IL1B_HUMAN
ID IL1B_HUMAN Reviewed; 269 AA.
AC P01584; Q53X59; Q53XX2; Q7M4S7; Q7RU01; Q96HE5; Q9UCT6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 248.
DE RecName: Full=Interleukin-1 beta {ECO:0000303|PubMed:1919436};
DE Short=IL-1 beta {ECO:0000303|PubMed:1919436};
DE AltName: Full=Catabolin;
DE Flags: Precursor;
GN Name=IL1B {ECO:0000312|HGNC:HGNC:5992}; Synonyms=IL1F2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6083565; DOI=10.1073/pnas.81.24.7907;
RA Auron P.E., Webb A.C., Rosenwasser L.J., Mucci S.F., Rich A., Wolff S.M.,
RA Dinarello C.A.;
RT "Nucleotide sequence of human monocyte interleukin 1 precursor cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7907-7911(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2989698; DOI=10.1038/315641a0;
RA March C.J., Mosley B., Larsen A., Cerretti D.P., Braedt G., Price V.,
RA Gillis S., Henney C.S., Kronheim S.R., Grabstein K., Conlon P.J.,
RA Hopp T.P., Cosman D.;
RT "Cloning, sequence and expression of two distinct human interleukin-1
RT complementary DNAs.";
RL Nature 315:641-647(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=3490654; DOI=10.1093/nar/14.20.7897;
RA Clark B.D., Collins K.L., Gandy M.S., Webb A.C., Auron P.E.;
RT "Genomic sequence for human prointerleukin 1 beta: possible evolution from
RT a reverse transcribed prointerleukin 1 alpha gene.";
RL Nucleic Acids Res. 14:7897-7914(1986).
RN [4]
RP ERRATUM OF PUBMED:3490654.
RA Clark B.D., Collins K.L., Gandy M.S., Webb A.C., Auron P.E.;
RL Nucleic Acids Res. 15:868-868(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Histiocytic lymphoma;
RX PubMed=3493774; DOI=10.1016/0006-291x(87)90671-1;
RA Nishida T., Nishino N., Takano M., Kawai K., Bando K., Masui Y., Nakai S.,
RA Hirai Y.;
RT "cDNA cloning of IL-1 alpha and IL-1 beta from mRNA of U937 cell line.";
RL Biochem. Biophys. Res. Commun. 143:345-352(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2954882; DOI=10.1016/0378-1119(87)90398-2;
RA Bensi G., Raugei G., Palla E., Carinci V., Buonamassa D.T., Melli M.;
RT "Human interleukin-1 beta gene.";
RL Gene 52:95-101(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Monocyte;
RX PubMed=2635664;
RA Kotenko S.V., Bulenkov M.T., Veiko V.P., Epishin S.M., Lomakin I.B.,
RA Emel'Yanov A.V., Kozlov A.P., Konusova V.G., Kotov A.Y., Kurbatova T.V.,
RA Reshetnikov V.L., Simbirtsev A.S., Ketlinskii S.A., Vinetskii Y.P.;
RT "Cloning of the cDNA coding for human prointerleukin-1 alpha and
RT prointerleukin-1 beta.";
RL Dokl. Akad. Nauk SSSR 309:1005-1008(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11991722; DOI=10.1006/geno.2002.6751;
RA Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G.,
RA Kornman K.;
RT "A sequence-based map of the nine genes of the human interleukin-1
RT cluster.";
RL Genomics 79:718-725(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP PROTEIN SEQUENCE OF 114-135.
RC TISSUE=Skin;
RX PubMed=1919436; DOI=10.1084/jem.174.4.821;
RA Mizutani H., Schechter N., Lazarus G., Black R.A., Kupper T.S.;
RT "Rapid and specific conversion of precursor interleukin 1 beta (IL-1 beta)
RT to an active IL-1 species by human mast cell chymase.";
RL J. Exp. Med. 174:821-825(1991).
RN [16]
RP PROTEIN SEQUENCE OF 117-155, VARIANT ASN-141, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3920526; DOI=10.1038/314266a0;
RA Van Damme J., De Ley M., Opdenakker G., Billiau A., De Somer P.,
RA Van Beeumen J.;
RT "Homogeneous interferon-inducing 22K factor is related to endogenous
RT pyrogen and interleukin-1.";
RL Nature 314:266-268(1985).
RN [17]
RP PROTEIN SEQUENCE OF 117-128.
RX PubMed=3281727;
RA Zsebo K.M., Wypych J., Yuschenkoff V.N., Lu H., Hunt P., Dukes P.P.,
RA Langley K.E.;
RT "Effects of hematopoietin-1 and interleukin 1 activities on early
RT hematopoietic cells of the bone marrow.";
RL Blood 71:962-968(1988).
RN [18]
RP RECEPTOR-BINDING.
RX PubMed=1837236; DOI=10.1016/0167-4838(91)90437-5;
RA Nanduri V.B., Hulmes J.D., Pan Y.C., Kilian P.L., Stern A.S.;
RT "The role of arginine residues in interleukin 1 receptor binding.";
RL Biochim. Biophys. Acta 1118:25-35(1991).
RN [19]
RP FUNCTION.
RX PubMed=10653850; DOI=10.1093/intimm/12.2.151;
RA Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K., Hada T.,
RA Okamura H., Nakanishi K.;
RT "IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
RT human T cells.";
RL Int. Immunol. 12:151-160(2000).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=11728343; DOI=10.1016/s1074-7613(01)00229-1;
RA MacKenzie A., Wilson H.L., Kiss-Toth E., Dower S.K., North R.A.,
RA Surprenant A.;
RT "Rapid secretion of interleukin-1beta by microvesicle shedding.";
RL Immunity 15:825-835(2001).
RN [21]
RP FUNCTION.
RX PubMed=12794819; DOI=10.1002/art.11143;
RA Nakahara H., Song J., Sugimoto M., Hagihara K., Kishimoto T., Yoshizaki K.,
RA Nishimoto N.;
RT "Anti-interleukin-6 receptor antibody therapy reduces vascular endothelial
RT growth factor production in rheumatoid arthritis.";
RL Arthritis Rheum. 48:1521-1529(2003).
RN [22]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY LPS, AND PROCESSING
RP BY THE INFLAMMASOME.
RX PubMed=15192144; DOI=10.1073/pnas.0308558101;
RA Andrei C., Margiocco P., Poggi A., Lotti L.V., Torrisi M.R., Rubartelli A.;
RT "Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion:
RT Implications for inflammatory processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9745-9750(2004).
RN [23]
RP INTERACTION WITH MEFV.
RX PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
RA Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
RA Grutter C., Grutter M., Tschopp J.;
RT "The SPRY domain of Pyrin, mutated in familial Mediterranean fever
RT patients, interacts with inflammasome components and inhibits proIL-1beta
RT processing.";
RL Cell Death Differ. 14:1457-1466(2007).
RN [24]
RP INDUCTION BY M.TUBERCULOSIS.
RC TISSUE=Macrophage;
RX PubMed=20148899; DOI=10.1111/j.1462-5822.2010.01450.x;
RA Mishra B.B., Moura-Alves P., Sonawane A., Hacohen N., Griffiths G.,
RA Moita L.F., Anes E.;
RT "Mycobacterium tuberculosis protein ESAT-6 is a potent activator of the
RT NLRP3/ASC inflammasome.";
RL Cell. Microbiol. 12:1046-1063(2010).
RN [25]
RP INDUCTION BY ENDOCANNABINOID ANANDAMIDE AND HIGH GLUCOSE.
RX PubMed=23955712; DOI=10.1038/nm.3265;
RA Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J., Tam J.,
RA Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M., Czech M.P.,
RA Kunos G.;
RT "Activation of the Nlrp3 inflammasome in infiltrating macrophages by
RT endocannabinoids mediates beta cell loss in type 2 diabetes.";
RL Nat. Med. 19:1132-1140(2013).
RN [26]
RP REVIEW ON SECRETION, AND SUBCELLULAR LOCATION.
RX PubMed=24201029; DOI=10.1016/j.smim.2013.10.007;
RA Piccioli P., Rubartelli A.;
RT "The secretion of IL-1beta and options for release.";
RL Semin. Immunol. 25:425-429(2013).
RN [27]
RP MUTAGENESIS OF ASP-27 AND ASP-116.
RX PubMed=24952504; DOI=10.1038/ni.2919;
RA Baroja-Mazo A., Martin-Sanchez F., Gomez A.I., Martinez C.M.,
RA Amores-Iniesta J., Compan V., Barbera-Cremades M., Yaguee J.,
RA Ruiz-Ortiz E., Anton J., Bujan S., Couillin I., Brough D., Arostegui J.I.,
RA Pelegrin P.;
RT "The NLRP3 inflammasome is released as a particulate danger signal that
RT amplifies the inflammatory response.";
RL Nat. Immunol. 15:738-748(2014).
