TLR8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TLR8_HUMAN
• UniProt AC: Q9NR97
• Protein Name: Toll-like receptor 8
• Gene Name: TLR8
• Organism: Homo sapiens (Human).
• Sequence Length: 1041
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response..
• Protein Sequence: MENMFLQSSMLTCIFLLISGSCELCAEENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGNPGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKVCEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFPCVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSFNYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLSENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPDIACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNLKVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASLTELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSNLLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDVTAVILFFFTFFITTMVMLAALAHHLFYWDVWFIYNVCLAKVKGYRSLSTSQTFYDAYISYDTKDASVTDWVINELRYHLEESRDKNVLLCLEERDWDPGLAIIDNLMQSINQSKKTVFVLTKKYAKSWNFKTAFYLALQRLMDENMDVIIFILLEPVLQHSQYLRLRQRICKSSILQWPDNPKAEGLFWQTLRNVVLTENDSRYNNMYVDSIKQY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	N-linked_Glycosylation	CELCAEENFSRSYPC CHHHHHCCCCCCCCC	31.53	UniProtKB CARBOHYD
42	N-linked_Glycosylation	PCDEKKQNDSVIAEC CCCCHHCCCCHHHHH	53.02	UniProtKB CARBOHYD
80	N-linked_Glycosylation	NFITHITNESFQGLQ CEEHHHCCCCCHHHH	42.16	19159218
88	N-linked_Glycosylation	ESFQGLQNLTKINLN CCCHHHHHCCEEECC	55.51	19159218
115	N-linked_Glycosylation	GIQSNGLNITDGAFL CCCCCCCCCCCCCEE	36.19	UniProtKB CARBOHYD
160	N-linked_Glycosylation	LIQNNIYNITKEGIS HHHCCCHHCCHHHHH	31.49	UniProtKB CARBOHYD
247	N-linked_Glycosylation	EDFKGLINLTLLDLS HHHCHHHEEEEEECC	31.83	UniProtKB CARBOHYD
285	N-linked_Glycosylation	IDRFAFQNLTQLRYL ECHHHHCCCCHHHHC	38.30	UniProtKB CARBOHYD
293	N-linked_Glycosylation	LTQLRYLNLSSTSLR CCHHHHCCCCCCCHH	29.01	23520111
345	Phosphorylation	RLEILDLSFNYIKGS CCEEEEEECCCCCCC	15.88	24719451
348	Phosphorylation	ILDLSFNYIKGSYPQ EEEEECCCCCCCCCC	11.29	24719451
358	N-linked_Glycosylation	GSYPQHINISRNFSK CCCCCCEEECCCHHH	24.86	UniProtKB CARBOHYD
362	N-linked_Glycosylation	QHINISRNFSKLLSL CCEEECCCHHHHHHH	38.46	UniProtKB CARBOHYD
368	Phosphorylation	RNFSKLLSLRALHLR CCHHHHHHHHHHHHH	26.67	-
395	N-linked_Glycosylation	QPLMQLPNLSTINLG HHHHCCCCCCEEEEC	56.04	23520111
416	N-linked_Glycosylation	IDFKLFQNFSNLEII CCHHHCCCCCCCEEE	34.67	UniProtKB CARBOHYD
431	Phosphorylation	YLSENRISPLVKDTR EEECCCCCHHHHHHH	14.67	24719451
443	N-linked_Glycosylation	DTRQSYANSSSFQRH HHHHHHHCCHHHHHH	33.90	UniProtKB CARBOHYD
511	N-linked_Glycosylation	LPDIACLNLSANSNA CCCEEEEECCCCCCC	31.65	23520111
546	N-linked_Glycosylation	NNRLDFDNASALTEL CCCCCCCCCHHHHHC	35.47	23520111
582	N-linked_Glycosylation	HHLEFIQNFTNLKVL HHHHHHHHCCCCEEE	40.68	UniProtKB CARBOHYD
590	N-linked_Glycosylation	FTNLKVLNLSHNNIY CCCCEEEECCCCCEE	42.35	23520111
633	Phosphorylation	DDDNRYISIFKGLKN CCCCCEEEHHHCCCC	17.03	24719451
640	N-linked_Glycosylation	SIFKGLKNLTRLDLS EHHHCCCCCCHHHCC	52.25	23520111
680	N-linked_Glycosylation	DNMLKFFNWTLLQQF HHHHHHCCHHHHHHC	33.68	23520111
736	Phosphorylation	SGFLSEVSSLKHLDL CCHHHHHHCCCCCCC	26.38	28060719
737	Phosphorylation	GFLSEVSSLKHLDLS CHHHHHHCCCCCCCC	46.76	28060719
752	N-linked_Glycosylation	SNLLKTINKSALETK HHHHHHHCHHHCCCC	37.14	UniProtKB CARBOHYD
762	Phosphorylation	ALETKTTTKLSMLEL HCCCCCCCEEHHEEC	34.91	-
765	Phosphorylation	TKTTTKLSMLELHGN CCCCCEEHHEECCCC	23.91	-
880	Phosphorylation	LSTSQTFYDAYISYD CCCCCCCHHEEEECC	11.75	17868034
886	Phosphorylation	FYDAYISYDTKDASV CHHEEEECCCCCCCH	20.34	17868034
935	Phosphorylation	IIDNLMQSINQSKKT HHHHHHHHHCCCCCE	15.00	-
939	Phosphorylation	LMQSINQSKKTVFVL HHHHHCCCCCEEEEE	31.47	-
1030	Phosphorylation	LTENDSRYNNMYVDS ECCCCCCCCCCCCCC	18.16	17868034

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF216	Q9NWF9	PMID:31385713

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TLR8_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TLR8_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TLR8_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• 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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-80 AND ASN-88, AND MASSSPECTROMETRY.
PubMed: 19159218