dbPTM

TLR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TLR2_HUMAN
UniProt AC	O60603
Protein Name	Toll-like receptor 2
Gene Name	TLR2
Organism	Homo sapiens (Human).
Sequence Length	784
Subcellular Localization	Membrane Single-pass type I membrane protein . Cytoplasmic vesicle, phagosome membrane Single-pass type I membrane protein . Membrane raft . Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the prese
Protein Description	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]
Protein Sequence	MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNIDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	WVLGVIISLSKEESS HHHHHHHHCCCHHCC	18.57	24719451
45	Phosphorylation	GSSGSLNSIPSGLTE CCCCCCCCCCCCHHH	40.96	-
48	Phosphorylation	GSLNSIPSGLTEAVK CCCCCCCCCHHHHHH	44.77	-
114	N-linked_Glycosylation	LSYNYLSNLSSSWFK CCHHHHHCCCCCCCC	41.15	15173186
138	Phosphorylation	LLGNPYKTLGETSLF HCCCCCCCCCCCCHH	33.87	-
142	Phosphorylation	PYKTLGETSLFSHLT CCCCCCCCCHHHHHH	29.00	-
143	Phosphorylation	YKTLGETSLFSHLTK CCCCCCCCHHHHHHH	24.10	27732954
146	Phosphorylation	LGETSLFSHLTKLQI CCCCCHHHHHHHHHE	23.92	27732954
149	Phosphorylation	TSLFSHLTKLQILRV CCHHHHHHHHHEEEE	25.04	27732954
193	Phosphorylation	LQSYEPKSLKSIQNV HHHCCCCCHHHHHHH	52.31	24719451
196	Phosphorylation	YEPKSLKSIQNVSHL CCCCCHHHHHHHHHH	34.40	24719451
199	N-linked_Glycosylation	KSLKSIQNVSHLILH CCHHHHHHHHHHHHH	35.27	15173186
249	Phosphorylation	LSTGETNSLIKKFTF CCCCCCCCHHHHHHC	38.60	24719451
262	Phosphorylation	TFRNVKITDESLFQV HCCCCCCCCHHHHHH	28.17	-
323	Phosphorylation	RLHIPRFYLFYDLST ECCCCEEEEEEEHHH	9.36	-
346	Phosphorylation	KRITVENSKVFLVPC HHCEECCCEEEHHHH	19.38	22210691
401	Phosphorylation	LRQNHLASLEKTGET HHHCCHHHHHHHCCE	43.34	29396449
405	Phosphorylation	HLASLEKTGETLLTL CHHHHHHHCCEEEEE	30.76	29396449
408	Phosphorylation	SLEKTGETLLTLKNL HHHHHCCEEEEECCC	28.54	29396449
411	Phosphorylation	KTGETLLTLKNLTNI HHCCEEEEECCCCCC	38.51	29396449
414	N-linked_Glycosylation	ETLLTLKNLTNIDIS CEEEEECCCCCCCCC	56.03	17889651
440	Phosphorylation	QWPEKMKYLNLSSTR CCCCHHCEECCCCCE	9.42	26074081
442	N-linked_Glycosylation	PEKMKYLNLSSTRIH CCHHCEECCCCCEEE	34.48	15173186
444	Phosphorylation	KMKYLNLSSTRIHSV HHCEECCCCCEEEEE	28.70	26074081
445	Phosphorylation	MKYLNLSSTRIHSVT HCEECCCCCEEEEEC	25.52	26074081
446	Phosphorylation	KYLNLSSTRIHSVTG CEECCCCCEEEEECC	30.21	26074081
450	Phosphorylation	LSSTRIHSVTGCIPK CCCCEEEEECCCCCC	21.00	26074081
452	Phosphorylation	STRIHSVTGCIPKTL CCEEEEECCCCCCCE	29.38	26074081
609	S-palmitoylation	ILLTGVLCHRFHGLW HHHHHHHHHHHHHHH	1.69	25371237
653	Phosphorylation	SYSERDAYWVENLMV CHHHHHHHHHHHHHH	17.80	-
754	Ubiquitination	QRFCKLRKIMNTKTY HHHHHHHHHHCCCCC	57.66	PubMed
758	Phosphorylation	KLRKIMNTKTYLEWP HHHHHHCCCCCEECC	13.84	29759185
761	Phosphorylation	KIMNTKTYLEWPMDE HHHCCCCCEECCCCH	12.27	29759185

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of TLR2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
442	N	Glycosylation	15173186
Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2.
754	K	ubiquitylation	27805901
Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TLR2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LY96_HUMAN	LY96	physical	11160242
TOLIP_HUMAN	TOLLIP	physical	11751856
TLR1_HUMAN	TLR1	physical	12077222
TLR2_HUMAN	TLR2	physical	10395652
IRAK1_HUMAN	IRAK1	physical	10395652
TIRAP_HUMAN	TIRAP	physical	17258210
TIRAP_HUMAN	TIRAP	physical	18221795
CLC4M_HUMAN	CLEC4M	physical	21899704
CLC7A_HUMAN	CLEC7A	physical	21899704
GAG_HV1H2	gag	physical	26347747
STA5A_HUMAN	STAT5A	physical	28514442
TM214_HUMAN	TMEM214	physical	28514442
AVR2A_HUMAN	ACVR2A	physical	28514442
BMR1A_HUMAN	BMPR1A	physical	28514442
IPRI_HUMAN	ITPRIP	physical	28514442
UBP33_HUMAN	USP33	physical	28514442
S11IP_HUMAN	STK11IP	physical	28514442
LGR4_HUMAN	LGR4	physical	28514442
AP1M1_HUMAN	AP1M1	physical	28514442

Drug and Disease Associations

Kegg Disease
H00344	Leprosy; Hansen disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TLR2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of the TLR1-TLR2 heterodimer induced by binding ofa 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). Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-509 IN COMPLEX WITH TLR1AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, AND GLYCOSYLATIONAT ASN-114; ASN-199; ASN-414 AND ASN-442.	17889651 [Abstract]
"Four N-linked glycosylation sites in human toll-like receptor 2cooperate to direct efficient biosynthesis and secretion."; Weber A.N., Morse M.A., Gay N.J.; J. Biol. Chem. 279:34589-34594(2004). Cited for: GLYCOSYLATION AT ASN-114; ASN-199 AND ASN-442, AND MUTAGENESIS OFASN-114; ASN-199; THR-416 AND ASN-442.	15173186 [Abstract]

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