RN [28]
RP INTERACTION WITH INTEGRINS ITGAV:ITGB3 AND ITGA5:ITGB1, SITES IMPORTANT FOR
RP INTEGRIN BINDING, AND MUTAGENESIS OF LYS-171; LYS-179; LYS-181; LYS-190;
RP LYS-204; GLU-221; PHE-233 AND GLU-244.
RX PubMed=29030430; DOI=10.1074/jbc.m117.818302;
RA Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.;
RT "Direct binding to integrins and loss of disulfide linkage in interleukin-
RT 1beta (IL-1beta) are involved in the agonistic action of IL-1beta.";
RL J. Biol. Chem. 292:20067-20075(2017).
RN [29]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10; HSP90AB AND HSP90B1.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [30]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33377178; DOI=10.1111/iej.13469;
RA Tian X.X., Li R., Liu C., Liu F., Yang L.J., Wang S.P., Wang C.L.;
RT "NLRP6-caspase 4 inflammasome activation in response to cariogenic
RT bacterial lipoteichoic acid in human dental pulp inflammation.";
RL Int. Endod. J. 54:916-925(2021).
RN [31]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 6-GLU--ASP-27 AND 87-GLU--GLU-111.
RX PubMed=33883744; DOI=10.1038/s41586-021-03478-3;
RA Xia S., Zhang Z., Magupalli V.G., Pablo J.L., Dong Y., Vora S.M., Wang L.,
RA Fu T.M., Jacobson M.P., Greka A., Lieberman J., Ruan J., Wu H.;
RT "Gasdermin D pore structure reveals preferential release of mature
RT interleukin-1.";
RL Nature 593:607-611(2021).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=3259176; DOI=10.1002/j.1460-2075.1988.tb02818.x;
RA Priestle J.P., Schar H.-P., Grutter M.G.;
RT "Crystal structure of the cytokine interleukin-1 beta.";
RL EMBO J. 7:339-343(1988).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2585509; DOI=10.1016/0022-2836(89)90606-2;
RA Finzel B.C., Clancy L.L., Holland D.R., Muchmore S.W., Watenpaugh K.D.,
RA Einspahr H.M.;
RT "Crystal structure of recombinant human interleukin-1 beta at 2.0-A
RT resolution.";
RL J. Mol. Biol. 209:779-791(1989).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2602367; DOI=10.1073/pnas.86.24.9667;
RA Priestle J.P., Schar H.-P., Gruetter M.G.;
RT "Crystallographic refinement of interleukin 1 beta at 2.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9667-9671(1989).
RN [35]
RP STRUCTURE BY NMR.
RX PubMed=2372550; DOI=10.1021/bi00471a023;
RA Driscoll P.C., Gronenborn A.M., Wingfield P.T., Clore G.M.;
RT "Determination of the secondary structure and molecular topology of
RT interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-
RT 1H NMR spectroscopy.";
RL Biochemistry 29:4668-4682(1990).
RN [36]
RP STRUCTURE BY NMR.
RX PubMed=2001363; DOI=10.1021/bi00223a005;
RA Clore G.M., Wingfield P.T., Gronenborn A.M.;
RT "High-resolution three-dimensional structure of interleukin 1 beta in
RT solution by three- and four-dimensional nuclear magnetic resonance
RT spectroscopy.";
RL Biochemistry 30:2315-2323(1991).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
RX PubMed=9062193; DOI=10.1038/386190a0;
RA Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.;
RT "Crystal structure of the type-I interleukin-1 receptor complexed with
RT interleukin-1beta.";
RL Nature 386:190-194(1997).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 117-269 IN COMPLEX WITH IL1R2 AND
RP IL1RAP.
RX PubMed=20802483; DOI=10.1038/ni.1925;
RA Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
RT "Structural insights into the assembly and activation of IL-1beta with its
RT receptors.";
RL Nat. Immunol. 11:905-911(2010).
CC -!- FUNCTION: Potent pro-inflammatory cytokine (PubMed:3920526,
CC PubMed:10653850, PubMed:12794819). Initially discovered as the major
CC endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx
CC and activation, T-cell activation and cytokine production, B-cell
CC activation and antibody production, and fibroblast proliferation and
CC collagen production (PubMed:3920526). Promotes Th17 differentiation of
CC T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis
CC from T-helper 1 (Th1) cells (PubMed:10653850). Plays a role in
CC angiogenesis by inducing VEGF production synergistically with TNF and
CC IL6 (PubMed:12794819). Involved in transduction of inflammation
CC downstream of pyroptosis: its mature form is specifically released in
CC the extracellular milieu by passing through the gasdermin-D (GSDMD)
CC pore (PubMed:33377178, PubMed:33883744). {ECO:0000269|PubMed:10653850,
CC ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:33377178,
CC ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:3920526}.
