IL1AP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IL1AP_MOUSE
• UniProt AC: Q61730
• Protein Name: Interleukin-1 receptor accessory protein
• Gene Name: Il1rap
• Organism: Mus musculus (Mouse).
• Sequence Length: 570
• Subcellular Localization: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Secreted.
• Protein Description: Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD. [PubMed: 25908590 May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity; Isoform 2: Associates with secreted ligand-bound IL1R2 and increases the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling.; Isoform 3: Required for Src phosphorylation by IL1B. Required for IL1B-potentiated NMDA-induced calcium influx in neurons acting in cooperation with IL1R1 isoform 2 to mediate Akt kinase activation.]
• Protein Sequence: MGLLWYLMSLSFYGILQSHASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSAMRFPVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFHLTRTVTVKVVGSPKDALPPQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVTPEDLRRNYVCHARNTKGEAEQAAKVKQKVIPPRYTVELACGFGATVFLVVVLIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNVEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKDMKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSNDKQGLSYSSLKNV

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
57	N-linked_Glycosylation	FEHFLKYNYSTAHSS HHHHHHCCHHHHCCC	23.77	25908590
107	N-linked_Glycosylation	WFRPTLLNDTGNYTC EECCCCCCCCCCEEE	48.16	25908590
111	N-linked_Glycosylation	TLLNDTGNYTCMLRN CCCCCCCCEEEEEEC	30.91	25908590
118	N-linked_Glycosylation	NYTCMLRNTTYCSKV CEEEEEECCCCCCEE	32.58	25908590
196	N-linked_Glycosylation	NVLPEGMNLSFFIPL HCCCCCCCEEEEEEE	43.31	-
209	N-linked_Glycosylation	PLVSNNGNYTCVVTY EEEECCCCEEEEEEE	30.94	25908590
299	N-linked_Glycosylation	VTVDITINESVSYSS EEEEEEECCCCCCCC	27.17	-
395	Phosphorylation	FYRAHFGTDETILDG HHHHHHCCCCEECCC	29.71	17622165
398	Phosphorylation	AHFGTDETILDGKEY HHHCCCCEECCCCEE	29.65	17622165
540	Ubiquitination	YPQGRFWKQLQVAMP CCCCCHHEEEEEEEE	38.12	-
555	Phosphorylation	VKKSPRWSSNDKQGL CCCCCCCCCCCCCCC	22.12	26745281
556	Phosphorylation	KKSPRWSSNDKQGLS CCCCCCCCCCCCCCC	41.93	26745281
559	Ubiquitination	PRWSSNDKQGLSYSS CCCCCCCCCCCCHHH	50.98	22790023
563	Phosphorylation	SNDKQGLSYSSLKNV CCCCCCCCHHHCCCC	29.78	29472430
564	Phosphorylation	NDKQGLSYSSLKNV- CCCCCCCHHHCCCC-	13.81	29514104
565	Phosphorylation	DKQGLSYSSLKNV-- CCCCCCHHHCCCC--	26.31	26745281
566	Phosphorylation	KQGLSYSSLKNV--- CCCCCHHHCCCC---	34.82	27600695
584 (in isoform 3)	Phosphorylation	-		29899451
589 (in isoform 3)	Phosphorylation	-		-
589	Phosphorylation	-------------------------- --------------------------		-
589	Phosphorylation	-------------------------- --------------------------		-
597 (in isoform 3)	Phosphorylation	-		-
597	Phosphorylation	---------------------------------- ----------------------------------		-
597	Phosphorylation	---------------------------------- ----------------------------------		-
599 (in isoform 3)	Phosphorylation	-		-
599	Phosphorylation	------------------------------------ ------------------------------------		-
599	Phosphorylation	------------------------------------ ------------------------------------		-

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

Oops, there are no upstream regulatory protein records of IL1AP_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IL1AP_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IL1AP_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYD88_HUMAN	MYD88	physical	11880380
IRAK1_MOUSE	Irak1	physical	18562480

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395 AND THR-398, ANDMASS SPECTROMETRY.
PubMed: 17622165