TLR3_HUMAN - dbPTM
TLR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLR3_HUMAN
UniProt AC O15455
Protein Name Toll-like receptor 3
Gene Name TLR3
Organism Homo sapiens (Human).
Sequence Length 904
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein. Endosome membrane. Early endosome .
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. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response..
Protein Sequence MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHGLFNVRYLNLKRSFTKQSISLASLPKIDDFSFQWLKCLEHLNMEDNDIPGIKSNMFTGLINLKYLSLSNSFTSLRTLTNETFVSLAHSPLHILNLTKNKISKIESDAFSWLGHLEVLDLGLNEIGQELTGQEWRGLENIFEIYLSYNKYLQLTRNSFALVPSLQRLMLRRVALKNVDSSPSPFQPLRNLTILDLSNNNIANINDDMLEGLEKLEILDLQHNNLARLWKHANPGGPIYFLKGLSHLHILNLESNGFDEIPVEVFKDLFELKIIDLGLNNLNTLPASVFNNQVSLKSLNLQKNLITSVEKKVFGPAFRNLTELDMRFNPFDCTCESIAWFVNWINETHTNIPELSSHYLCNTPPHYHGFPVRLFDTSSCKDSAPFELFFMINTSILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRQTEQFEYAAYIIHAYKDKDWVWEHFSSMEKEDQSLKFCLEERDFEAGVFELEAIVNSIKRSRKIIFVITHHLLKDPLCKRFKVHHAVQQAIEQNLDSIILVFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERIGAFRHKLQVALGSKNSVH
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 Orthologous
Protein Cluster
52N-linked_GlycosylationVPDDLPTNITVLNLT
CCCCCCCCEEEEECC		26.4516043704
57N-linked_GlycosylationPTNITVLNLTHNQLR
CCCEEEEECCHHHHH		38.2619159218
70N-linked_GlycosylationLRRLPAANFTRYSQL
HHCCCCCCCCCHHHC		40.7116043704
72PhosphorylationRLPAANFTRYSQLTS
CCCCCCCCCHHHCEE		28.62-
118PhosphorylationLSQLSDKTFAFCTNL
HHHCCCCHHHHHCCH		25.7827732954
123PhosphorylationDKTFAFCTNLTELHL
CCHHHHHCCHHHHHH		27.1527732954
124N-linked_GlycosylationKTFAFCTNLTELHLM
CHHHHHCCHHHHHHH		46.2615961631
126PhosphorylationFAFCTNLTELHLMSN
HHHHCCHHHHHHHHH		38.2727732954
132PhosphorylationLTELHLMSNSIQKIK
HHHHHHHHHHHHHHH		33.5127732954
151PhosphorylationVKQKNLITLDLSHNG
CCCCCEEEEECCCCC		19.8623898821
155PhosphorylationNLITLDLSHNGLSST
CEEEEECCCCCCCCC		17.9923898821
196N-linked_GlycosylationEELDIFANSSLKKLE
HHCHHHCCCCCCHHH		22.7616043704
205PhosphorylationSLKKLELSSNQIKEF
CCCHHHCCHHHHHHH		20.1918452278
206PhosphorylationLKKLELSSNQIKEFS
CCHHHCCHHHHHHHC		45.4318452278
247N-linked_GlycosylationKLCLELANTSIRNLS
HHHHHHHCCCCCCCC		47.1622579623
252N-linked_GlycosylationLANTSIRNLSLSNSQ
HHCCCCCCCCCCCCC		32.1016043704
265N-linked_GlycosylationSQLSTTSNTTFLGLK
CCCCCCCCCEEEEEE		40.8316043704
275N-linked_GlycosylationFLGLKWTNLTMLDLS
EEEEEEECCEEEECC		32.1916043704
291N-linked_GlycosylationNNLNVVGNDSFAWLP
CCCCEECCCCHHHHH		30.0916043704
332PhosphorylationRYLNLKRSFTKQSIS
HHHEECCCCCCCCEE		35.3624719451
350PhosphorylationLPKIDDFSFQWLKCL
CCCCCCCCHHHHHHH		24.42-
383PhosphorylationTGLINLKYLSLSNSF
HHCCEEHHHHHCCCC		12.51-
391PhosphorylationLSLSNSFTSLRTLTN
HHHCCCCCCHHHHCC		27.03-
392PhosphorylationSLSNSFTSLRTLTNE
HHCCCCCCHHHHCCH		17.53-
398N-linked_GlycosylationTSLRTLTNETFVSLA
CCHHHHCCHHHHHHC		49.8016043704
413N-linked_GlycosylationHSPLHILNLTKNKIS
CCHHHHHHHCCCCHH		45.0916043704
481PhosphorylationNSFALVPSLQRLMLR
CCCCHHHHHHHHHHH		29.6526091039
507N-linked_GlycosylationSPFQPLRNLTILDLS
CCCCCCCCCEEEECC		49.5816043704
600PhosphorylationLGLNNLNTLPASVFN
CCCCCCCCCCHHHHC		36.9722210691
604PhosphorylationNLNTLPASVFNNQVS
