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O60603 (TLR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toll-like receptor 2
Alternative name(s):
Toll/interleukin-1 receptor-like protein 4
CD_antigen=CD282
Gene names
Name:TLR2
Synonyms:TIL4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. 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.

Subunit structure

Interacts with LY96, TLR1 and TLR6 (via extracellular domain). Binds MYD88 (via TIR domain). Interacts with TICAM1. Ligand binding induces the formation of a heterodimer with TLR1 or TLR6. Interacts with CNPY3 By similarity. Interacts with ATG16L1. Ref.10 Ref.12

Subcellular location

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

Tissue specificity

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.

Domain

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 (Ref.12).

Post-translational modification

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

Polymorphism

Genetic variations in TLR2 are associated with susceptibility to leprosy [MIM: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.

Sequence similarities

Belongs to the Toll-like receptor family.

Contains 19 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 TIR domain.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   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 phosphorylation

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement Ref.9. Source: ProtInc

cell surface pattern recognition receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cellular response to bacterial lipopeptide

Traceable author statement PubMed 15356140. Source: BHF-UCL

cellular response to diacyl bacterial lipopeptide

Inferred from direct assay PubMed 19931471. Source: MGI

cellular response to lipoteichoic acid

Inferred from direct assay PubMed 12594207. Source: MGI

cellular response to peptidoglycan

Inferred from electronic annotation. Source: Ensembl

cellular response to triacyl bacterial lipopeptide

Inferred from direct assay PubMed 19931471. Source: MGI

central nervous system myelin formation

Inferred from electronic annotation. Source: Ensembl

chloramphenicol transport

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from direct assay PubMed 11521063. Source: UniProtKB

detection of diacyl bacterial lipopeptide

Inferred from direct assay PubMed 19931471. Source: MGI

detection of triacyl bacterial lipopeptide

Inferred from direct assay PubMed 19931471. Source: MGI

immune response

Traceable author statement PubMed 10426995. Source: ProtInc

induction by symbiont of defense-related host nitric oxide production

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement PubMed 15356140. Source: BHF-UCL

leukotriene metabolic process

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Traceable author statement PubMed 11518816. Source: GOC

microglial cell activation involved in immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-17 production

Inferred from electronic annotation. Source: Ensembl

nitric oxide metabolic process

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 NF-kappaB import into nucleus

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 12594207. Source: MGI

positive regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 16601243. Source: BHF-UCL

positive regulation of chemokine production

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred by curator PubMed 19740627. Source: BHF-UCL

positive regulation of interferon-beta production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-10 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-18 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

positive regulation of interleukin-8 production

Inferred from direct assay PubMed 17128265PubMed 19740627. Source: BHF-UCL

positive regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage cytokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of toll-like receptor signaling pathway

Inferred from direct assay PubMed 17128265. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of tumor necrosis factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: BHF-UCL

response to fatty acid

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to molecule of fungal origin

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 11044375. Source: UniProtKB

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentToll-like receptor 1-Toll-like receptor 2 protein complex

Inferred from direct assay Ref.14. Source: MGI

Toll-like receptor 2-Toll-like receptor 6 protein complex

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 12443841. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Inferred from direct assay PubMed 19740627. Source: BHF-UCL

   Molecular_functiondiacyl lipopeptide binding

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide receptor activity

Traceable author statement PubMed 11518816. Source: UniProtKB

lipoteichoic acid binding

Inferred from electronic annotation. Source: Ensembl

peptidoglycan binding

Inferred from direct assay PubMed 11986301. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.14. Source: MGI

receptor activity

Inferred from direct assay PubMed 11672593. Source: UniProtKB

signaling pattern recognition receptor activity

Inferred from direct assay PubMed 10384090. Source: UniProtKB

transmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

triacyl lipopeptide binding

Inferred from direct assay Ref.14. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAUFC3PTT63EBI-973722,EBI-3505892

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 784766Toll-like receptor 2
PRO_0000034710

Regions

Topological domain19 – 588570Extracellular Potential
Transmembrane589 – 60921Helical; Potential
Topological domain610 – 784175Cytoplasmic Potential
Repeat54 – 7724LRR 1
Repeat78 – 10124LRR 2
Repeat102 – 12524LRR 3
Repeat126 – 15025LRR 4
Repeat151 – 17525LRR 5
Repeat176 – 19924LRR 6
Repeat200 – 22324LRR 7
Repeat224 – 25027LRR 8
Repeat251 – 27828LRR 9
Repeat279 – 30830LRR 10
Repeat309 – 33729LRR 11
Repeat338 – 36124LRR 12
Repeat362 – 38827LRR 13
Repeat389 – 41426LRR 14
Repeat415 – 43723LRR 15
Repeat438 – 45720LRR 16
Repeat458 – 47821LRR 17
Repeat479 – 50022LRR 18
Repeat501 – 52424LRR 19
Domain525 – 57955LRRCT
Domain639 – 784146TIR
Motif761 – 77818ATG16L1-binding motif

