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Protein

Toll-like receptor 3

Gene

TLR3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response.9 Publications

GO - Molecular functioni

  • double-stranded RNA binding Source: UniProtKB
  • receptor activity Source: ProtInc
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164342-MONOMER.
ReactomeiR-HSA-140534. Ligand-dependent caspase activation.
R-HSA-166166. MyD88-independent TLR3/TLR4 cascade.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-168164. Toll Like Receptor 3 (TLR3) Cascade.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-2562578. TRIF-mediated programmed cell death.
R-HSA-5602410. TLR3 deficiency - HSE.
R-HSA-5602415. UNC93B1 deficiency - HSE.
R-HSA-5602566. TICAM1 deficiency - HSE.
R-HSA-5602571. TRAF3 deficiency - HSE.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
SignaLinkiO15455.
SIGNORiO15455.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 3
Alternative name(s):
CD_antigen: CD283
Gene namesi
Name:TLR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11849. TLR3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 704LumenalSequence analysisAdd BLAST681
Transmembranei705 – 725HelicalSequence analysisAdd BLAST21
Topological domaini726 – 904CytoplasmicSequence analysisAdd BLAST179

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • early endosome Source: UniProtKB-SubCell
  • endolysosome membrane Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • endosome membrane Source: Reactome
  • Golgi membrane Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • intracellular Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Herpes simplex encephalitis 2 (HSE2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry. TLR3 mutations predispose otherwise healthy individuals to isolated herpes simplex encephalitis through a mechanism that involves impaired IFNs production and reduced immune defense against viral infection in the central nervous system.
Disease descriptionA rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.
See also OMIM:613002
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054887554P → S in HSE2; causes TLR3 deficiency and predisposition to herpes simplex encephalitis. 1 PublicationCorresponds to variant rs121434431dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95C → A: Reduced response to ds-RNA. 1 Publication1
Mutagenesisi122C → A: Reduced response to ds-RNA. 1 Publication1
Mutagenesisi196N → G: Reduced expression levels; when associated with R-247. 1 Publication1
Mutagenesisi247N → R: Reduced response to ds-RNA. Reduced expression levels; when associated with G-196. 1 Publication1
Mutagenesisi539H → A: No effect. 1 Publication1
Mutagenesisi539H → E: Loss of RNA binding. Constitutive activation of NF-kappa-B. 1 Publication1
Mutagenesisi541N → A: Loss of RNA binding. Abolishes activation of NF-kappa-B. 1 Publication1
Mutagenesisi759Y → F: Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA. Loss of interaction with WDFY1. 2 Publications1
Mutagenesisi858Y → F: Loss of interaction with WDFY1. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7098.
MalaCardsiTLR3.
MIMi613002. phenotype.
OpenTargetsiENSG00000164342.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA36551.

Chemistry databases

ChEMBLiCHEMBL1075113.

Polymorphism and mutation databases

BioMutaiTLR3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000003471524 – 904Toll-like receptor 3Add BLAST881

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 37
Glycosylationi52N-linked (GlcNAc...)3 Publications1
Glycosylationi57N-linked (GlcNAc...)1 Publication1
Glycosylationi70N-linked (GlcNAc...)2 Publications1
Disulfide bondi95 ↔ 122
Glycosylationi124N-linked (GlcNAc...)2 Publications1
Glycosylationi196N-linked (GlcNAc...)1 Publication1
Glycosylationi247N-linked (GlcNAc...)1 Publication1
Glycosylationi252N-linked (GlcNAc...)3 Publications1
Glycosylationi265N-linked (GlcNAc...)2 Publications1
Glycosylationi275N-linked (GlcNAc...)3 Publications1
Glycosylationi291N-linked (GlcNAc...)3 Publications1
Glycosylationi398N-linked (GlcNAc...)3 Publications1
Glycosylationi413N-linked (GlcNAc...)3 Publications1
Glycosylationi507N-linked (GlcNAc...)3 Publications1
Glycosylationi636N-linked (GlcNAc...)1 Publication1
Disulfide bondi649 ↔ 677
Disulfide bondi651 ↔ 696
Glycosylationi662N-linked (GlcNAc...)Sequence analysis1
Modified residuei759Phosphotyrosine1 Publication1
Modified residuei858Phosphotyrosine1 Publication1

Post-translational modificationi

Heavily N-glycosylated, except on that part of the surface of the ectodomain that is involved in ligand binding.4 Publications
TLR3 signaling requires a proteolytic cleavage mediated by cathepsins CTSB and CTSH, the cleavage occurs between amino acids 252 and 346. The cleaved form of TLR3 is the predominant form found in endosomes.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO15455.
PaxDbiO15455.
PeptideAtlasiO15455.
PRIDEiO15455.