CC -!- SUBUNIT: Monomer. In its precursor form, weakly interacts with full-
CC length MEFV; the mature cytokine does not interact at all
CC (PubMed:17431422). Interacts with integrins ITGAV:ITGBV and
CC ITGA5:ITGB1; integrin-binding is required for IL1B signaling
CC (PubMed:29030430). Interacts with cargo receptor TMED10; the
CC interaction is direct and is required for the secretion of IL1B mature
CC form (PubMed:32272059). Interacts with HSP90AB1; the interaction
CC facilitates cargo translocation into the ERGIC (PubMed:32272059).
CC Interacts with HSP90B1; the interaction facilitates cargo translocation
CC into the ERGIC (PubMed:32272059). {ECO:0000269|PubMed:17431422,
CC ECO:0000269|PubMed:20802483, ECO:0000269|PubMed:29030430,
CC ECO:0000269|PubMed:32272059}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15192144}.
CC Secreted {ECO:0000269|PubMed:11728343, ECO:0000269|PubMed:15192144,
CC ECO:0000269|PubMed:33883744}. Lysosome {ECO:0000269|PubMed:15192144}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}.
CC Note=The precursor is cytosolic (PubMed:15192144). In response to
CC inflammasome-activating signals, such as ATP for NLRP3 inflammasome or
CC bacterial flagellin for NLRC4 inflammasome, cleaved and secreted
CC (PubMed:24201029, PubMed:33377178, PubMed:33883744). Mature form is
CC secreted and released in the extracellular milieu by passing through
CC the gasdermin-D (GSDMD) pore (PubMed:33883744). In contrast, the
CC precursor form is not released, due to the presence of an acidic region
CC that is proteolytically removed by CASP1 during maturation
CC (PubMed:33883744). The secretion is dependent on protein unfolding and
CC facilitated by the cargo receptor TMED10 (PubMed:32272059).
CC {ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:24201029,
CC ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33377178,
CC ECO:0000269|PubMed:33883744}.
CC -!- TISSUE SPECIFICITY: Expressed in activated monocytes/macrophages (at
CC protein level). {ECO:0000269|PubMed:15192144}.
CC -!- INDUCTION: By LPS (PubMed:15192144). Transcription and translation
CC induced by M.tuberculosis and a number of different M.tuberculosis
CC components in macrophages; EsxA is the most potent activator tested (at
CC protein level) (PubMed:20148899). In pancreatic islets, release is
CC increased by high glucose treatment. In pancreatic islets and
CC macrophages, release is also increased by endocannabinoid
CC anandamide/AEA (PubMed:23955712). {ECO:0000269|PubMed:15192144,
CC ECO:0000269|PubMed:20148899, ECO:0000269|PubMed:23955712}.
CC -!- PTM: Activation of the IL1B precursor involves a CASP1-catalyzed
CC proteolytic cleavage. Processing and secretion are temporarily
CC associated. {ECO:0000269|PubMed:15192144}.
CC -!- MISCELLANEOUS: The IL1B production occurs in 2 steps, each being
CC controlled by different stimuli. First, inflammatory signals, such as
CC LPS, stimulate the synthesis and promote the accumulation of cytosolic
CC stores of pro-IL1B (priming). Then additional signals are required for
CC inflammasome assembly, leading to CASP1 activation, pro-IL1B processing
CC and eventually secretion of the active cytokine. IL1B processing and
CC secretion are temporarily associated. {ECO:0000269|PubMed:15192144}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL1BID40950ch2q13.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_1";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il1b/";
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DR EMBL; K02770; AAA36106.1; -; mRNA.
DR EMBL; M54933; AAA59136.1; ALT_SEQ; mRNA.
DR EMBL; X02532; CAA26372.1; -; mRNA.
DR EMBL; X04500; CAA28185.1; -; Genomic_DNA.
DR EMBL; M15330; AAA59135.1; -; mRNA.
DR EMBL; M15840; AAA74137.1; -; Genomic_DNA.
DR EMBL; X56087; CAA39567.1; -; mRNA.
DR EMBL; BN000002; CAD29872.1; -; Genomic_DNA.
DR EMBL; BT007213; AAP35877.1; -; mRNA.
DR EMBL; CR407679; CAG28607.1; -; mRNA.
DR EMBL; AY137079; AAM88883.1; -; Genomic_DNA.
DR EMBL; AC079753; AAX88888.1; -; Genomic_DNA.
DR EMBL; CH471217; EAW73605.1; -; Genomic_DNA.