Sites

Site3491Interaction with bacterial lipopeptide

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Ref.11 Ref.14
Glycosylation1991N-linked (GlcNAc...) Ref.11 Ref.14
Glycosylation4141N-linked (GlcNAc...) Ref.14
Glycosylation4421N-linked (GlcNAc...) Ref.11 Ref.14
Disulfide bond30 ↔ 36 Ref.14
Disulfide bond353 ↔ 382 Ref.14
Disulfide bond432 ↔ 454 Ref.14

Natural variations

Natural variant891N → D. Ref.17
VAR_066349
Natural variant4111T → I Reduces TLR2-mediated NF-kappa-B activation. Ref.17
Corresponds to variant rs5743699 [ dbSNP | Ensembl ].
VAR_026765
Natural variant5711R → H. Ref.17
Corresponds to variant rs61735277 [ dbSNP | Ensembl ].
VAR_066350
Natural variant5791R → H.
Corresponds to variant rs5743703 [ dbSNP | Ensembl ].
VAR_026766
Natural variant6311P → H Reduces TLR2-mediated NF-kappa-B activation. Ref.5 Ref.17
Corresponds to variant rs5743704 [ dbSNP | Ensembl ].
VAR_024663
Natural variant6361S → R. Ref.17
Corresponds to variant rs137853177 [ dbSNP | Ensembl ].
VAR_066351
Natural variant6771R → W. Ref.15 Ref.16
VAR_031236
Natural variant7151Y → N.
Corresponds to variant rs5743706 [ dbSNP | Ensembl ].
VAR_052360
Natural variant7531R → Q Reduces TLR2-mediated NF-kappa-B activation. Ref.5 Ref.17
Corresponds to variant rs5743708 [ dbSNP | Ensembl ].
VAR_031237

Experimental info

Mutagenesis1141N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11
Mutagenesis1991N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11
Mutagenesis4161T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11
Mutagenesis4421N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. Ref.11
Mutagenesis6811P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain.
Sequence conflict591L → Q in AAM23001. Ref.8
Sequence conflict681S → C in AAM23001. Ref.8
Sequence conflict7261D → E in AAC34133. Ref.2

Secondary structure

............................................................................................................. 784
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60603 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7DBE6B24CF1FAF8B

FASTA78489,838
        10         20         30         40         50         60 
MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL TEAVKSLDLS 

        70         80         90        100        110        120 
NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG SLEHLDLSYN YLSNLSSSWF 

       130        140        150        160        170        180 
KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK LQILRVGNMD TFTKIQRKDF AGLTFLEELE 

       190        200        210        220        230        240 
IDASDLQSYE PKSLKSIQNV SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS 

       250        260        270        280        290        300 
ELSTGETNSL IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN 

       310        320        330        340        350        360 
DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL VPCLLSQHLK 

       370        380        390        400        410        420 
SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA SLEKTGETLL TLKNLTNIDI 

       430        440        450        460        470        480 
SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK 

       490        500        510        520        530        540 
ELYISRNKLM TLPDASLLPM LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE 

       550        560        570        580        590        600 
FLSFTQEQQA LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL 

       610        620        630        640        650        660 
LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER DAYWVENLMV 

       670        680        690        700        710        720 
QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV FVLSENFVKS EWCKYELDFS 

       730        740        750        760        770        780 
HFRLFDENND AAILILLEPI EKKAIPQRFC KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA 


