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Q9EQU3

- TLR9_MOUSE

UniProt

Q9EQU3 - TLR9_MOUSE

Protein

Toll-like receptor 9

Gene

Tlr9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (14 Dec 2011)
      Previous versions | rss
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    Functioni

    Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Plays a role in defense against systemic mouse cytomegalovirus infection. Controls lymphocyte response to Helicobacter infection.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. siRNA binding Source: UniProtKB
    3. transmembrane signaling receptor activity Source: InterPro
    4. unmethylated CpG binding Source: Ensembl

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: Ensembl
    2. cellular response to metal ion Source: Ensembl
    3. defense response to bacterium Source: Ensembl
    4. defense response to virus Source: MGI
    5. immune response Source: MGI
    6. inflammatory response Source: UniProtKB-KW
    7. innate immune response Source: BHF-UCL
    8. maintenance of gastrointestinal epithelium Source: BHF-UCL
    9. male gonad development Source: Ensembl
    10. microglial cell activation involved in immune response Source: Ensembl
    11. MyD88-dependent toll-like receptor signaling pathway Source: InterPro
    12. negative regulation of interleukin-6 production Source: BHF-UCL
    13. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
    14. positive regulation of autophagy Source: Ensembl
    15. positive regulation of inflammatory response Source: InterPro
    16. positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
    17. positive regulation of interferon-beta biosynthetic process Source: UniProtKB
    18. positive regulation of interferon-beta production Source: BHF-UCL
    19. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
    20. positive regulation of interleukin-10 production Source: BHF-UCL
    21. positive regulation of interleukin-12 production Source: BHF-UCL
    22. positive regulation of interleukin-18 production Source: BHF-UCL
    23. positive regulation of interleukin-6 production Source: BHF-UCL
    24. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
    25. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    26. positive regulation of tumor necrosis factor production Source: BHF-UCL
    27. regulation of cytokine secretion Source: InterPro
    28. regulation of inflammatory response Source: BHF-UCL
    29. response to molecule of bacterial origin Source: BHF-UCL
    30. response to virus Source: MGI
    31. toll-like receptor 9 signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_198976. Trafficking and processing of endosomal TLR.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Toll-like receptor 9
    Alternative name(s):
    CD_antigen: CD289
    Gene namesi
    Name:Tlr9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1932389. Tlr9.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome 1 Publication. Lysosome 1 Publication. Cytoplasmic vesiclephagosome 1 Publication
    Note: Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist.

    GO - Cellular componenti

    1. early phagosome Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. endosome Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. lysosome Source: UniProtKB
    7. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Reduced proliferation of lymphocytes, reduced interferon-gamma production by splenocytes and reduced neutrophil numbers following Helicobacter infection.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi499 – 4991L → P: Highly susceptible to mouse cytomegalovirus infection. Shows low level of cytokine induction and natural killer activation on viral infection. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 10321007Toll-like receptor 9PRO_0000034738Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi695 – 6951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi732 – 7321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9EQU3.
    PRIDEiQ9EQU3.

    PTM databases

    PhosphoSiteiQ9EQU3.

    Expressioni

    Tissue specificityi

    Expressed in the basolateral region of gastric epithelial cells with high levels detected in antrum and body mucosa (at protein level). Detected in spleen and stomach at higher levels in C57BL/6 mice than BALB/C.1 Publication

    Inductioni

    Following Helicobacter infection, down-regulated in C57BL/6 mice and up-regulated in BALB/C mice.1 Publication

    Gene expression databases

    BgeeiQ9EQU3.
    CleanExiMM_TLR9.
    GenevestigatoriQ9EQU3.

