 - v3
Checksum:i6040978428B93A28
GO

Sequence cautioni

The sequence BAC98297.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129487 mRNA. Translation: BAC98297.1. Different initiation.
U71126 mRNA. Translation: AAB17380.1.
L47239 mRNA. Translation: AAA93532.1.
CCDSiCCDS25349.1.
RefSeqiNP_001003817.1. NM_001003817.1.
UniGeneiMm.290822.

Genome annotation databases

EnsembliENSMUST00000058295; ENSMUSP00000053897; ENSMUSG00000062312.
GeneIDi13866.
KEGGimmu:13866.
UCSCiuc007lgi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129487 mRNA. Translation: BAC98297.1. Different initiation.
U71126 mRNA. Translation: AAB17380.1.
L47239 mRNA. Translation: AAA93532.1.
CCDSiCCDS25349.1.
RefSeqiNP_001003817.1. NM_001003817.1.
UniGeneiMm.290822.

3D structure databases

ProteinModelPortaliP70424.
SMRiP70424. Positions 23-630, 678-1010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199496. 7 interactions.
DIPiDIP-40912N.
IntActiP70424. 4 interactions.
MINTiMINT-138121.
STRINGi10090.ENSMUSP00000053897.

Chemistry

ChEMBLiCHEMBL2311234.

PTM databases

PhosphoSiteiP70424.

Proteomic databases

MaxQBiP70424.
PaxDbiP70424.
PRIDEiP70424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058295; ENSMUSP00000053897; ENSMUSG00000062312.
GeneIDi13866.
KEGGimmu:13866.
UCSCiuc007lgi.1. mouse.

Organism-specific databases

CTDi2064.
MGIiMGI:95410. Erbb2.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP70424.
KOiK05083.
OMAiACYPLCA.
OrthoDBiEOG7V49XM.
PhylomeDBiP70424.
TreeFamiTF106002.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_285824. GRB7 events in ERBB2 signaling.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_323938. Downregulation of ERBB2:ERBB3 signaling.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

NextBioi284764.
PROiP70424.
SOURCEiSearch...

Gene expression databases

BgeeiP70424.
ExpressionAtlasiP70424. baseline and differential.
GenevisibleiP70424. MM.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. 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.
IPR000494. Rcpt_L-dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "Differential expression of the erbB2 gene in the periimplantation mouse uterus: potential mediator of signaling by epidermal growth factor-like growth factors."
    Lim J., Dey S.K., Das S.K.
    Endocrinology 138:1328-1337(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 786-934.
    Strain: CD-1.
    Tissue: Uterus.
  3. "Synapse-associated expression of an acetylcholine receptor-inducing protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in developing mammalian muscle."
    Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R.
    Dev. Biol. 172:158-169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1012-1107.
  4. "Direct and specific interaction of c-Src with Neu is involved in signaling by the epidermal growth factor receptor."
    Muthuswamy S.K., Muller W.J.
    Oncogene 11:271-279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRC.
  5. "The ERBB2/HER2 receptor differentially interacts with ERBIN and PICK1 PSD-95/DLG/ZO-1 domain proteins."
    Jaulin-Bastard F., Saito H., Le Bivic A., Ollendorff V., Marchetto S., Birnbaum D., Borg J.-P.
    J. Biol. Chem. 276:15256-15263(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCABP.
  6. "Myocilin mediates myelination in the peripheral nervous system through ErbB2/3 signaling."
    Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C., Tomarev S.I.
    J. Biol. Chem. 288:26357-26371(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYOC.

Entry informationi

Entry nameiERBB2_MOUSE
AccessioniPrimary (citable) accession number: P70424
Secondary accession number(s): Q61525, Q6ZPE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 27, 2005
Last modified: June 24, 2015
This is version 165 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.