O60603 (TLR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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 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. Interacts with CNPY3 By similarity. Ref.9
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.
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 14 LRR (leucine-rich) repeats. 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 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 triacyl bacterial lipopeptide Inferred from direct assay PubMed 19931471. Source: MGI 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 of apoptosis Traceable author statement Ref.8. Source: ProtInc inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement PubMed 15356140. Source: BHF-UCL 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 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 19740627PubMed 17128265. Source: BHF-UCL 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 production Inferred from sequence or structural similarity. Source: BHF-UCL 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.12. Source: MGI cytoplasm Inferred from direct assay PubMed 19740627. Source: BHF-UCL 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 lipopolysaccharide receptor activity Traceable author statement PubMed 11518816. Source: UniProtKB peptidoglycan binding Inferred from direct assay PubMed 11986301. Source: UniProtKB protein heterodimerization activity Inferred from direct assay Ref.12. Source: MGI transmembrane signaling receptor activity Inferred from electronic annotation. Source: InterPro triacyl lipopeptide binding Inferred from direct assay Ref.12. 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

18

Potential

Chain

19 – 784

766

Toll-like receptor 2

PRO_0000034710

Regions

Topological domain

19 – 588

570

Extracellular Potential

Transmembrane

589 – 609

21

Helical; Potential

Topological domain

610 – 784

175

Cytoplasmic Potential

Repeat

51 – 74

24

LRR 1

Repeat

75 – 98

24

LRR 2

Repeat

99 – 122

24

LRR 3

Repeat

124 – 147

24

LRR 4

Repeat

148 – 172

25

LRR 5

Repeat

173 – 196

24

LRR 6

Repeat

221 – 244

24

LRR 7

Repeat

359 – 384

26

LRR 8

Repeat

386 – 411

26

LRR 9

Repeat

412 – 436

25

LRR 10

Repeat

438 – 456

19

LRR 11

Repeat

457 – 476

20

LRR 12

Repeat

477 – 499

23

LRR 13

Repeat

501 – 521

21

LRR 14

Domain

639 – 784

146

TIR

Sites

Site

349

1

Interaction with bacterial lipopeptide

Amino acid modifications

Glycosylation

114

1

N-linked (GlcNAc...) Ref.10 Ref.12

Glycosylation

199

1

N-linked (GlcNAc...) Ref.10 Ref.12

Glycosylation

414

1

N-linked (GlcNAc...) Ref.12

Glycosylation

442

1

N-linked (GlcNAc...) Ref.10 Ref.12

Disulfide bond

30 ↔ 36

Ref.12

Disulfide bond

353 ↔ 382

Ref.12

Disulfide bond

432 ↔ 454

Ref.12

Natural variations

Natural variant

89

1

N → D. Ref.15

VAR_066349

Natural variant

411

1

T → I Reduces TLR2-mediated NF-kappa-B activation. Ref.15
Corresponds to variant rs5743699 [ dbSNP | Ensembl ].

VAR_026765

Natural variant

571

1

R → H. Ref.15

VAR_066350

Natural variant

579

1

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

VAR_026766

Natural variant

631

1

P → H Reduces TLR2-mediated NF-kappa-B activation. Ref.15
Corresponds to variant rs5743704 [ dbSNP | Ensembl ].

VAR_024663

Natural variant

636

1

S → R. Ref.15

VAR_066351

Natural variant

677

1

R → W. Ref.13 Ref.14

VAR_031236

Natural variant

715

1

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

VAR_052360

Natural variant

753

1

R → Q Reduces TLR2-mediated NF-kappa-B activation. Ref.15
Corresponds to variant rs5743708 [ dbSNP | Ensembl ].

VAR_031237

Experimental info

Mutagenesis

114

1

N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.10

Mutagenesis

199

1

N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.10

Mutagenesis

416

1

T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. Ref.10

Mutagenesis

442

1

N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. Ref.10

Mutagenesis

681

1

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

Sequence conflict

59

1

L → Q in AAM23001. Ref.7

Sequence conflict

68

1

S → C in AAM23001. Ref.7

Sequence conflict

726

1

D → E in AAC34133. Ref.2

Secondary structure

1

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784

Helix Strand Turn

Details...

Beta strand

80 – 82

3

Beta strand

96 – 99

4

Beta strand

104 – 106

3

Turn

117 – 122

6

Beta strand

128 – 132

5

Beta strand

152 – 157

6

Turn

159 – 161

3

Beta strand

174 – 182

9

Beta strand

193 – 196

4

Beta strand

199 – 206

8

Helix

213 – 217

5

Turn

218 – 223

6

Beta strand

224 – 231

8

Beta strand

252 – 258

7

Beta strand

260 – 262

3

Helix

263 – 273

11

Beta strand

281 – 286

6

Beta strand

288 – 291

4

Beta strand

311 – 316

6

Helix

322 – 324

3

Helix

329 – 334

6

Beta strand

340 – 346

7

Helix

353 – 358

6

Beta strand

364 – 366

3

Helix

374 – 380

7

Beta strand

391 – 393

3

Helix

402 – 408

7

Helix

409 – 411

3

Beta strand

417 – 419

3

Beta strand

440 – 442

3

Beta strand

460 – 463

4

Beta strand

481 – 483

3

Helix

495 – 497

3

Beta strand

503 – 505

3

Helix

518 – 520

3

Beta strand

527 – 529

3

Helix

539 – 548

10

Turn

549 – 551

3

Turn

553 – 555

3

Beta strand

556 – 558

3

Beta strand

641 – 646

6

Helix

652 – 656

5

Helix

658 – 663

6

Beta strand

666 – 668

3

Beta strand

672 – 674

3

Turn

675 – 677

3

Beta strand

681 – 683

3

Helix

685 – 695

11

Beta strand

696 – 703

8

Helix

705 – 711

7

Helix

713 – 716

4

Turn

723 – 725

3

Helix

726 – 728

3

Beta strand

733 – 736

4

Helix

742 – 744

3

Helix

750 – 758

9

Beta strand

761 – 763

3

Helix

768 – 770

3

Helix

771 – 782

12

Sequences

	Sequence		Length	Mass (Da)
	O60603 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 7DBE6B24CF1FAF8B	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

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: 9596645] [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: 9435236] [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: 9751057] [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: 18810425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	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. , 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].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Blood.
[7]	"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.
[8]	"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: 10426996] [Abstract] Cited for: RESPONSE TO BACTERIAL LIPOPROTEINS.
[9]	"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: 12471095] [Abstract] Cited for: INTERACTION WITH TICAM1.
[10]	"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: 15173186] [Abstract] Cited for: GLYCOSYLATION AT ASN-114; ASN-199 AND ASN-442, MUTAGENESIS OF ASN-114; ASN-199; THR-416 AND ASN-442.
[11]	"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: 11081518] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 639-784, MUTAGENESIS.
[12]	"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: 17889651] [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.
[13]	"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: 11476982] [Abstract] Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
[14]	"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: 12646604] [Abstract] Cited for: VARIANT TRP-677, ASSOCIATION WITH LEPROSIS.
[15]	"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: 21618349] [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.
CH471056 Genomic DNA. Translation: EAX04952.1.
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.

SMR

O60603. Positions 27-568, 636-784.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35138N.

IntAct

O60603. 3 interactions.

MINT

MINT-3000106.

STRING

O60603.

Proteomic databases

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

GC04P154606.

H-InvDB

HIX0004581.

HGNC

HGNC:11848. TLR2.

MIM

246300. phenotype.
603028. gene.

neXtProt

NX_O60603.

PharmGKB

PA36550.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG251801.

GeneTree

ENSGT00650000092942.

HOGENOM

HOG000110611.

HOVERGEN

HBG108574.

InParanoid

O60603.

KO

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.
IPR004075. IL1_rcpt_1.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR017241. Toll-like_receptor.
[Graphical view]

Pfam

PF01582. TIR. 1 hit.
[Graphical view]

PIRSF

PIRSF037595. Toll-like_receptor. 1 hit.

PRINTS

PR01537. INTRLKN1R1F.

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

EvolutionaryTrace

O60603.

NextBio

27765.

SOURCE

Search...

Entry information

Entry name

TLR2_HUMAN

Accession

Primary (citable) accession number: O60603
Secondary accession number(s): B3Y612, O15454, Q8NI00

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	August 1, 1998
Last modified:	May 16, 2012
This is version 134 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.