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Q9QUN7

- TLR2_MOUSE

UniProt

Q9QUN7 - TLR2_MOUSE

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Protein

Toll-like receptor 2

Gene

Tlr2

Organism
Mus musculus (Mouse)
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 By similarity.By similarity

Sites

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

GO - Molecular functioni

  1. diacyl lipopeptide binding Source: MGI
  2. lipoteichoic acid binding Source: MGI
  3. protein heterodimerization activity Source: MGI
  4. transmembrane signaling receptor activity Source: InterPro
  5. triacyl lipopeptide binding Source: MGI

GO - Biological processi

  1. cell surface pattern recognition receptor signaling pathway Source: MGI
  2. cellular response to bacterial lipopeptide Source: BHF-UCL
  3. cellular response to lipoteichoic acid Source: MGI
  4. cellular response to peptidoglycan Source: MGI
  5. chloramphenicol transport Source: MGI
  6. defense response to Gram-positive bacterium Source: MGI
  7. induction by symbiont of defense-related host nitric oxide production Source: MGI
  8. inflammatory response Source: UniProtKB-KW
  9. innate immune response Source: BHF-UCL
  10. MyD88-dependent toll-like receptor signaling pathway Source: MGI
  11. negative regulation of growth of symbiont in host Source: MGI
  12. negative regulation of interleukin-12 production Source: MGI
  13. negative regulation of interleukin-17 production Source: MGI
  14. positive regulation of chemokine production Source: MGI
  15. positive regulation of cytokine secretion Source: MGI
  16. positive regulation of inflammatory response Source: InterPro
  17. positive regulation of interferon-beta production Source: BHF-UCL
  18. positive regulation of interleukin-12 production Source: BHF-UCL
  19. positive regulation of interleukin-18 production Source: BHF-UCL
  20. positive regulation of interleukin-6 production Source: BHF-UCL
  21. positive regulation of leukocyte migration Source: MGI
  22. positive regulation of macrophage cytokine production Source: MGI
  23. positive regulation of nitric oxide biosynthetic process Source: MGI
  24. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  25. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  26. positive regulation of tumor necrosis factor biosynthetic process Source: MGI
  27. positive regulation of tumor necrosis factor production Source: BHF-UCL
  28. response to bacterium Source: MGI
  29. response to molecule of fungal origin Source: MGI
  30. response to peptidoglycan Source: MGI
  31. toll-like receptor 2 signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 2
Alternative name(s):
CD_antigen: CD282
Gene namesi
Name:Tlr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1346060. Tlr2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
  2. external side of plasma membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: MGI
  5. Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
  6. Toll-like receptor 2-Toll-like receptor 6 protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi681 – 6811P → H: Abolishes MYD88-binding and response to microbial cell wall components. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 784760Toll-like receptor 2PRO_0000034712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 36
Glycosylationi147 – 1471N-linked (GlcNAc...)2 Publications
Disulfide bondi353 ↔ 382
Glycosylationi414 – 4141N-linked (GlcNAc...)2 Publications
Disulfide bondi432 ↔ 454
Glycosylationi442 – 4421N-linked (GlcNAc...)2 Publications

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9QUN7.

PTM databases

PhosphoSiteiQ9QUN7.

Expressioni

Tissue specificityi

Detected in a macrophage cell line, smooth muscle, lung, spleen, thymus, brain and adipose tissue.

Gene expression databases

CleanExiMM_TLR2.
GenevestigatoriQ9QUN7.

Interactioni

Subunit structurei

Interacts with ATG16L1 By similarity. 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 similarity2 Publications

Protein-protein interaction databases

IntActiQ9QUN7. 2 interactions.
STRINGi10090.ENSMUSP00000029623.

