UniProt ID | IL1R1_MOUSE | |
---|---|---|
UniProt AC | P13504 | |
Protein Name | Interleukin-1 receptor type 1 | |
Gene Name | Il1r1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 576 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein. Cell membrane . Secreted. |
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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 (By similarity).; Isoform 2: Unable to mediate canonical IL-1 signaling. Cooperates with IL1RAP isoform 3 to mediate IL1B-induced neuronal activity including IL1B-potentiated NMDA-induced calcium influx mediated by Akt kinase activation.. | |
Protein Sequence | MENMKVLLGLICLMVPLLSLEIDVCTEYPNQIVLFLSVNEIDIRKCPLTPNKMHGDTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVLENDPGLCYSTQATFPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQYPVTRVIQFITIDENKRDRPVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQFYRYPFICVVKNTNIFESAHVQLIYPVPDFKNYLIGGFIILTATIVCCVCIYKVFKVDIVLWYRDSCSGFLPSKASDGKTYDAYILYPKTLGEGSFSDLDTFVFKLLPEVLEGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSWLGQSSEEQIAIYNALIQEGIKIVLLELEKIQDYEKMPDSIQFIKQKHGVICWSGDFQERPQSAKTRFWKNLRYQMPAQRRSPLSKHRLLTLDPVRDTKEKLPAATHLPLG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
63 | N-linked_Glycosylation | DTIIWYKNDSKTPIS CEEEEEECCCCCCCC | 42.99 | - | |
103 | N-linked_Glycosylation | YYYCIVRNSTYCLKT EEEEEEECCEEEEEE | 28.01 | - | |
147 | Phosphorylation | DGSLVCPYVSYFKDE CCCEECCEEEEECCC | 9.26 | 28576409 | |
150 | Phosphorylation | LVCPYVSYFKDENNE EECCEEEEECCCCCC | 12.47 | 28576409 | |
174 | N-linked_Glycosylation | CKPLLLDNVSFFGVK CCEEEECCCEEECCC | 31.16 | - | |
236 | N-linked_Glycosylation | PVILSPRNETIEADP CEEECCCCCCEECCC | 54.90 | - | |
252 | N-linked_Glycosylation | SMIQLICNVTGQFSD CEEEHHHHHHCCCCC | 27.65 | - | |
266 | N-linked_Glycosylation | DLVYWKWNGSEIEWN CEEEEEECCCCCEEC | 40.15 | - | |
293 | Phosphorylation | HPSTKRKYTLITTLN CCCCCCEEEEEEEEE | 15.71 | 30635358 | |
294 | Phosphorylation | PSTKRKYTLITTLNI CCCCCEEEEEEEEEH | 18.08 | 30635358 | |
297 | Phosphorylation | KRKYTLITTLNISEV CCEEEEEEEEEHHHH | 28.48 | 30635358 | |
298 | Phosphorylation | RKYTLITTLNISEVK CEEEEEEEEEHHHHH | 15.71 | 30635358 | |
300 | N-linked_Glycosylation | YTLITTLNISEVKSQ EEEEEEEEHHHHHHH | 33.38 | - | |
302 | Phosphorylation | LITTLNISEVKSQFY EEEEEEHHHHHHHHH | 34.95 | 30635358 | |
402 | Phosphorylation | PKTLGEGSFSDLDTF CCCCCCCCCHHHHHH | 19.78 | 25338131 | |
499 | Phosphorylation | ELEKIQDYEKMPDSI EHHHHCCHHHCCCHH | 10.90 | - | |
501 | Ubiquitination | EKIQDYEKMPDSIQF HHHCCHHHCCCHHHH | 49.88 | 22790023 | |
505 | Phosphorylation | DYEKMPDSIQFIKQK CHHHCCCHHHHHHHH | 16.66 | 23984901 | |
547 | Phosphorylation | QMPAQRRSPLSKHRL CCCCCCCCCCCCCCE | 32.17 | 22324799 | |
550 | Phosphorylation | AQRRSPLSKHRLLTL CCCCCCCCCCCEEEC | 29.78 | 22324799 | |
556 | Phosphorylation | LSKHRLLTLDPVRDT CCCCCEEECCCCCCC | 33.43 | 22817900 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
556 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
556 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
556 | T | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IL1R1_MOUSE !! |
* 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_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
IRAK4_MOUSE | Irak4 | physical | 17507369 | |
IL1A_MOUSE | Il1a | physical | 17507369 | |
IL1AP_MOUSE | Il1rap | physical | 17507369 | |
MYD88_MOUSE | Myd88 | physical | 17507369 | |
IRAK1_MOUSE | Irak1 | physical | 17507369 | |
IRAK1_HUMAN | IRAK1 | physical | 9426216 | |
IRAK4_MOUSE | Irak4 | physical | 15292196 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phorbol ester induces phosphorylation of the 80 kilodalton murineinterleukin 1 receptor at a single threonine residue."; Bird T.A., Woodward A., Jackson J.L., Dower S.K., Sims J.E.; Biochem. Biophys. Res. Commun. 177:61-67(1991). Cited for: PHOSPHORYLATION AT THR-556. |