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Q62799

- ERBB3_RAT

UniProt

Q62799 - ERBB3_RAT

Protein

Receptor tyrosine-protein kinase erbB-3

Gene

Erbb3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Binds and is activated by neuregulins and NTAK. May also be activated by CSPG5.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei740 – 7401ATPPROSITE-ProRule annotation
    Active sitei832 – 8321Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi713 – 7219ATPPROSITE-ProRule annotation
    Nucleotide bindingi786 – 7883ATPPROSITE-ProRule annotation
    Nucleotide bindingi832 – 8376ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. neuregulin binding Source: RGD
    3. neuregulin receptor activity Source: RGD
    4. receptor signaling protein tyrosine kinase activity Source: InterPro
    5. transmembrane receptor protein tyrosine kinase activity Source: RGD

    GO - Biological processi

    1. axonogenesis Source: RGD
    2. cellular response to insulin stimulus Source: RGD
    3. circadian rhythm Source: RGD
    4. epidermal growth factor receptor signaling pathway Source: RGD
    5. mammary gland involution Source: RGD
    6. odontogenesis Source: RGD
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. positive regulation of glucose import Source: RGD
    9. response to drug Source: RGD
    10. response to wounding Source: RGD
    11. skeletal muscle tissue development Source: RGD
    12. tongue development Source: RGD
    13. transmembrane receptor protein tyrosine kinase signaling pathway Source: RGD

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor tyrosine-protein kinase erbB-3 (EC:2.7.10.1)
    Alternative name(s):
    Proto-oncogene-like protein c-ErbB-3
    Gene namesi
    Name:Erbb3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69323. Erbb3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: RGD
    2. nucleus Source: RGD
    3. postsynaptic membrane Source: RGD

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 13391320Receptor tyrosine-protein kinase erbB-3PRO_0000016673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi186 ↔ 194By similarity
    Disulfide bondi190 ↔ 202By similarity
    Disulfide bondi210 ↔ 218By similarity
    Disulfide bondi214 ↔ 226By similarity
    Disulfide bondi227 ↔ 235By similarity
    Disulfide bondi231 ↔ 243By similarity
    Disulfide bondi246 ↔ 255By similarity
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi259 ↔ 286By similarity
    Disulfide bondi290 ↔ 301By similarity
    Disulfide bondi305 ↔ 320By similarity
    Disulfide bondi323 ↔ 327By similarity
    Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi500 ↔ 509By similarity
    Disulfide bondi504 ↔ 517By similarity
    Disulfide bondi520 ↔ 529By similarity
    Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi533 ↔ 549By similarity
    Disulfide bondi556 ↔ 573By similarity
    Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi576 ↔ 585By similarity
    Disulfide bondi589 ↔ 610By similarity
    Disulfide bondi613 ↔ 621By similarity
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi617 ↔ 629By similarity

    Post-translational modificationi

    Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ62799.
    PRIDEiQ62799.

    PTM databases

    PhosphoSiteiQ62799.

    Expressioni

    Gene expression databases

    GenevestigatoriQ62799.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Heterodimer with each of the other ERBB receptors Potential. Interacts with CSPG5, PA2G4, GRB7, MYOC and MUC1 By similarity.By similarityCurated

    Protein-protein interaction databases

    BioGridi248136. 2 interactions.
    MINTiMINT-132305.
    STRINGi10116.ENSRNOP00000006796.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62799.
    SMRiQ62799. Positions 25-630, 665-977.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 643624ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini663 – 1339677CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei644 – 66219HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini707 – 964258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi183 – 25977Cys-richAdd
    BLAST

    Domaini

    The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.

    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.
    InParanoidiQ62799.
    KOiK05084.
    PhylomeDBiQ62799.

    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.
    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. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS50011. 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.

    Q62799-1 [UniParc]FASTAAdd to Basket

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    MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY     50
    KLYEKCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP 100
    NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLKFTQLT EILSGGVYIE 150
    KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG ANCPPCHEVC KGRCWGPGPD 200
    DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD TDCFACRRFN 250
    DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF 300
    CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG 350
    FVNCTKILGN LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ 400
    SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS 450
    AGRVYISANQ QLCYHHSLNW TRLLRGPSEE RLDIKYDRPL GECLAEGKVC 500
    DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP REFVHEAQCF 550
    SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI 600
    YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL 650
    AVILMILGGS FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR 700
    IFKETELRKL KVLGSGVFGT VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS 750
    FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS LQLVTQYLPL GSLLDHVKQH 800
    RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML KSPSQVQVAD 850
    FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW 900
    ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE 950
    NIRPTFKELA NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE 1000
    AELEPELDLD LDLEAEEEGL ATSLGSALSL PTGTLTRPRG SQSLLSPSSG 1050
    YMPMNQSSLG EACLDSAVLG GREQFSRPIS LHPIPRGRPA SESSEGHVTG 1100
    SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV TPLSPPGLEE 1150
    EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK 1200
    RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG 1250
    TTPDEDYEYM NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP 1300
    HVRYARLKTL RSLEATDSAF DNPDYWHSRL FPKANAQRT 1339
    Length:1,339
    Mass (Da):147,546
    Last modified:June 6, 2002 - v3
    Checksum:i0AA5F2402BBFDF1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1028 – 10281L → P in AAC53050. (PubMed:9030624)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29339 mRNA. Translation: AAC28498.2.
    U52530 mRNA. Translation: AAC53050.1.
    PIRiJC4387.
    RefSeqiNP_058914.2. NM_017218.3.
    UniGeneiRn.10228.

    Genome annotation databases

    GeneIDi29496.
    KEGGirno:29496.
    UCSCiRGD:69323. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29339 mRNA. Translation: AAC28498.2 .
    U52530 mRNA. Translation: AAC53050.1 .
    PIRi JC4387.
    RefSeqi NP_058914.2. NM_017218.3.
    UniGenei Rn.10228.

    3D structure databases

    ProteinModelPortali Q62799.
    SMRi Q62799. Positions 25-630, 665-977.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248136. 2 interactions.
    MINTi MINT-132305.
    STRINGi 10116.ENSRNOP00000006796.

    PTM databases

    PhosphoSitei Q62799.

    Proteomic databases

    PaxDbi Q62799.
    PRIDEi Q62799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29496.
    KEGGi rno:29496.
    UCSCi RGD:69323. rat.

    Organism-specific databases

    CTDi 2065.
    RGDi 69323. Erbb3.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230982.
    HOVERGENi HBG000490.
    InParanoidi Q62799.
    KOi K05084.
    PhylomeDBi Q62799.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.

    Miscellaneous databases

    NextBioi 609384.
    PROi Q62799.

    Gene expression databases

    Genevestigatori Q62799.

    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.
    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. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the rat ErbB3 cDNA and characterization of the recombinant protein."
      Hellyer N.J., Kim H.-H., Greaves C.H., Sierke S.L., Koland J.G.
      Gene 165:279-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    2. Hellyer N.J., Koland J.G.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 85; 513 AND 565.
    3. "Expression of neuregulins and their putative receptors, ErbB2 and ErbB3, is induced during Wallerian degeneration."
      Carroll S.L., Miller M.L., Frohnert P.W., Kim S.S., Corbett J.A.
      J. Neurosci. 17:1642-1659(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 922-1097.
      Strain: Sprague-Dawley.
      Tissue: Sciatic nerve.

    Entry informationi

    Entry nameiERBB3_RAT
    AccessioniPrimary (citable) accession number: Q62799
    Secondary accession number(s): Q62955
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 127 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3