PTM databases

iPTMnetiO15455.
PhosphoSitePlusiO15455.

Expressioni

Tissue specificityi

Expressed at high level in placenta and pancreas. Also detected in CD11c+ immature dendritic cells. Only expressed in dendritic cells and not in other leukocytes, including monocyte precursors. TLR3 is the TLR that is expressed most strongly in the brain, especially in astrocytes, glia, and neurons.1 Publication

Gene expression databases

BgeeiENSG00000164342.
CleanExiHS_TLR3.
ExpressionAtlasiO15455. baseline and differential.
GenevisibleiO15455. HS.

Organism-specific databases

HPAiCAB025658.

Interactioni

Subunit structurei

Monomer and homodimer; dimerization is triggered by ligand-binding, the signaling unit is composed of one ds-RNA of around 40 bp and two TLR3 molecules, and lateral clustering of signaling units along the length of the ds-RNA ligand is required for TLR3 signal transduction. Interacts (via transmembrane domain) with UNC93B1; the interaction is required for transport from the ER to the endosomes. Interacts with SRC; upon binding of double-stranded RNA. Interacts with TICAM1 (via the TIR domain) in response to poly(I:C) and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). The tyrosine-phosphorylated form (via TIR domain) interacts with WDFY1 (via WD repeat 2) in response to poly(I:C) (PubMed:25736436).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6116630,EBI-6116630
PIK3R1P279862EBI-6116630,EBI-79464

Protein-protein interaction databases

BioGridi112953. 19 interactors.
DIPiDIP-29660N.
IntActiO15455. 7 interactors.
MINTiMINT-2840066.
STRINGi9606.ENSP00000296795.