CCCCCCHHHHCCCCC		25.8722210691
636N-linked_GlycosylationVFGPAFRNLTELDMR
HHCHHHCCCCHHHCC		44.8816043704
662N-linked_GlycosylationAWFVNWINETHTNIP
HHHHHHHCCCCCCCH		39.46UniProtKB CARBOHYD
759PhosphorylationEQFEYAAYIIHAYKD
HHHHHHHHHHHHHHC		7.7017178723
818PhosphorylationRKIIFVITHHLLKDP
CCEEEEEEHHHHCCH		9.6520058876
858PhosphorylationFLEEIPDYKLNHALC
EHHHCCCCCCHHHHH		16.4217178723
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
759YPhosphorylationKinaseSRCP12931
PSP
858YPhosphorylationKinaseEGFRP00533
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLR3_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 TLR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYD88_HUMANMYD88physical
12646618
IRAK2_HUMANIRAK2physical
17878161
TRI69_HUMANTRIM69physical
21911421
TBK1_HUMANTBK1physical
21911421
TRAF6_HUMANTRAF6physical
21911421
TRAF3_HUMANTRAF3physical
21903422
TOLIP_HUMANTOLLIPphysical
21903422
TRAF6_HUMANTRAF6physical
12609980
M3K7_HUMANMAP3K7physical
12609980
TAB2_HUMANTAB2physical
12609980
MP2K6_HUMANMAP2K6physical
12609980
RIPK1_HUMANRIPK1physical
16115877
M3K7_HUMANMAP3K7physical
16115877
TRAF6_HUMANTRAF6physical
16115877
P85A_HUMANPIK3R1physical
15502848
KSYK_HUMANSYKphysical
23962979
DRA_HUMANHLA-DRAphysical
24600555
TCAM1_HUMANTICAM1physical
25736436
WDFY1_HUMANWDFY1physical
25736436
TCAM1_HUMANTICAM1physical
27810922
RIPK1_HUMANRIPK1physical
27810922
TBK1_HUMANTBK1physical
27810922
RNF31_HUMANRNF31physical
27810922
SHRPN_HUMANSHARPINphysical
27810922
CASP8_HUMANCASP8physical
27810922
FADD_HUMANFADDphysical
27810922
HOIL1_HUMANRBCK1physical
27810922
NEMO_HUMANIKBKGphysical
27810922
BIRC2_HUMANBIRC2physical
27810922
BIRC3_HUMANBIRC3physical
27810922
TRAF6_HUMANTRAF6physical
27810922
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613002Herpes simplex encephalitis 2 (HSE2)
Kegg Drug
D09661 Rintatolimod (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLR3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of human toll-like receptor 3 (TLR3) ectodomain.";
Choe J., Kelker M.S., Wilson I.A.;
Science 309:581-585(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-700, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-124; ASN-252; ASN-275; ASN-291; ASN-398; ASN-413AND ASN-507.
"The molecular structure of the Toll-like receptor 3 ligand-bindingdomain.";
Bell J.K., Botos I., Hall P.R., Askins J., Shiloach J., Segal D.M.,Davies D.R.;
Proc. Natl. Acad. Sci. U.S.A. 102:10976-10980(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-703, FUNCTION, MASSSPECTROMETRY, DISULFIDE BONDS, SUBUNIT, AND GLYCOSYLATION AT ASN-52;ASN-70; ASN-196; ASN-252; ASN-265; ASN-275; ASN-291; ASN-398; ASN-413;ASN-507 AND ASN-636.
"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-52 AND ASN-57, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Two tyrosine residues of Toll-like receptor 3 trigger different stepsof NF-kappa B activation.";
Sarkar S.N., Elco C.P., Peters K.L., Chattopadhyay S., Sen G.C.;
J. Biol. Chem. 282:3423-3427(2007).
Cited for: PHOSPHORYLATION AT TYR-759 AND TYR-858, FUNCTION, AND MUTAGENESIS OFTYR-759.

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