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Protein

Toll-like receptor 2

Gene

TLR2

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

Functioni

Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins (PubMed:10426996). Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6 (PubMed:11441107). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36). The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse) (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (By similarity).By similarity6 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: UniProtKB
  • lipopolysaccharide receptor activity Source: UniProtKB
  • peptidoglycan binding Source: UniProtKB
  • protein heterodimerization activity Source: MGI
  • receptor activity Source: UniProtKB
  • signaling pattern recognition receptor activity Source: UniProtKB
  • Toll-like receptor binding Source: UniProtKB
  • transmembrane signaling receptor activity Source: InterPro
  • triacyl lipopeptide binding Source: MGI

GO - Biological processi

  • apoptotic process Source: ProtInc
  • cellular response to bacterial lipopeptide Source: BHF-UCL
  • cellular response to diacyl bacterial lipopeptide Source: UniProtKB
  • cellular response to lipoteichoic acid Source: MGI
  • cellular response to triacyl bacterial lipopeptide Source: UniProtKB
  • central nervous system myelin formation Source: Ensembl
  • cytokine secretion involved in immune response Source: CACAO
  • defense response to Gram-positive bacterium Source: UniProtKB
  • detection of diacyl bacterial lipopeptide Source: MGI
  • detection of triacyl bacterial lipopeptide Source: MGI
  • I-kappaB phosphorylation Source: BHF-UCL
  • immune response Source: ProtInc
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: BHF-UCL
  • interleukin-10 production Source: CACAO
  • leukotriene metabolic process Source: Ensembl
  • microglial cell activation Source: Ensembl
  • MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  • negative regulation of cell proliferation Source: Ensembl
  • nitric oxide metabolic process Source: Ensembl
  • positive regulation of chemokine production Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of inflammatory response Source: BHF-UCL
  • positive regulation of interferon-beta production Source: BHF-UCL
  • positive regulation of interleukin-10 production Source: Ensembl
  • positive regulation of interleukin-12 production Source: BHF-UCL
  • positive regulation of interleukin-18 production Source: BHF-UCL
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of interleukin-8 production Source: BHF-UCL
  • positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • positive regulation of oligodendrocyte differentiation Source: Ensembl
  • positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of Wnt signaling pathway Source: BHF-UCL
  • regulation of cytokine secretion Source: InterPro
  • response to fatty acid Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to insulin Source: Ensembl
  • response to progesterone Source: Ensembl
  • response to toxic substance Source: Ensembl
  • signal transduction Source: UniProtKB
  • toll-like receptor 2 signaling pathway Source: InterPro
  • toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  • toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137462-MONOMER.
ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-1461957. Beta defensins.
R-HSA-166058. MyD88:Mal cascade initiated on plasma membrane.
R-HSA-168179. Toll Like Receptor TLR1:TLR2 Cascade.
R-HSA-168188. Toll Like Receptor TLR6:TLR2 Cascade.
R-HSA-5602498. MyD88 deficiency (TLR2/4).
R-HSA-5603041. IRAK4 deficiency (TLR2/4).
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiO60603.
SIGNORiO60603.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 2
Alternative name(s):
Toll/interleukin-1 receptor-like protein 4
CD_antigen: CD282
Gene namesi
Name:TLR2
Synonyms:TIL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11848. TLR2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 588ExtracellularSequence analysisAdd BLAST568
Transmembranei589 – 609HelicalSequence analysisAdd BLAST21
Topological domaini610 – 784CytoplasmicSequence analysisAdd BLAST175

GO - Cellular componenti

  • cell body Source: Ensembl
  • cell projection Source: Ensembl
  • cell surface Source: UniProtKB
  • cytoplasm Source: BHF-UCL
  • Golgi apparatus Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • intrinsic component of plasma membrane Source: UniProtKB
  • membrane raft Source: UniProtKB
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: BHF-UCL
  • Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi199N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi416T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi442N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi681P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain. 1 Publication1

Organism-specific databases

DisGeNETi7097.
MalaCardsiTLR2.
MIMi246300. phenotype.
OpenTargetsiENSG00000137462.
PharmGKBiPA36550.

