Toll-like receptor 2 precursor - Homo sapiens (Human)

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O60603 (TLR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 145. History...

Clusters with 100%, 90%, 50% identity |

Documents (7) |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Toll-like receptor 2

Alternative name(s):
Toll/interleukin-1 receptor-like protein 4
CD_antigen=CD282

Gene names

Name:	TLR2
Synonyms:	TIL4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Immunity Inflammatory response Innate immunity
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB phosphorylation Inferred from direct assay PubMed 19740627. Source: BHF-UCL MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome cell surface pattern recognition receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara cellular response to triacyl bacterial lipopeptide Inferred from direct assay PubMed 19931471. Source: MGI chloramphenicol transport Inferred from electronic annotation. Source: Compara defense response to Gram-positive bacterium Inferred from electronic annotation. Source: Compara 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 induction by symbiont of defense-related host nitric oxide production Inferred from electronic annotation. Source: Compara induction of apoptosis Traceable author statement Ref.9. Source: ProtInc inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement PubMed 15356140. Source: BHF-UCL negative regulation of growth of symbiont in host Inferred from electronic annotation. Source: Compara negative regulation of interleukin-12 production Inferred from electronic annotation. Source: Compara negative regulation of interleukin-17 production Inferred from electronic annotation. Source: Compara 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 receptor 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: Compara 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-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 17128265 PubMed 19740627. Source: BHF-UCL positive regulation of leukocyte migration Inferred from electronic annotation. Source: Compara positive regulation of macrophage cytokine production Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL 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: Compara positive regulation of tumor necrosis factor production Inferred from sequence or structural similarity. Source: BHF-UCL response to molecule of fungal origin Inferred from electronic annotation. Source: Compara toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	Toll-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: Compara 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: Compara integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	Gram-positive bacterial cell surface binding Inferred from direct assay PubMed 11521063. Source: UniProtKB diacyl lipopeptide binding Inferred from electronic annotation. Source: Compara lipopolysaccharide receptor activity Traceable author statement PubMed 11518816. Source: UniProtKB lipoteichoic acid binding Inferred from electronic annotation. Source: Compara peptidoglycan binding Inferred from direct assay PubMed 11986301. Source: UniProtKB protein heterodimerization activity Inferred from direct assay Ref.14. Source: MGI 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
PAUF	C3PTT6	3	EBI-973722,EBI-3505892

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Chain

19 – 784

766

Toll-like receptor 2

PRO_0000034710

Regions

Topological domain

19 – 588

570

Extracellular Potential

Transmembrane

589 – 609

Helical; Potential

Topological domain

610 – 784

175

Cytoplasmic Potential

Repeat

54 – 77

LRR 1

Repeat

78 – 101

LRR 2

Repeat

102 – 125

LRR 3

Repeat

126 – 150

LRR 4

Repeat

151 – 175

LRR 5

Repeat

176 – 199

LRR 6

Repeat

200 – 223

LRR 7

Repeat

224 – 250

LRR 8

Repeat

251 – 278

LRR 9

Repeat

279 – 308

LRR 10

Repeat

309 – 337

LRR 11

Repeat

338 – 361

LRR 12

Repeat

362 – 388

LRR 13

Repeat

389 – 414

LRR 14

Repeat

415 – 437

LRR 15

Repeat

438 – 457

LRR 16

Repeat

458 – 478

LRR 17

Repeat

479 – 500

LRR 18

Repeat

501 – 524

LRR 19

Domain

525 – 579

LRRCT

Domain

639 – 784

146

TIR

Motif

761 – 778

ATG16L1-binding motif

Sites

Site

349

Interaction with bacterial lipopeptide

Amino acid modifications

Glycosylation

114

N-linked (GlcNAc...) Ref.11 Ref.14

Glycosylation

199

N-linked (GlcNAc...) Ref.11 Ref.14

Glycosylation

414

N-linked (GlcNAc...) Ref.14

Glycosylation

442

N-linked (GlcNAc...) Ref.11 Ref.14

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

N → D. Ref.17

VAR_066349

Natural variant

411

T → I Reduces TLR2-mediated NF-kappa-B activation. Ref.17
Corresponds to variant rs5743699 [ dbSNP | Ensembl ].

