IL1R1_HUMAN - dbPTM
IL1R1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL1R1_HUMAN
UniProt AC P14778
Protein Name Interleukin-1 receptor type 1
Gene Name IL1R1
Organism Homo sapiens (Human).
Sequence Length 569
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell membrane . Secreted .
Protein Description Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK 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. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells. [PubMed: 10653850]
Protein Sequence MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG
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
16PhosphorylationCFIALLISSLEADKC
HHHHHHHHHHCHHHC		28.9230243723
17PhosphorylationFIALLISSLEADKCK
HHHHHHHHHCHHHCH		24.2030243723
100N-linked_GlycosylationHYYCVVRNSSYCLRI
EEEEEEECCCEEEEE		24.57UniProtKB CARBOHYD
193N-linked_GlycosylationVAEKHRGNYTCHASY
EHHHHCCCEEEEEEE		28.97UniProtKB CARBOHYD
233N-linked_GlycosylationPVIVSPANETMEVDL
CEEEECCCCCEEEEC		48.97UniProtKB CARBOHYD
249N-linked_GlycosylationSQIQLICNVTGQLSD
HHEEEEEECCCCHHC		27.65UniProtKB CARBOHYD
263N-linked_GlycosylationDIAYWKWNGSVIDED
CEEEEEECCEECCCC		29.18UniProtKB CARBOHYD
278PhosphorylationDPVLGEDYYSVENPA
CCCCCCCCCCCCCCC		8.0426074081
279PhosphorylationPVLGEDYYSVENPAN
CCCCCCCCCCCCCCC		20.6826074081
280PhosphorylationVLGEDYYSVENPANK
CCCCCCCCCCCCCCC		19.4126074081
290PhosphorylationNPANKRRSTLITVLN
CCCCCCCCEEEEEEE		31.4326074081
291PhosphorylationPANKRRSTLITVLNI
CCCCCCCEEEEEEEH		21.9926074081
294PhosphorylationKRRSTLITVLNISEI
CCCCEEEEEEEHHHH		23.2726074081
297N-linked_GlycosylationSTLITVLNISEIESR
CEEEEEEEHHHHHHH		31.25UniProtKB CARBOHYD
299PhosphorylationLITVLNISEIESRFY
EEEEEEHHHHHHHHH		31.2926074081
409UbiquitinationDCDIFVFKVLPEVLE
CCCEEEEEEHHHHHH		37.24-
496PhosphorylationELEKIQDYEKMPESI
EHHHHCCHHHCCHHH		10.9022817900
536PhosphorylationRFWKNVRYHMPVQRR
HHHEEEEECCCCCCC		9.7424719451
544PhosphorylationHMPVQRRSPSSKHQL
CCCCCCCCCCCCCCC		31.1824719451
553PhosphorylationSSKHQLLSPATKEKL
CCCCCCCCHHHHHHH		22.5330108239
556PhosphorylationHQLLSPATKEKLQRE
CCCCCHHHHHHHHHH		43.0230108239
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 IL1R1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL1R1_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 IL1R1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIGIR_HUMANSIGIRRphysical
12925853
IL1AP_HUMANIL1RAPphysical
9371760
P85A_HUMANPIK3R1physical
9360994
TOLIP_HUMANTOLLIPphysical
10854325
MYD88_HUMANMYD88physical
10854325
MYD88_HUMANMYD88physical
9374458
IL1RA_HUMANIL1RNphysical
9062194
TOLIP_HUMANTOLLIPphysical
17113392
TOM1_HUMANTOM1physical
17113392
MYD88_HUMANMYD88physical
12609980
IRAK4_HUMANIRAK4physical
12609980
IRAK1_HUMANIRAK1physical
12609980
TRAF6_HUMANTRAF6physical
12609980
IRAK1_HUMANIRAK1physical
12242293
TRAF6_HUMANTRAF6physical
12242293
MARH8_HUMANMARCH8physical
22904187
MYD88_HUMANMYD88physical
22904187
IRAK1_HUMANIRAK1physical
22904187
MYD88_HUMANMYD88physical
9575168
TCAM2_HUMANTICAM2physical
12721283
IRAK1_HUMANIRAK1physical
8599092
IRAK1_HUMANIRAK1physical
16024789
HERP1_HUMANHERPUD1physical
20054003
TRAF6_HUMANTRAF6physical
20064081
IRAK1_HUMANIRAK1physical
24735611
MYD88_HUMANMYD88physical
24735611
AT2A3_HUMANATP2A3physical
28514442
ICK_HUMANICKphysical
28514442
TBB8_HUMANTUBB8physical
28514442
MFAP3_HUMANMFAP3physical
28514442
TR10B_HUMANTNFRSF10Bphysical
28514442
BMR1A_HUMANBMPR1Aphysical
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 IL1R1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556, AND MASSSPECTROMETRY.

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