TLR4_HUMAN - dbPTM
TLR4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLR4_HUMAN
UniProt AC O00206
Protein Name Toll-like receptor 4
Gene Name TLR4
Organism Homo sapiens (Human).
Sequence Length 839
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Early endosome . Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis (PubMed:20037584). Colocalizes with RFTN1 at cell membrane and then together with RFT
Protein Description Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). [PubMed: 27022195 Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response]
Protein Sequence MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI
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
35N-linked_GlycosylationPCVEVVPNITYQCME
CCEEECCCCEEEEEE		27.8511706042
173N-linked_GlycosylationKLPEYFSNLTNLEHL
CCHHHHHCCCCCHHC		40.7711706042
175PhosphorylationPEYFSNLTNLEHLDL
HHHHHCCCCCHHCCC		41.8416786156
191PhosphorylationSNKIQSIYCTDLRVL
CCCCCEEEECCHHHH		8.4422210691
193PhosphorylationKIQSIYCTDLRVLHQ
CCCEEEECCHHHHHH		22.5422210691
205N-linked_GlycosylationLHQMPLLNLSLDLSL
HHHCCCCCEEECCCC		34.9511706042
282N-linked_GlycosylationSALEGLCNLTIEEFR
HHHHHHHCCCHHHHH		45.3111706042
309N-linked_GlycosylationDLFNCLTNVSSFSLV
HHHHHHHCCCCCEEE		20.8011706042
357PhosphorylationLKSLKRLTFTSNKGG
ECCCEEEEEECCCCC		28.9730206219
359PhosphorylationSLKRLTFTSNKGGNA
CCEEEEEECCCCCCC		26.5930206219
360PhosphorylationLKRLTFTSNKGGNAF
CEEEEEECCCCCCCC		32.1430206219
386PhosphorylationDLSRNGLSFKGCCSQ
CCCCCCCCCCCCCCC		26.7224719451
407PhosphorylationSLKYLDLSFNGVITM
CCEECEEEECCEEEE		19.1426074081
497N-linked_GlycosylationDIFTELRNLTFLDLS
HHHHHHHCCCCCCCC		56.9311706042
512PhosphorylationQCQLEQLSPTAFNSL
HHCHHHCCHHHHHCC		21.6526074081
514PhosphorylationQLEQLSPTAFNSLSS
CHHHCCHHHHHCCCC		40.2726074081
518PhosphorylationLSPTAFNSLSSLQVL
CCHHHHHCCCCCEEE		24.1526074081
520PhosphorylationPTAFNSLSSLQVLNM
HHHHHCCCCCEEECC		28.9026074081
521PhosphorylationTAFNSLSSLQVLNMS
HHHHCCCCCEEECCC		28.2826074081
526N-linked_GlycosylationLSSLQVLNMSHNNFF
CCCCEEECCCCCCCC		30.9311706042
526N-linked_GlycosylationLSSLQVLNMSHNNFF
CCCCEEECCCCCCCC		30.9311706042
528PhosphorylationSLQVLNMSHNNFFSL
CCEEECCCCCCCCCC		23.2226074081
551PhosphorylationNSLQVLDYSLNHIMT
CHHHHHHHHHHHHHC		15.7622210691
552PhosphorylationSLQVLDYSLNHIMTS
HHHHHHHHHHHHHCC		23.5122210691
558PhosphorylationYSLNHIMTSKKQELQ
HHHHHHHCCCHHHHH		36.4722210691
575N-linked_GlycosylationPSSLAFLNLTQNDFA
CCCCHHHCCCCCCCE		34.2911706042
575N-linked_GlycosylationPSSLAFLNLTQNDFA
CCCCHHHCCCCCCCE		34.2911706042
624N-linked_GlycosylationGMPVLSLNITCQMNK
CCEEEEEEEEEECCC		24.9311706042
630N-linked_GlycosylationLNITCQMNKTIIGVS
EEEEEECCCCCCCHH		16.67UniProtKB CARBOHYD
674PhosphorylationYGRGENIYDAFVIYS
HCCCCCEEEEEEEEC		16.8922817900
680PhosphorylationIYDAFVIYSSQDEDW
EEEEEEEECCCCCHH		9.2922817900
730PhosphorylationIHEGFHKSRKVIVVV
HHCCCCCCCEEEEEE		28.8520058876
738PhosphorylationRKVIVVVSQHFIQSR
CEEEEEEEHHHHHHC		13.31-
790PhosphorylationVELYRLLSRNTYLEW
HHHHHHHHCCCCCCC		28.2420557879
800PhosphorylationTYLEWEDSVLGRHIF
CCCCCHHHHHHHHHH		14.02-
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
790SPhosphorylationKinasePRKD1Q15139
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF216Q9NWF9
PMID:15107846
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
526NGlycosylation

