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Q9NR97 (TLR8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toll-like receptor 8
Alternative name(s):
CD_antigen=CD288
Gene names
Name:TLR8
ORF Names:UNQ249/PRO286
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1041 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11

Subunit structure

Interacts with MYD88 via their respective TIR domains. Interacts with UNC93B1 By similarity. Homodimer. Interacts with BTK. Ref.9 Ref.11

Subcellular location

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

Tissue specificity

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

Sequence similarities

Belongs to the Toll-like receptor family.

Contains 23 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 TIR domain.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 12032557. Source: UniProtKB

MyD88-dependent toll-like receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype PubMed 16188996. Source: UniProtKB

immunoglobulin mediated immune response

Traceable author statement PubMed 16123302. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Non-traceable author statement PubMed 12032557. Source: UniProtKB

microglial cell activation involved in immune response

Inferred from electronic annotation. Source: Ensembl

pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of innate immune response

Inferred from direct assay PubMed 16123302. Source: UniProtKB

positive regulation of interferon-alpha biosynthetic process

Inferred from direct assay PubMed 16286015. Source: UniProtKB

positive regulation of interferon-beta biosynthetic process

Inferred from direct assay PubMed 16286015. Source: UniProtKB

positive regulation of interferon-gamma biosynthetic process

Inferred from direct assay PubMed 16286015. Source: UniProtKB

positive regulation of interleukin-8 biosynthetic process

Inferred from mutant phenotype PubMed 16188996. Source: UniProtKB

regulation of cytokine secretion

Inferred from electronic annotation. Source: InterPro

response to virus

Inferred from direct assay PubMed 12032557. Source: UniProtKB

toll-like receptor 8 signaling pathway

Inferred from electronic annotation. Source: InterPro

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

endolysosome membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred by curator PubMed 12032557. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 16123302. Source: UniProtKB

RNA binding

Traceable author statement PubMed 16123302. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 16111635. Source: UniProtKB

drug binding

Inferred from electronic annotation. Source: Ensembl

receptor activity

Non-traceable author statement PubMed 12032557. Source: UniProtKB

single-stranded RNA binding

Inferred from direct assay PubMed 14976262. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NR97-1)

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.
Isoform 2 (identifier: Q9NR97-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 10411015Toll-like receptor 8
PRO_0000034735

Regions

Topological domain27 – 827801Extracellular Potential
Transmembrane828 – 84821Helical; Potential
Topological domain849 – 1041193Cytoplasmic Potential
Repeat126 – 14722LRR 1
Repeat148 – 16821LRR 2
Repeat171 – 19323LRR 3
Repeat202 – 22322LRR 4
Repeat224 – 24421LRR 5
Repeat247 – 26822LRR 6
Repeat288 – 30922LRR 7
Repeat312 – 33423LRR 8
Repeat338 – 36023LRR 9
Repeat368 – 38922LRR 10
Repeat395 – 41622LRR 11
Repeat419 – 44022LRR 12
Repeat482 – 50322LRR 13
Repeat506 – 52722LRR 14
Repeat531 – 55121LRR 15
Repeat555 – 57723LRR 16
Repeat585 – 60622LRR 17
Repeat609 – 63022LRR 18
Repeat640 – 66122LRR 19
Repeat665 – 68521LRR 20
Repeat689 – 71022LRR 21
Repeat713 – 73422LRR 22
Repeat737 – 75822LRR 23
Domain772 – 82453LRRCT
Domain878 – 1025148TIR

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Ref.10
Glycosylation881N-linked (GlcNAc...) Ref.10
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Ref.11
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Ref.11
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Ref.11
Glycosylation5461N-linked (GlcNAc...) Ref.11
Glycosylation5821N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Ref.11
Glycosylation6401N-linked (GlcNAc...) Ref.11
Glycosylation6801N-linked (GlcNAc...) Ref.11
Glycosylation7521N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 49 Ref.11
Disulfide bond181 ↔ 187 Ref.11
Disulfide bond257 ↔ 270 Ref.11
Disulfide bond260 ↔ 267 Ref.11
Disulfide bond479 ↔ 509 Ref.11
Disulfide bond776 ↔ 803 Ref.11

Natural variations

Alternative sequence11M → MKESSLQNSSCSLGKETKK in isoform 2.
VSP_053412
Natural variant101M → V.
Corresponds to variant rs5744077 [ dbSNP | Ensembl ].
VAR_024667
Natural variant7151R → Q.
Corresponds to variant rs5744082 [ dbSNP | Ensembl ].
VAR_052363

Experimental info

Mutagenesis3481Y → A: Abolishes activation of NF-kappa-B. Ref.11
Mutagenesis3781V → A: Increases activation of NF-kappa-B. Ref.11
Mutagenesis4051F → A: Abolishes activation of NF-kappa-B. Ref.11
Mutagenesis5201V → A: Strongly decreases activation of NF-kappa-B.
Mutagenesis5431D → A: Abolishes activation of NF-kappa-B. Ref.11
Mutagenesis5741T → A: Strongly decreases activation of NF-kappa-B.
Sequence conflict2171P → S in AAF64061. Ref.1
Sequence conflict3281A → V in AAQ88663. Ref.5
Sequence conflict3661L → P in AAF64061. Ref.1
Sequence conflict4101D → N in AAZ95439. Ref.4
Sequence conflict8671V → I in AAF64061. Ref.1

Secondary structure

......................................................................................................................................... 1041
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 39A38B60629291C8