AIKS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two Toll/Interleukin-1 receptor-like genes TIL3 and TIL4: evidence for a multi-gene receptor family in humans."
Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M., Jasmin A., Trask B.J., Hood L., Nelson P.S.
Blood 91:4020-4027(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leukocyte and Prostate.
[2]"A family of human receptors structurally related to Drosophila Toll."
Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.
Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling."
Yang R.-B., Mark M.R., Gray A.M., Huang A., Xie M.-H., Zhang M., Goddard A.D., Wood W.I., Gurney A.L., Godowski P.J.
Nature 395:284-288(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RESPONSE TO LIPOPOLYSACCHARIDE.
Tissue: Fetal lung.
[4]"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].
[5]"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 [MRNA], VARIANTS HIS-631 AND GLN-753.
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Blood.
[8]"Cloning and sequencing of extracellular domain and its N-terminal and C-terminal fragments of Toll-like receptor 2."
Zhang L., Yu W.B., Ma Y.Y.
Di 4 Jun Yi Da Xue Xue Bao 23:1085-1089(2002)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-586.
[9]"Cell activation and apoptosis by bacterial lipoproteins through Toll-like receptor-2."
Aliprantis A.O., Yang R.-B., Mark M.R., Suggett S., Devaux B., Radolf J.D., Klimpel G.R., Godowski P.J., Zychlinsky A.
Science 285:736-739(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: RESPONSE TO BACTERIAL LIPOPROTEINS.
[10]"A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling."
Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S.
J. Immunol. 169:6668-6672(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TICAM1.
[11]"Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion."
Weber A.N., Morse M.A., Gay N.J.
J. Biol. Chem. 279:34589-34594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-114; ASN-199 AND ASN-442, MUTAGENESIS OF ASN-114; ASN-199; THR-416 AND ASN-442.
[12]"TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3."
Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C., Pimentel-Muinos F.X.
EMBO J. 32:566-582(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG16L1.
[13]"Structural basis for signal transduction by the Toll/interleukin-1 receptor domains."
Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.
Nature 408:111-115(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 639-784, MUTAGENESIS.
[14]"Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide."
Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H., Lee J.-O.
Cell 130:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-509 IN COMPLEX WITH TLR1 AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, GLYCOSYLATION AT ASN-114; ASN-199; ASN-414 AND ASN-442.
[15]"Detection of Toll-like receptor 2 (TLR2) mutation in the lepromatous leprosy patients."
Kang T.-J., Chae G.-T.
FEMS Immunol. Med. Microbiol. 31:53-58(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
[16]"A Toll-like receptor 2 polymorphism that is associated with lepromatous leprosy is unable to mediate mycobacterial signaling."
Bochud P.-Y., Hawn T.R., Aderem A.
J. Immunol. 170:3451-3454(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
[17]"Functional characterization of naturally occurring genetic variants in the human TLR1-2-6 gene family."
Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M., Pellegrini S., Quintana-Murci L.
Hum. Mutat. 32:643-652(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-89; ILE-411; HIS-571; HIS-631; ARG-636 AND GLN-753, CHARACTERIZATION OF VARIANTS ILE-411; HIS-631 AND GLN-753.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003255.2. NM_003264.3.
XP_005263250.1. XM_005263193.1.
XP_005263251.1. XM_005263194.1.
XP_005263252.1. XM_005263195.1.
XP_005263253.1. XM_005263196.1.
XP_005263254.1. XM_005263197.1.
UniGeneHs.519033.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYWX-ray3.00A636-784[»]
1FYXX-ray2.80A636-784[»]
1O77X-ray3.20A/B/C/D/E639-784[»]
2Z7XX-ray2.10A27-509[»]
2Z80X-ray1.80A/B1-284[»]
ProteinModelPortalO60603.
SMRO60603. Positions 27-553, 636-784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112952. 12 interactions.
DIPDIP-35138N.
IntActO60603. 8 interactions.
MINTMINT-3000106.
STRING9606.ENSP00000260010.

Chemistry

BindingDBO60603.
ChEMBLCHEMBL4163.
GuidetoPHARMACOLOGY1752.

PTM databases

PhosphoSiteO60603.

Proteomic databases

PaxDbO60603.
PRIDEO60603.

Protocols and materials databases

DNASU7097.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260010; ENSP00000260010; ENSG00000137462.
GeneID7097.
KEGGhsa:7097.
UCSCuc003inq.3. human.

Organism-specific databases

CTD7097.
GeneCardsGC04P154612.
HGNCHGNC:11848. TLR2.
MIM246300. phenotype.
603028. gene.
neXtProtNX_O60603.
PharmGKBPA36550.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251801.
HOGENOMHOG000110611.
HOVERGENHBG108574.
InParanoidO60603.
KOK10159.
OMALNINDIC.
OrthoDBEOG7SBNN7.
PhylomeDBO60603.
TreeFamTF351113.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkO60603.

Gene expression databases

ArrayExpressO60603.
BgeeO60603.
CleanExHS_TLR2.
GenevestigatorO60603.

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.
IPR027185. TLR2.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERPTHR24365:SF175. PTHR24365:SF175. 1 hit.
PfamPF01582. TIR. 1 hit.
[Graphical view]
PIRSFPIRSF037595. Toll-like_receptor. 1 hit.
SMARTSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS51450. LRR. 11 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60603.
GeneWikiTLR_2.
GenomeRNAi7097.
NextBio27765.
PROO60603.
SOURCESearch...

Entry information

Entry nameTLR2_HUMAN
AccessionPrimary (citable) accession number: O60603
Secondary accession number(s): B3Y612 expand/collapse secondary AC list , D1CS45, D1CS48, D1CS49, O15454, Q8NI00
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 155 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries