dbPTM

IL1RA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IL1RA_HUMAN
UniProt AC	P18510
Protein Name	Interleukin-1 receptor antagonist protein
Gene Name	IL1RN
Organism	Homo sapiens (Human).
Sequence Length	177
Subcellular Localization	Isoform 1: Secreted. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm.
Protein Description	Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. Binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unsure..
Protein Sequence	MEICRGLRSHLITLLLFLFHSETICRPSGRKSSKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQEDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
94	S-nitrosylation	GGKMCLSCVKSGDET CCEEEEEECCCCCCE	2.63	24105792
97	Phosphorylation	MCLSCVKSGDETRLQ EEEEECCCCCCEEEE	30.95	22210691
109	N-linked_Glycosylation	RLQLEAVNITDLSEN EEEEEEEECCCCCCC	38.19	16335952
111	Phosphorylation	QLEAVNITDLSENRK EEEEEECCCCCCCCC	26.19	22210691
114	Phosphorylation	AVNITDLSENRKQDK EEECCCCCCCCCCCC	35.32	22210691
128	Phosphorylation	KRFAFIRSDSGPTTS CCEEEEECCCCCCCC	31.17	28348404
130	Phosphorylation	FAFIRSDSGPTTSFE EEEEECCCCCCCCCH	48.17	28348404
133	Phosphorylation	IRSDSGPTTSFESAA EECCCCCCCCCHHCC	38.30	28348404
134	Phosphorylation	RSDSGPTTSFESAAC ECCCCCCCCCHHCCC	34.25	28348404
135	Phosphorylation	SDSGPTTSFESAACP CCCCCCCCCHHCCCC	29.51	28348404
138	Phosphorylation	GPTTSFESAACPGWF CCCCCCHHCCCCCEE	21.11	28348404

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 IL1RA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IL1RA_HUMAN !!

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 IL1RA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IL1RA_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612628	Microvascular complications of diabetes 4 (MVCD4)
612852	Interleukin 1 receptor antagonist deficiency (DIRA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IL1RA_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Interleukin-1 receptor antagonist activity of a human interleukin-1inhibitor."; Hannum C.H., Wilcox C.J., Arend W.P., Joslin F.G., Dripps D.J.,Heimdal P.L., Armes L.G., Sommer A., Eisenberg S.P., Thompson R.C.; Nature 343:336-340(1990). Cited for: PROTEIN SEQUENCE OF 26-45, AND GLYCOSYLATION AT ASN-109.	2137200 [Abstract]