    Interactioni

    Subunit structurei

    Interacts with MYD88 via their respective TIR domains By similarity. Interacts with BTK By similarity. Interacts (via transmembrane domain) with UNC93B1. Interacts with CD300LH; the interaction may promote full activation of TLR9-triggered innate responses. Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum.By similarity4 Publications

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000082207.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4QDHX-ray2.40A/B480-753[»]
    ProteinModelPortaliQ9EQU3.
    SMRiQ9EQU3. Positions 34-1013.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 818793ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini840 – 1032193CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei819 – 83921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati62 – 8524LRR 1Add
    BLAST
    Repeati87 – 11024LRR 2Add
    BLAST
    Repeati122 – 14726LRR 3Add
    BLAST
    Repeati150 – 16617LRR 4Add
    BLAST
    Repeati167 – 19024LRR 5Add
    BLAST
    Repeati198 – 22124LRR 6Add
    BLAST
    Repeati223 – 24220LRR 7Add
    BLAST
    Repeati243 – 26826LRR 8Add
    BLAST
    Repeati283 – 30624LRR 9Add
    BLAST
    Repeati308 – 33225LRR 10Add
    BLAST
    Repeati333 – 35624LRR 11Add
    BLAST
    Repeati363 – 38624LRR 12Add
    BLAST
    Repeati390 – 41324LRR 13Add
    BLAST
    Repeati415 – 44026LRR 14Add
    BLAST
    Repeati471 – 49525LRR 15Add
    BLAST
    Repeati497 – 52024LRR 16Add
    BLAST
    Repeati521 – 54424LRR 17Add
    BLAST
    Repeati546 – 57328LRR 18Add
    BLAST
    Repeati575 – 59925LRR 19Add
    BLAST
    Repeati601 – 62323LRR 20Add
    BLAST
    Repeati628 – 65124LRR 21Add
    BLAST
    Repeati653 – 67624LRR 22Add
    BLAST
    Repeati677 – 70024LRR 23Add
    BLAST
    Repeati702 – 72423LRR 24Add
    BLAST
    Repeati725 – 74824LRR 25Add
    BLAST
    Repeati750 – 77324LRR 26Add
    BLAST
    Domaini868 – 1016149TIRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 26 LRR (leucine-rich) repeats.Curated
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4886.
    GeneTreeiENSGT00750000117479.
    HOGENOMiHOG000230468.
    HOVERGENiHBG018601.
    InParanoidiQ4L0K3.
    KOiK10161.
    OMAiLYLHFFQ.
    OrthoDBiEOG7C8GGD.
    TreeFamiTF325595.

    Family and domain databases

    Gene3Di3.40.50.10140. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027181. TLR9.
    [Graphical view]
    PANTHERiPTHR24373:SF37. PTHR24373:SF37. 1 hit.
    PfamiPF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 5 hits.
    PF01582. TIR. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS51450. LRR. 16 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9EQU3-1 [UniParc]FASTAAdd to Basket

