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Q9QUN7

- TLR2_MOUSE

UniProt

Q9QUN7 - TLR2_MOUSE

Protein

Toll-like receptor 2

Gene

Tlr2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei349 – 3491Interaction with bacterial lipopeptideBy similarity

    GO - Molecular functioni

    1. diacyl lipopeptide binding Source: MGI
    2. lipoteichoic acid binding Source: MGI
    3. protein binding Source: BHF-UCL
    4. protein heterodimerization activity Source: MGI
    5. transmembrane signaling receptor activity Source: InterPro
    6. triacyl lipopeptide binding Source: MGI

    GO - Biological processi

    1. cell surface pattern recognition receptor signaling pathway Source: MGI
    2. cellular response to bacterial lipopeptide Source: BHF-UCL
    3. cellular response to lipoteichoic acid Source: MGI
    4. cellular response to peptidoglycan Source: MGI
    5. chloramphenicol transport Source: MGI
    6. defense response to Gram-positive bacterium Source: MGI
    7. induction by symbiont of defense-related host nitric oxide production Source: MGI
    8. inflammatory response Source: UniProtKB-KW
    9. innate immune response Source: BHF-UCL
    10. MyD88-dependent toll-like receptor signaling pathway Source: MGI
    11. negative regulation of growth of symbiont in host Source: MGI
    12. negative regulation of interleukin-12 production Source: MGI
    13. negative regulation of interleukin-17 production Source: MGI
    14. positive regulation of chemokine production Source: MGI
    15. positive regulation of cytokine secretion Source: MGI
    16. positive regulation of inflammatory response Source: InterPro
    17. positive regulation of interferon-beta production Source: BHF-UCL
    18. positive regulation of interleukin-12 production Source: BHF-UCL
    19. positive regulation of interleukin-18 production Source: BHF-UCL
    20. positive regulation of interleukin-6 production Source: BHF-UCL
    21. positive regulation of leukocyte migration Source: MGI
    22. positive regulation of macrophage cytokine production Source: MGI
    23. positive regulation of nitric oxide biosynthetic process Source: MGI
    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 biosynthetic process Source: MGI
    27. positive regulation of tumor necrosis factor production Source: BHF-UCL
    28. response to bacterium Source: MGI
    29. response to molecule of fungal origin Source: MGI
    30. response to peptidoglycan Source: MGI
    31. toll-like receptor 2 signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Toll-like receptor 2
    Alternative name(s):
    CD_antigen: CD282
    Gene namesi
    Name:Tlr2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1346060. Tlr2.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. integral component of membrane Source: UniProtKB-KW
    3. phagocytic vesicle membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: MGI
    5. Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
    6. Toll-like receptor 2-Toll-like receptor 6 protein complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi681 – 6811P → H: Abolishes MYD88-binding and response to microbial cell wall components. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 784760Toll-like receptor 2PRO_0000034712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 36
    Glycosylationi147 – 1471N-linked (GlcNAc...)2 Publications
    Disulfide bondi353 ↔ 382
    Glycosylationi414 – 4141N-linked (GlcNAc...)2 Publications
    Disulfide bondi432 ↔ 454
    Glycosylationi442 – 4421N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9QUN7.

    PTM databases

    PhosphoSiteiQ9QUN7.

    Expressioni

    Tissue specificityi

    Detected in a macrophage cell line, smooth muscle, lung, spleen, thymus, brain and adipose tissue.

    Gene expression databases

    CleanExiMM_TLR2.
    GenevestigatoriQ9QUN7.

    Interactioni

    Subunit structurei

    Interacts with ATG16L1 By similarity. Interacts with LY96, TLR1 and TLR6 (via extracellular domain). Binds MYD88 (via TIR domain). Interacts with TICAM1. Ligand binding induces the formation of a heterodimer with TLR1 or TLR6. Interacts with CNPY3.By similarity2 Publications

    Protein-protein interaction databases

    IntActiQ9QUN7. 1 interaction.
    STRINGi10090.ENSMUSP00000029623.

    Structurei

    Secondary structure

    1
    784
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi44 – 463
    Beta strandi56 – 583
    Beta strandi71 – 744
    Beta strandi80 – 823
    Turni93 – 986
    Beta strandi104 – 1063
    Helixi117 – 1204
    Beta strandi128 – 1303
    Beta strandi137 – 1393
    Beta strandi153 – 1619
    Turni167 – 1726
    Beta strandi175 – 1839
    Turni191 – 1966
    Beta strandi198 – 2069
    Beta strandi208 – 2103
    Helixi213 – 2197
    Turni221 – 2233
    Beta strandi224 – 2318
    Beta strandi245 – 2473
    Beta strandi253 – 2586
    Beta strandi260 – 2623
    Helixi263 – 2708
    Helixi271 – 2755
    Beta strandi281 – 2866
    Beta strandi288 – 2903
    Turni299 – 3013
    Helixi304 – 3063
    Beta strandi311 – 3166
    Helixi322 – 3243
    Helixi330 – 3345
    Beta strandi340 – 3467
    Helixi353 – 3586
    Beta strandi364 – 3663
    Helixi374 – 3807
    Beta strandi391 – 3933
    Helixi402 – 4087
    Helixi409 – 4113
    Beta strandi417 – 4193
    Beta strandi440 – 4423
    Beta strandi460 – 4634
    Beta strandi481 – 4833
    Helixi495 – 4973
    Beta strandi503 – 5053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z81X-ray1.80A27-506[»]
    2Z82X-ray2.60A27-506[»]
    3A79X-ray2.90A1-506[»]
    3A7BX-ray2.53A1-506[»]
    3A7CX-ray2.40A1-506[»]
    ProteinModelPortaliQ9QUN7.
    SMRiQ9QUN7. Positions 27-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QUN7.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 587563ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini609 – 784176CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei588 – 60821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati54 – 7724LRR 11 PublicationAdd
    BLAST
    Repeati78 – 10124LRR 21 PublicationAdd
    BLAST
    Repeati102 – 12524LRR 31 PublicationAdd
    BLAST
    Repeati126 – 15025LRR 41 PublicationAdd
    BLAST
    Repeati151 – 17525LRR 51 PublicationAdd
    BLAST
    Repeati176 – 19924LRR 61 PublicationAdd
    BLAST
    Repeati200 – 22324LRR 71 PublicationAdd
    BLAST
    Repeati224 – 25027LRR 81 PublicationAdd
    BLAST
    Repeati251 – 27828LRR 91 PublicationAdd
    BLAST
    Repeati279 – 30830LRR 101 PublicationAdd
    BLAST
    Repeati309 – 33729LRR 111 PublicationAdd
    BLAST
    Repeati338 – 36124LRR 121 PublicationAdd
    BLAST
    Repeati362 – 38827LRR 131 PublicationAdd
    BLAST
    Repeati389 – 41426LRR 141 PublicationAdd
    BLAST
    Repeati415 – 43723LRR 151 PublicationAdd
    BLAST
    Repeati438 – 45720LRR 161 PublicationAdd
    BLAST
    Repeati458 – 47821LRR 171 PublicationAdd
    BLAST
    Repeati479 – 50022LRR 181 PublicationAdd
    BLAST
    Repeati501 – 52424LRR 191 PublicationAdd
    BLAST
    Domaini525 – 57652LRRCTAdd
    BLAST
    Domaini639 – 784146TIRPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi761 – 77818ATG16L1-binding motifAdd
    BLAST

    Domaini

    Ester-bound lipid substrates are bound through a crevice formed between the LRR 11 and LRR 12.
    The ATG16L1-binding motif mediates interaction with ATG16L1.By similarity

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 19 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG251801.
    HOGENOMiHOG000110611.
    HOVERGENiHBG108574.
    InParanoidiQ9QUN7.
    KOiK10159.
    PhylomeDBiQ9QUN7.

    Family and domain databases

    Gene3Di3.40.50.10140. 1 hit.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027185. TLR2.
    IPR017241. Toll-like_receptor.
    [Graphical view]
    PANTHERiPTHR24365:SF17. PTHR24365:SF17. 1 hit.
    PfamiPF13504. LRR_7. 2 hits.
    PF13855. LRR_8. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
    SMARTiSM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS51450. LRR. 9 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9QUN7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRALWLFWI LVAITVLFSK RCSAQESLSC DASGVCDGRS RSFTSIPSGL    50
    TAAMKSLDLS FNKITYIGHG DLRACANLQV LILKSSRINT IEGDAFYSLG 100
    SLEHLDLSDN HLSSLSSSWF GPLSSLKYLN LMGNPYQTLG VTSLFPNLTN 150
    LQTLRIGNVE TFSEIRRIDF AGLTSLNELE IKALSLRNYQ SQSLKSIRDI 200
    HHLTLHLSES AFLLEIFADI LSSVRYLELR DTNLARFQFS PLPVDEVSSP 250
    MKKLAFRGSV LTDESFNELL KLLRYILELS EVEFDDCTLN GLGDFNPSES 300
    DVVSELGKVE TVTIRRLHIP QFYLFYDLST VYSLLEKVKR ITVENSKVFL 350
    VPCSFSQHLK SLEFLDLSEN LMVEEYLKNS ACKGAWPSLQ TLVLSQNHLR 400
    SMQKTGEILL TLKNLTSLDI SRNTFHPMPD SCQWPEKMRF LNLSSTGIRV 450
    VKTCIPQTLE VLDVSNNNLD SFSLFLPRLQ ELYISRNKLK TLPDASLFPV 500
    LLVMKIRENA VSTFSKDQLG SFPKLETLEA GDNHFVCSCE LLSFTMETPA 550
    LAQILVDWPD SYLCDSPPRL HGHRLQDARP SVLECHQAAL VSGVCCALLL 600
    LILLVGALCH HFHGLWYLRM MWAWLQAKRK PKKAPCRDVC YDAFVSYSEQ 650
    DSHWVENLMV QQLENSDPPF KLCLHKRDFV PGKWIIDNII DSIEKSHKTV 700
    FVLSENFVRS EWCKYELDFS HFRLFDENND AAILVLLEPI ERKAIPQRFC 750
    KLRKIMNTKT YLEWPLDEGQ QEVFWVNLRT AIKS 784
    Length:784
    Mass (Da):89,449
    Last modified:May 1, 2000 - v1
    Checksum:i606D56BF85F320A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591L → P in BAB23770. (PubMed:16141072)Curated
    Sequence conflicti82 – 821I → M in BAB23770. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF185284 mRNA. Translation: AAF04277.1.
    AF124741 mRNA. Translation: AAD46481.1.
    AF216289 mRNA. Translation: AAF28345.1.
    AF165189 mRNA. Translation: AAD49335.1.
    AK005043 mRNA. Translation: BAB23770.1.
    AK154504 mRNA. Translation: BAE32635.1.
    CCDSiCCDS17435.1.
    RefSeqiNP_036035.3. NM_011905.3.
    UniGeneiMm.87596.

