TLR9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TLR9_HUMAN
• UniProt AC: Q9NR96
• Protein Name: Toll-like receptor 9
• Gene Name: TLR9
• Organism: Homo sapiens (Human).
• Sequence Length: 1032
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass type I membrane protein . Endosome . Lysosome . Cytoplasmic vesicle, phagosome . Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist. Exit from the ER requires UNC
• 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. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. [PubMed: 11564765]
• Protein Sequence: MGFCRSALHPLSLLVQAIMLAMTLALGTLPAFLPCELQPHGLVNCNWLFLKSVPHFSMAAPRGNVTSLSLSSNRIHHLHDSDFAHLPSLRHLNLKWNCPPVGLSPMHFPCHMTIEPSTFLAVPTLEELNLSYNNIMTVPALPKSLISLSLSHTNILMLDSASLAGLHALRFLFMDGNCYYKNPCRQALEVAPGALLGLGNLTHLSLKYNNLTVVPRNLPSSLEYLLLSYNRIVKLAPEDLANLTALRVLDVGGNCRRCDHAPNPCMECPRHFPQLHPDTFSHLSRLEGLVLKDSSLSWLNASWFRGLGNLRVLDLSENFLYKCITKTKAFQGLTQLRKLNLSFNYQKRVSFAHLSLAPSFGSLVALKELDMHGIFFRSLDETTLRPLARLPMLQTLRLQMNFINQAQLGIFRAFPGLRYVDLSDNRISGASELTATMGEADGGEKVWLQPGDLAPAPVDTPSSEDFRPNCSTLNFTLDLSRNNLVTVQPEMFAQLSHLQCLRLSHNCISQAVNGSQFLPLTGLQVLDLSHNKLDLYHEHSFTELPRLEALDLSYNSQPFGMQGVGHNFSFVAHLRTLRHLSLAHNNIHSQVSQQLCSTSLRALDFSGNALGHMWAEGDLYLHFFQGLSGLIWLDLSQNRLHTLLPQTLRNLPKSLQVLRLRDNYLAFFKWWSLHFLPKLEVLDLAGNQLKALTNGSLPAGTRLRRLDVSCNSISFVAPGFFSKAKELRELNLSANALKTVDHSWFGPLASALQILDVSANPLHCACGAAFMDFLLEVQAAVPGLPSRVKCGSPGQLQGLSIFAQDLRLCLDEALSWDCFALSLLAVALGLGVPMLHHLCGWDLWYCFHLCLAWLPWRGRQSGRDEDALPYDAFVVFDKTQSAVADWVYNELRGQLEECRGRWALRLCLEERDWLPGKTLFENLWASVYGSRKTLFVLAHTDRVSGLLRASFLLAQQRLLEDRKDVVVLVILSPDGRRSRYVRLRQRLCRQSVLLWPHQPSGQRSFWAQLGMALTRDNHHFYNRNFCQGPTAE

