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UniProtKB - O60603 (TLR2_HUMAN)

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Protein

Toll-like receptor 2

Gene

TLR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:21078852, PubMed:17889651). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins (PubMed:10426995, PubMed:10426996). 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 (PubMed:11441107). Stimulation of monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4 (PubMed:16622205). MAPK activation in response to bacterial peptidoglycan also occurs via this receptor (PubMed:16622205). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36); the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse) (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (By similarity).By similarity9 Publications

GO - Molecular functioni

  • amyloid-beta binding Source: ARUK-UCL
  • identical protein binding Source: IntAct
  • lipopolysaccharide binding Source: UniProtKB
  • lipopolysaccharide receptor activity Source: UniProtKB
  • peptidoglycan binding Source: UniProtKB
  • protein-containing complex binding Source: ARUK-UCL
  • protein heterodimerization activity Source: MGI
  • signaling pattern recognition receptor activity Source: UniProtKB
  • signaling receptor activity Source: ProtInc
  • Toll-like receptor binding Source: UniProtKB
  • triacyl lipopeptide binding Source: MGI
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • apoptotic process Source: ProtInc
  • cell activation Source: AgBase
  • cellular response to bacterial lipopeptide Source: BHF-UCL
  • cellular response to diacyl bacterial lipopeptide Source: UniProtKB
  • cellular response to interferon-gamma Source: UniProtKB
  • cellular response to lipoteichoic acid Source: MGI
  • cellular response to triacyl bacterial lipopeptide Source: UniProtKB
  • central nervous system myelin formation Source: Ensembl
  • cytokine secretion involved in immune response Source: CACAO
  • defense response to Gram-positive bacterium Source: UniProtKB
  • detection of diacyl bacterial lipopeptide Source: MGI
  • detection of triacyl bacterial lipopeptide Source: MGI
  • I-kappaB phosphorylation Source: BHF-UCL
  • immune response Source: ProtInc
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: BHF-UCL
  • interleukin-10 production Source: CACAO
  • learning Source: ARUK-UCL
  • leukotriene metabolic process Source: Ensembl
  • microglia development Source: ARUK-UCL
  • microglial cell activation Source: Ensembl
  • MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of phagocytosis Source: ARUK-UCL
  • negative regulation of synapse assembly Source: ARUK-UCL
  • neutrophil degranulation Source: Reactome
  • nitric oxide metabolic process Source: Ensembl
  • positive regulation of cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  • positive regulation of chemokine production Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of inflammatory response Source: BHF-UCL
  • positive regulation of interferon-beta production Source: BHF-UCL
  • positive regulation of interleukin-10 production Source: Ensembl
  • positive regulation of interleukin-12 production Source: BHF-UCL
  • positive regulation of interleukin-18 production Source: BHF-UCL
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of interleukin-8 production Source: BHF-UCL
  • positive regulation of interleukin-8 secretion Source: ARUK-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of NIK/NF-kappaB signaling Source: BHF-UCL
  • positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • positive regulation of oligodendrocyte differentiation Source: Ensembl
  • positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
  • positive regulation of transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of Wnt signaling pathway Source: BHF-UCL
  • response to fatty acid Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to insulin Source: Ensembl
  • response to progesterone Source: Ensembl
  • response to toxic substance Source: Ensembl
  • signal transduction Source: UniProtKB
  • toll-like receptor 2 signaling pathway Source: InterPro
  • toll-like receptor signaling pathway Source: Reactome
  • toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  • toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  • tumor necrosis factor production Source: ARUK-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionReceptor
Biological processImmunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-HSA-1236974 ER-Phagosome pathway
R-HSA-1461957 Beta defensins
R-HSA-166058 MyD88:Mal cascade initiated on plasma membrane
R-HSA-168179 Toll Like Receptor TLR1:TLR2 Cascade
R-HSA-168188 Toll Like Receptor TLR6:TLR2 Cascade
R-HSA-5602498 MyD88 deficiency (TLR2/4)
R-HSA-5603041 IRAK4 deficiency (TLR2/4)
R-HSA-5686938 Regulation of TLR by endogenous ligand
R-HSA-6798695 Neutrophil degranulation
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000137462.6
HGNCiHGNC:11848 TLR2
MIMi603028 gene
neXtProtiNX_O60603

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 588ExtracellularSequence analysisAdd BLAST568
Transmembranei589 – 609HelicalSequence analysisAdd BLAST21
Topological domaini610 – 784CytoplasmicSequence analysisAdd BLAST175

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114N → S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi199N → D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi416T → A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi442N → D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain. 1 Publication1
Mutagenesisi681P → F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain. 1 Publication1
Mutagenesisi709K → R: Reduced protein stability. 1 Publication1
Mutagenesisi714K → R: Reduced protein stability. 1 Publication1
Mutagenesisi742 – 743KK → RR: Reduced protein stability. 1 Publication2
Mutagenesisi751K → R: Reduced protein stability. 1 Publication1
Mutagenesisi754K → R: Loss of PPP1R11-mediated ubiquitination and degradation. 1 Publication1