Structurei

Secondary structure

1
784
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Beta strandi44 – 463Combined sources
Beta strandi56 – 583Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 823Combined sources
Turni93 – 986Combined sources
Beta strandi104 – 1063Combined sources
Helixi117 – 1204Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi153 – 1619Combined sources
Turni167 – 1726Combined sources
Beta strandi175 – 1839Combined sources
Turni191 – 1966Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi208 – 2103Combined sources
Helixi213 – 2197Combined sources
Turni221 – 2233Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 2708Combined sources
Helixi271 – 2755Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi288 – 2903Combined sources
Turni299 – 3013Combined sources
Helixi304 – 3063Combined sources
Beta strandi311 – 3166Combined sources
Helixi322 – 3243Combined sources
Helixi330 – 3345Combined sources
Beta strandi340 – 3467Combined sources
Helixi353 – 3586Combined sources
Beta strandi364 – 3663Combined sources
Helixi374 – 3807Combined sources
Beta strandi391 – 3933Combined sources
Helixi402 – 4087Combined sources
Helixi409 – 4113Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi481 – 4833Combined sources
Helixi495 – 4973Combined sources
Beta strandi503 – 5053Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z81X-ray1.80A27-506[»]
2Z82X-ray2.60A27-506[»]
3A79X-ray2.90A1-506[»]
3A7BX-ray2.53A1-506[»]
3A7CX-ray2.40A1-506[»]
ProteinModelPortaliQ9QUN7.
SMRiQ9QUN7. Positions 27-784.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QUN7.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 587563ExtracellularSequence AnalysisAdd
BLAST
Topological domaini609 – 784176CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei588 – 60821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 7724LRR 11 PublicationAdd
BLAST
Repeati78 – 10124LRR 21 PublicationAdd
BLAST
Repeati102 – 12524LRR 31 PublicationAdd
BLAST
Repeati126 – 15025LRR 41 PublicationAdd
BLAST
Repeati151 – 17525LRR 51 PublicationAdd
BLAST
Repeati176 – 19924LRR 61 PublicationAdd
BLAST
Repeati200 – 22324LRR 71 PublicationAdd
BLAST
Repeati224 – 25027LRR 81 PublicationAdd
BLAST
Repeati251 – 27828LRR 91 PublicationAdd
BLAST
Repeati279 – 30830LRR 101 PublicationAdd
BLAST
Repeati309 – 33729LRR 111 PublicationAdd
BLAST
Repeati338 – 36124LRR 121 PublicationAdd
BLAST
Repeati362 – 38827LRR 131 PublicationAdd
BLAST
Repeati389 – 41426LRR 141 PublicationAdd
BLAST
Repeati415 – 43723LRR 151 PublicationAdd
BLAST
Repeati438 – 45720LRR 161 PublicationAdd
BLAST
Repeati458 – 47821LRR 171 PublicationAdd
BLAST
Repeati479 – 50022LRR 181 PublicationAdd
BLAST
Repeati501 – 52424LRR 191 PublicationAdd
BLAST
Domaini525 – 57652LRRCTAdd
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.
The ATG16L1-binding motif mediates interaction with ATG16L1.By similarity

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.
HOGENOMiHOG000110611.
HOVERGENiHBG108574.
InParanoidiQ9QUN7.
KOiK10159.
PhylomeDBiQ9QUN7.

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.
PfamiPF13504. LRR_7. 2 hits.
PF13855. LRR_8. 1 hit.
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. 9 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9QUN7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRALWLFWI LVAITVLFSK RCSAQESLSC DASGVCDGRS RSFTSIPSGL
60 70 80 90 100
TAAMKSLDLS FNKITYIGHG DLRACANLQV LILKSSRINT IEGDAFYSLG
110 120 130 140 150
SLEHLDLSDN HLSSLSSSWF GPLSSLKYLN LMGNPYQTLG VTSLFPNLTN
160 170 180 190 200
LQTLRIGNVE TFSEIRRIDF AGLTSLNELE IKALSLRNYQ SQSLKSIRDI
210 220 230 240 250
HHLTLHLSES AFLLEIFADI LSSVRYLELR DTNLARFQFS PLPVDEVSSP
260 270 280 290 300
MKKLAFRGSV LTDESFNELL KLLRYILELS EVEFDDCTLN GLGDFNPSES
310 320 330 340 350
DVVSELGKVE TVTIRRLHIP QFYLFYDLST VYSLLEKVKR ITVENSKVFL
360 370 380 390 400
VPCSFSQHLK SLEFLDLSEN LMVEEYLKNS ACKGAWPSLQ TLVLSQNHLR
410 420 430 440 450
SMQKTGEILL TLKNLTSLDI SRNTFHPMPD SCQWPEKMRF LNLSSTGIRV
460 470 480 490 500
VKTCIPQTLE VLDVSNNNLD SFSLFLPRLQ ELYISRNKLK TLPDASLFPV
510 520 530 540 550
LLVMKIRENA VSTFSKDQLG SFPKLETLEA GDNHFVCSCE LLSFTMETPA
560 570 580 590 600
LAQILVDWPD SYLCDSPPRL HGHRLQDARP SVLECHQAAL VSGVCCALLL
610 620 630 640 650
LILLVGALCH HFHGLWYLRM MWAWLQAKRK PKKAPCRDVC YDAFVSYSEQ
660 670 680 690 700
DSHWVENLMV QQLENSDPPF KLCLHKRDFV PGKWIIDNII DSIEKSHKTV
710 720 730 740 750
FVLSENFVRS EWCKYELDFS HFRLFDENND AAILVLLEPI ERKAIPQRFC
760 770 780
KLRKIMNTKT YLEWPLDEGQ QEVFWVNLRT AIKS
Length:784
Mass (Da):89,449
Last modified:May 1, 2000 - v1
Checksum:i606D56BF85F320A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591L → P in BAB23770. (PubMed:16141072)Curated
Sequence conflicti82 – 821I → M in BAB23770. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF185284 mRNA. Translation: AAF04277.1.
AF124741 mRNA. Translation: AAD46481.1.
AF216289 mRNA. Translation: AAF28345.1.
AF165189 mRNA. Translation: AAD49335.1.
AK005043 mRNA. Translation: BAB23770.1.
AK154504 mRNA. Translation: BAE32635.1.
CCDSiCCDS17435.1.
RefSeqiNP_036035.3. NM_011905.3.
UniGeneiMm.87596.