Chemistry databases

ChEMBLiCHEMBL4163.
DrugBankiDB00045. OspA lipoprotein.
GuidetoPHARMACOLOGYi1752.

Polymorphism and mutation databases

BioMutaiTLR2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003471021 – 784Toll-like receptor 2Add BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 361 Publication
Glycosylationi114N-linked (GlcNAc...)2 Publications1
Glycosylationi199N-linked (GlcNAc...)2 Publications1
Disulfide bondi353 ↔ 3821 Publication
Glycosylationi414N-linked (GlcNAc...)1 Publication1
Disulfide bondi432 ↔ 4541 Publication
Glycosylationi442N-linked (GlcNAc...)2 Publications1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO60603.
PeptideAtlasiO60603.
PRIDEiO60603.

PTM databases

iPTMnetiO60603.
PhosphoSitePlusiO60603.
SwissPalmiO60603.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000137462.
CleanExiHS_TLR2.
ExpressionAtlasiO60603. baseline and differential.
GenevisibleiO60603. HS.

Interactioni

Subunit structurei

Interacts with LY96, TLR1 and TLR6 (via extracellular domain) (PubMed:17889651). TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before stimulation by the ligand. The heterodimers form bigger oligomers in response to their corresponding ligands as well as further heterotypic associations with other receptors such as CD14 and/or CD36 (PubMed:16880211). Binds MYD88 (via TIR domain). Interacts with TICAM1 (PubMed:12471095). Interacts with CNPY3 (By similarity). Interacts with ATG16L1 (PubMed:23376921).By similarity4 Publications
(Microbial infection) Interacts with M.tuberculosis EsxA (PubMed:20800577). Interacts with M.bovis MPB83 (PubMed:20800577).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei349Interaction with bacterial lipopeptide1

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005332EBI-973722,EBI-297353
PAUFC3PTT63EBI-973722,EBI-3505892

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI
  • Toll-like receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112952. 23 interactors.
DIPiDIP-35138N.
IntActiO60603. 21 interactors.
MINTiMINT-3000106.
STRINGi9606.ENSP00000260010.

Chemistry databases

BindingDBiO60603.

