IL1B
entrez
3553
canonical
uniprot
P01584
canonical
ensembl
ENSG00000125538
resolver
ensp
ENSP00000263341
resolver
enst
ENST00000263341
resolver
genesymbol
IL1B
resolver
genesymbol_syn
IL1F2
resolver
hgnc
HGNC:5992
resolver
uniprot
Q53X59
resolver
uniprot
Q53XX2
resolver
uniprot
Q7M4S7
resolver
uniprot
Q7RU01
resolver
uniprot
Q96HE5
resolver
uniprot
Q9UCT6
resolver
uniprot_entry
IL1B_HUMAN
resolver
uniprot_sec
Q53X59
resolver
uniprot_sec
Q53XX2
resolver
uniprot_sec
Q7M4S7
resolver
uniprot_sec
Q7RU01
resolver
uniprot_sec
Q96HE5
resolver
uniprot_sec
Q9UCT6
resolver
activity_regulation
ACTIVITY REGULATION: (Microbial infection) Cleavage by S.pyogenes cysteine protease SpeB promotes its activation independently of CASP1 (PubMed:28331908, PubMed:32719155). SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota (PubMed:28331908, PubMed:32719155). {ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:32719155}.
uniprot
proteins
amino_acid_sequence
MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
uniprot
proteins
function
FUNCTION: Potent pro-inflammatory cytokine (PubMed:10653850, PubMed:12794819, PubMed:28331908, PubMed:3920526). Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production (PubMed:3920526). Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6 (PubMed:12794819). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33377178, PubMed:33883744). Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection (PubMed:28331908). {ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:3920526}.
uniprot
proteins
mass_dalton
30748
uniprot
proteins
mutagenesis
MUTAGEN 6..27; /note="ELASEMMAYYSGNEDDLFFEAD->ALASAMMAYYSGNAAALFFAAA: Promotes release of IL1B precursors through the Gasdermin-D (GSDMD) ring-shaped pore complex."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 27; /note="D->A: Loss of activation by CASP1; when associated with A-116."; /evidence="ECO:0000269|PubMed:24952504"; MUTAGEN 87..111; /note="ENDLSTFFPFIFEEEPIFFDTWDNE->ANDLSTFFPFIFAAAPIFFATWANA: Promotes release of IL1B precursors through the Gasdermin-D (GSDMD) ring-shaped pore complex."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 116; /note="D->A: Abolishes cleavage of pro-IL1B. Loss of activation by CASP1; when associated with A-27."; /evidence="ECO:0000269|PubMed:24952504, ECO:0000269|PubMed:2787508"; MUTAGEN 171; /note="K->E: Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-190; E-204 and C-233."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 179; /note="K->E: Suppression of integrin binding; when associated with E-181 and K-244. Markedly reduced activity; when associated with E-181; E-190; E-204 and C-233."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 181; /note="K->E: Suppression of integrin binding; when associated with E-179 and K-244. Markedly reduced activity; when associated with E-179; E-190; E-204 and C-233."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 190; /note="K->E: Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-171; E-204 and C-233. Markedly reduced activity; when associated with E-179; E-181; E-204 and C-233."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 204; /note="K->E: Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-171; E-190 and C-233. Markedly reduced activity; when associated with E-179; E-181; E-190 and C-233."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 221; /note="E->K: Enhanced integrin binding."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 233; /note="F->C: No effect on binding to IL1R or on IL1B activity. Markedly reduced activity; when associated with E-171; E-190 and E-204. Markedly reduced activity; when associated with E-179; E-181; E-190 and E-204."; /evidence="ECO:0000269|PubMed:29030430"; MUTAGEN 244; /note="E->K: Increased affinity for integrin ITGAV:ITGB3. Suppression of integrin binding; when associated with E-171; E-190 or E-204. Suppression of integrin binding; when associated with E-179 and E-181."; /evidence="ECO:0000269|PubMed:29030430
uniprot
proteins
post_translational_modification
PTM: Synthesized as an inactive precursor pro-IL1B. Its activation requires proteolytic processing by caspase-1 (CASP1), which cleaves the precursor to remove the N-terminal pro-peptide, thereby generating the mature, biologically active cytokine. {ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:2787508}.; PTM: (Microbial infection) Cleavage by S.pyogenes cysteine protease SpeB promotes its activation independently of CASP1. {ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:32719155, ECO:0000269|PubMed:7689226}.
uniprot
proteins
protein_family
IL-1 family
uniprot
proteins
pubmed
10653850
uniprot
proteins
pubmed
11728343
uniprot
proteins
pubmed
11991722
uniprot
proteins
pubmed
12794819
uniprot
proteins
pubmed
15192144
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1574116
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17431422
uniprot
proteins
pubmed
1837236
uniprot
proteins
pubmed
1919436
uniprot
proteins
pubmed
2001363
uniprot
proteins
pubmed
20148899
uniprot
proteins
pubmed
20802483
uniprot
proteins
pubmed
2372550
uniprot
proteins
pubmed
23955712
uniprot
proteins
pubmed
24201029
uniprot
proteins
pubmed
24952504
uniprot
proteins
pubmed
2585509
uniprot
proteins
pubmed
2602367
uniprot
proteins
pubmed
2635664
uniprot
proteins
pubmed
2787508
uniprot
proteins
pubmed
28331908
uniprot
proteins
pubmed
29030430
uniprot
proteins
pubmed
2954882
uniprot
proteins
pubmed
2989698
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
3259176
uniprot
proteins
pubmed
32719155
uniprot
proteins
pubmed
3281727
uniprot
proteins
pubmed
33377178
uniprot
proteins
pubmed
33883744
uniprot
proteins
pubmed
3490654
uniprot
proteins
pubmed
3493774
uniprot
proteins
pubmed
3920526
uniprot
proteins
pubmed
6083565
uniprot
proteins
pubmed
7689226
uniprot
proteins
pubmed
9062193
uniprot
proteins
sequence_length
269
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15192144}. Secreted {ECO:0000269|PubMed:11728343, ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:33883744}. Lysosome {ECO:0000269|PubMed:15192144}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic (PubMed:15192144). In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted (PubMed:24201029, PubMed:33377178, PubMed:33883744). Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation (PubMed:33883744). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:24201029, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:33883744}.
uniprot
proteins