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 36Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi54 – 57Combined sources4
Helixi68 – 74Combined sources7
Beta strandi78 – 81Combined sources4
Helixi94 – 97Combined sources4
Beta strandi103 – 105Combined sources3
Turni118 – 121Combined sources4
Beta strandi126 – 129Combined sources4
Turni142 – 145Combined sources4
Beta strandi151 – 153Combined sources3
Beta strandi166 – 168Combined sources3
Beta strandi175 – 177Combined sources3
Helixi188 – 191Combined sources4
Helixi192 – 194Combined sources3
Beta strandi198 – 203Combined sources6
Helixi216 – 219Combined sources4
Beta strandi220 – 223Combined sources4
Beta strandi225 – 227Combined sources3
Helixi234 – 245Combined sources12
Beta strandi252 – 254Combined sources3
Turni265 – 268Combined sources4
Helixi269 – 273Combined sources5
Beta strandi278 – 280Combined sources3
Turni291 – 296Combined sources6
Beta strandi302 – 304Combined sources3
Beta strandi310 – 313Combined sources4
Turni315 – 320Combined sources6
Beta strandi326 – 328Combined sources3
Beta strandi338 – 340Combined sources3
Turni348 – 353Combined sources6
Beta strandi359 – 361Combined sources3
Turni372 – 377Combined sources6
Beta strandi383 – 385Combined sources3
Turni398 – 401Combined sources4
Helixi402 – 404Combined sources3
Beta strandi411 – 413Combined sources3
Turni424 – 429Combined sources6
Beta strandi435 – 437Combined sources3
Beta strandi444 – 446Combined sources3
Helixi450 – 452Combined sources3
Beta strandi460 – 462Combined sources3
Beta strandi467 – 470Combined sources4
Turni473 – 478Combined sources6
Beta strandi484 – 486Combined sources3
Turni501 – 504Combined sources4
Beta strandi510 – 512Combined sources3
Turni523 – 528Combined sources6
Beta strandi534 – 536Combined sources3
Helixi543 – 546Combined sources4
Turni557 – 560Combined sources4
Beta strandi566 – 568Combined sources3
Turni579 – 584Combined sources6
Beta strandi590 – 592Combined sources3
Turni603 – 608Combined sources6
Beta strandi614 – 616Combined sources3
Helixi627 – 634Combined sources8
Beta strandi638 – 641Combined sources4
Beta strandi655 – 658Combined sources4
Helixi671 – 674Combined sources4
Beta strandi676 – 680Combined sources5
Helixi688 – 690Combined sources3
Helixi700 – 727Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZIWX-ray2.10A27-700[»]
2A0ZX-ray2.40A22-703[»]
2MK9NMR-A/B698-730[»]
2MKANMR-A/B/C698-730[»]
3ULUX-ray3.52A22-702[»]
3ULVX-ray3.52A22-702[»]
5GS0X-ray3.27A/B27-697[»]
ProteinModelPortaliO15455.
SMRiO15455.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15455.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 51LRRNTAdd BLAST28
Repeati52 – 73LRR 1Add BLAST22
Repeati76 – 97LRR 2Add BLAST22
Repeati100 – 121LRR 3Add BLAST22
Repeati124 – 145LRR 4Add BLAST22
Repeati148 – 168LRR 5Add BLAST21
Repeati172 – 193LRR 6Add BLAST22
Repeati198 – 219LRR 7Add BLAST22
Repeati222 – 244LRR 8Add BLAST23
Repeati249 – 270LRR 9Add BLAST22
Repeati275 – 296LRR 10Add BLAST22
Repeati299 – 320LRR 11Add BLAST22
Repeati323 – 344LRR 12Add BLAST22
Repeati356 – 377LRR 13Add BLAST22
Repeati380 – 400LRR 14Add BLAST21
Repeati408 – 429LRR 15Add BLAST22
Repeati432 – 454LRR 16Add BLAST23
Repeati465 – 486LRR 17Add BLAST22
Repeati507 – 528LRR 18Add BLAST22
Repeati531 – 552LRR 19Add BLAST22
Repeati563 – 584LRR 20Add BLAST22
Repeati587 – 608LRR 21Add BLAST22
Repeati611 – 632LRR 22Add BLAST22
Domaini645 – 698LRRCTAdd BLAST54
Domaini754 – 896TIRPROSITE-ProRule annotationAdd BLAST143

Domaini

ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18.

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 22 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000251618.
HOVERGENiHBG023181.
InParanoidiO15455.
KOiK05401.
OMAiTHEVADC.
OrthoDBiEOG091G02Q2.
PhylomeDBiO15455.
TreeFamiTF325595.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027173. TLR3.
[Graphical view]
PANTHERiPTHR24365:SF5. PTHR24365:SF5. 2 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 16 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 19 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. AlignAdd to basket

Isoform 1 (identifier: O15455-1) [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
MRQTLPCIYF WGGLLPFGML CASSTTKCTV SHEVADCSHL KLTQVPDDLP
60 70 80 90 100
TNITVLNLTH NQLRRLPAAN FTRYSQLTSL DVGFNTISKL EPELCQKLPM
110 120 130 140 150
LKVLNLQHNE LSQLSDKTFA FCTNLTELHL MSNSIQKIKN NPFVKQKNLI
160 170 180 190 200
TLDLSHNGLS STKLGTQVQL ENLQELLLSN NKIQALKSEE LDIFANSSLK
210 220 230 240 250
KLELSSNQIK EFSPGCFHAI GRLFGLFLNN VQLGPSLTEK LCLELANTSI
260 270 280 290 300
RNLSLSNSQL STTSNTTFLG LKWTNLTMLD LSYNNLNVVG NDSFAWLPQL
310 320 330 340 350
EYFFLEYNNI QHLFSHSLHG LFNVRYLNLK RSFTKQSISL ASLPKIDDFS
360 370 380 390 400
FQWLKCLEHL NMEDNDIPGI KSNMFTGLIN LKYLSLSNSF TSLRTLTNET
410 420 430 440 450
FVSLAHSPLH ILNLTKNKIS KIESDAFSWL GHLEVLDLGL NEIGQELTGQ
460 470 480 490 500
EWRGLENIFE IYLSYNKYLQ LTRNSFALVP SLQRLMLRRV ALKNVDSSPS
510 520 530 540 550
PFQPLRNLTI LDLSNNNIAN INDDMLEGLE KLEILDLQHN NLARLWKHAN
560 570 580 590 600
PGGPIYFLKG LSHLHILNLE SNGFDEIPVE VFKDLFELKI IDLGLNNLNT
610 620 630 640 650
LPASVFNNQV SLKSLNLQKN LITSVEKKVF GPAFRNLTEL DMRFNPFDCT
660 670 680 690 700
CESIAWFVNW INETHTNIPE LSSHYLCNTP PHYHGFPVRL FDTSSCKDSA
710 720 730 740 750
PFELFFMINT SILLIFIFIV LLIHFEGWRI SFYWNVSVHR VLGFKEIDRQ
760 770 780 790 800
TEQFEYAAYI IHAYKDKDWV WEHFSSMEKE DQSLKFCLEE RDFEAGVFEL
810 820 830 840 850
EAIVNSIKRS RKIIFVITHH LLKDPLCKRF KVHHAVQQAI EQNLDSIILV
860 870 880 890 900
FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERIGAFR HKLQVALGSK

NSVH
Length:904
Mass (Da):103,829
Last modified:January 1, 1998 - v1
Checksum:i034E05ECA7A4D2F7
GO
Isoform 2 (identifier: O15455-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-277: Missing.

Note: No experimental confirmation available.
Show »
Length:627
Mass (Da):72,937
Checksum:i0D376D88306EBEFC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti290G → R in BAG36884 (PubMed:14702039).Curated1
Sequence conflicti575D → N in AAH94737 (PubMed:15489334).Curated1
Sequence conflicti605V → A in BAG36884 (PubMed:14702039).Curated1
Sequence conflicti663E → G in BAG36884 (PubMed:14702039).Curated1

Polymorphismi

The Phe-412 allele (dbSNP:rs3775291) occurs with a frequency of 30% in populations with European and Asian ancestry, and confers some natural resistance to HIV-1 infection.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052361284N → I.Corresponds to variant rs5743316dbSNPEnsembl.1
Natural variantiVAR_052362307Y → D.Corresponds to variant rs5743317dbSNPEnsembl.1
Natural variantiVAR_021976412L → F.4 PublicationsCorresponds to variant rs3775291dbSNPEnsembl.1
Natural variantiVAR_054887554P → S in HSE2; causes TLR3 deficiency and predisposition to herpes simplex encephalitis. 1 PublicationCorresponds to variant rs121434431dbSNPEnsembl.1
Natural variantiVAR_024664737S → T.Corresponds to variant rs5743318dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0541881 – 277Missing in isoform 2. 1 PublicationAdd BLAST277

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88879 mRNA. Translation: AAC34134.1.
DQ445682 mRNA. Translation: ABE01399.1.
AB445631 mRNA. Translation: BAG55028.1.
DQ360814 Genomic DNA. Translation: ABC86908.1.
DQ360815 Genomic DNA. Translation: ABC86909.1.
DQ360816 Genomic DNA. Translation: ABC86910.1.
AK302143 mRNA. Translation: BAH13636.1.
AK314208 mRNA. Translation: BAG36884.1.
AC104070 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04628.1.
BC094737 mRNA. Translation: AAH94737.1.
BC096333 mRNA. Translation: AAH96333.1.
BC096334 mRNA. Translation: AAH96334.1.
BC096335 mRNA. Translation: AAH96335.1.
CCDSiCCDS3846.1. [O15455-1]
RefSeqiNP_003256.1. NM_003265.2. [O15455-1]
XP_016864066.1. XM_017008577.1. [O15455-2]
UniGeneiHs.657724.