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
64	N-linked_Glycosylation	SMAAPRGNVTSLSLS EECCCCCCEEEEECC	34.86	UniProtKB CARBOHYD
88	Phosphorylation	SDFAHLPSLRHLNLK CCCCCCCCCCCCCCC	44.38	24719451
129	N-linked_Glycosylation	VPTLEELNLSYNNIM CCCHHHHCCCCCCCC	30.16	UniProtKB CARBOHYD
200	N-linked_Glycosylation	GALLGLGNLTHLSLK CCEECCCCCEEEEEE	46.97	UniProtKB CARBOHYD
202	Phosphorylation	LLGLGNLTHLSLKYN EECCCCCEEEEEEEC	25.44	-
205	Phosphorylation	LGNLTHLSLKYNNLT CCCCEEEEEEECCEE	18.40	24719451
210	N-linked_Glycosylation	HLSLKYNNLTVVPRN EEEEEECCEEEEECC	33.72	UniProtKB CARBOHYD
242	N-linked_Glycosylation	LAPEDLANLTALRVL HCHHHHHCCCEEEEE	45.26	UniProtKB CARBOHYD
244	Phosphorylation	PEDLANLTALRVLDV HHHHHCCCEEEEEEC	24.37	24719451
300	N-linked_Glycosylation	DSSLSWLNASWFRGL CCCCHHHCHHHHCCC	26.18	UniProtKB CARBOHYD
340	N-linked_Glycosylation	LTQLRKLNLSFNYQK HHHHHHCCCCCCCHH	36.35	UniProtKB CARBOHYD
345	Phosphorylation	KLNLSFNYQKRVSFA HCCCCCCCHHCCEEE	17.25	-
355	Phosphorylation	RVSFAHLSLAPSFGS CCEEEEEEECCCCHH	16.78	24667141
362	Phosphorylation	SLAPSFGSLVALKEL EECCCCHHHHHHEEE	20.05	24667141
419	Phosphorylation	RAFPGLRYVDLSDNR HHCCCCEEEECCCCC	11.89	-
423	Phosphorylation	GLRYVDLSDNRISGA CCEEEECCCCCCCCC	28.51	-
434	Phosphorylation	ISGASELTATMGEAD CCCCCHHEEEEECCC	18.94	24114839
469	N-linked_Glycosylation	SSEDFRPNCSTLNFT CCCCCCCCCCEECEE	28.28	UniProtKB CARBOHYD
474	N-linked_Glycosylation	RPNCSTLNFTLDLSR CCCCCEECEEEECCC	28.13	UniProtKB CARBOHYD
513	N-linked_Glycosylation	NCISQAVNGSQFLPL CHHHHHHCCCCCCCC	47.62	UniProtKB CARBOHYD
567	N-linked_Glycosylation	GMQGVGHNFSFVAHL CCCCCCCCHHHHHHH	28.47	UniProtKB CARBOHYD
642	Phosphorylation	LSQNRLHTLLPQTLR CCCCCHHHHHHHHHH	34.28	28348404
693	Phosphorylation	GNQLKALTNGSLPAG CHHHHHHHCCCCCCC	42.25	24719451
694	N-linked_Glycosylation	NQLKALTNGSLPAGT HHHHHHHCCCCCCCC	38.62	UniProtKB CARBOHYD
696	Phosphorylation	LKALTNGSLPAGTRL HHHHHCCCCCCCCCC	33.00	24719451
731	N-linked_Glycosylation	AKELRELNLSANALK HHHHHHCCCCHHCHH	27.48	UniProtKB CARBOHYD
738	Acetylation	NLSANALKTVDHSWF CCCHHCHHCCCCCCH	44.05	24884251
789	Ubiquitination	PGLPSRVKCGSPGQL CCCCCCCCCCCCCCC	31.59	-
972	Phosphorylation	VVVLVILSPDGRRSR EEEEEEECCCCCHHH	15.15	24114839
1004	Phosphorylation	HQPSGQRSFWAQLGM CCCCCCCCHHHHHCH	19.77	24719451

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:15107846

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TLR9_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 TLR9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RN216_HUMAN	RNF216	physical	15107846
CHIP_HUMAN	STUB1	physical	21911421
MYD88_HUMAN	MYD88	physical	21911421
IRAK1_HUMAN	IRAK1	physical	21911421
TRI69_HUMAN	TRIM69	physical	21911421
TBK1_HUMAN	TBK1	physical	21911421
TRAF6_HUMAN	TRAF6	physical	21911421
HSP7C_HUMAN	HSPA8	physical	21911421
SRC_HUMAN	SRC	physical	21911421
KPCZ_HUMAN	PRKCZ	physical	21911421
PALD_HUMAN	PALD1	physical	21903422
TRAF3_HUMAN	TRAF3	physical	21903422
UN93B_HUMAN	UNC93B1	physical	21903422
CLGN_HUMAN	CLGN	physical	21903422
S11IP_HUMAN	STK11IP	physical	21903422
TOLIP_HUMAN	TOLLIP	physical	21903422
UGGG1_HUMAN	UGGT1	physical	21903422
KSYK_HUMAN	SYK	physical	23962979

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.