I18RA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: I18RA_HUMAN
• UniProt AC: O95256
• Protein Name: Interleukin-18 receptor accessory protein
• Gene Name: IL18RAP {ECO:0000312|HGNC:HGNC:5989}
• Organism: Homo sapiens (Human).
• Sequence Length: 599
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Within the IL18 receptor complex, does not mediate IL18-binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation. [PubMed: 9792649]
• Protein Sequence: MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERNIILEKVTQRDLRRKFVCFVQNSIGNTTQSVQLKEKRGVVLLYILLGTIGTLVAVLAASALLYRHWIEIVLLYRTYQSKDQTLGDKKDFDAFVSYAKWSSFPSEATSSLSEEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGPSIFELQAAVNLALDDQTLKLILIKFCYFQEPESLPHLVKKALRVLPTVTWRGLKSVPPNSRFWAKMRYHMPVKNSQGFTWNQLRITSRIFQWKGLSRTETTGRSSQPKEW

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
21	N-linked_Glycosylation	GERIKGFNISGCSTK CCCCCCCCCCCCCCC	35.86	UniProtKB CARBOHYD
63	Phosphorylation	FCHRNRLSPKQVPEH CCCCCCCCHHHCCCC	27.15	26091039
100	Phosphorylation	PLEDIRKSYPHIIQD CHHHHHHHCCCHHCC	33.76	27067055
101	Phosphorylation	LEDIRKSYPHIIQDK HHHHHHHCCCHHCCC	11.23	27067055
110 (in isoform 3)	Phosphorylation	-	29.07	25954137
110	Phosphorylation	HIIQDKCTLHFLTPG CHHCCCCEEEECCCC	29.07	28111955
115 (in isoform 3)	Phosphorylation	-	19.63	25954137
115	Phosphorylation	KCTLHFLTPGVNNSG CCEEEECCCCCCCCC	19.63	28111955
119	N-linked_Glycosylation	HFLTPGVNNSGSYIC EECCCCCCCCCCEEC	42.75	25500532
121	Phosphorylation	LTPGVNNSGSYICRP CCCCCCCCCCEECCH	24.74	28111955
123	Phosphorylation	PGVNNSGSYICRPKM CCCCCCCCEECCHHH	15.90	28111955
123 (in isoform 3)	Phosphorylation	-	15.90	25954137
124	Phosphorylation	GVNNSGSYICRPKMI CCCCCCCEECCHHHC	13.94	28111955
133	Phosphorylation	CRPKMIKSPYDVACC CCHHHCCCHHHHHHH	20.12	24719451
140 (in isoform 3)	Phosphorylation	-	2.07	25954137
152	N-linked_Glycosylation	LEVKPQTNASCEYSA HEECCCCCCCCCEEC	25.30	25500532
199	Phosphorylation	YKNGKLLSVERSNRI EECCEEEEEEECCCE	32.16	24719451
294	Phosphorylation	IKWYIKDSDLEWEVS EEEEECCCCCCEEEE	38.81	-
307	Phosphorylation	VSVPEAKSIKSTLKD EECCCHHHHHHHHHH	42.15	-
342	Phosphorylation	FVCFVQNSIGNTTQS EEEEEECCCCCCCCE	18.12	-
345	N-linked_Glycosylation	FVQNSIGNTTQSVQL EEECCCCCCCCEEEC	37.98	25500532
392	Phosphorylation	WIEIVLLYRTYQSKD HHHHHHHHHHHCCCC	9.21	26657352
401	Phosphorylation	TYQSKDQTLGDKKDF HHCCCCCCCCCHHHH	42.73	22817900
469	Phosphorylation	VYAEDIVSIIKRSRR CCHHHHHHHHHHHCC	20.94	24719451
474	Phosphorylation	IVSIIKRSRRGIFIL HHHHHHHHCCCEEEE	22.71	24275569
522	Phosphorylation	CYFQEPESLPHLVKK HHHCCCCCHHHHHHH	58.89	29083192
543	Acetylation	TVTWRGLKSVPPNSR CCCCCCCCCCCCCCC	52.83	7971365
554	Methylation	PNSRFWAKMRYHMPV CCCCCEEEEEEECCC	17.95	23644510
554	Acetylation	PNSRFWAKMRYHMPV CCCCCEEEEEEECCC	17.95	7971375
557	Phosphorylation	RFWAKMRYHMPVKNS CCEEEEEEECCCCCC	10.04	22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of I18RA_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of I18RA_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 I18RA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
PIGA_HUMAN	PIGA	physical	28514442
PIGH_HUMAN	PIGH	physical	28514442

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

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND MASSSPECTROMETRY.
PubMed: 18187866