Structurei

Secondary structure

1784
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Beta strandi56 – 58Combined sources3
Turni69 – 74Combined sources6
Beta strandi80 – 82Combined sources3
Turni93 – 98Combined sources6
Beta strandi104 – 106Combined sources3
Helixi117 – 120Combined sources4
Beta strandi127 – 130Combined sources4
Beta strandi137 – 139Combined sources3
Beta strandi153 – 161Combined sources9
Turni167 – 172Combined sources6
Beta strandi175 – 183Combined sources9
Turni191 – 196Combined sources6
Beta strandi198 – 206Combined sources9
Helixi213 – 220Combined sources8
Turni221 – 223Combined sources3
Beta strandi224 – 231Combined sources8
Beta strandi253 – 258Combined sources6
Beta strandi260 – 262Combined sources3
Helixi263 – 274Combined sources12
Beta strandi281 – 283Combined sources3
Beta strandi288 – 291Combined sources4
Beta strandi311 – 316Combined sources6
Helixi322 – 324Combined sources3
Helixi329 – 334Combined sources6
Beta strandi340 – 346Combined sources7
Helixi353 – 358Combined sources6
Beta strandi364 – 366Combined sources3
Helixi374 – 380Combined sources7
Beta strandi391 – 393Combined sources3
Helixi402 – 408Combined sources7
Helixi409 – 411Combined sources3
Beta strandi417 – 419Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi460 – 463Combined sources4
Beta strandi481 – 483Combined sources3
Helixi495 – 497Combined sources3
Beta strandi503 – 505Combined sources3
Beta strandi641 – 646Combined sources6
Helixi649 – 651Combined sources3
Helixi652 – 656Combined sources5
Helixi658 – 663Combined sources6
Beta strandi666 – 668Combined sources3
Beta strandi672 – 674Combined sources3
Helixi675 – 678Combined sources4
Beta strandi681 – 683Combined sources3
Helixi685 – 695Combined sources11
Beta strandi696 – 703Combined sources8
Helixi705 – 711Combined sources7
Helixi713 – 716Combined sources4
Turni717 – 719Combined sources3
Helixi720 – 722Combined sources3
Turni723 – 725Combined sources3
Helixi726 – 728Combined sources3
Beta strandi733 – 738Combined sources6
Turni742 – 744Combined sources3
Helixi750 – 758Combined sources9
Beta strandi761 – 763Combined sources3
Helixi768 – 770Combined sources3
Helixi771 – 783Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO60603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati54 – 77LRR 1Add BLAST24
Repeati78 – 101LRR 2Add BLAST24
Repeati102 – 125LRR 3Add BLAST24
Repeati126 – 150LRR 4Add BLAST25
Repeati151 – 175LRR 5Add BLAST25
Repeati176 – 199LRR 6Add BLAST24
Repeati200 – 223LRR 7Add BLAST24
Repeati224 – 250LRR 8Add BLAST27
Repeati251 – 278LRR 9Add BLAST28
Repeati279 – 308LRR 10Add BLAST30
Repeati309 – 337LRR 11Add BLAST29
Repeati338 – 361LRR 12Add BLAST24
Repeati362 – 388LRR 13Add BLAST27
Repeati389 – 414LRR 14Add BLAST26
Repeati415 – 437LRR 15Add BLAST23
Repeati438 – 457LRR 16Add BLAST20
Repeati458 – 478LRR 17Add BLAST21
Repeati479 – 500LRR 18Add BLAST22
Repeati501 – 524LRR 19Add BLAST24
Domaini525 – 579LRRCTAdd BLAST55
Domaini639 – 784TIRPROSITE-ProRule annotationAdd BLAST146

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi761 – 778ATG16L1-binding motifAdd BLAST18

Domaini

Ester-bound lipid substrates are bound through a crevice formed between the LRR 11 and LRR 12.By similarity
The ATG16L1-binding motif mediates interaction with ATG16L1.1 Publication

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 19 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000110611.
HOVERGENiHBG108574.
InParanoidiO60603.
KOiK10159.
OMAiHLILHMK.
OrthoDBiEOG091G05L8.
PhylomeDBiO60603.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027185. TLR2.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERiPTHR24365:SF17. PTHR24365:SF17. 1 hit.
PfamiPF13855. LRR_8. 2 hits.
PF01463. LRRCT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O60603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL
60 70 80 90 100
TEAVKSLDLS NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG
110 120 130 140 150
SLEHLDLSYN YLSNLSSSWF KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK
160 170 180 190 200
LQILRVGNMD TFTKIQRKDF AGLTFLEELE IDASDLQSYE PKSLKSIQNV
210 220 230 240 250
SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS ELSTGETNSL
260 270 280 290 300
IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN
310 320 330 340 350
DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL
360 370 380 390 400
VPCLLSQHLK SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA
410 420 430 440 450
SLEKTGETLL TLKNLTNIDI SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS
460 470 480 490 500
VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK ELYISRNKLM TLPDASLLPM
510 520 530 540 550
LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE FLSFTQEQQA
560 570 580 590 600
LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL
610 620 630 640 650
LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER
660 670 680 690 700
DAYWVENLMV QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV
710 720 730 740 750
FVLSENFVKS EWCKYELDFS HFRLFDENND AAILILLEPI EKKAIPQRFC
760 770 780
KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA AIKS
Length:784
Mass (Da):89,838
Last modified:August 1, 1998 - v1
Checksum:i7DBE6B24CF1FAF8B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59L → Q in AAM23001 (Ref. 8) Curated1
Sequence conflicti68S → C in AAM23001 (Ref. 8) Curated1
Sequence conflicti726D → E in AAC34133 (PubMed:9435236).Curated1