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    MVLRRRTLHP LSLLVQAAVL AETLALGTLP AFLPCELKPH GLVDCNWLFL     50
    KSVPRFSAAA SCSNITRLSL ISNRIHHLHN SDFVHLSNLR QLNLKWNCPP 100
    TGLSPLHFSC HMTIEPRTFL AMRTLEELNL SYNGITTVPR LPSSLVNLSL 150
    SHTNILVLDA NSLAGLYSLR VLFMDGNCYY KNPCTGAVKV TPGALLGLSN 200
    LTHLSLKYNN LTKVPRQLPP SLEYLLVSYN LIVKLGPEDL ANLTSLRVLD 250
    VGGNCRRCDH APNPCIECGQ KSLHLHPETF HHLSHLEGLV LKDSSLHTLN 300
    SSWFQGLVNL SVLDLSENFL YESITHTNAF QNLTRLRKLN LSFNYRKKVS 350
    FARLHLASSF KNLVSLQELN MNGIFFRLLN KYTLRWLADL PKLHTLHLQM 400
    NFINQAQLSI FGTFRALRFV DLSDNRISGP STLSEATPEE ADDAEQEELL 450
    SADPHPAPLS TPASKNFMDR CKNFKFTMDL SRNNLVTIKP EMFVNLSRLQ 500
    CLSLSHNSIA QAVNGSQFLP LTNLQVLDLS HNKLDLYHWK SFSELPQLQA 550
    LDLSYNSQPF SMKGIGHNFS FVTHLSMLQS LSLAHNDIHT RVSSHLNSNS 600
    VRFLDFSGNG MGRMWDEGGL YLHFFQGLSG LLKLDLSQNN LHILRPQNLD 650
    NLPKSLKLLS LRDNYLSFFN WTSLSFLPNL EVLDLAGNQL KALTNGTLPN 700
    GTLLQKLDVS SNSIVSVVPA FFALAVELKE VNLSHNILKT VDRSWFGPIV 750
    MNLTVLDVRS NPLHCACGAA FVDLLLEVQT KVPGLANGVK CGSPGQLQGR 800
    SIFAQDLRLC LDEVLSWDCF GLSLLAVAVG MVVPILHHLC GWDVWYCFHL 850
    CLAWLPLLAR SRRSAQTLPY DAFVVFDKAQ SAVADWVYNE LRVRLEERRG 900
    RRALRLCLED RDWLPGQTLF ENLWASIYGS RKTLFVLAHT DRVSGLLRTS 950
    FLLAQQRLLE DRKDVVVLVI LRPDAHRSRY VRLRQRLCRQ SVLFWPQQPN 1000
    GQGGFWAQLS TALTRDNRHF YNQNFCRGPT AE 1032
    Length:1,032
    Mass (Da):116,412
    Last modified:December 14, 2011 - v3
    Checksum:iC13A7888588CE297
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti325 – 3251T → N in BAB19260. (PubMed:11130078)Curated
    Sequence conflicti325 – 3251T → N in AAK29625. (PubMed:11470918)Curated
    Sequence conflicti325 – 3251T → N in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti325 – 3251T → N in AAU04980. (PubMed:17474149)Curated
    Sequence conflicti378 – 3781L → S in BAB19260. (PubMed:11130078)Curated
    Sequence conflicti378 – 3781L → S in AAK29625. (PubMed:11470918)Curated
    Sequence conflicti378 – 3781L → S in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti378 – 3781L → S in AAU04980. (PubMed:17474149)Curated
    Sequence conflicti554 – 5541S → G in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti562 – 5621M → I in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti573 – 5731T → A in AAK29625. (PubMed:11470918)Curated
    Sequence conflicti573 – 5731T → A in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti573 – 5731T → A in AAU04980. (PubMed:17474149)Curated
    Sequence conflicti579 – 5791Q → H in AAK29625. (PubMed:11470918)Curated
    Sequence conflicti579 – 5791Q → H in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti579 – 5791Q → H in AAU04980. (PubMed:17474149)Curated
    Sequence conflicti867 – 8671T → A in AAK29625. (PubMed:11470918)Curated
    Sequence conflicti867 – 8671T → A in AAK28488. (PubMed:11867692)Curated
    Sequence conflicti867 – 8671T → A in AAU04980. (PubMed:17474149)Curated
    Sequence conflicti897 – 8971E → G in AAK28488. (PubMed:11867692)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045181 mRNA. Translation: BAB19260.1.
    AF348140 mRNA. Translation: AAK29625.1.
    AF314224 mRNA. Translation: AAK28488.1.
    AC164430 Genomic DNA. No translation available.
    AY649790 Genomic DNA. Translation: AAU04980.1.
    AY649791 Genomic DNA. Translation: AAU04981.1.
    CCDSiCCDS40755.1.
    RefSeqiNP_112455.2. NM_031178.2.
    UniGeneiMm.44889.

