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Q9NR97

- TLR8_HUMAN

UniProt

Q9NR97 - TLR8_HUMAN

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Protein

Toll-like receptor 8

Gene

TLR8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9NR97.
CleanExiHS_TLR8.
ExpressionAtlasiQ9NR97. baseline and differential.
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.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ9NR97.
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

        10         20         30         40         50
MENMFLQSSM LTCIFLLISG SCELCAEENF SRSYPCDEKK QNDSVIAECS
60 70 80 90 100
NRRLQEVPQT VGKYVTELDL SDNFITHITN ESFQGLQNLT KINLNHNPNV
110 120 130 140 150
QHQNGNPGIQ SNGLNITDGA FLNLKNLREL LLEDNQLPQI PSGLPESLTE
160 170 180 190 200
LSLIQNNIYN ITKEGISRLI NLKNLYLAWN CYFNKVCEKT NIEDGVFETL
210 220 230 240 250
TNLELLSLSF NSLSHVPPKL PSSLRKLFLS NTQIKYISEE DFKGLINLTL
260 270 280 290 300
LDLSGNCPRC FNAPFPCVPC DGGASINIDR FAFQNLTQLR YLNLSSTSLR
310 320 330 340 350
KINAAWFKNM PHLKVLDLEF NYLVGEIASG AFLTMLPRLE ILDLSFNYIK
360 370 380 390 400
GSYPQHINIS RNFSKLLSLR ALHLRGYVFQ ELREDDFQPL MQLPNLSTIN
410 420 430 440 450
LGINFIKQID FKLFQNFSNL EIIYLSENRI SPLVKDTRQS YANSSSFQRH
460 470 480 490 500
IRKRRSTDFE FDPHSNFYHF TRPLIKPQCA AYGKALDLSL NSIFFIGPNQ
510 520 530 540 550
FENLPDIACL NLSANSNAQV LSGTEFSAIP HVKYLDLTNN RLDFDNASAL
560 570 580 590 600
TELSDLEVLD LSYNSHYFRI AGVTHHLEFI QNFTNLKVLN LSHNNIYTLT
610 620 630 640 650
DKYNLESKSL VELVFSGNRL DILWNDDDNR YISIFKGLKN LTRLDLSLNR
660 670 680 690 700
LKHIPNEAFL NLPASLTELH INDNMLKFFN WTLLQQFPRL ELLDLRGNKL
710 720 730 740 750
LFLTDSLSDF TSSLRTLLLS HNRISHLPSG FLSEVSSLKH LDLSSNLLKT
760 770 780 790 800
INKSALETKT TTKLSMLELH GNPFECTCDI GDFRRWMDEH LNVKIPRLVD
810 820 830 840 850
VICASPGDQR GKSIVSLELT TCVSDVTAVI LFFFTFFITT MVMLAALAHH
860 870 880 890 900
LFYWDVWFIY NVCLAKVKGY RSLSTSQTFY DAYISYDTKD ASVTDWVINE
910 920 930 940 950
LRYHLEESRD KNVLLCLEER DWDPGLAIID NLMQSINQSK KTVFVLTKKY
960 970 980 990 1000
AKSWNFKTAF YLALQRLMDE NMDVIIFILL EPVLQHSQYL RLRQRICKSS
1010 1020 1030 1040
ILQWPDNPKA EGLFWQTLRN VVLTENDSRY NNMYVDSIKQ Y
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]
CCDS14153.1. [Q9NR97-2]
RefSeqiNP_057694.2. NM_016610.3. [Q9NR97-2]
NP_619542.1. NM_138636.5. [Q9NR97-1]
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 ]
CCDS14153.1. [Q9NR97-2 ]
RefSeqi NP_057694.2. NM_016610.3. [Q9NR97-2 ]
NP_619542.1. NM_138636.5. [Q9NR97-1 ]
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 CHEMBL3137288.
DrugBanki DB00724. Imiquimod.
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.
GeneTreei ENSGT00760000119006.
HOGENOMi HOG000230468.
HOVERGENi HBG018601.
InParanoidi Q9NR97.
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

Bgeei Q9NR97.
CleanExi HS_TLR8.
ExpressionAtlasi Q9NR97. baseline and differential.
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

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  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 29, 2014
This is version 132 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

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