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O60603

- TLR2_HUMAN

UniProt

O60603 - TLR2_HUMAN

Protein

Toll-like receptor 2

Gene

TLR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.

    Sites

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

    GO - Molecular functioni

    1. diacyl lipopeptide binding Source: Ensembl
    2. lipopolysaccharide receptor activity Source: UniProtKB
    3. lipoteichoic acid binding Source: Ensembl
    4. peptidoglycan binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein heterodimerization activity Source: MGI
    7. receptor activity Source: UniProtKB
    8. signaling pattern recognition receptor activity Source: UniProtKB
    9. transmembrane signaling receptor activity Source: InterPro
    10. triacyl lipopeptide binding Source: MGI

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cell surface pattern recognition receptor signaling pathway Source: Ensembl
    3. cellular response to bacterial lipopeptide Source: BHF-UCL
    4. cellular response to diacyl bacterial lipopeptide Source: MGI
    5. cellular response to lipoteichoic acid Source: MGI
    6. cellular response to peptidoglycan Source: Ensembl
    7. cellular response to triacyl bacterial lipopeptide Source: MGI
    8. central nervous system myelin formation Source: Ensembl
    9. chloramphenicol transport Source: Ensembl
    10. defense response to Gram-positive bacterium Source: UniProtKB
    11. detection of diacyl bacterial lipopeptide Source: MGI
    12. detection of triacyl bacterial lipopeptide Source: MGI
    13. I-kappaB phosphorylation Source: BHF-UCL
    14. immune response Source: ProtInc
    15. induction by symbiont of defense-related host nitric oxide production Source: Ensembl
    16. inflammatory response Source: UniProtKB-KW
    17. innate immune response Source: BHF-UCL
    18. leukotriene metabolic process Source: Ensembl
    19. lipopolysaccharide-mediated signaling pathway Source: GOC
    20. microglial cell activation involved in immune response Source: Ensembl
    21. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    22. negative regulation of cell proliferation Source: Ensembl
    23. negative regulation of growth of symbiont in host Source: Ensembl
    24. negative regulation of interleukin-12 production Source: Ensembl
    25. negative regulation of interleukin-17 production Source: Ensembl
    26. nitric oxide metabolic process Source: Ensembl
    27. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
    28. positive regulation of chemokine production Source: BHF-UCL
    29. positive regulation of cytokine secretion Source: Ensembl
    30. positive regulation of inflammatory response Source: BHF-UCL
    31. positive regulation of interferon-beta production Source: BHF-UCL
    32. positive regulation of interleukin-10 production Source: Ensembl
    33. positive regulation of interleukin-12 production Source: BHF-UCL
    34. positive regulation of interleukin-18 production Source: BHF-UCL
    35. positive regulation of interleukin-6 production Source: BHF-UCL
    36. positive regulation of interleukin-8 production Source: BHF-UCL
    37. positive regulation of leukocyte migration Source: Ensembl
    38. positive regulation of macrophage cytokine production Source: Ensembl
    39. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
    40. positive regulation of NF-kappaB transcription factor activity Source: MGI
    41. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    42. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
    43. positive regulation of oligodendrocyte differentiation Source: Ensembl
    44. positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
    45. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    46. positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
    47. positive regulation of tumor necrosis factor production Source: BHF-UCL
    48. positive regulation of Wnt signaling pathway Source: BHF-UCL
    49. response to fatty acid Source: Ensembl
    50. response to hypoxia Source: Ensembl
    51. response to insulin Source: Ensembl
    52. response to molecule of fungal origin Source: Ensembl
    53. response to progesterone Source: Ensembl
    54. response to toxic substance Source: Ensembl
    55. signal transduction Source: UniProtKB
    56. toll-like receptor 2 signaling pathway Source: Reactome
    57. toll-like receptor 4 signaling pathway Source: Reactome
    58. toll-like receptor signaling pathway Source: Reactome
    59. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    60. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_115897. Beta defensins.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    REACT_8005. Toll Like Receptor TLR1:TLR2 Cascade.
    REACT_8006. Toll Like Receptor TLR6:TLR2 Cascade.
    SignaLinkiO60603.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Toll-like receptor 2
    Alternative name(s):
    Toll/interleukin-1 receptor-like protein 4
    CD_antigen: CD282
    Gene namesi
    Name:TLR2
    Synonyms:TIL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11848. TLR2.

    Subcellular locationi

    Membrane By similarity; Single-pass type I membrane protein By similarity

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. cell projection Source: Ensembl
    3. cell surface Source: UniProtKB
    4. cytoplasm Source: BHF-UCL
    5. external side of plasma membrane Source: Ensembl
    6. integral component of plasma membrane Source: ProtInc
    7. plasma membrane Source: BHF-UCL
    8. Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
    9. Toll-like receptor 2-Toll-like receptor 6 protein complex Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 2 Publications
    Mutagenesisi199 – 1991N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 2 Publications
    Mutagenesisi416 – 4161T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 2 Publications
    Mutagenesisi442 – 4421N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. 2 Publications
    Mutagenesisi681 – 6811P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain. 1 Publication

    Organism-specific databases

    MIMi246300. phenotype.
    PharmGKBiPA36550.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 784766Toll-like receptor 2PRO_0000034710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 361 Publication
    Glycosylationi114 – 1141N-linked (GlcNAc...)2 Publications
    Glycosylationi199 – 1991N-linked (GlcNAc...)2 Publications
    Disulfide bondi353 ↔ 3821 Publication
    Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
    Disulfide bondi432 ↔ 4541 Publication
    Glycosylationi442 – 4421N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO60603.
    PRIDEiO60603.

    PTM databases

    PhosphoSiteiO60603.

    Expressioni

    Tissue specificityi

    Highly expressed in peripheral blood leukocytes, in particular in monocytes, in bone marrow, lymph node and in spleen. Also detected in lung and in fetal liver. Levels are low in other tissues.

    Gene expression databases

    ArrayExpressiO60603.
    BgeeiO60603.
    CleanExiHS_TLR2.
    GenevestigatoriO60603.

    Interactioni

    Subunit structurei

    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 similarity. Interacts with ATG16L1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAUFC3PTT63EBI-973722,EBI-3505892

    Protein-protein interaction databases

    BioGridi112952. 12 interactions.
    DIPiDIP-35138N.
    IntActiO60603. 9 interactions.
    MINTiMINT-3000106.
    STRINGi9606.ENSP00000260010.

    Structurei

    Secondary structure

    1
    784
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi56 – 583
    Turni69 – 746
    Beta strandi80 – 823
    Turni93 – 986
    Beta strandi104 – 1063
    Helixi117 – 1204
    Beta strandi127 – 1304
    Beta strandi137 – 1393
    Beta strandi153 – 1619
    Turni167 – 1726
    Beta strandi175 – 1839
    Turni191 – 1966
    Beta strandi198 – 2069
    Helixi213 – 2208
    Turni221 – 2233
    Beta strandi224 – 2318
    Beta strandi253 – 2586
    Beta strandi260 – 2623
    Helixi263 – 27412
    Beta strandi281 – 2833
    Beta strandi288 – 2914
    Beta strandi311 – 3166
    Helixi322 – 3243
    Helixi329 – 3346
    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
    Beta strandi641 – 6466
    Helixi649 – 6513
    Helixi652 – 6565
    Helixi658 – 6636
    Beta strandi666 – 6683
    Beta strandi672 – 6743
    Helixi675 – 6784
    Beta strandi681 – 6833
    Helixi685 – 69511
    Beta strandi696 – 7038
    Helixi705 – 7117
    Helixi713 – 7164
    Turni717 – 7193
    Helixi720 – 7223
    Turni723 – 7253
    Helixi726 – 7283
    Beta strandi733 – 7386
    Turni742 – 7443
    Helixi750 – 7589
    Beta strandi761 – 7633
    Helixi768 – 7703
    Helixi771 – 78313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYWX-ray3.00A636-784[»]
    1FYXX-ray2.80A636-784[»]
    1O77X-ray3.20A/B/C/D/E639-784[»]
    2Z7XX-ray2.10A27-506[»]
    2Z80X-ray1.80A/B1-284[»]
    ProteinModelPortaliO60603.
    SMRiO60603. Positions 27-553, 636-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60603.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 588570ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini610 – 784175CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei589 – 60921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati54 – 7724LRR 1Add
    BLAST
    Repeati78 – 10124LRR 2Add
    BLAST
    Repeati102 – 12524LRR 3Add
    BLAST
    Repeati126 – 15025LRR 4Add
    BLAST
    Repeati151 – 17525LRR 5Add
    BLAST
    Repeati176 – 19924LRR 6Add
    BLAST
    Repeati200 – 22324LRR 7Add
    BLAST
    Repeati224 – 25027LRR 8Add
    BLAST
    Repeati251 – 27828LRR 9Add
    BLAST
    Repeati279 – 30830LRR 10Add
    BLAST
    Repeati309 – 33729LRR 11Add
    BLAST
    Repeati338 – 36124LRR 12Add
    BLAST
    Repeati362 – 38827LRR 13Add
    BLAST
    Repeati389 – 41426LRR 14Add
    BLAST
    Repeati415 – 43723LRR 15Add
    BLAST
    Repeati438 – 45720LRR 16Add
    BLAST
    Repeati458 – 47821LRR 17Add
    BLAST
    Repeati479 – 50022LRR 18Add
    BLAST
    Repeati501 – 52424LRR 19Add
    BLAST
    Domaini525 – 57955LRRCTAdd
    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.By similarity
    The ATG16L1-binding motif mediates interaction with ATG16L1.1 Publication