    Genome annotation databases

    EnsembliENSMUST00000062241; ENSMUSP00000082207; ENSMUSG00000045322.
    GeneIDi81897.
    KEGGimmu:81897.
    UCSCiuc009rjh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045181 mRNA. Translation: BAB19260.1 .
    AF348140 mRNA. Translation: AAK29625.1 .
    AF314224 mRNA. Translation: AAK28488.1 .
    AC164430 Genomic DNA. No translation available.
    AY649790 Genomic DNA. Translation: AAU04980.1 .
    AY649791 Genomic DNA. Translation: AAU04981.1 .
    CCDSi CCDS40755.1.
    RefSeqi NP_112455.2. NM_031178.2.
    UniGenei Mm.44889.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4QDH X-ray 2.40 A/B 480-753 [» ]
    ProteinModelPortali Q9EQU3.
    SMRi Q9EQU3. Positions 34-1013.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000082207.

    Chemistry

    ChEMBLi CHEMBL6128.

    PTM databases

    PhosphoSitei Q9EQU3.

    Proteomic databases

    PaxDbi Q9EQU3.
    PRIDEi Q9EQU3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000062241 ; ENSMUSP00000082207 ; ENSMUSG00000045322 .
    GeneIDi 81897.
    KEGGi mmu:81897.
    UCSCi uc009rjh.1. mouse.

    Organism-specific databases

    CTDi 54106.
    MGIi MGI:1932389. Tlr9.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00750000117479.
    HOGENOMi HOG000230468.
    HOVERGENi HBG018601.
    InParanoidi Q4L0K3.
    KOi K10161.
    OMAi LYLHFFQ.
    OrthoDBi EOG7C8GGD.
    TreeFami TF325595.

    Enzyme and pathway databases

    Reactomei REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_198976. Trafficking and processing of endosomal TLR.

    Miscellaneous databases

    NextBioi 350461.
    PROi Q9EQU3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EQU3.
    CleanExi MM_TLR9.
    Genevestigatori Q9EQU3.

    Family and domain databases

    Gene3Di 3.40.50.10140. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027181. TLR9.
    [Graphical view ]
    PANTHERi PTHR24373:SF37. PTHR24373:SF37. 1 hit.
    Pfami PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 5 hits.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS51450. LRR. 16 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition."
      Bauer S.M., Kirschning C.J., Hacker H., Redecke V., Hausmann S., Akira S., Wagner H., Lipford G.B.
      Proc. Natl. Acad. Sci. U.S.A. 98:9237-9242(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    3. "Toll-like receptor 9 mediates CpG-DNA signaling."
      Chuang T.-H., Lee J., Kline L., Mathison J.C., Ulevitch R.J.
      J. Leukoc. Biol. 71:538-544(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "TLR9 polymorphisms determine murine lymphocyte responses to Helicobacter: results from a genome-wide scan."
      Anderson A.E., Worku M.L., Khamri W., Bamford K.B., Walker M.M., Thursz M.R.
      Eur. J. Immunol. 37:1548-1561(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-964, FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
      Strain: BALB/c and C57BL/6.
    6. "Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection."
      Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.
      Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOMEGALOVIRUS INFECTION, MUTAGENESIS OF LEU-499.
    7. "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling."
      Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.
      J. Cell Biol. 177:265-275(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UNC93B1.
    8. "A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors."
      Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K.
      Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNPY3.
    9. "UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes."
      Kim Y.M., Brinkmann M.M., Paquet M.E., Ploegh H.L.
      Nature 452:234-238(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNPY3 AND HSP90B1.
    11. Erratum
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 3:653-653(2012)
    12. "CMRF-35-like molecule 3 preferentially promotes TLR9-triggered proinflammatory cytokine production in macrophages by enhancing TNF receptor-associated factor 6 ubiquitination."
      Wu Y., Zhu X., Li N., Chen T., Yang M., Yao M., Liu X., Jin B., Wang X., Cao X.
      J. Immunol. 187:4881-4889(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD300LH.

    Entry informationi

    Entry nameiTLR9_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQU3
    Secondary accession number(s): F8VPN5
    , Q4L0K3, Q4L0K4, Q99MF2, Q99MQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 126 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3