DR EMBL; BC008678; AAH08678.1; -; mRNA.
DR CCDS; CCDS2102.1; -.
DR PIR; A21851; A21851.
DR PIR; A25542; ICHU1B.
DR RefSeq; NP_000567.1; NM_000576.2.
DR PDB; 1HIB; X-ray; 2.40 A; A=117-269.
DR PDB; 1I1B; X-ray; 2.00 A; A=117-269.
DR PDB; 1IOB; X-ray; 2.00 A; A=117-269.
DR PDB; 1ITB; X-ray; 2.50 A; A=117-269.
DR PDB; 1L2H; X-ray; 1.54 A; A=117-269.
DR PDB; 1S0L; X-ray; 2.34 A; A=117-269.
DR PDB; 1T4Q; X-ray; 2.10 A; A=117-269.
DR PDB; 1TOO; X-ray; 2.10 A; A=117-269.
DR PDB; 1TP0; X-ray; 2.20 A; A=117-269.
DR PDB; 1TWE; X-ray; 2.10 A; A=117-269.
DR PDB; 1TWM; X-ray; 2.26 A; A=117-269.
DR PDB; 21BI; X-ray; 2.00 A; A=117-269.
DR PDB; 2I1B; X-ray; 2.00 A; A=117-269.
DR PDB; 2KH2; NMR; -; A=117-269.
DR PDB; 2NVH; X-ray; 1.53 A; A=117-269.
DR PDB; 31BI; X-ray; 2.00 A; A=117-269.
DR PDB; 3LTQ; X-ray; 2.10 A; A=117-269.
DR PDB; 3O4O; X-ray; 3.30 A; A=117-269.
DR PDB; 3POK; X-ray; 1.70 A; A=117-269.
DR PDB; 41BI; X-ray; 2.90 A; A=117-269.
DR PDB; 4DEP; X-ray; 3.10 A; A/D=117-269.
DR PDB; 4G6J; X-ray; 2.03 A; A=117-269.
DR PDB; 4G6M; X-ray; 1.81 A; A=118-267.
DR PDB; 4GAF; X-ray; 2.15 A; A=117-269.
DR PDB; 4GAI; X-ray; 1.49 A; A/B=117-269.
DR PDB; 4I1B; X-ray; 2.00 A; A=117-269.
DR PDB; 5BVP; X-ray; 2.20 A; I=117-269.
DR PDB; 5I1B; X-ray; 2.10 A; A=117-269.
DR PDB; 5MVZ; X-ray; 2.15 A; U/V=117-269.
DR PDB; 5R7W; X-ray; 1.27 A; A=117-269.
DR PDB; 5R85; X-ray; 1.44 A; A=117-269.
DR PDB; 5R86; X-ray; 1.50 A; A=117-269.
DR PDB; 5R87; X-ray; 1.47 A; A=117-269.
DR PDB; 5R88; X-ray; 1.48 A; A=117-269.
DR PDB; 5R89; X-ray; 1.65 A; A=117-269.
DR PDB; 5R8A; X-ray; 1.47 A; A=117-269.
DR PDB; 5R8B; X-ray; 1.49 A; A=117-269.
DR PDB; 5R8C; X-ray; 1.54 A; A=117-269.
DR PDB; 5R8D; X-ray; 1.47 A; A=117-269.
DR PDB; 5R8E; X-ray; 1.35 A; A=117-269.
DR PDB; 5R8F; X-ray; 1.41 A; A=117-269.
DR PDB; 5R8G; X-ray; 1.43 A; A=117-269.
DR PDB; 5R8H; X-ray; 1.50 A; A=117-269.
DR PDB; 5R8I; X-ray; 1.47 A; A=117-269.
DR PDB; 5R8J; X-ray; 1.62 A; A=117-269.
DR PDB; 5R8K; X-ray; 1.47 A; A=117-269.
DR PDB; 5R8L; X-ray; 1.56 A; A=117-269.
DR PDB; 5R8M; X-ray; 1.39 A; A=117-269.
DR PDB; 5R8N; X-ray; 1.48 A; A=117-269.
DR PDB; 5R8O; X-ray; 1.42 A; A=117-269.
DR PDB; 5R8P; X-ray; 1.53 A; A=117-269.
DR PDB; 5R8Q; X-ray; 1.23 A; A=117-269.
DR PDB; 6I1B; NMR; -; A=117-269.
DR PDB; 6Y8I; X-ray; 1.46 A; A=117-269.
DR PDB; 6Y8M; X-ray; 1.90 A; A=117-269.
DR PDB; 7CHY; X-ray; 2.65 A; I=117-269.