Organism-specific databases

DisGeNETi7097
MalaCardsiTLR2
MIMi246300 phenotype
OpenTargetsiENSG00000137462
PharmGKBiPA36550

Chemistry databases

ChEMBLiCHEMBL4163
DrugBankiDB00045 OspA lipoprotein
DB03963 S-(Dimethylarsenic)Cysteine
DB05475 SCV-07
GuidetoPHARMACOLOGYi1752

Polymorphism and mutation databases

BioMutaiTLR2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003471021 – 784Toll-like receptor 2Add BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 361 Publication
Glycosylationi114N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi199N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi353 ↔ 3821 Publication
Glycosylationi414N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi432 ↔ 4541 Publication
Glycosylationi442N-linked (GlcNAc...) asparagine2 Publications1
Cross-linki754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2.2 Publications
Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation (PubMed:27805901). Deubiquitinated by USP2 (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiO60603
PaxDbiO60603
PeptideAtlasiO60603
PRIDEiO60603
ProteomicsDBi49481

PTM databases

iPTMnetiO60603
PhosphoSitePlusiO60603
SwissPalmiO60603

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

BgeeiENSG00000137462
CleanExiHS_TLR2
ExpressionAtlasiO60603 baseline and differential
GenevisibleiO60603 HS

Organism-specific databases

HPAiHPA060231
HPA071546

Interactioni

Subunit structurei

Interacts with LY96, TLR1 and TLR6 (via extracellular domain) (PubMed:17889651). TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before stimulation by the ligand. The heterodimers form bigger oligomers in response to their corresponding ligands as well as further heterotypic associations with other receptors such as CD14 and/or CD36 (PubMed:16880211). Binds MYD88 (via TIR domain). Interacts with TICAM1 (PubMed:12471095). Interacts with CNPY3 (By similarity). Interacts with ATG16L1 (PubMed:23376921). Interacts with PPP1R11 (By similarity).By similarity4 Publications
(Microbial infection) Interacts with M.tuberculosis EsxA.1 Publication
(Microbial infection) Interacts with M.bovis MPB83.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei349Interaction with bacterial lipopeptide1

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: MGI
  • Toll-like receptor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi112952, 27 interactors
DIPiDIP-35138N
IntActiO60603, 28 interactors
MINTiO60603
STRINGi9606.ENSP00000260010

Chemistry databases

BindingDBiO60603

Structurei

Secondary structure

1784
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Beta strandi56 – 58Combined sources3
Turni69 – 74Combined sources6
Beta strandi80 – 82Combined sources3
Turni93 – 98Combined sources6
Beta strandi104 – 106Combined sources3
Helixi117 – 120Combined sources4
Beta strandi127 – 130Combined sources4
Beta strandi137 – 139Combined sources3
Beta strandi153 – 161Combined sources9
Turni167 – 172Combined sources6
Beta strandi175 – 183Combined sources9
Turni191 – 196Combined sources6
Beta strandi198 – 206Combined sources9
Helixi213 – 220Combined sources8
Turni221 – 223Combined sources3
Beta strandi224 – 231Combined sources8
Beta strandi253 – 258Combined sources6
Beta strandi260 – 262Combined sources3
Helixi263 – 274Combined sources12
Beta strandi281 – 283Combined sources3
Beta strandi288 – 291Combined sources4
Beta strandi311 – 316Combined sources6
Helixi322 – 324Combined sources3
Helixi329 – 334Combined sources6
Beta strandi340 – 346Combined sources7
Helixi353 – 358Combined sources6
Beta strandi364 – 366Combined sources3
Helixi374 – 380Combined sources7
Beta strandi391 – 393Combined sources3
Helixi402 – 408Combined sources7
Helixi409 – 411Combined sources3
Beta strandi417 – 419Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi460 – 463Combined sources4
Beta strandi481 – 483Combined sources3
Helixi495 – 497Combined sources3
Beta strandi503 – 505Combined sources3
Helixi518 – 520Combined sources3
Beta strandi527 – 529Combined sources3
Helixi539 – 544Combined sources6
Turni545 – 547Combined sources3
Beta strandi548 – 550Combined sources3
Beta strandi641 – 646Combined sources6
Helixi649 – 651Combined sources3
Helixi652 – 656Combined sources5
Helixi658 – 663Combined sources6
Beta strandi666 – 668Combined sources3
Beta strandi672 – 674Combined sources3
Helixi675 – 678Combined sources4
Beta strandi681 – 683Combined sources3
Helixi685 – 695Combined sources11
Beta strandi696 – 703Combined sources8
Helixi705 – 711Combined sources7
Helixi713 – 716Combined sources4
Turni717 – 719Combined sources3
Helixi720 – 722Combined sources3
Turni723 – 725Combined sources3
Helixi726 – 728Combined sources3
Beta strandi733 – 738Combined sources6
Turni742 – 744Combined sources3
Helixi750 – 758Combined sources9
Beta strandi761 – 763Combined sources3
Helixi768 – 770Combined sources3
Helixi771 – 783Combined sources13

3D structure databases

ProteinModelPortaliO60603
SMRiO60603
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60603

