IL1R2_HUMAN - dbPTM
IL1R2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL1R2_HUMAN
UniProt AC P27930
Protein Name Interleukin-1 receptor type 2
Gene Name IL1R2
Organism Homo sapiens (Human).
Sequence Length 398
Subcellular Localization Isoform Short: Secreted .
Isoform Long: Cell membrane
Single-pass type I membrane protein.
Protein Description Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors..
Protein Sequence MLRLYVLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKEASSTFSWGIVLAPLSLAFLVLGGIWMHRRCKHRTGKADGLTVLWPHHQDFQSYPK
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 Orthologous
Protein Cluster
66N-linked_GlycosylationASVSPRINLTWHKND
EEECCCEEEEEECCC		32.47UniProtKB CARBOHYD
68PhosphorylationVSPRINLTWHKNDSA
ECCCEEEEEECCCCC		22.4932142685
72N-linked_GlycosylationINLTWHKNDSARTVP
EEEEEECCCCCCCCC		35.27UniProtKB CARBOHYD
112N-linked_GlycosylationTYVCTTRNASYCDKM
EEEEECCCCHHCCCC		31.0120802483
210PhosphorylationGYYRCVLTFAHEGQQ
CEEEEEEEECCCCCE		9.81-
219N-linked_GlycosylationAHEGQQYNITRSIEL
CCCCCEEEEEEEEEE		25.4720802483
235PhosphorylationIKKKKEETIPVIISP
ECCCCCCCCCEEEEC		31.50-
241PhosphorylationETIPVIISPLKTISA
CCCCEEEECCCHHHC		17.0422210691
252PhosphorylationTISASLGSRLTIPCK
HHHCHHCCCCEEEEE		29.4322210691
277N-linked_GlycosylationTMLWWTANDTHIESA
EEEEEECCCCCCCCC		47.54UniProtKB CARBOHYD
395PhosphorylationPHHQDFQSYPK----
CCCCCCCCCCC----		43.3124719451
396PhosphorylationHHQDFQSYPK-----
CCCCCCCCCC-----		12.3129759185
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 IL1R2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL1R2_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 IL1R2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IL1RA_HUMANIL1RNphysical
1834644
EXC6B_HUMANEXOC6Bphysical
28514442
CCD51_HUMANCCDC51physical
28514442
EXOC6_HUMANEXOC6physical
28514442
NUD16_HUMANNUDT16physical
28514442
EXOC5_HUMANEXOC5physical
28514442
EXOC7_HUMANEXOC7physical
28514442
EXOC1_HUMANEXOC1physical
28514442
MTU1_HUMANTRMUphysical
28514442
EXOC2_HUMANEXOC2physical
28514442
LONP2_HUMANLONP2physical
28514442
EXOC3_HUMANEXOC3physical
28514442
NDUAC_HUMANNDUFA12physical
28514442
EXOC8_HUMANEXOC8physical
28514442
QSOX1_HUMANQSOX1physical
28514442
SE6L2_HUMANSEZ6L2physical
28514442
DUSTY_HUMANDSTYKphysical
28514442
NDUS4_HUMANNDUFS4physical
28514442
SCRIB_HUMANSCRIBphysical
28514442
RHBT3_HUMANRHOBTB3physical
28514442
EXOC4_HUMANEXOC4physical
28514442
MYADM_HUMANMYADMphysical
28514442
LRRC1_HUMANLRRC1physical
28514442
AT2B2_HUMANATP2B2physical
28514442
RSPRY_HUMANRSPRY1physical
28514442
ZNT5_HUMANSLC30A5physical
28514442
GNPAT_HUMANGNPATphysical
28514442
ATLA2_HUMANATL2physical
28514442
CISD2_HUMANCISD2physical
28514442
DYN3_HUMANDNM3physical
28514442
NLRX1_HUMANNLRX1physical
28514442
OCRL_HUMANOCRLphysical
28514442
TBCD_HUMANTBCDphysical
28514442
MRRP3_HUMANKIAA0391physical
28514442
SYAM_HUMANAARS2physical
28514442
ORC4_HUMANORC4physical
28514442
CIP2A_HUMANKIAA1524physical
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
D02934 Anakinra (USAN/INN); Kineret (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IL1R2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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 14-343 IN COMPLEX WITH IL1RAPAND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-112 ANDASN-219.

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