VAR_026765

Natural variant

571

R → H. Ref.17

VAR_066350

Natural variant

579

R → H.
Corresponds to variant rs5743703 [ dbSNP | Ensembl ].

VAR_026766

Natural variant

631

P → H Reduces TLR2-mediated NF-kappa-B activation. Ref.5 Ref.17
Corresponds to variant rs5743704 [ dbSNP | Ensembl ].

VAR_024663

Natural variant

636

S → R. Ref.17

VAR_066351

Natural variant

677

R → W. Ref.15 Ref.16

VAR_031236

Natural variant

715

Y → N.
Corresponds to variant rs5743706 [ dbSNP | Ensembl ].

VAR_052360

Natural variant

753

R → Q Reduces TLR2-mediated NF-kappa-B activation. Ref.5 Ref.17
Corresponds to variant rs5743708 [ dbSNP | Ensembl ].

VAR_031237

Experimental info

Mutagenesis

114

N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11

Mutagenesis

199

N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11

Mutagenesis

416

T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.11

Mutagenesis

442

N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. Ref.11

Mutagenesis

681

P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain.

Sequence conflict

L → Q in AAM23001. Ref.8

Sequence conflict

S → C in AAM23001. Ref.8

Sequence conflict

726

D → E in AAC34133. Ref.2

Secondary structure

784

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O60603 [UniParc].

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

784

89,838

        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' referencesShow '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. 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.

IPI

IPI00019006.

RefSeq

NP_003255.2. NM_003264.3.

UniGene

Hs.519033.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FYW	X-ray	3.00	A	636-784	[»]
1FYX	X-ray	2.80	A	636-784	[»]
1O77	X-ray	3.20	A/B/C/D/E	639-784	[»]
2Z7X	X-ray	2.10	A	27-509	[»]
2Z80	X-ray	1.80	A/B	1-284	[»]

ProteinModelPortal

O60603.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35138N.

IntAct

O60603. 3 interactions.

MINT

MINT-3000106.

STRING

9606.ENSP00000260010.

PTM databases

PhosphoSite

O60603.

Proteomic databases

PaxDb

O60603.

PRIDE

O60603.

Protocols and materials databases

DNASU

7097.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260010; ENSP00000260010; ENSG00000137462.

GeneID

7097.

KEGG

hsa:7097.

UCSC

uc003inq.3. human.

Organism-specific databases

CTD

7097.

GeneCards

GC04P154612.

HGNC

HGNC:11848. TLR2.

MIM

246300. phenotype.
603028. gene.

neXtProt

NX_O60603.

PharmGKB

PA36550.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG251801.

HOGENOM

HOG000110611.

HOVERGEN

HBG108574.

InParanoid

O60603.

K10159.

OMA

LNINDIC.

OrthoDB

EOG4SN1N6.

PhylomeDB

O60603.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O60603.

Bgee

O60603.

CleanEx

HS_TLR2.

Genevestigator

O60603.

GermOnline

ENSG00000137462. Homo sapiens.

Family and domain databases

InterPro

IPR000483. 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]

PANTHER

PTHR24365:SF17. PTHR24365:SF17. 1 hit.

Pfam

PF01582. TIR. 1 hit.
[Graphical view]

PIRSF

PIRSF037595. Toll-like_receptor. 1 hit.

SMART

SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF52200. TIR. 1 hit.

PROSITE

PS51450. LRR. 11 hits.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O60603.

ChEMBL

CHEMBL4163.

EvolutionaryTrace

O60603.

GenomeRNAi

7097.

NextBio

27765.

SOURCE

Search...

Entry information

Entry name

TLR2_HUMAN

Accession

Primary (citable) accession number: O60603
Secondary accession number(s): B3Y612

Q8NI00

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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

Human chromosome 4

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents