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O60603

- TLR2_HUMAN

UniProt

O60603 - TLR2_HUMAN

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Protein

Toll-like receptor 2

Gene

TLR2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei349 – 3491Interaction with bacterial lipopeptide

GO - Molecular functioni

  1. diacyl lipopeptide binding Source: Ensembl
  2. lipopolysaccharide receptor activity Source: UniProtKB
  3. lipoteichoic acid binding Source: Ensembl
  4. peptidoglycan binding Source: UniProtKB
  5. protein heterodimerization activity Source: MGI
  6. receptor activity Source: UniProtKB
  7. signaling pattern recognition receptor activity Source: UniProtKB
  8. transmembrane signaling receptor activity Source: InterPro
  9. triacyl lipopeptide binding Source: MGI

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cell surface pattern recognition receptor signaling pathway Source: Ensembl
  3. cellular response to bacterial lipopeptide Source: BHF-UCL
  4. cellular response to diacyl bacterial lipopeptide Source: MGI
  5. cellular response to lipoteichoic acid Source: MGI
  6. cellular response to peptidoglycan Source: Ensembl
  7. cellular response to triacyl bacterial lipopeptide Source: MGI
  8. central nervous system myelin formation Source: Ensembl
  9. chloramphenicol transport Source: Ensembl
  10. defense response to Gram-positive bacterium Source: UniProtKB
  11. detection of diacyl bacterial lipopeptide Source: MGI
  12. detection of triacyl bacterial lipopeptide Source: MGI
  13. I-kappaB phosphorylation Source: BHF-UCL
  14. immune response Source: ProtInc
  15. induction by symbiont of defense-related host nitric oxide production Source: Ensembl
  16. inflammatory response Source: UniProtKB-KW
  17. innate immune response Source: BHF-UCL
  18. leukotriene metabolic process Source: Ensembl
  19. lipopolysaccharide-mediated signaling pathway Source: GOC
  20. microglial cell activation involved in immune response Source: Ensembl
  21. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  22. negative regulation of cell proliferation Source: Ensembl
  23. negative regulation of growth of symbiont in host Source: Ensembl
  24. negative regulation of interleukin-12 production Source: Ensembl
  25. negative regulation of interleukin-17 production Source: Ensembl
  26. nitric oxide metabolic process Source: Ensembl
  27. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
  28. positive regulation of chemokine production Source: BHF-UCL
  29. positive regulation of cytokine secretion Source: Ensembl
  30. positive regulation of inflammatory response Source: BHF-UCL
  31. positive regulation of interferon-beta production Source: BHF-UCL
  32. positive regulation of interleukin-10 production Source: Ensembl
  33. positive regulation of interleukin-12 production Source: BHF-UCL
  34. positive regulation of interleukin-18 production Source: BHF-UCL
  35. positive regulation of interleukin-6 production Source: BHF-UCL
  36. positive regulation of interleukin-8 production Source: BHF-UCL
  37. positive regulation of leukocyte migration Source: Ensembl
  38. positive regulation of macrophage cytokine production Source: Ensembl
  39. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  40. positive regulation of NF-kappaB transcription factor activity Source: MGI
  41. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  42. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  43. positive regulation of oligodendrocyte differentiation Source: Ensembl
  44. positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
  45. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  46. positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  47. positive regulation of tumor necrosis factor production Source: BHF-UCL
  48. positive regulation of Wnt signaling pathway Source: BHF-UCL
  49. response to fatty acid Source: Ensembl
  50. response to hypoxia Source: Ensembl
  51. response to insulin Source: Ensembl
  52. response to molecule of fungal origin Source: Ensembl
  53. response to progesterone Source: Ensembl
  54. response to toxic substance Source: Ensembl
  55. signal transduction Source: UniProtKB
  56. toll-like receptor 2 signaling pathway Source: Reactome
  57. toll-like receptor 4 signaling pathway Source: Reactome
  58. toll-like receptor signaling pathway Source: Reactome
  59. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  60. 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

ReactomeiREACT_115897. Beta defensins.
REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
REACT_8005. Toll Like Receptor TLR1:TLR2 Cascade.
REACT_8006. Toll Like Receptor TLR6:TLR2 Cascade.
SignaLinkiO60603.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11848. TLR2.

