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Q9NR97

- TLR8_HUMAN

UniProt

Q9NR97 - TLR8_HUMAN

Protein

Toll-like receptor 8

Gene

TLR8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.2 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. double-stranded RNA binding Source: UniProtKB
    3. drug binding Source: Ensembl
    4. receptor activity Source: UniProtKB
    5. RNA binding Source: UniProtKB
    6. single-stranded RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to mechanical stimulus Source: UniProtKB
    2. defense response to virus Source: UniProtKB
    3. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. immunoglobulin mediated immune response Source: UniProtKB
    5. inflammatory response Source: UniProtKB-KW
    6. innate immune response Source: UniProtKB
    7. microglial cell activation involved in immune response Source: Ensembl
    8. MyD88-dependent toll-like receptor signaling pathway Source: InterPro
    9. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
    10. positive regulation of innate immune response Source: UniProtKB
    11. positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
    12. positive regulation of interferon-beta biosynthetic process Source: UniProtKB
    13. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
    14. positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
    15. regulation of cytokine secretion Source: InterPro
    16. response to virus Source: UniProtKB
    17. toll-like receptor 8 signaling pathway Source: InterPro
    18. toll-like receptor 9 signaling pathway Source: Reactome
    19. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_9020. Toll Like Receptor 7/8 (TLR7/8) Cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Toll-like receptor 8
    Alternative name(s):
    CD_antigen: CD288
    Gene namesi
    Name:TLR8
    ORF Names:UNQ249/PRO286
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:15632. TLR8.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endolysosome membrane Source: Reactome
    2. endoplasmic reticulum membrane Source: Reactome
    3. endosome membrane Source: Reactome
    4. Golgi membrane Source: Reactome
    5. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi348 – 3481Y → A: Abolishes activation of NF-kappa-B. 1 Publication
    Mutagenesisi378 – 3781V → A: Increases activation of NF-kappa-B. 1 Publication
    Mutagenesisi405 – 4051F → A: Abolishes activation of NF-kappa-B. 1 Publication
    Mutagenesisi520 – 5201V → A: Strongly decreases activation of NF-kappa-B.
    Mutagenesisi543 – 5431D → A: Abolishes activation of NF-kappa-B. 1 Publication
    Mutagenesisi574 – 5741T → A: Strongly decreases activation of NF-kappa-B.

    Organism-specific databases

    PharmGKBiPA38009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 10411015Toll-like receptor 8PRO_0000034735Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi36 ↔ 491 Publication
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi80 – 801N-linked (GlcNAc...)1 Publication
    Glycosylationi88 – 881N-linked (GlcNAc...)1 Publication
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi181 ↔ 1871 Publication
    Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi257 ↔ 2701 Publication
    Disulfide bondi260 ↔ 2671 Publication
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)1 Publication
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)1 Publication
    Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi479 ↔ 5091 Publication
    Glycosylationi511 – 5111N-linked (GlcNAc...)1 Publication
    Glycosylationi546 – 5461N-linked (GlcNAc...)1 Publication
    Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi590 – 5901N-linked (GlcNAc...)1 Publication
    Glycosylationi640 – 6401N-linked (GlcNAc...)1 Publication
    Glycosylationi680 – 6801N-linked (GlcNAc...)1 Publication
    Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi776 ↔ 8031 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9NR97.
    PRIDEiQ9NR97.

    PTM databases

    PhosphoSiteiQ9NR97.

    Expressioni

    Tissue specificityi

    Detected in brain, heart, lung, liver, placenta, in monocytes, and at lower levels in CD11c+ immature dendritic cells.

    Gene expression databases

    ArrayExpressiQ9NR97.
    BgeeiQ9NR97.
    CleanExiHS_TLR8.
    GenevestigatoriQ9NR97.

    Organism-specific databases

    HPAiHPA001608.

    Interactioni

    Subunit structurei

    Interacts with MYD88 via their respective TIR domains. Interacts with UNC93B1 By similarity. Homodimer. Interacts with BTK.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119462. 2 interactions.
    STRINGi9606.ENSP00000218032.