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati54 – 77LRR 1Add BLAST24
Repeati78 – 101LRR 2Add BLAST24
Repeati102 – 125LRR 3Add BLAST24
Repeati126 – 150LRR 4Add BLAST25
Repeati151 – 175LRR 5Add BLAST25
Repeati176 – 199LRR 6Add BLAST24
Repeati200 – 223LRR 7Add BLAST24
Repeati224 – 250LRR 8Add BLAST27
Repeati251 – 278LRR 9Add BLAST28
Repeati279 – 308LRR 10Add BLAST30
Repeati309 – 337LRR 11Add BLAST29
Repeati338 – 361LRR 12Add BLAST24
Repeati362 – 388LRR 13Add BLAST27
Repeati389 – 414LRR 14Add BLAST26
Repeati415 – 437LRR 15Add BLAST23
Repeati438 – 457LRR 16Add BLAST20
Repeati458 – 478LRR 17Add BLAST21
Repeati479 – 500LRR 18Add BLAST22
Repeati501 – 524LRR 19Add BLAST24
Domaini525 – 579LRRCTAdd BLAST55
Domaini639 – 784TIRPROSITE-ProRule annotationAdd BLAST146

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi761 – 778ATG16L1-binding motifAdd BLAST18

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

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4641 Eukaryota
COG4886 LUCA
GeneTreeiENSGT00760000119006
HOGENOMiHOG000110611
HOVERGENiHBG108574
InParanoidiO60603
KOiK10159
OMAiIPQRFCK
OrthoDBiEOG091G05L8
PhylomeDBiO60603
TreeFamiTF351113

Family and domain databases

Gene3Di3.40.50.10140, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR000483 Cys-rich_flank_reg_C
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR000157 TIR_dom
IPR027185 TLR2
IPR035897 Toll_tir_struct_dom_sf
PANTHERiPTHR24365:SF17 PTHR24365:SF17, 1 hit
PfamiView protein in Pfam
PF13855 LRR_8, 2 hits
PF01463 LRRCT, 1 hit
PF01582 TIR, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 7 hits
SM00082 LRRCT, 1 hit
SM00255 TIR, 1 hit
SUPFAMiSSF52200 SSF52200, 1 hit
PROSITEiView protein in PROSITE
PS51450 LRR, 11 hits
PS50104 TIR, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti59L → Q in AAM23001 (Ref. 8) Curated1
Sequence conflicti68S → C in AAM23001 (Ref. 8) Curated1
Sequence conflicti726D → E in AAC34133 (PubMed:9435236).Curated1

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.2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06634989N → D1 PublicationCorresponds to variant dbSNP:rs137853176EnsemblClinVar.1
Natural variantiVAR_026765411T → I Reduces TLR2-mediated NF-kappa-B activation. 1 PublicationCorresponds to variant dbSNP:rs5743699Ensembl.1
Natural variantiVAR_066350571R → H1 PublicationCorresponds to variant dbSNP:rs61735277Ensembl.1
Natural variantiVAR_026766579R → H. Corresponds to variant dbSNP:rs5743703Ensembl.1
Natural variantiVAR_024663631P → H Reduces TLR2-mediated NF-kappa-B activation. 2 PublicationsCorresponds to variant dbSNP:rs5743704Ensembl.1
Natural variantiVAR_066351636S → R1 PublicationCorresponds to variant dbSNP:rs137853177EnsemblClinVar.1
Natural variantiVAR_031236677R → W2 PublicationsCorresponds to variant dbSNP:rs121917864EnsemblClinVar.1
Natural variantiVAR_052360715Y → N. Corresponds to variant dbSNP:rs5743706Ensembl.1
Natural variantiVAR_031237753R → Q Reduces TLR2-mediated NF-kappa-B activation. 2 PublicationsCorresponds to variant dbSNP:rs5743708EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001305716.1, NM_001318787.1
NP_001305718.1, NM_001318789.1
NP_001305719.1, NM_001318790.1
NP_001305720.1, NM_001318791.1
NP_001305722.1, NM_001318793.1
NP_001305724.1, NM_001318795.1
NP_001305725.1, NM_001318796.1
NP_003255.2, NM_003264.4
XP_011530517.1, XM_011532215.2
XP_011530518.1, XM_011532216.2
XP_016864062.1, XM_017008573.1
XP_016864063.1, XM_017008574.1
XP_016864064.1, XM_017008575.1
XP_016864065.1, XM_017008576.1
UniGeneiHs.519033

Genome annotation databases

EnsembliENST00000260010; ENSP00000260010; ENSG00000137462
ENST00000642580; ENSP00000495339; ENSG00000137462
ENST00000642700; ENSP00000494425; ENSG00000137462
ENST00000644308; ENSP00000496321; ENSG00000137462
GeneIDi7097
KEGGihsa:7097
UCSCiuc063aif.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTLR2_HUMAN
AccessioniPrimary (citable) accession number: O60603
Secondary accession number(s): B3Y612
, D1CS45, D1CS48, D1CS49, O15454, Q8NI00
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: August 1, 1998
Last modified: July 18, 2018
This is version 202 of the entry and version 1 of the sequence. See 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

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