DR PDB; 7CHZ; X-ray; 2.50 A; I=117-269.
DR PDB; 7I1B; NMR; -; A=117-269.
DR PDB; 9ILB; X-ray; 2.28 A; A=117-269.
DR PDBsum; 1HIB; -.
DR PDBsum; 1I1B; -.
DR PDBsum; 1IOB; -.
DR PDBsum; 1ITB; -.
DR PDBsum; 1L2H; -.
DR PDBsum; 1S0L; -.
DR PDBsum; 1T4Q; -.
DR PDBsum; 1TOO; -.
DR PDBsum; 1TP0; -.
DR PDBsum; 1TWE; -.
DR PDBsum; 1TWM; -.
DR PDBsum; 21BI; -.
DR PDBsum; 2I1B; -.
DR PDBsum; 2KH2; -.
DR PDBsum; 2NVH; -.
DR PDBsum; 31BI; -.
DR PDBsum; 3LTQ; -.
DR PDBsum; 3O4O; -.
DR PDBsum; 3POK; -.
DR PDBsum; 41BI; -.
DR PDBsum; 4DEP; -.
DR PDBsum; 4G6J; -.
DR PDBsum; 4G6M; -.
DR PDBsum; 4GAF; -.
DR PDBsum; 4GAI; -.
DR PDBsum; 4I1B; -.
DR PDBsum; 5BVP; -.
DR PDBsum; 5I1B; -.
DR PDBsum; 5MVZ; -.
DR PDBsum; 5R7W; -.
DR PDBsum; 5R85; -.
DR PDBsum; 5R86; -.
DR PDBsum; 5R87; -.
DR PDBsum; 5R88; -.
DR PDBsum; 5R89; -.
DR PDBsum; 5R8A; -.
DR PDBsum; 5R8B; -.
DR PDBsum; 5R8C; -.
DR PDBsum; 5R8D; -.
DR PDBsum; 5R8E; -.
DR PDBsum; 5R8F; -.
DR PDBsum; 5R8G; -.
DR PDBsum; 5R8H; -.
DR PDBsum; 5R8I; -.
DR PDBsum; 5R8J; -.
DR PDBsum; 5R8K; -.
DR PDBsum; 5R8L; -.
DR PDBsum; 5R8M; -.
DR PDBsum; 5R8N; -.
DR PDBsum; 5R8O; -.
DR PDBsum; 5R8P; -.
DR PDBsum; 5R8Q; -.
DR PDBsum; 6I1B; -.
DR PDBsum; 6Y8I; -.
DR PDBsum; 6Y8M; -.
DR PDBsum; 7CHY; -.
DR PDBsum; 7CHZ; -.
DR PDBsum; 7I1B; -.
DR PDBsum; 9ILB; -.
DR AlphaFoldDB; P01584; -.
DR BMRB; P01584; -.
DR SMR; P01584; -.
DR BioGRID; 109769; 44.
DR DIP; DIP-474N; -.
DR IntAct; P01584; 8.
DR STRING; 9606.ENSP00000263341; -.
DR BindingDB; P01584; -.
DR ChEMBL; CHEMBL1909490; -.
DR DrugBank; DB05767; Andrographolide.
DR DrugBank; DB11967; Binimetinib.
DR DrugBank; DB06168; Canakinumab.
DR DrugBank; DB12140; Dilmapimod.
DR DrugBank; DB00843; Donepezil.
DR DrugBank; DB05442; Etiprednol dicloacetate.
DR DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DR DrugBank; DB05260; Gallium nitrate.
DR DrugBank; DB12119; Gevokizumab.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB06372; Rilonacept.
DR DrugBank; DB05412; Talmapimod.
DR DrugBank; DB05133; VP025.
DR DrugBank; DB05470; VX-702.
DR DrugBank; DB05507; VX-765.
DR DrugCentral; P01584; -.
DR TCDB; 1.A.109.1.2; the interleukin 1 (il1) family.
DR iPTMnet; P01584; -.
DR PhosphoSitePlus; P01584; -.
DR SwissPalm; P01584; -.
DR BioMuta; IL1B; -.
DR DMDM; 62906858; -.
DR EPD; P01584; -.
DR MassIVE; P01584; -.
DR MaxQB; P01584; -.
DR PaxDb; P01584; -.
DR PeptideAtlas; P01584; -.
DR PRIDE; P01584; -.
DR ProteomicsDB; 51391; -.
DR ABCD; P01584; 8 sequenced antibodies.
DR Antibodypedia; 771; 2277 antibodies from 49 providers.
DR DNASU; 3553; -.
DR Ensembl; ENST00000263341.7; ENSP00000263341.2; ENSG00000125538.12.
DR GeneID; 3553; -.
DR KEGG; hsa:3553; -.
DR MANE-Select; ENST00000263341.7; ENSP00000263341.2; NM_000576.3; NP_000567.1.
DR UCSC; uc002tii.2; human.
DR CTD; 3553; -.
DR DisGeNET; 3553; -.
DR GeneCards; IL1B; -.
DR HGNC; HGNC:5992; IL1B.
DR HPA; ENSG00000125538; Tissue enhanced (bone marrow, urinary bladder).
DR MalaCards; IL1B; -.
DR MIM; 147720; gene.
DR neXtProt; NX_P01584; -.
DR OpenTargets; ENSG00000125538; -.
DR PharmGKB; PA29808; -.
DR VEuPathDB; HostDB:ENSG00000125538; -.
DR eggNOG; ENOG502S3E9; Eukaryota.
DR GeneTree; ENSGT00950000182943; -.
DR HOGENOM; CLU_083639_0_0_1; -.
DR InParanoid; P01584; -.
DR OMA; QHYSKGF; -.
DR OrthoDB; 1243742at2759; -.
DR PhylomeDB; P01584; -.
DR TreeFam; TF300203; -.
DR PathwayCommons; P01584; -.
DR Reactome; R-HSA-448706; Interleukin-1 processing.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; P01584; -.
DR SIGNOR; P01584; -.
DR BioGRID-ORCS; 3553; 41 hits in 1067 CRISPR screens.
DR ChiTaRS; IL1B; human.
DR EvolutionaryTrace; P01584; -.
DR GeneWiki; IL1B; -.
DR GenomeRNAi; 3553; -.
DR Pharos; P01584; Tclin.
DR PRO; PR:P01584; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01584; protein.
DR Bgee; ENSG00000125538; Expressed in periodontal ligament and 158 other tissues.
DR ExpressionAtlas; P01584; baseline and differential.
DR Genevisible; P01584; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0005149; F:interleukin-1 receptor binding; NAS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0097398; P:cellular response to interleukin-17; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; TAS:BHF-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0070487; P:monocyte aggregation; IDA:UniProtKB.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; ISS:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
DR GO; GO:1903597; P:negative regulation of gap junction assembly; IDA:ARUK-UCL.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:BHF-UCL.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; ISS:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:BHF-UCL.
DR GO; GO:0050768; P:negative regulation of neurogenesis; TAS:ARUK-UCL.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:ARUK-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; NAS:BHF-UCL.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0045917; P:positive regulation of complement activation; IGI:ARUK-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IGI:ARUK-UCL.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; NAS:BHF-UCL.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; NAS:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:ARUK-UCL.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; ISS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IDA:UniProtKB.
DR GO; GO:0035505; P:positive regulation of myosin light chain kinase activity; IDA:BHF-UCL.
DR GO; GO:0150078; P:positive regulation of neuroinflammatory response; TAS:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISS:BHF-UCL.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; NAS:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:1902680; P:positive regulation of RNA biosynthetic process; IDA:ARUK-UCL.
DR GO; GO:0002711; P:positive regulation of T cell mediated immunity; IC:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IC:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0050796; P:regulation of insulin secretion; IDA:BHF-UCL.
DR GO; GO:0050767; P:regulation of neurogenesis; ISS:ARUK-UCL.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR GO; GO:0070555; P:response to interleukin-1; IDA:ARUK-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:ARUK-UCL.
DR GO; GO:0030730; P:sequestering of triglyceride; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0014805; P:smooth muscle adaptation; NAS:BHF-UCL.
DR GO; GO:0010573; P:vascular endothelial growth factor production; IDA:UniProtKB.
DR InterPro; IPR003296; IL-1_beta.
DR InterPro; IPR020877; IL-1_CS.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003502; IL-1_propep.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF30; PTHR10078:SF30; 1.
DR Pfam; PF00340; IL1; 1.
DR Pfam; PF02394; IL1_propep; 1.
DR PRINTS; PR00264; INTERLEUKIN1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00253; INTERLEUKIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Cytoplasm; Direct protein sequencing;
KW Inflammatory response; Lysosome; Mitogen; Pyrogen; Reference proteome;
KW Secreted.