    Structurei

    Secondary structure

    1
    1041
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 393
    Beta strandi46 – 483
    Beta strandi66 – 694
    Turni80 – 856
    Beta strandi91 – 933
    Beta strandi96 – 983
    Turni118 – 1236
    Beta strandi129 – 1313
    Beta strandi149 – 1524
    Helixi163 – 1664
    Beta strandi174 – 1763
    Beta strandi179 – 1813
    Turni194 – 1996
    Beta strandi205 – 2073
    Beta strandi225 – 2284
    Turni241 – 2444
    Beta strandi250 – 2523
    Helixi271 – 2733
    Turni280 – 2856
    Beta strandi291 – 2933
    Helixi304 – 3074
    Beta strandi315 – 3173
    Beta strandi320 – 3223
    Helixi324 – 3296
    Helixi331 – 3355
    Beta strandi341 – 3433
    Helixi361 – 3655
    Beta strandi371 – 3733
    Beta strandi380 – 3823
    Helixi384 – 3907
    Beta strandi398 – 4003
    Helixi411 – 4166
    Beta strandi417 – 4193
    Beta strandi421 – 4244
    Beta strandi467 – 4693
    Helixi477 – 4804
    Beta strandi485 – 4873
    Turni498 – 5036
    Beta strandi508 – 5114
    Turni525 – 5284
    Beta strandi533 – 5364
    Turni547 – 5526
    Beta strandi558 – 5603
    Helixi565 – 5684
    Turni571 – 5733
    Helixi578 – 5825
    Beta strandi588 – 5903
    Beta strandi607 – 6093
    Beta strandi612 – 6143
    Helixi620 – 6234
    Turni630 – 6378
    Beta strandi638 – 6403
    Beta strandi643 – 6453
    Helixi656 – 6605
    Beta strandi667 – 6704
    Helixi681 – 6866
    Beta strandi692 – 6943
    Helixi707 – 7093
    Beta strandi716 – 7183
    Turni729 – 7335
    Beta strandi740 – 7423
    Helixi753 – 7564
    Beta strandi758 – 7603
    Beta strandi765 – 7684
    Helixi778 – 7803
    Helixi781 – 7899
    Beta strandi792 – 7943
    Helixi798 – 8003
    Beta strandi801 – 8066
    Turni807 – 8115
    Helixi814 – 8163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3W3GX-ray2.30A/B27-827[»]
    3W3JX-ray2.00A/B27-827[»]
    3W3KX-ray2.30A/B27-827[»]
    3W3LX-ray2.33A/B/C/D27-827[»]
    3W3MX-ray2.70A27-827[»]
    3W3NX-ray2.10A/B27-827[»]
    3WN4X-ray1.81A27-827[»]
    ProteinModelPortaliQ9NR97.
    SMRiQ9NR97. Positions 31-818, 876-1022.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 827801ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini849 – 1041193CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei828 – 84821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati126 – 14722LRR 11 PublicationAdd
    BLAST
    Repeati148 – 16821LRR 21 PublicationAdd
    BLAST
    Repeati171 – 19323LRR 31 PublicationAdd
    BLAST
    Repeati202 – 22322LRR 41 PublicationAdd
    BLAST
    Repeati224 – 24421LRR 51 PublicationAdd
    BLAST
    Repeati247 – 26822LRR 61 PublicationAdd
    BLAST
    Repeati288 – 30922LRR 71 PublicationAdd
    BLAST
    Repeati312 – 33423LRR 81 PublicationAdd
    BLAST
    Repeati338 – 36023LRR 91 PublicationAdd
    BLAST
    Repeati368 – 38922LRR 101 PublicationAdd
    BLAST
    Repeati395 – 41622LRR 111 PublicationAdd
    BLAST
    Repeati419 – 44022LRR 121 PublicationAdd
    BLAST
    Repeati482 – 50322LRR 131 PublicationAdd
    BLAST
    Repeati506 – 52722LRR 141 PublicationAdd
    BLAST
    Repeati531 – 55121LRR 151 PublicationAdd
    BLAST
    Repeati555 – 57723LRR 161 PublicationAdd
    BLAST
    Repeati585 – 60622LRR 171 PublicationAdd
    BLAST
    Repeati609 – 63022LRR 181 PublicationAdd
    BLAST
    Repeati640 – 66122LRR 191 PublicationAdd
    BLAST
    Repeati665 – 68521LRR 201 PublicationAdd
    BLAST
    Repeati689 – 71022LRR 211 PublicationAdd
    BLAST
    Repeati713 – 73422LRR 221 PublicationAdd
    BLAST
    Repeati737 – 75822LRR 231 PublicationAdd
    BLAST
    Domaini772 – 82453LRRCTAdd
    BLAST
    Domaini878 – 1025148TIRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 23 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

    eggNOGiCOG4886.
    HOGENOMiHOG000230468.
    HOVERGENiHBG018601.
    KOiK10170.
    OMAiTHHLEFI.
    OrthoDBiEOG7VB2DM.
    PhylomeDBiQ9NR97.
    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.
    IPR027175. TLR8.
    [Graphical view]
    PANTHERiPTHR24365:SF227. PTHR24365:SF227. 1 hit.
    PfamiPF13855. LRR_8. 5 hits.
    PF01582. TIR. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS51450. LRR. 20 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR97-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MENMFLQSSM LTCIFLLISG SCELCAEENF SRSYPCDEKK QNDSVIAECS     50
    NRRLQEVPQT VGKYVTELDL SDNFITHITN ESFQGLQNLT KINLNHNPNV 100
    QHQNGNPGIQ SNGLNITDGA FLNLKNLREL LLEDNQLPQI PSGLPESLTE 150
    LSLIQNNIYN ITKEGISRLI NLKNLYLAWN CYFNKVCEKT NIEDGVFETL 200
    TNLELLSLSF NSLSHVPPKL PSSLRKLFLS NTQIKYISEE DFKGLINLTL 250
    LDLSGNCPRC FNAPFPCVPC DGGASINIDR FAFQNLTQLR YLNLSSTSLR 300
    KINAAWFKNM PHLKVLDLEF NYLVGEIASG AFLTMLPRLE ILDLSFNYIK 350
    GSYPQHINIS RNFSKLLSLR ALHLRGYVFQ ELREDDFQPL MQLPNLSTIN 400
    LGINFIKQID FKLFQNFSNL EIIYLSENRI SPLVKDTRQS YANSSSFQRH 450
    IRKRRSTDFE FDPHSNFYHF TRPLIKPQCA AYGKALDLSL NSIFFIGPNQ 500
    FENLPDIACL NLSANSNAQV LSGTEFSAIP HVKYLDLTNN RLDFDNASAL 550
    TELSDLEVLD LSYNSHYFRI AGVTHHLEFI QNFTNLKVLN LSHNNIYTLT 600
    DKYNLESKSL VELVFSGNRL DILWNDDDNR YISIFKGLKN LTRLDLSLNR 650
    LKHIPNEAFL NLPASLTELH INDNMLKFFN WTLLQQFPRL ELLDLRGNKL 700
    LFLTDSLSDF TSSLRTLLLS HNRISHLPSG FLSEVSSLKH LDLSSNLLKT 750
    INKSALETKT TTKLSMLELH GNPFECTCDI GDFRRWMDEH LNVKIPRLVD 800
    VICASPGDQR GKSIVSLELT TCVSDVTAVI LFFFTFFITT MVMLAALAHH 850
    LFYWDVWFIY NVCLAKVKGY RSLSTSQTFY DAYISYDTKD ASVTDWVINE 900
    LRYHLEESRD KNVLLCLEER DWDPGLAIID NLMQSINQSK KTVFVLTKKY 950
    AKSWNFKTAF YLALQRLMDE NMDVIIFILL EPVLQHSQYL RLRQRICKSS 1000
    ILQWPDNPKA EGLFWQTLRN VVLTENDSRY NNMYVDSIKQ Y 1041
    Length:1,041
    Mass (Da):119,828
    Last modified:October 1, 2000 - v1
    Checksum:i39A38B60629291C8
    GO
    Isoform 2 (identifier: Q9NR97-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKESSLQNSSCSLGKETKK

    Show »
    Length:1,059
    Mass (Da):121,764
    Checksum:i27803D560E09D7BF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti217 – 2171P → S in AAF64061. (PubMed:11022119)Curated
    Sequence conflicti328 – 3281A → V in AAQ88663. (PubMed:12975309)Curated
    Sequence conflicti366 – 3661L → P in AAF64061. (PubMed:11022119)Curated
    Sequence conflicti410 – 4101D → N in AAZ95439. (PubMed:19924287)Curated
    Sequence conflicti867 – 8671V → I in AAF64061. (PubMed:11022119)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101M → V.
    Corresponds to variant rs5744077 [ dbSNP | Ensembl ].
    VAR_024667
    Natural varianti715 – 7151R → Q.
    Corresponds to variant rs5744082 [ dbSNP | Ensembl ].
    VAR_052363

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MKESSLQNSSCSLGKETKK in isoform 2. 1 PublicationVSP_053412

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF246971 mRNA. Translation: AAF64061.1.
    AF245703 mRNA. Translation: AAF78036.1.
    AB445666 mRNA. Translation: BAG55063.1.
    DQ023132 Genomic DNA. Translation: AAZ95433.1.
    DQ023133 Genomic DNA. Translation: AAZ95434.1.
    DQ023134 Genomic DNA. Translation: AAZ95435.1.
    DQ023135 Genomic DNA. Translation: AAZ95436.1.
    DQ023136 Genomic DNA. Translation: AAZ95437.1.
    DQ023137 Genomic DNA. Translation: AAZ95438.1.
    DQ023138 Genomic DNA. Translation: AAZ95439.1.
    DQ023139 Genomic DNA. Translation: AAZ95440.1.
    DQ023140 Genomic DNA. Translation: AAZ95441.1.
    CH471074 Genomic DNA. Translation: EAW98808.1.
    AY358296 mRNA. Translation: AAQ88663.1.
    AC005859 Genomic DNA. No translation available.
    AC139705 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98809.1.
    BC101076 mRNA. Translation: AAI01077.1.
    BC101077 mRNA. Translation: AAI01078.1.
    CCDSiCCDS14152.1. [Q9NR97-1]
    RefSeqiNP_619542.1. NM_138636.5. [Q9NR97-1]
    XP_005274600.1. XM_005274543.2. [Q9NR97-2]
    UniGeneiHs.660543.

    Genome annotation databases

    EnsembliENST00000218032; ENSP00000218032; ENSG00000101916. [Q9NR97-1]
    ENST00000311912; ENSP00000312082; ENSG00000101916. [Q9NR97-2]
    GeneIDi51311.
    KEGGihsa:51311.
    UCSCiuc004cvd.3. human.
    uc004cve.3. human. [Q9NR97-1]

    Polymorphism databases

    DMDMi20140873.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF246971 mRNA. Translation: AAF64061.1 .
    AF245703 mRNA. Translation: AAF78036.1 .
    AB445666 mRNA. Translation: BAG55063.1 .
    DQ023132 Genomic DNA. Translation: AAZ95433.1 .
    DQ023133 Genomic DNA. Translation: AAZ95434.1 .
    DQ023134 Genomic DNA. Translation: AAZ95435.1 .
    DQ023135 Genomic DNA. Translation: AAZ95436.1 .
    DQ023136 Genomic DNA. Translation: AAZ95437.1 .
    DQ023137 Genomic DNA. Translation: AAZ95438.1 .
    DQ023138 Genomic DNA. Translation: AAZ95439.1 .
    DQ023139 Genomic DNA. Translation: AAZ95440.1 .
    DQ023140 Genomic DNA. Translation: AAZ95441.1 .
    CH471074 Genomic DNA. Translation: EAW98808.1 .
    AY358296 mRNA. Translation: AAQ88663.1 .
    AC005859 Genomic DNA. No translation available.
    AC139705 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98809.1 .
    BC101076 mRNA. Translation: AAI01077.1 .
    BC101077 mRNA. Translation: AAI01078.1 .
    CCDSi CCDS14152.1. [Q9NR97-1 ]
    RefSeqi NP_619542.1. NM_138636.5. [Q9NR97-1 ]
    XP_005274600.1. XM_005274543.2. [Q9NR97-2 ]
    UniGenei Hs.660543.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3W3G X-ray 2.30 A/B 27-827 [» ]
    3W3J X-ray 2.00 A/B 27-827 [» ]
    3W3K X-ray 2.30 A/B 27-827 [» ]
    3W3L X-ray 2.33 A/B/C/D 27-827 [» ]
    3W3M X-ray 2.70 A 27-827 [» ]
    3W3N X-ray 2.10 A/B 27-827 [» ]
    3WN4 X-ray 1.81 A 27-827 [» ]
    ProteinModelPortali Q9NR97.
    SMRi Q9NR97. Positions 31-818, 876-1022.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119462. 2 interactions.
    STRINGi 9606.ENSP00000218032.