FASTA1,041119,828
        10         20         30         40         50         60 
MENMFLQSSM LTCIFLLISG SCELCAEENF SRSYPCDEKK QNDSVIAECS NRRLQEVPQT 

        70         80         90        100        110        120 
VGKYVTELDL SDNFITHITN ESFQGLQNLT KINLNHNPNV QHQNGNPGIQ SNGLNITDGA 

       130        140        150        160        170        180 
FLNLKNLREL LLEDNQLPQI PSGLPESLTE LSLIQNNIYN ITKEGISRLI NLKNLYLAWN 

       190        200        210        220        230        240 
CYFNKVCEKT NIEDGVFETL TNLELLSLSF NSLSHVPPKL PSSLRKLFLS NTQIKYISEE 

       250        260        270        280        290        300 
DFKGLINLTL LDLSGNCPRC FNAPFPCVPC DGGASINIDR FAFQNLTQLR YLNLSSTSLR 

       310        320        330        340        350        360 
KINAAWFKNM PHLKVLDLEF NYLVGEIASG AFLTMLPRLE ILDLSFNYIK GSYPQHINIS 

       370        380        390        400        410        420 
RNFSKLLSLR ALHLRGYVFQ ELREDDFQPL MQLPNLSTIN LGINFIKQID FKLFQNFSNL 

       430        440        450        460        470        480 
EIIYLSENRI SPLVKDTRQS YANSSSFQRH IRKRRSTDFE FDPHSNFYHF TRPLIKPQCA 

       490        500        510        520        530        540 
AYGKALDLSL NSIFFIGPNQ FENLPDIACL NLSANSNAQV LSGTEFSAIP HVKYLDLTNN 

       550        560        570        580        590        600 
RLDFDNASAL TELSDLEVLD LSYNSHYFRI AGVTHHLEFI QNFTNLKVLN LSHNNIYTLT 

       610        620        630        640        650        660 
DKYNLESKSL VELVFSGNRL DILWNDDDNR YISIFKGLKN LTRLDLSLNR LKHIPNEAFL 

       670        680        690        700        710        720 
NLPASLTELH INDNMLKFFN WTLLQQFPRL ELLDLRGNKL LFLTDSLSDF TSSLRTLLLS 

       730        740        750        760        770        780 
HNRISHLPSG FLSEVSSLKH LDLSSNLLKT INKSALETKT TTKLSMLELH GNPFECTCDI 

       790        800        810        820        830        840 
GDFRRWMDEH LNVKIPRLVD VICASPGDQR GKSIVSLELT TCVSDVTAVI LFFFTFFITT 

       850        860        870        880        890        900 
MVMLAALAHH LFYWDVWFIY NVCLAKVKGY RSLSTSQTFY DAYISYDTKD ASVTDWVINE 

       910        920        930        940        950        960 
LRYHLEESRD KNVLLCLEER DWDPGLAIID NLMQSINQSK KTVFVLTKKY AKSWNFKTAF 

       970        980        990       1000       1010       1020 
YLALQRLMDE NMDVIIFILL EPVLQHSQYL RLRQRICKSS ILQWPDNPKA EGLFWQTLRN 

      1030       1040 
VVLTENDSRY NNMYVDSIKQ Y 

« Hide

Isoform 2 [UniParc].

Checksum: 27803D560E09D7BF
Show »

FASTA1,059121,764

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_619542.1. NM_138636.5.
XP_005274600.1. XM_005274543.2.
UniGeneHs.660543.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9NR97.
SMRQ9NR97. Positions 31-818, 876-1022.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119462. 2 interactions.
STRING9606.ENSP00000218032.

Chemistry

BindingDBQ9NR97.
ChEMBLCHEMBL5805.
GuidetoPHARMACOLOGY1758.

PTM databases

PhosphoSiteQ9NR97.

Polymorphism databases

DMDM20140873.

Proteomic databases

PaxDbQ9NR97.
PRIDEQ9NR97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218032; ENSP00000218032; ENSG00000101916. [Q9NR97-1]
ENST00000311912; ENSP00000312082; ENSG00000101916. [Q9NR97-2]
GeneID51311.
KEGGhsa:51311.
UCSCuc004cve.3. human. [Q9NR97-1]

Organism-specific databases

CTD51311.
GeneCardsGC0XP012924.
H-InvDBHIX0176772.
HGNCHGNC:15632. TLR8.
HPAHPA001608.
MIM300366. gene.
neXtProtNX_Q9NR97.
PharmGKBPA38009.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000230468.
HOVERGENHBG018601.
KOK10170.
OrthoDBEOG7VB2DM.
PhylomeDBQ9NR97.
TreeFamTF351113.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9NR97.
BgeeQ9NR97.
CleanExHS_TLR8.
GenevestigatorQ9NR97.

Family and domain databases

Gene3D3.40.50.10140. 1 hit.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027175. TLR8.
[Graphical view]
PANTHERPTHR24365:SF173. PTHR24365:SF173. 1 hit.
PfamPF01582. TIR. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS51450. LRR. 20 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTLR8.
GenomeRNAi51311.
NextBio35489044.
PROQ9NR97.
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Entry information

Entry nameTLR8_HUMAN
AccessionPrimary (citable) accession number: Q9NR97
Secondary accession number(s): B3Y654 expand/collapse secondary AC list , D1CS70, D1CS76, Q495P4, Q6UXL6, Q9NYG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

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