    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.
    InParanoidiO60603.
    KOiK10159.
    OMAiLGNPYKT.
    OrthoDBiEOG7SBNN7.
    PhylomeDBiO60603.
    TreeFamiTF351113.

    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.
    PfamiPF13855. LRR_8. 3 hits.
    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. 11 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O60603-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL    50
    TEAVKSLDLS NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG 100
    SLEHLDLSYN YLSNLSSSWF KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK 150
    LQILRVGNMD TFTKIQRKDF AGLTFLEELE IDASDLQSYE PKSLKSIQNV 200
    SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS ELSTGETNSL 250
    IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN 300
    DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL 350
    VPCLLSQHLK SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA 400
    SLEKTGETLL TLKNLTNIDI SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS 450
    VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK ELYISRNKLM TLPDASLLPM 500
    LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE FLSFTQEQQA 550
    LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL 600
    LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER 650
    DAYWVENLMV QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV 700
    FVLSENFVKS EWCKYELDFS HFRLFDENND AAILILLEPI EKKAIPQRFC 750
    KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA AIKS 784
    Length:784
    Mass (Da):89,838
    Last modified:August 1, 1998 - v1
    Checksum:i7DBE6B24CF1FAF8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591L → Q in AAM23001. 1 PublicationCurated
    Sequence conflicti68 – 681S → C in AAM23001. 1 PublicationCurated
    Sequence conflicti726 – 7261D → E in AAC34133. (PubMed:9435236)Curated

    Polymorphismi

    Genetic variations in TLR2 are associated with susceptibility to leprosy [MIMi:246300]. Leprosy is a chronic disease associated with depressed cellular (but not humoral) immunity, the bacterium requires a lower temperature than 37 degrees Celsius and thrives particularly in peripheral Schwann cells and macrophages. The Trp-677 polymorphism in the intracellular domain of TLR2 has a role in susceptibility to lepromatous leprosy. Wild-type TLR2 mediates CD14-enhanced Mycobacterium leprae-dependent activation of NFKB1, but TLR2 containing the Trp-677 polymorphism did not. The impaired function of the Trp-677 polymorphism provides a molecular mechanism for the poor cellular immune response associated with lepromatous leprosy.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891N → D.1 Publication
    VAR_066349
    Natural varianti411 – 4111T → I Reduces TLR2-mediated NF-kappa-B activation. 1 Publication
    Corresponds to variant rs5743699 [ dbSNP | Ensembl ].
    VAR_026765
    Natural varianti571 – 5711R → H.1 Publication
    Corresponds to variant rs61735277 [ dbSNP | Ensembl ].
    VAR_066350
    Natural varianti579 – 5791R → H.
    Corresponds to variant rs5743703 [ dbSNP | Ensembl ].
    VAR_026766
    Natural varianti631 – 6311P → H Reduces TLR2-mediated NF-kappa-B activation. 2 Publications
    Corresponds to variant rs5743704 [ dbSNP | Ensembl ].
    VAR_024663
    Natural varianti636 – 6361S → R.1 Publication
    Corresponds to variant rs137853177 [ dbSNP | Ensembl ].
    VAR_066351
    Natural varianti677 – 6771R → W.2 Publications
    VAR_031236
    Natural varianti715 – 7151Y → N.
    Corresponds to variant rs5743706 [ dbSNP | Ensembl ].
    VAR_052360
    Natural varianti753 – 7531R → Q Reduces TLR2-mediated NF-kappa-B activation. 2 Publications
    Corresponds to variant rs5743708 [ dbSNP | Ensembl ].
    VAR_031237