    Chemistry

    BindingDBi Q9NR97.
    ChEMBLi CHEMBL5805.
    GuidetoPHARMACOLOGYi 1758.

    PTM databases

    PhosphoSitei Q9NR97.

    Polymorphism databases

    DMDMi 20140873.

    Proteomic databases

    PaxDbi Q9NR97.
    PRIDEi Q9NR97.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218032 ; ENSP00000218032 ; ENSG00000101916 . [Q9NR97-1 ]
    ENST00000311912 ; ENSP00000312082 ; ENSG00000101916 . [Q9NR97-2 ]
    GeneIDi 51311.
    KEGGi hsa:51311.
    UCSCi uc004cvd.3. human.
    uc004cve.3. human. [Q9NR97-1 ]

    Organism-specific databases

    CTDi 51311.
    GeneCardsi GC0XP012924.
    H-InvDB HIX0176772.
    HGNCi HGNC:15632. TLR8.
    HPAi HPA001608.
    MIMi 300366. gene.
    neXtProti NX_Q9NR97.
    PharmGKBi PA38009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000230468.
    HOVERGENi HBG018601.
    KOi K10170.
    OMAi THHLEFI.
    OrthoDBi EOG7VB2DM.
    PhylomeDBi Q9NR97.
    TreeFami TF351113.

    Enzyme and pathway databases

    Reactomei REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_9020. Toll Like Receptor 7/8 (TLR7/8) Cascade.

    Miscellaneous databases

    GeneWikii TLR8.
    GenomeRNAii 51311.
    NextBioi 35489044.
    PROi Q9NR97.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR97.
    Bgeei Q9NR97.
    CleanExi HS_TLR8.
    Genevestigatori Q9NR97.

    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.
    IPR027175. TLR8.
    [Graphical view ]
    PANTHERi PTHR24365:SF227. PTHR24365:SF227. 1 hit.
    Pfami PF13855. LRR_8. 5 hits.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS51450. LRR. 20 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Three novel mammalian Toll-like receptors: gene structure, expression, and evolution."
      Du X., Poltorak A., Wei Y., Beutler B.
      Eur. Cytokine Netw. 11:362-371(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Placenta.
    2. "Cloning and characterization of a sub-family of human Toll-like receptors: hTLR7, hTLR8 and hTLR9."
      Chuang T.-H., Ulevitch R.J.
      Eur. Cytokine Netw. 11:372-378(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "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] (ISOFORM 1).
    4. "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 [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
    9. "Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine kinase."
      Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A.
      J. Biol. Chem. 282:36953-36960(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BTK.
    10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-88.
      Tissue: Liver.
    11. "Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands."
      Tanji H., Ohto U., Shibata T., Miyake K., Shimizu T.
      Science 339:1426-1429(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-827 IN COMPLEXES WITH RESIQUIMOD AND OTHER SYNTHETIC AGONISTS, FUNCTION, SUBUNIT, LEUCINE-RICH REPEATS, MUTAGENESIS OF TYR-348; VAL-378; PHE-405 AND ASP-543, GLYCOSYLATION AT ASN-293; ASN-395; ASN-511; VAL-520; ASN-546; THR-574; ASN-590; ASN-640 AND ASN-680, DISULFIDE BONDS.

    Entry informationi

    Entry nameiTLR8_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR97
    Secondary accession number(s): B3Y654
    , D1CS70, D1CS76, Q495P4, Q6UXL6, Q9NYG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 131 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 X
      Human chromosome X: 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