Genome annotation databases

GeneIDi24088.
KEGGimmu:24088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF185284 mRNA. Translation: AAF04277.1 .
AF124741 mRNA. Translation: AAD46481.1 .
AF216289 mRNA. Translation: AAF28345.1 .
AF165189 mRNA. Translation: AAD49335.1 .
AK005043 mRNA. Translation: BAB23770.1 .
AK154504 mRNA. Translation: BAE32635.1 .
CCDSi CCDS17435.1.
RefSeqi NP_036035.3. NM_011905.3.
UniGenei Mm.87596.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Z81 X-ray 1.80 A 27-506 [» ]
2Z82 X-ray 2.60 A 27-506 [» ]
3A79 X-ray 2.90 A 1-506 [» ]
3A7B X-ray 2.53 A 1-506 [» ]
3A7C X-ray 2.40 A 1-506 [» ]
ProteinModelPortali Q9QUN7.
SMRi Q9QUN7. Positions 27-784.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9QUN7. 2 interactions.
STRINGi 10090.ENSMUSP00000029623.

Chemistry

ChEMBLi CHEMBL3137289.

PTM databases

PhosphoSitei Q9QUN7.

Proteomic databases

PRIDEi Q9QUN7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24088.
KEGGi mmu:24088.

Organism-specific databases

CTDi 7097.
MGIi MGI:1346060. Tlr2.

Phylogenomic databases

eggNOGi NOG251801.
HOGENOMi HOG000110611.
HOVERGENi HBG108574.
InParanoidi Q9QUN7.
KOi K10159.
PhylomeDBi Q9QUN7.

Miscellaneous databases

EvolutionaryTracei Q9QUN7.
NextBioi 304101.
PROi Q9QUN7.
SOURCEi Search...

Gene expression databases

CleanExi MM_TLR2.
Genevestigatori Q9QUN7.

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 PF13504. LRR_7. 2 hits.
PF13855. LRR_8. 1 hit.
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. 9 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens."
    Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A.
    Nature 401:811-815(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-681.
  2. "Cells that carry a null allele for Toll-like receptor 2 are capable of responding to endotoxin."
    Heine H., Kirschning C.J., Lien E., Monks B.G., Rothe M., Golenbock D.T.
    J. Immunol. 162:6971-6975(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  3. "Gene expressions of lipopolysaccharide receptors, Toll-like receptors 2 and 4, are differently regulated in mouse T lymphocytes."
    Matsuguchi T., Takagi K., Musikacharoen T., Yoshikai Y.
    Blood 95:1378-1385(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  4. "The lipopolysaccharide-activated Toll-like receptor (TLR)-4 induces synthesis of the closely related receptor TLR-2 in adipocytes."
    Lin Y., Lee H., Berg A.H., Lisanti M.P., Shapiro L., Scherer P.E.
    J. Biol. Chem. 275:24255-24263(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipocyte.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver.
  6. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 405-413 AND 754-759, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  7. "A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors."
    Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K.
    Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNPY3.
  8. "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 27-506, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442.
  9. "Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer."
    Kang J.Y., Nan X., Jin M.S., Youn S.J., Ryu Y.H., Mah S., Han S.H., Lee H., Paik S.G., Lee J.O.
    Immunity 31:873-884(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-506 IN COMPLEX WITH TLR6 AND LIPOPEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442, FUNCTION, LRR REPEATS, SUBUNIT.

Entry informationi

Entry nameiTLR2_MOUSE
AccessioniPrimary (citable) accession number: Q9QUN7
Secondary accession number(s): Q3U400, Q9DBC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3