Genome annotation databases

EnsembliENST00000296795; ENSP00000296795; ENSG00000164342. [O15455-1]
ENST00000504367; ENSP00000423684; ENSG00000164342. [O15455-2]
GeneIDi7098.
KEGGihsa:7098.
UCSCiuc003iyq.4. human. [O15455-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

TLR3base

TLR3 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88879 mRNA. Translation: AAC34134.1.
DQ445682 mRNA. Translation: ABE01399.1.
AB445631 mRNA. Translation: BAG55028.1.
DQ360814 Genomic DNA. Translation: ABC86908.1.
DQ360815 Genomic DNA. Translation: ABC86909.1.
DQ360816 Genomic DNA. Translation: ABC86910.1.
AK302143 mRNA. Translation: BAH13636.1.
AK314208 mRNA. Translation: BAG36884.1.
AC104070 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04628.1.
BC094737 mRNA. Translation: AAH94737.1.
BC096333 mRNA. Translation: AAH96333.1.
BC096334 mRNA. Translation: AAH96334.1.
BC096335 mRNA. Translation: AAH96335.1.
CCDSiCCDS3846.1. [O15455-1]
RefSeqiNP_003256.1. NM_003265.2. [O15455-1]
XP_016864066.1. XM_017008577.1. [O15455-2]
UniGeneiHs.657724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZIWX-ray2.10A27-700[»]
2A0ZX-ray2.40A22-703[»]
2MK9NMR-A/B698-730[»]
2MKANMR-A/B/C698-730[»]
3ULUX-ray3.52A22-702[»]
3ULVX-ray3.52A22-702[»]
5GS0X-ray3.27A/B27-697[»]
ProteinModelPortaliO15455.
SMRiO15455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112953. 19 interactors.
DIPiDIP-29660N.
IntActiO15455. 7 interactors.
MINTiMINT-2840066.
STRINGi9606.ENSP00000296795.

Chemistry databases

ChEMBLiCHEMBL1075113.

PTM databases

iPTMnetiO15455.
PhosphoSitePlusiO15455.

Polymorphism and mutation databases

BioMutaiTLR3.

Proteomic databases

MaxQBiO15455.
PaxDbiO15455.
PeptideAtlasiO15455.
PRIDEiO15455.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296795; ENSP00000296795; ENSG00000164342. [O15455-1]
ENST00000504367; ENSP00000423684; ENSG00000164342. [O15455-2]
GeneIDi7098.
KEGGihsa:7098.
UCSCiuc003iyq.4. human. [O15455-1]

Organism-specific databases

CTDi7098.
DisGeNETi7098.
GeneCardsiTLR3.
HGNCiHGNC:11849. TLR3.
HPAiCAB025658.
MalaCardsiTLR3.
MIMi603029. gene.
613002. phenotype.
neXtProtiNX_O15455.
OpenTargetsiENSG00000164342.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA36551.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000251618.
HOVERGENiHBG023181.
InParanoidiO15455.
KOiK05401.
OMAiTHEVADC.
OrthoDBiEOG091G02Q2.
PhylomeDBiO15455.
TreeFamiTF325595.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164342-MONOMER.
ReactomeiR-HSA-140534. Ligand-dependent caspase activation.
R-HSA-166166. MyD88-independent TLR3/TLR4 cascade.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-168164. Toll Like Receptor 3 (TLR3) Cascade.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-2562578. TRIF-mediated programmed cell death.
R-HSA-5602410. TLR3 deficiency - HSE.
R-HSA-5602415. UNC93B1 deficiency - HSE.
R-HSA-5602566. TICAM1 deficiency - HSE.
R-HSA-5602571. TRAF3 deficiency - HSE.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
SignaLinkiO15455.
SIGNORiO15455.

Miscellaneous databases

EvolutionaryTraceiO15455.
GeneWikiiTLR_3.
GenomeRNAii7098.
PROiO15455.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164342.
CleanExiHS_TLR3.
ExpressionAtlasiO15455. baseline and differential.
GenevisibleiO15455. HS.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027173. TLR3.
[Graphical view]
PANTHERiPTHR24365:SF5. PTHR24365:SF5. 2 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 6 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 16 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 19 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTLR3_HUMAN
AccessioniPrimary (citable) accession number: O15455
Secondary accession number(s): B2RAI7
, B7Z7K0, E6Y0F0, E6Y0F1, E9PGH4, Q4VAL2, Q504W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 170 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, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.