dbPTM

TLR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TLR1_HUMAN
UniProt AC	Q15399
Protein Name	Toll-like receptor 1
Gene Name	TLR1
Organism	Homo sapiens (Human).
Sequence Length	786
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Cytoplasmic vesicle, phagosome membrane Single-pass type I membrane protein . Membrane raft . Golgi apparatus . Does not reside in lipid rafts before stimulation but accumulates increasingly in
Protein Description	Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. [PubMed: 21078852 Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway]
Protein Sequence	MTSIFHFAIIFMLILQIRIQLSEESEFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELGEFVKNIDQVSSEVLEGWPDSYKCDYPESYRGTLLKDFHMSELSCNITLLIVTIVATMLVLAVTVTSLCSYLDLPWYLRMVCQWTQTRRRARNIPLEELQRNLQFHAFISYSGHDSFWVKNELLPNLEKEGMQICLHERNFVPGKSIVENIITCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHNLFHEGSNSLILILLEPIPQYSIPSSYHKLKSLMARRTYLEWPKEKSKRGLFWANLRAAINIKLTEQAKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTSIFHFAI ------CCHHHHHHH	30.45	24043423
3	Phosphorylation	-----MTSIFHFAII -----CCHHHHHHHH	23.20	24043423
44	Phosphorylation	IHVPKDLSQKTTILN EECCCCHHCCCEEEE	39.50	-
48	Phosphorylation	KDLSQKTTILNISQN CCHHCCCEEEEECHH	30.42	-
51	N-linked_Glycosylation	SQKTTILNISQNYIS HCCCEEEEECHHHHH	28.19	17889651
53	Phosphorylation	KTTILNISQNYISEL CCEEEEECHHHHHHH	15.99	-
56	Phosphorylation	ILNISQNYISELWTS EEEECHHHHHHHHHH	9.74	-
67	Phosphorylation	LWTSDILSLSKLRIL HHHHHHHHCCCCEEE	30.82	24719451
137	N-linked_Glycosylation	PICKEFGNMSQLKFL HHHHHHCCHHHHHHC	32.05	UniProtKB CARBOHYD
148	Phosphorylation	LKFLGLSTTHLEKSS HHHCCCCCCCCCCCC	24.23	27251275
149	Phosphorylation	KFLGLSTTHLEKSSV HHCCCCCCCCCCCCC	22.53	27251275
154	Phosphorylation	STTHLEKSSVLPIAH CCCCCCCCCCCCEEE	19.12	22210691
155	Phosphorylation	TTHLEKSSVLPIAHL CCCCCCCCCCCEEEC	38.45	22210691
163	N-linked_Glycosylation	VLPIAHLNISKVLLV CCCEEECCHHHHHHH	26.98	17889651
330	N-linked_Glycosylation	FSNMNIKNFTVSGTR HHCCCCEEEEEECCE	33.74	17889651
416	Methylation	SVSYDEKKGDCSWTK CCCCCCCCCCCHHHH	58.91	-
416	Trimethylation	SVSYDEKKGDCSWTK CCCCCCCCCCCHHHH	58.91	-
420	Phosphorylation	DEKKGDCSWTKSLLS CCCCCCCHHHHHHHC	42.39	-
422	Phosphorylation	KKGDCSWTKSLLSLN CCCCCHHHHHHHCCC	8.41	-
429	N-linked_Glycosylation	TKSLLSLNMSSNILT HHHHHCCCCCCCCCH	25.55	17889651
431	Phosphorylation	SLLSLNMSSNILTDT HHHCCCCCCCCCHHH	21.11	-
529	Phosphorylation	GDNPFQCTCELGEFV CCCCEEEEEEHHHHH	9.76	-
537	Ubiquitination	CELGEFVKNIDQVSS EEHHHHHHCHHHHCH	54.21	-
578	N-linked_Glycosylation	HMSELSCNITLLIVT CHHHHHCCCHHHHHH	27.23	UniProtKB CARBOHYD
678	Phosphorylation	RNFVPGKSIVENIIT CCCCCCHHHHHHHHH	37.47	-
685	Phosphorylation	SIVENIITCIEKSYK HHHHHHHHHHHHHCC	12.02	-
690	Phosphorylation	IITCIEKSYKSIFVL HHHHHHHHCCEEEEE	25.63	-
691	Phosphorylation	ITCIEKSYKSIFVLS HHHHHHHCCEEEEEC	21.59	-

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 TLR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TLR1_HUMAN !!

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 TLR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLR2_HUMAN	TLR2	physical	12077222
TLR6_HUMAN	TLR6	physical	28514442
A16A1_HUMAN	ALDH16A1	physical	28514442
DEOC_HUMAN	DERA	physical	28514442
CNPY3_HUMAN	CNPY3	physical	28514442
TBC24_HUMAN	TBC1D24	physical	28514442
TM214_HUMAN	TMEM214	physical	28514442
PLXB2_HUMAN	PLXNB2	physical	28514442
MAVS_HUMAN	MAVS	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 TLR1_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 (2.1 ANGSTROMS) OF 25-476 IN COMPLEX WITH TLR1AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, AND GLYCOSYLATIONAT ASN-51; ASN-163; ASN-330 AND ASN-429.	17889651 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163, AND MASSSPECTROMETRY.	19159218 [Abstract]