Polymorphismi

Genetic variations in TLR2 are associated with susceptibility to leprosy [MIMi:246300]. Leprosy is a chronic disease associated with depressed cellular (but not humoral) immunity, the bacterium requires a lower temperature than 37 degrees Celsius and thrives particularly in peripheral Schwann cells and macrophages. The Trp-677 polymorphism in the intracellular domain of TLR2 has a role in susceptibility to lepromatous leprosy. Wild-type TLR2 mediates CD14-enhanced Mycobacterium leprae-dependent activation of NFKB1, but TLR2 containing the Trp-677 polymorphism did not. The impaired function of the Trp-677 polymorphism provides a molecular mechanism for the poor cellular immune response associated with lepromatous leprosy.2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06634989N → D.1 PublicationCorresponds to variant rs137853176dbSNPEnsembl.1
Natural variantiVAR_026765411T → I Reduces TLR2-mediated NF-kappa-B activation. 1 PublicationCorresponds to variant rs5743699dbSNPEnsembl.1
Natural variantiVAR_066350571R → H.1 PublicationCorresponds to variant rs61735277dbSNPEnsembl.1
Natural variantiVAR_026766579R → H.Corresponds to variant rs5743703dbSNPEnsembl.1
Natural variantiVAR_024663631P → H Reduces TLR2-mediated NF-kappa-B activation. 2 PublicationsCorresponds to variant rs5743704dbSNPEnsembl.1
Natural variantiVAR_066351636S → R.1 PublicationCorresponds to variant rs137853177dbSNPEnsembl.1
Natural variantiVAR_031236677R → W.2 PublicationsCorresponds to variant rs121917864dbSNPEnsembl.1
Natural variantiVAR_052360715Y → N.Corresponds to variant rs5743706dbSNPEnsembl.1
Natural variantiVAR_031237753R → Q Reduces TLR2-mediated NF-kappa-B activation. 2 PublicationsCorresponds to variant rs5743708dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051152 mRNA. Translation: AAC34377.1.
U88878 mRNA. Translation: AAC34133.1.
AB445624 mRNA. Translation: BAG55021.1.
DQ012265 mRNA. Translation: AAY85644.1.
DQ012266 mRNA. Translation: AAY85645.1.
DQ012267 mRNA. Translation: AAY85646.1.
DQ012268 mRNA. Translation: AAY85647.1.
DQ012269 mRNA. Translation: AAY85648.1.
DQ012270 mRNA. Translation: AAY85649.1.
DQ012271 mRNA. Translation: AAY85650.1.
CH471056 Genomic DNA. Translation: EAX04952.1.
CH471056 Genomic DNA. Translation: EAX04953.1.
BC033756 mRNA. Translation: AAH33756.1.
AF502291 mRNA. Translation: AAM23001.1.
CCDSiCCDS3784.1.
RefSeqiNP_001305716.1. NM_001318787.1.
NP_001305718.1. NM_001318789.1.
NP_001305719.1. NM_001318790.1.
NP_001305720.1. NM_001318791.1.
NP_001305722.1. NM_001318793.1.
NP_001305724.1. NM_001318795.1.
NP_001305725.1. NM_001318796.1.
NP_003255.2. NM_003264.4.
XP_011530517.1. XM_011532215.2.
XP_011530518.1. XM_011532216.2.
XP_016864062.1. XM_017008573.1.
XP_016864063.1. XM_017008574.1.
XP_016864064.1. XM_017008575.1.
XP_016864065.1. XM_017008576.1.
UniGeneiHs.519033.

Genome annotation databases

EnsembliENST00000260010; ENSP00000260010; ENSG00000137462.
GeneIDi7097.
KEGGihsa:7097.
UCSCiuc063aif.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051152 mRNA. Translation: AAC34377.1.
U88878 mRNA. Translation: AAC34133.1.
AB445624 mRNA. Translation: BAG55021.1.
DQ012265 mRNA. Translation: AAY85644.1.
DQ012266 mRNA. Translation: AAY85645.1.
DQ012267 mRNA. Translation: AAY85646.1.
DQ012268 mRNA. Translation: AAY85647.1.
DQ012269 mRNA. Translation: AAY85648.1.
DQ012270 mRNA. Translation: AAY85649.1.
DQ012271 mRNA. Translation: AAY85650.1.
CH471056 Genomic DNA. Translation: EAX04952.1.
CH471056 Genomic DNA. Translation: EAX04953.1.
BC033756 mRNA. Translation: AAH33756.1.
AF502291 mRNA. Translation: AAM23001.1.
CCDSiCCDS3784.1.
RefSeqiNP_001305716.1. NM_001318787.1.
NP_001305718.1. NM_001318789.1.
NP_001305719.1. NM_001318790.1.
NP_001305720.1. NM_001318791.1.
NP_001305722.1. NM_001318793.1.
NP_001305724.1. NM_001318795.1.
NP_001305725.1. NM_001318796.1.
NP_003255.2. NM_003264.4.
XP_011530517.1. XM_011532215.2.
XP_011530518.1. XM_011532216.2.
XP_016864062.1. XM_017008573.1.
XP_016864063.1. XM_017008574.1.
XP_016864064.1. XM_017008575.1.
XP_016864065.1. XM_017008576.1.
UniGeneiHs.519033.

3D structure databases

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

Protein-protein interaction databases

BioGridi112952. 23 interactors.
DIPiDIP-35138N.
IntActiO60603. 21 interactors.
MINTiMINT-3000106.
STRINGi9606.ENSP00000260010.

Chemistry databases

BindingDBiO60603.
ChEMBLiCHEMBL4163.
DrugBankiDB00045. OspA lipoprotein.
GuidetoPHARMACOLOGYi1752.

PTM databases

iPTMnetiO60603.
PhosphoSitePlusiO60603.
SwissPalmiO60603.

Polymorphism and mutation databases

BioMutaiTLR2.

Proteomic databases

PaxDbiO60603.
PeptideAtlasiO60603.
PRIDEiO60603.

Protocols and materials databases

DNASUi7097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260010; ENSP00000260010; ENSG00000137462.
GeneIDi7097.
KEGGihsa:7097.
UCSCiuc063aif.1. human.

Organism-specific databases

CTDi7097.
DisGeNETi7097.
GeneCardsiTLR2.
HGNCiHGNC:11848. TLR2.
MalaCardsiTLR2.
MIMi246300. phenotype.
603028. gene.
neXtProtiNX_O60603.
OpenTargetsiENSG00000137462.
PharmGKBiPA36550.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000110611.
HOVERGENiHBG108574.
InParanoidiO60603.
KOiK10159.
OMAiHLILHMK.
OrthoDBiEOG091G05L8.
PhylomeDBiO60603.
TreeFamiTF351113.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137462-MONOMER.
ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-1461957. Beta defensins.
R-HSA-166058. MyD88:Mal cascade initiated on plasma membrane.
R-HSA-168179. Toll Like Receptor TLR1:TLR2 Cascade.
R-HSA-168188. Toll Like Receptor TLR6:TLR2 Cascade.
R-HSA-5602498. MyD88 deficiency (TLR2/4).
R-HSA-5603041. IRAK4 deficiency (TLR2/4).
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiO60603.
SIGNORiO60603.

Miscellaneous databases

EvolutionaryTraceiO60603.
GeneWikiiTLR_2.
GenomeRNAii7097.
PROiO60603.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137462.
CleanExiHS_TLR2.
ExpressionAtlasiO60603. baseline and differential.
GenevisibleiO60603. HS.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027185. TLR2.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERiPTHR24365:SF17. PTHR24365:SF17. 1 hit.
PfamiPF13855. LRR_8. 2 hits.
PF01463. LRRCT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTLR2_HUMAN
AccessioniPrimary (citable) accession number: O60603
Secondary accession number(s): B3Y612
, D1CS45, D1CS48, D1CS49, O15454, Q8NI00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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.