FT PROPEP 1..116
FT /note="Removed in mature form; by CASP1"
FT /evidence="ECO:0000269|PubMed:3281727,
FT ECO:0000269|PubMed:3920526"
FT /id="PRO_0000015301"
FT CHAIN 117..269
FT /note="Interleukin-1 beta"
FT /evidence="ECO:0000269|PubMed:2001363"
FT /id="PRO_0000015302"
FT MOTIF 228..241
FT /note="Involved in interaction with TMED10 C-terminus"
FT /evidence="ECO:0000269|PubMed:32272059"
FT SITE 120
FT /note="Involved in receptor binding"
FT SITE 171
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:29030430"
FT SITE 179
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:29030430"
FT SITE 181
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:29030430"
FT SITE 190
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:29030430"
FT SITE 204
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:29030430"
FT VARIANT 141
FT /note="E -> N (requires 2 nucleotide substitutions;
FT dbSNP:rs144640380)"
FT /evidence="ECO:0000269|PubMed:3920526"
FT /id="VAR_073951"
FT MUTAGEN 6..27
FT /note="ELASEMMAYYSGNEDDLFFEAD->ALASAMMAYYSGNAAALFFAAA:
FT Promotes release of IL1B precursors through the Gasdermin-D
FT (GSDMD) ring-shaped pore complex."
FT /evidence="ECO:0000269|PubMed:33883744"
FT MUTAGEN 27
FT /note="D->A: Loss of activation by CASP1; when associated
FT with A-116."
FT /evidence="ECO:0000269|PubMed:24952504"
FT MUTAGEN 87..111
FT /note="ENDLSTFFPFIFEEEPIFFDTWDNE->ANDLSTFFPFIFAAAPIFFATWANA
FT : Promotes release of IL1B precursors through the
FT Gasdermin-D (GSDMD) ring-shaped pore complex."
FT /evidence="ECO:0000269|PubMed:33883744"
FT MUTAGEN 116
FT /note="D->A: Loss of activation by CASP1; when associated
FT with A-27."
FT /evidence="ECO:0000269|PubMed:24952504"
FT MUTAGEN 171
FT /note="K->E: Suppression of integrin binding; when
FT associated with K-244. Markedly reduced activity; when
FT associated with E-190; E-204 and C-233."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 179
FT /note="K->E: Suppression of integrin binding; when
FT associated with E-181 and K-244. Markedly reduced activity;
FT when associated with E-181; E-190; E-204 and C-233."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 181
FT /note="K->E: Suppression of integrin binding; when
FT associated with E-179 and K-244. Markedly reduced activity;
FT when associated with E-179; E-190; E-204 and C-233."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 190
FT /note="K->E: Suppression of integrin binding; when
FT associated with K-244. Markedly reduced activity; when
FT associated with E-171; E-204 and C-233. Markedly reduced
FT activity; when associated with E-179; E-181; E-204 and C-
FT 233."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 204
FT /note="K->E: Suppression of integrin binding; when
FT associated with K-244. Markedly reduced activity; when
FT associated with E-171; E-190 and C-233. Markedly reduced
FT activity; when associated with E-179; E-181; E-190 and C-
FT 233."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 221
FT /note="E->K: Enhanced integrin binding."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 233
FT /note="F->C: No effect on binding to IL1R or on IL1B
FT activity. Markedly reduced activity; when associated with
FT E-171; E-190 and E-204. Markedly reduced activity; when
FT associated with E-179; E-181; E-190 and E-204."
FT /evidence="ECO:0000269|PubMed:29030430"
FT MUTAGEN 244
FT /note="E->K: Increased affinity for integrin ITGAV:ITGB3.
FT Suppression of integrin binding; when associated with E-
FT 171; E-190 or E-204. Suppression of integrin binding; when
FT associated with E-179 and E-181."
FT /evidence="ECO:0000269|PubMed:29030430"
FT CONFLICT 6
FT /note="E -> K (in Ref. 1; AAA36106/AAA59136 and 10;
FT CAG28607)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="C -> A (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Q -> D (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5R8Q"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:5R8Q"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:5R8Q"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:5R8F"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:5R8Q"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5R8Q"
SQ SEQUENCE 269 AA; 30748 MW; 9BF73C3673C6FD66 CRC64;
MAEVPELASE MMAYYSGNED DLFFEADGPK QMKCSFQDLD LCPLDGGIQL RISDHHYSKG
FRQAASVVVA MDKLRKMLVP CPQTFQENDL STFFPFIFEE EPIFFDTWDN EAYVHDAPVR
SLNCTLRDSQ QKSLVMSGPY ELKALHLQGQ DMEQQVVFSM SFVQGEESND KIPVALGLKE
KNLYLSCVLK DDKPTLQLES VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST
SQAENMPVFL GGTKGGQDIT DFTMQFVSS