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051152 mRNA. Translation: AAC34377.1.
    U88878 mRNA. Translation: AAC34133.1.
    AB445624 mRNA. Translation: BAG55021.1.
    DQ012265 mRNA. Translation: AAY85644.1.
    DQ012266 mRNA. Translation: AAY85645.1.
    DQ012267 mRNA. Translation: AAY85646.1.
    DQ012268 mRNA. Translation: AAY85647.1.
    DQ012269 mRNA. Translation: AAY85648.1.
    DQ012270 mRNA. Translation: AAY85649.1.
    DQ012271 mRNA. Translation: AAY85650.1.
    CH471056 Genomic DNA. Translation: EAX04952.1.
    CH471056 Genomic DNA. Translation: EAX04953.1.
    BC033756 mRNA. Translation: AAH33756.1.
    AF502291 mRNA. Translation: AAM23001.1.
    CCDSiCCDS3784.1.
    RefSeqiNP_003255.2. NM_003264.3.
    XP_005263250.1. XM_005263193.1.
    XP_005263251.1. XM_005263194.1.
    XP_005263252.1. XM_005263195.1.
    XP_005263253.1. XM_005263196.1.
    XP_005263254.1. XM_005263197.1.
    UniGeneiHs.519033.

    Genome annotation databases

    EnsembliENST00000260010; ENSP00000260010; ENSG00000137462.
    GeneIDi7097.
    KEGGihsa:7097.
    UCSCiuc003inq.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051152 mRNA. Translation: AAC34377.1 .
    U88878 mRNA. Translation: AAC34133.1 .
    AB445624 mRNA. Translation: BAG55021.1 .
    DQ012265 mRNA. Translation: AAY85644.1 .
    DQ012266 mRNA. Translation: AAY85645.1 .
    DQ012267 mRNA. Translation: AAY85646.1 .
    DQ012268 mRNA. Translation: AAY85647.1 .
    DQ012269 mRNA. Translation: AAY85648.1 .
    DQ012270 mRNA. Translation: AAY85649.1 .
    DQ012271 mRNA. Translation: AAY85650.1 .
    CH471056 Genomic DNA. Translation: EAX04952.1 .
    CH471056 Genomic DNA. Translation: EAX04953.1 .
    BC033756 mRNA. Translation: AAH33756.1 .
    AF502291 mRNA. Translation: AAM23001.1 .
    CCDSi CCDS3784.1.
    RefSeqi NP_003255.2. NM_003264.3.
    XP_005263250.1. XM_005263193.1.
    XP_005263251.1. XM_005263194.1.
    XP_005263252.1. XM_005263195.1.
    XP_005263253.1. XM_005263196.1.
    XP_005263254.1. XM_005263197.1.
    UniGenei Hs.519033.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FYW X-ray 3.00 A 636-784 [» ]
    1FYX X-ray 2.80 A 636-784 [» ]
    1O77 X-ray 3.20 A/B/C/D/E 639-784 [» ]
    2Z7X X-ray 2.10 A 27-506 [» ]
    2Z80 X-ray 1.80 A/B 1-284 [» ]
    ProteinModelPortali O60603.
    SMRi O60603. Positions 27-553, 636-784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112952. 12 interactions.
    DIPi DIP-35138N.
    IntActi O60603. 9 interactions.
    MINTi MINT-3000106.
    STRINGi 9606.ENSP00000260010.

    Chemistry

    BindingDBi O60603.
    ChEMBLi CHEMBL4163.
    GuidetoPHARMACOLOGYi 1752.

    PTM databases

    PhosphoSitei O60603.

    Proteomic databases

    PaxDbi O60603.
    PRIDEi O60603.

    Protocols and materials databases

    DNASUi 7097.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260010 ; ENSP00000260010 ; ENSG00000137462 .
    GeneIDi 7097.
    KEGGi hsa:7097.
    UCSCi uc003inq.3. human.

    Organism-specific databases

    CTDi 7097.
    GeneCardsi GC04P154612.
    HGNCi HGNC:11848. TLR2.
    MIMi 246300. phenotype.
    603028. gene.
    neXtProti NX_O60603.
    PharmGKBi PA36550.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251801.
    HOGENOMi HOG000110611.
    HOVERGENi HBG108574.
    InParanoidi O60603.
    KOi K10159.
    OMAi LGNPYKT.
    OrthoDBi EOG7SBNN7.
    PhylomeDBi O60603.
    TreeFami TF351113.