Subcellular locationi

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

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. cell projection Source: Ensembl
  3. cell surface Source: UniProtKB
  4. cytoplasm Source: BHF-UCL
  5. external side of plasma membrane Source: Ensembl
  6. integral component of plasma membrane Source: ProtInc
  7. plasma membrane Source: BHF-UCL
  8. Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
  9. Toll-like receptor 2-Toll-like receptor 6 protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication
Mutagenesisi199 – 1991N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication
Mutagenesisi416 – 4161T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication
Mutagenesisi442 – 4421N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. 1 Publication
Mutagenesisi681 – 6811P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain. 1 Publication

Organism-specific databases

MIMi246300. phenotype.
PharmGKBiPA36550.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 784766Toll-like receptor 2PRO_0000034710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 361 Publication
Glycosylationi114 – 1141N-linked (GlcNAc...)2 Publications
Glycosylationi199 – 1991N-linked (GlcNAc...)2 Publications
Disulfide bondi353 ↔ 3821 Publication
Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
Disulfide bondi432 ↔ 4541 Publication
Glycosylationi442 – 4421N-linked (GlcNAc...)2 Publications

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.
PRIDEiO60603.

PTM databases

PhosphoSiteiO60603.

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

BgeeiO60603.
CleanExiHS_TLR2.
ExpressionAtlasiO60603. baseline and differential.
GenevestigatoriO60603.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112952. 13 interactions.
DIPiDIP-35138N.
IntActiO60603. 10 interactions.
MINTiMINT-3000106.
STRINGi9606.ENSP00000260010.

Structurei

Secondary structure

1
784
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374
Beta strandi56 – 583
Turni69 – 746
Beta strandi80 – 823
Turni93 – 986
Beta strandi104 – 1063
Helixi117 – 1204
Beta strandi127 – 1304
Beta strandi137 – 1393
Beta strandi153 – 1619
Turni167 – 1726
Beta strandi175 – 1839
Turni191 – 1966
Beta strandi198 – 2069
Helixi213 – 2208
Turni221 – 2233
Beta strandi224 – 2318
Beta strandi253 – 2586
Beta strandi260 – 2623
Helixi263 – 27412
Beta strandi281 – 2833
Beta strandi288 – 2914
Beta strandi311 – 3166
Helixi322 – 3243
Helixi329 – 3346
Beta strandi340 – 3467
Helixi353 – 3586
Beta strandi364 – 3663
Helixi374 – 3807
Beta strandi391 – 3933
Helixi402 – 4087
Helixi409 – 4113
Beta strandi417 – 4193
Beta strandi440 – 4423
Beta strandi460 – 4634
Beta strandi481 – 4833
Helixi495 – 4973
Beta strandi503 – 5053
Beta strandi641 – 6466
Helixi649 – 6513
Helixi652 – 6565
Helixi658 – 6636
Beta strandi666 – 6683
Beta strandi672 – 6743
Helixi675 – 6784
Beta strandi681 – 6833
Helixi685 – 69511
Beta strandi696 – 7038
Helixi705 – 7117
Helixi713 – 7164
Turni717 – 7193
Helixi720 – 7223
Turni723 – 7253
Helixi726 – 7283
Beta strandi733 – 7386
Turni742 – 7443
Helixi750 – 7589
Beta strandi761 – 7633
Helixi768 – 7703
Helixi771 – 78313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 27-586, 636-784.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60603.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 588570ExtracellularSequence AnalysisAdd
BLAST
Topological domaini610 – 784175CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei589 – 60921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 7724LRR 1Add
BLAST
Repeati78 – 10124LRR 2Add
BLAST
Repeati102 – 12524LRR 3Add
BLAST
Repeati126 – 15025LRR 4Add
BLAST
Repeati151 – 17525LRR 5Add
BLAST
Repeati176 – 19924LRR 6Add
BLAST
Repeati200 – 22324LRR 7Add
BLAST
Repeati224 – 25027LRR 8Add
BLAST
Repeati251 – 27828LRR 9Add
BLAST
Repeati279 – 30830LRR 10Add
BLAST
Repeati309 – 33729LRR 11Add
BLAST
Repeati338 – 36124LRR 12Add
BLAST
Repeati362 – 38827LRR 13Add
BLAST
Repeati389 – 41426LRR 14Add
BLAST
Repeati415 – 43723LRR 15Add
BLAST
Repeati438 – 45720LRR 16Add
BLAST
Repeati458 – 47821LRR 17Add
BLAST
Repeati479 – 50022LRR 18Add
BLAST
Repeati501 – 52424LRR 19Add
BLAST
Domaini525 – 57955LRRCTAdd
BLAST
Domaini639 – 784146TIRPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi761 – 77818ATG16L1-binding motifAdd
BLAST

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

eggNOGiNOG251801.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000110611.
HOVERGENiHBG108574.
InParanoidiO60603.
KOiK10159.
OMAiLGNPYKT.
OrthoDBiEOG7SBNN7.
PhylomeDBiO60603.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. 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]
PANTHERiPTHR24365:SF17. PTHR24365:SF17. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591L → Q in AAM23001. 1 PublicationCurated
Sequence conflicti68 – 681S → C in AAM23001. 1 PublicationCurated
Sequence conflicti726 – 7261D → E in AAC34133. (PubMed:9435236)Curated

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891N → D.1 Publication
VAR_066349
Natural varianti411 – 4111T → I Reduces TLR2-mediated NF-kappa-B activation. 1 Publication
Corresponds to variant rs5743699 [ dbSNP | Ensembl ].
VAR_026765
Natural varianti571 – 5711R → H.1 Publication
Corresponds to variant rs61735277 [ dbSNP | Ensembl ].
VAR_066350
Natural varianti579 – 5791R → H.
Corresponds to variant rs5743703 [ dbSNP | Ensembl ].
VAR_026766
Natural varianti631 – 6311P → H Reduces TLR2-mediated NF-kappa-B activation. 2 Publications
Corresponds to variant rs5743704 [ dbSNP | Ensembl ].
VAR_024663
Natural varianti636 – 6361S → R.1 Publication
Corresponds to variant rs137853177 [ dbSNP | Ensembl ].
VAR_066351
Natural varianti677 – 6771R → W.2 Publications
VAR_031236
Natural varianti715 – 7151Y → N.
Corresponds to variant rs5743706 [ dbSNP | Ensembl ].
VAR_052360
Natural varianti753 – 7531R → Q Reduces TLR2-mediated NF-kappa-B activation. 2 Publications
Corresponds to variant rs5743708 [ dbSNP | Ensembl ].
VAR_031237

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_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.
UniGeneiHs.519033.

Genome annotation databases

EnsembliENST00000260010; ENSP00000260010; ENSG00000137462.
GeneIDi7097.
KEGGihsa:7097.
UCSCiuc003inq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3784.1.
RefSeqi NP_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.
UniGenei Hs.519033.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 27-506 [» ]
2Z80 X-ray 1.80 A/B 1-284 [» ]
ProteinModelPortali O60603.
SMRi O60603. Positions 27-586, 636-784.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112952. 13 interactions.
DIPi DIP-35138N.
IntActi O60603. 10 interactions.
MINTi MINT-3000106.
STRINGi 9606.ENSP00000260010.

Chemistry

BindingDBi O60603.
ChEMBLi CHEMBL4163.
DrugBanki DB00045. OspA lipoprotein.
GuidetoPHARMACOLOGYi 1752.

PTM databases

PhosphoSitei O60603.

Proteomic databases

PaxDbi O60603.
PRIDEi O60603.

Protocols and materials databases

DNASUi 7097.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260010 ; ENSP00000260010 ; ENSG00000137462 .
GeneIDi 7097.
KEGGi hsa:7097.
UCSCi uc003inq.3. human.

Organism-specific databases

CTDi 7097.
GeneCardsi GC04P154612.
HGNCi HGNC:11848. TLR2.
MIMi 246300. phenotype.
603028. gene.
neXtProti NX_O60603.
PharmGKBi PA36550.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251801.
GeneTreei ENSGT00760000119006.
HOGENOMi HOG000110611.
HOVERGENi HBG108574.
InParanoidi O60603.
KOi K10159.
OMAi LGNPYKT.
OrthoDBi EOG7SBNN7.
PhylomeDBi O60603.
TreeFami TF351113.

Enzyme and pathway databases

Reactomei REACT_115897. Beta defensins.
REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
REACT_8005. Toll Like Receptor TLR1:TLR2 Cascade.
REACT_8006. Toll Like Receptor TLR6:TLR2 Cascade.
SignaLinki O60603.

Miscellaneous databases

EvolutionaryTracei O60603.
GeneWikii TLR_2.
GenomeRNAii 7097.
NextBioi 27765.
PROi O60603.
SOURCEi Search...

Gene expression databases

Bgeei O60603.
CleanExi HS_TLR2.
ExpressionAtlasi O60603. baseline and differential.
Genevestigatori O60603.

Family and domain databases

Gene3Di 3.40.50.10140. 1 hit.
InterProi 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 ]
PANTHERi PTHR24365:SF17. PTHR24365:SF17. 1 hit.
Pfami PF13855. LRR_8. 3 hits.
PF01582. TIR. 1 hit.
[Graphical view ]
PIRSFi PIRSF037595. Toll-like_receptor. 1 hit.
SMARTi SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS51450. LRR. 11 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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: October 29, 2014
This is version 161 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

External Data

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