IL1AP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IL1AP_HUMAN
• UniProt AC: Q9NPH3
• Protein Name: Interleukin-1 receptor accessory protein
• Gene Name: IL1RAP
• Organism: Homo sapiens (Human).
• Sequence Length: 570
• Subcellular Localization: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Secreted.; Isoform 3: Secreted.
• Protein Description: Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity). 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. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD (By similarity). May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (Probable).; 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. [PubMed: 12530978 Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling (By similarity; Isoform 4: Unable to mediate canonical IL-1 signaling]
• Protein Sequence: MTLLWCVVSLYFYGILQSDASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVELACGFGATVLLVVILIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKETKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRRSSSDEQGLSYSSLKNV

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	FEHFLKFNYSTAHSA HHHHHHCCHHHHHHC	28.40	UniProtKB CARBOHYD
104	Phosphorylation	DVLWFRPTLLNDTGN CEEEECCCCCCCCCC	39.35	-
107	N-linked_Glycosylation	WFRPTLLNDTGNYTC EECCCCCCCCCCEEE	48.16	20802483
111	N-linked_Glycosylation	TLLNDTGNYTCMLRN CCCCCCCCEEEEEEC	30.91	20802483
112	Phosphorylation	LLNDTGNYTCMLRNT CCCCCCCEEEEEECC	11.58	-
113	Phosphorylation	LNDTGNYTCMLRNTT CCCCCCEEEEEECCC	8.74	-
118	N-linked_Glycosylation	NYTCMLRNTTYCSKV CEEEEEECCCCCCEE	32.58	20802483
134	Acetylation	FPLEVVQKDSCFNSP EEEEEEECCCCCCCC	39.74	7407695
143	Acetylation	SCFNSPMKLPVHKLY CCCCCCCCCCCHHHH	53.69	7407705
166	Phosphorylation	TCPNVDGYFPSSVKP ECCCCCCCCCCCCCC	14.09	22817900
178	Phosphorylation	VKPTITWYMGCYKIQ CCCEEEEEEECEEEE	3.80	22817900
182	Phosphorylation	ITWYMGCYKIQNFNN EEEEEECEEEECCCC	12.85	22817900
196	N-linked_Glycosylation	NVIPEGMNLSFLIAL CCCCCCCCHHHEEEH	43.31	UniProtKB CARBOHYD
209	N-linked_Glycosylation	ALISNNGNYTCVVTY EHHHCCCCEEEEEEE	30.94	20802483
293	Phosphorylation	GKKPDDITIDVTINE CCCCCCEEEEEEECC	20.37	28450419
297	Phosphorylation	DDITIDVTINESISH CCEEEEEEECCCCCC	17.84	28450419
299	N-linked_Glycosylation	ITIDVTINESISHSR EEEEEEECCCCCCCC	27.83	UniProtKB CARBOHYD
301	Phosphorylation	IDVTINESISHSRTE EEEEECCCCCCCCCC	25.55	28450419
303	Phosphorylation	VTINESISHSRTEDE EEECCCCCCCCCCCC	25.37	28450419
305	Phosphorylation	INESISHSRTEDETR ECCCCCCCCCCCCHH	33.82	23911959
317	Phosphorylation	ETRTQILSIKKVTSE CHHHEEEEEEECCCH	33.71	24719451
469 (in isoform 5)	Phosphorylation	-	10.25	23663014
472 (in isoform 5)	Phosphorylation	-	13.11	23663014
474 (in isoform 5)	Phosphorylation	-	2.47	23663014
509	Phosphorylation	QYKAVKETKVKELKR ECEECCHHHHHHHHH	35.11	22817900
518 (in isoform 5)	Phosphorylation	-	43.10	29052541
518	Ubiquitination	VKELKRAKTVLTVIK HHHHHHCCEEEEEEE	43.10	-
520 (in isoform 5)	Phosphorylation	-	4.09	29052541
523 (in isoform 5)	Phosphorylation	-	3.56	29052541
532	Ubiquitination	KWKGEKSKYPQGRFW EECCCHHCCCCCHHH	72.52	-
551	Phosphorylation	VAMPVKKSPRRSSSD EEEECCCCCCCCCCC	20.23	28450419
555	Phosphorylation	VKKSPRRSSSDEQGL CCCCCCCCCCCCCCC	35.16	29255136
556	Phosphorylation	KKSPRRSSSDEQGLS CCCCCCCCCCCCCCC	39.74	29255136
557	Phosphorylation	KSPRRSSSDEQGLSY CCCCCCCCCCCCCCH	46.54	29255136
563	Phosphorylation	SSDEQGLSYSSLKNV CCCCCCCCHHHCCCC	29.78	30266825
564	Phosphorylation	SDEQGLSYSSLKNV- CCCCCCCHHHCCCC-	13.81	30266825
565	Phosphorylation	DEQGLSYSSLKNV-- CCCCCCHHHCCCC--	26.31	30266825
566	Phosphorylation	EQGLSYSSLKNV--- CCCCCHHHCCCC---	34.82	30266825
568	Ubiquitination	GLSYSSLKNV----- CCCHHHCCCC-----	58.58	-

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	MARCHF8	Q5T0T0	PMID:22904187

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IL1AP_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 IL1AP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TOLIP_HUMAN	TOLLIP	physical	10854325
IL1R1_HUMAN	IL1R1	physical	9371760
IRAK1_HUMAN	IRAK1	physical	9371760
RAC1_HUMAN	RAC1	physical	11416133
TIRAP_HUMAN	TIRAP	genetic	11544529
MYD88_HUMAN	MYD88	genetic	11544529
MARH8_HUMAN	MARCH8	physical	22904187
TCAM2_HUMAN	TICAM2	physical	12721283
IMA5_HUMAN	KPNA1	physical	21988832
MC4R_HUMAN	MC4R	physical	21988832
KPCI_HUMAN	PRKCI	physical	21988832
IRAK1_HUMAN	IRAK1	physical	24735611
IL1R1_HUMAN	IL1R1	physical	24735611

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

N-linked Glycosylation

"Structural insights into the assembly and activation of IL-1beta withits receptors.";
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
Nat. Immunol. 11:905-911(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 21-350 IN COMPLEX WITH IL1R2AND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-107;ASN-111; ASN-118 AND ASN-209.
PubMed: 20802483

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND MASSSPECTROMETRY.
PubMed: 19690332

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555; SER-556 ANDSER-557, AND MASS SPECTROMETRY.
PubMed: 19369195