11706042
575NGlycosylation

11706042
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 TLR4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIGIR_HUMANSIGIRRphysical
12925853
MYD88_HUMANMYD88physical
12646618
MYD88_HUMANMYD88physical
10952994
TOLIP_HUMANTOLLIPphysical
11751856
LY96_HUMANLY96physical
10359581
TLR1_HUMANTLR1physical
11932926
ECSIT_HUMANECSITgenetic
10465784
MYD88_HUMANMYD88genetic
11544529
TIRAP_HUMANTIRAPgenetic
11544529
PP4C_HUMANPPP4Cphysical
18634786
TIRAP_HUMANTIRAPphysical
17258210
TCAM2_HUMANTICAM2physical
17258210
MYD88_HUMANMYD88physical
17258210
TIRAP_HUMANTIRAPphysical
18221795
TCAM2_HUMANTICAM2physical
18221795
MYD88_HUMANMYD88physical
18221795
MYD88_HUMANMYD88physical
20048342
TIRAP_HUMANTIRAPphysical
20048342
CHIP_HUMANSTUB1physical
21911421
MYD88_HUMANMYD88physical
21911421
IRAK1_HUMANIRAK1physical
21911421
TRI69_HUMANTRIM69physical
21911421
TBK1_HUMANTBK1physical
21911421
TRAF6_HUMANTRAF6physical
21911421
HSP7C_HUMANHSPA8physical
21911421
SRC_HUMANSRCphysical
21911421
KPCZ_HUMANPRKCZphysical
21911421
S11IP_HUMANSTK11IPphysical
21903422
TRAF3_HUMANTRAF3physical
21903422
HGS_HUMANHGSphysical
16467847
KSYK_HUMANSYKphysical
23962979
SRC_HUMANSRCphysical
20379791
TNFL9_HUMANTNFSF9physical
24084649
UBQL1_HUMANUBQLN1physical
21695056
TCAM1_HUMANTICAM1physical
25736436
TCAM2_HUMANTICAM2physical
25736436
CAV1_HUMANCAV1physical
21715681
Drug and Disease Associations
Kegg Disease
H00821 Macular degeneration, including: Age-related macular degeneration (ARMD); Patterned dystrophy of ret
OMIM Disease
611488Macular degeneration, age-related, 10 (ARMD10)
Kegg Drug
D04043 Eritoran tetrasodium (USAN); E5564
D09573 Eritoran sodium (JAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLR4_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex.";
Park B.S., Song D.H., Kim H.M., Choi B.-S., Lee H., Lee J.-O.;
Nature 458:1191-1195(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-631 IN COMPLEX WITH LY96AND LIPOPOLYSACCHARIDE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-173;ASN-205; ASN-497 AND ASN-526 AND ASN-575.
"Crystal structure of the TLR4-MD-2 complex with bound endotoxinantagonist Eritoran.";
Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C.,Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O.;
Cell 130:906-917(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-228, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-35; ASN-173 AND ASN-205.
"MD-2 and TLR4 N-linked glycosylations are important for a functionallipopolysaccharide receptor.";
da Silva Correia J., Ulevitch R.J.;
J. Biol. Chem. 277:1845-1854(2002).
Cited for: GLYCOSYLATION AT ASN-35; ASN-173; ASN-205; ASN-282; ASN-309; ASN-497;ASN-526; ASN-575 AND ASN-624, AND MUTAGENESIS OF ASN-526 AND ASN-575.

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