    Genome annotation databases

    GeneIDi24088.
    KEGGimmu:24088.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF185284 mRNA. Translation: AAF04277.1 .
    AF124741 mRNA. Translation: AAD46481.1 .
    AF216289 mRNA. Translation: AAF28345.1 .
    AF165189 mRNA. Translation: AAD49335.1 .
    AK005043 mRNA. Translation: BAB23770.1 .
    AK154504 mRNA. Translation: BAE32635.1 .
    CCDSi CCDS17435.1.
    RefSeqi NP_036035.3. NM_011905.3.
    UniGenei Mm.87596.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z81 X-ray 1.80 A 27-506 [» ]
    2Z82 X-ray 2.60 A 27-506 [» ]
    3A79 X-ray 2.90 A 1-506 [» ]
    3A7B X-ray 2.53 A 1-506 [» ]
    3A7C X-ray 2.40 A 1-506 [» ]
    ProteinModelPortali Q9QUN7.
    SMRi Q9QUN7. Positions 27-784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QUN7. 1 interaction.
    STRINGi 10090.ENSMUSP00000029623.

    Chemistry

    ChEMBLi CHEMBL1075106.

    PTM databases

    PhosphoSitei Q9QUN7.

    Proteomic databases

    PRIDEi Q9QUN7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24088.
    KEGGi mmu:24088.

    Organism-specific databases

    CTDi 7097.
    MGIi MGI:1346060. Tlr2.

    Phylogenomic databases

    eggNOGi NOG251801.
    HOGENOMi HOG000110611.
    HOVERGENi HBG108574.
    InParanoidi Q9QUN7.
    KOi K10159.
    PhylomeDBi Q9QUN7.

    Miscellaneous databases

    EvolutionaryTracei Q9QUN7.
    NextBioi 304101.
    PROi Q9QUN7.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_TLR2.
    Genevestigatori Q9QUN7.

    Family and domain databases

    Gene3Di 3.40.50.10140. 1 hit.
    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027185. TLR2.
    IPR017241. Toll-like_receptor.
    [Graphical view ]
    PANTHERi PTHR24365:SF17. PTHR24365:SF17. 1 hit.
    Pfami PF13504. LRR_7. 2 hits.
    PF13855. LRR_8. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037595. Toll-like_receptor. 1 hit.
    SMARTi SM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS51450. LRR. 9 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens."
      Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A.
      Nature 401:811-815(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-681.
    2. "Cells that carry a null allele for Toll-like receptor 2 are capable of responding to endotoxin."
      Heine H., Kirschning C.J., Lien E., Monks B.G., Rothe M., Golenbock D.T.
      J. Immunol. 162:6971-6975(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    3. "Gene expressions of lipopolysaccharide receptors, Toll-like receptors 2 and 4, are differently regulated in mouse T lymphocytes."
      Matsuguchi T., Takagi K., Musikacharoen T., Yoshikai Y.
      Blood 95:1378-1385(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    4. "The lipopolysaccharide-activated Toll-like receptor (TLR)-4 induces synthesis of the closely related receptor TLR-2 in adipocytes."
      Lin Y., Lee H., Berg A.H., Lisanti M.P., Shapiro L., Scherer P.E.
      J. Biol. Chem. 275:24255-24263(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adipocyte.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Liver.
    6. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 405-413 AND 754-759, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    7. "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.
    8. "Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide."
      Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H., Lee J.-O.
      Cell 130:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-506, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442.
    9. "Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer."
      Kang J.Y., Nan X., Jin M.S., Youn S.J., Ryu Y.H., Mah S., Han S.H., Lee H., Paik S.G., Lee J.O.
      Immunity 31:873-884(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-506 IN COMPLEX WITH TLR6 AND LIPOPEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442, FUNCTION, LRR REPEATS, SUBUNIT.

    Entry informationi

    Entry nameiTLR2_MOUSE
    AccessioniPrimary (citable) accession number: Q9QUN7
    Secondary accession number(s): Q3U400, Q9DBC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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