    Enzyme and pathway databases

    Reactomei REACT_115897. Beta defensins.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    REACT_8005. Toll Like Receptor TLR1:TLR2 Cascade.
    REACT_8006. Toll Like Receptor TLR6:TLR2 Cascade.
    SignaLinki O60603.

    Miscellaneous databases

    EvolutionaryTracei O60603.
    GeneWikii TLR_2.
    GenomeRNAii 7097.
    NextBioi 27765.
    PROi O60603.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60603.
    Bgeei O60603.
    CleanExi HS_TLR2.
    Genevestigatori O60603.

    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 PF13855. LRR_8. 3 hits.
    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. 11 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of two Toll/Interleukin-1 receptor-like genes TIL3 and TIL4: evidence for a multi-gene receptor family in humans."
      Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M., Jasmin A., Trask B.J., Hood L., Nelson P.S.
      Blood 91:4020-4027(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leukocyte and Prostate.
    2. "A family of human receptors structurally related to Drosophila Toll."
      Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.
      Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling."
      Yang R.-B., Mark M.R., Gray A.M., Huang A., Xie M.-H., Zhang M., Goddard A.D., Wood W.I., Gurney A.L., Godowski P.J.
      Nature 395:284-288(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], RESPONSE TO LIPOPOLYSACCHARIDE.
      Tissue: Fetal lung.
    4. "Natural selection in the TLR-related genes in the course of primate evolution."
      Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.
      Immunogenetics 60:727-735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "The heterogeneous allelic repertoire of human Toll-Like receptor (TLR) genes."
      Georgel P., Macquin C., Bahram S.
      PLoS ONE 4:E7803-E7803(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-631 AND GLN-753.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Blood.
    8. "Cloning and sequencing of extracellular domain and its N-terminal and C-terminal fragments of Toll-like receptor 2."
      Zhang L., Yu W.B., Ma Y.Y.
      Di 4 Jun Yi Da Xue Xue Bao 23:1085-1089(2002)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-586.
    9. "Cell activation and apoptosis by bacterial lipoproteins through Toll-like receptor-2."
      Aliprantis A.O., Yang R.-B., Mark M.R., Suggett S., Devaux B., Radolf J.D., Klimpel G.R., Godowski P.J., Zychlinsky A.
      Science 285:736-739(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: RESPONSE TO BACTERIAL LIPOPROTEINS.
    10. "A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling."
      Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S.
      J. Immunol. 169:6668-6672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    11. "Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion."
      Weber A.N., Morse M.A., Gay N.J.
      J. Biol. Chem. 279:34589-34594(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-114; ASN-199 AND ASN-442, MUTAGENESIS OF ASN-114; ASN-199; THR-416 AND ASN-442.
    12. "TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3."
      Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C., Pimentel-Muinos F.X.
      EMBO J. 32:566-582(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG16L1.
    13. "Structural basis for signal transduction by the Toll/interleukin-1 receptor domains."
      Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.
      Nature 408:111-115(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 639-784, MUTAGENESIS.
    14. "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 1-509 IN COMPLEX WITH TLR1 AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, GLYCOSYLATION AT ASN-114; ASN-199; ASN-414 AND ASN-442.
    15. "Detection of Toll-like receptor 2 (TLR2) mutation in the lepromatous leprosy patients."
      Kang T.-J., Chae G.-T.
      FEMS Immunol. Med. Microbiol. 31:53-58(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
    16. "A Toll-like receptor 2 polymorphism that is associated with lepromatous leprosy is unable to mediate mycobacterial signaling."
      Bochud P.-Y., Hawn T.R., Aderem A.
      J. Immunol. 170:3451-3454(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
    17. "Functional characterization of naturally occurring genetic variants in the human TLR1-2-6 gene family."
      Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M., Pellegrini S., Quintana-Murci L.
      Hum. Mutat. 32:643-652(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-89; ILE-411; HIS-571; HIS-631; ARG-636 AND GLN-753, CHARACTERIZATION OF VARIANTS ILE-411; HIS-631 AND GLN-753.

    Entry informationi

    Entry nameiTLR2_HUMAN
    AccessioniPrimary (citable) accession number: O60603
    Secondary accession number(s): B3Y612
    , D1CS45, D1CS48, D1CS49, O15454, Q8NI00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3