TLR4_MOUSE - dbPTM
TLR4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLR4_MOUSE
UniProt AC Q9QUK6
Protein Name Toll-like receptor 4
Gene Name Tlr4
Organism Mus musculus (Mouse).
Sequence Length 835
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Early endosome . Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis. Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endoso
Protein Description Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). [PubMed: 9851930]
Protein Sequence MMPPWLLARTLIMALFFSCLTPGSLNPCIEVVPNITYQCMDQKLSKVPDDIPSSTKNIDLSFNPLKILKSYSFSNFSELQWLDLSRCEIETIEDKAWHGLHHLSNLILTGNPIQSFSPGSFSGLTSLENLVAVETKLASLESFPIGQLITLKKLNVAHNFIHSCKLPAYFSNLTNLVHVDLSYNYIQTITVNDLQFLRENPQVNLSLDMSLNPIDFIQDQAFQGIKLHELTLRGNFNSSNIMKTCLQNLAGLHVHRLILGEFKDERNLEIFEPSIMEGLCDVTIDEFRLTYTNDFSDDIVKFHCLANVSAMSLAGVSIKYLEDVPKHFKWQSLSIIRCQLKQFPTLDLPFLKSLTLTMNKGSISFKKVALPSLSYLDLSRNALSFSGCCSYSDLGTNSLRHLDLSFNGAIIMSANFMGLEELQHLDFQHSTLKRVTEFSAFLSLEKLLYLDISYTNTKIDFDGIFLGLTSLNTLKMAGNSFKDNTLSNVFANTTNLTFLDLSKCQLEQISWGVFDTLHRLQLLNMSHNNLLFLDSSHYNQLYSLSTLDCSFNRIETSKGILQHFPKSLAFFNLTNNSVACICEHQKFLQWVKEQKQFLVNVEQMTCATPVEMNTSLVLDFNNSTCYMYKTIISVSVVSVIVVSTVAFLIYHFYFHLILIAGCKKYSRGESIYDAFVIYSSQNEDWVRNELVKNLEEGVPRFHLCLHYRDFIPGVAIAANIIQEGFHKSRKVIVVVSRHFIQSRWCIFEYEIAQTWQFLSSRSGIIFIVLEKVEKSLLRQQVELYRLLSRNTYLEWEDNPLGRHIFWRRLKNALLDGKASNPEQTAEEEQETATWT
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
34N-linked_GlycosylationPCIEVVPNITYQCMD
CCEEECCCCCHHHHC		27.8517803912
75N-linked_GlycosylationLKSYSFSNFSELQWL
HHEECCCCCCCCEEE		42.3117803912
172N-linked_GlycosylationKLPAYFSNLTNLVHV
CCCHHHCCCCCEEEE		40.7717803912
204N-linked_GlycosylationLRENPQVNLSLDMSL
HHHCCCEEEEEECCC		20.7517803912
237N-linked_GlycosylationLTLRGNFNSSNIMKT
EEECCCCCCCHHHHH		48.8317803912
307N-linked_GlycosylationVKFHCLANVSAMSLA
HHHHHHHCCHHHHHH		18.4817803912
355PhosphorylationLPFLKSLTLTMNKGS
CHHHEEEEEEECCCC		27.5528059163
357PhosphorylationFLKSLTLTMNKGSIS
HHEEEEEEECCCCCC		17.2928059163
374PhosphorylationKVALPSLSYLDLSRN
EEECCCCCHHHCCCC		28.1722817900
375PhosphorylationVALPSLSYLDLSRNA
EECCCCCHHHCCCCC		14.9922817900
379PhosphorylationSLSYLDLSRNALSFS
CCCHHHCCCCCCCCC		24.1322817900
492N-linked_GlycosylationTLSNVFANTTNLTFL
CHHHHCCCCCCCEEE		35.6517803912
495N-linked_GlycosylationNVFANTTNLTFLDLS
HHCCCCCCCEEEECC		34.74-
524N-linked_GlycosylationLHRLQLLNMSHNNLL
HHHHHHHCCCCCCEE		38.2017803912
572N-linked_GlycosylationPKSLAFFNLTNNSVA
CCCCEEEECCCCCEE		39.2317803912
575N-linked_GlycosylationLAFFNLTNNSVACIC
CEEEECCCCCEEEEE		41.78-
613N-linked_GlycosylationCATPVEMNTSLVLDF
CCCCCCCCCEEEEEC		17.01-
621N-linked_GlycosylationTSLVLDFNNSTCYMY
CEEEEECCCCCEEEE		41.01-
622N-linked_GlycosylationSLVLDFNNSTCYMYK
EEEEECCCCCEEEEE		38.39-
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 TLR4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLR4_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRAK1_MOUSEIrak1physical
18562480
BCL10_MOUSEBcl10physical
16831874
TCAM2_MOUSETicam2physical
19378012
TIRAP_MOUSETirapphysical
19378012
MYD88_MOUSEMyd88physical
19378012
TRAF6_MOUSETraf6physical
19898473
MYD88_MOUSEMyd88physical
19898473
UBE2N_MOUSEUbe2nphysical
19898473
TRAF3_MOUSETraf3physical
19898473
TCAM1_MOUSETicam1physical
19898473
M3K7_MOUSEMap3k7physical
19898473
NEMO_MOUSEIkbkgphysical
19898473
BIRC2_MOUSEBirc2physical
19898473
BIRC3_MOUSEBirc3physical
19898473
MYD88_MOUSEMyd88physical
17618294
TLR4_MOUSETlr4physical
21628003
CNPY4_MOUSECnpy4physical
16338228
BECN1_MOUSEBecn1physical
18772134
TCAM1_MOUSETicam1physical
18772134
MYD88_MOUSEMyd88physical
18772134
IRAK4_MOUSEIrak4physical
18772134
TCAM1_MOUSETicam1physical
25736436
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLR4_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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 (2.84 ANGSTROMS) OF 27-625 IN COMPLEX WITH LY96,AND GLYCOSYLATION AT ASN-34; ASN-75; ASN-172; ASN-204; ASN-237;ASN-307; ASN-492; ASN-524 AND ASN-572.

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