TLR2
entrez
7097
canonical
uniprot
O60603
canonical
ensembl
ENSG00000137462
resolver
ensp
ENSP00000260010
resolver
ensp
ENSP00000493968
resolver
ensp
ENSP00000494425
resolver
ensp
ENSP00000495339
resolver
ensp
ENSP00000496208
resolver
ensp
ENSP00000496676
resolver
ensp
ENSP00000519700
resolver
ensp
ENSP00000519701
resolver
ensp
ENSP00000519702
resolver
ensp
ENSP00000519703
resolver
ensp
ENSP00000519704
resolver
ensp
ENSP00000525845
resolver
ensp
ENSP00000525846
resolver
ensp
ENSP00000525847
resolver
ensp
ENSP00000525848
resolver
ensp
ENSP00000525849
resolver
ensp
ENSP00000525850
resolver
ensp
ENSP00000525851
resolver
ensp
ENSP00000584292
resolver
ensp
ENSP00000584293
resolver
ensp
ENSP00000636851
resolver
ensp
ENSP00000636852
resolver
ensp
ENSP00000636853
resolver
ensp
ENSP00000636854
resolver
ensp
ENSP00000636855
resolver
ensp
ENSP00000636856
resolver
ensp
ENSP00000636857
resolver
ensp
ENSP00000636858
resolver
ensp
ENSP00000636859
resolver
enst
ENST00000260010
resolver
enst
ENST00000642580
resolver
enst
ENST00000642700
resolver
enst
ENST00000643501
resolver
enst
ENST00000646219
resolver
enst
ENST00000646900
resolver
enst
ENST00000714431
resolver
enst
ENST00000714432
resolver
enst
ENST00000714433
resolver
enst
ENST00000714434
resolver
enst
ENST00000714435
resolver
enst
ENST00000855786
resolver
enst
ENST00000855787
resolver
enst
ENST00000855788
resolver
enst
ENST00000855789
resolver
enst
ENST00000855790
resolver
enst
ENST00000855791
resolver
enst
ENST00000855792
resolver
enst
ENST00000914233
resolver
enst
ENST00000914234
resolver
enst
ENST00000966792
resolver
enst
ENST00000966793
resolver
enst
ENST00000966794
resolver
enst
ENST00000966795
resolver
enst
ENST00000966796
resolver
enst
ENST00000966797
resolver
enst
ENST00000966798
resolver
enst
ENST00000966799
resolver
enst
ENST00000966800
resolver
genesymbol
TLR2
resolver
genesymbol_syn
TIL4
resolver
hgnc
HGNC:11848
resolver
uniprot
A0A0S2Z4S4
resolver
uniprot
B3KWR9
resolver
uniprot
B3Y612
resolver
uniprot
D1CS45
resolver
uniprot
D1CS48
resolver
uniprot
D1CS49
resolver
uniprot
O15454
resolver
uniprot
Q8NI00
resolver
uniprot_entry
A0A0S2Z4S4_HUMAN
resolver
uniprot_entry
B3KWR9_HUMAN
resolver
uniprot_entry
TLR2_HUMAN
resolver
uniprot_sec
B3Y612
resolver
uniprot_sec
D1CS45
resolver
uniprot_sec
D1CS48
resolver
uniprot_sec
D1CS49
resolver
uniprot_sec
O15454
resolver
uniprot_sec
Q8NI00
resolver
amino_acid_sequence
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS
uniprot
proteins
function
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651, PubMed:21078852). 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). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:10426996, ECO:0000269|PubMed:11441107, ECO:0000269|PubMed:15809303, ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21078852}.
uniprot
proteins
mass_dalton
89838
uniprot
proteins
mutagenesis
MUTAGEN 114; /note="N->S: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain."; /evidence="ECO:0000269|PubMed:15173186"; MUTAGEN 199; /note="N->D: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain."; /evidence="ECO:0000269|PubMed:15173186"; MUTAGEN 416; /note="T->A: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain."; /evidence="ECO:0000269|PubMed:15173186"; MUTAGEN 442; /note="N->D: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain."; /evidence="ECO:0000269|PubMed:15173186"; MUTAGEN 681; /note="P->F: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain."; /evidence="ECO:0000269|PubMed:11081518"; MUTAGEN 709; /note="K->R: Reduced protein stability."; /evidence="ECO:0000269|PubMed:27805901"; MUTAGEN 714; /note="K->R: Reduced protein stability."; /evidence="ECO:0000269|PubMed:27805901"; MUTAGEN 742..743; /note="KK->RR: Reduced protein stability."; /evidence="ECO:0000269|PubMed:27805901"; MUTAGEN 751; /note="K->R: Reduced protein stability."; /evidence="ECO:0000269|PubMed:27805901"; MUTAGEN 754; /note="K->R: Loss of PPP1R11-mediated ubiquitination and degradation."; /evidence="ECO:0000269|PubMed:27805901
uniprot
proteins
post_translational_modification
PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000269|PubMed:15173186, ECO:0000269|PubMed:17889651}.; PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation (PubMed:27805901). Deubiquitinated by USP2 (By similarity). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:27805901}.
uniprot
proteins
protein_family
Toll-like receptor family
uniprot
proteins
pubmed
10426995
uniprot
proteins
pubmed
10426996
uniprot
proteins
pubmed
11081518
uniprot
proteins
pubmed
11441107
uniprot
proteins
pubmed
11476982
uniprot
proteins
pubmed
12471095
uniprot
proteins
pubmed
12646604
uniprot
proteins
pubmed
15173186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15809303
uniprot
proteins
pubmed
16622205
uniprot
proteins
pubmed
16880211
uniprot
proteins
pubmed
17322885
uniprot
proteins
pubmed
17889651
uniprot
proteins
pubmed
18810425
uniprot
proteins
pubmed
19362712
uniprot
proteins
pubmed
19924287
uniprot
proteins
pubmed
20800577
uniprot
proteins
pubmed
21078852
uniprot
proteins
pubmed
21618349
uniprot
proteins
pubmed
22665377
uniprot
proteins
pubmed
23376921
uniprot
proteins
pubmed
25385819
uniprot
proteins
pubmed
27805901
uniprot
proteins
pubmed
34133077
uniprot
proteins
pubmed
9435236
uniprot
proteins
pubmed
9596645
uniprot
proteins
pubmed
9751057
uniprot
proteins
sequence_length
784
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:16880211}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determines the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000269|PubMed:16880211}.
uniprot
proteins
transmembrane_region
TRANSMEM 589..609; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins