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Interleukin-1 beta (IL-1 beta) (Catabolin)

 IL1B_HUMAN              Reviewed;         269 AA.
P01584; Q53X59; Q53XX2; Q7M4S7; Q7RU01; Q96HE5; Q9UCT6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
02-JUN-2021, entry version 244.
RecName: Full=Interleukin-1 beta {ECO:0000303|PubMed:1919436};
Short=IL-1 beta {ECO:0000303|PubMed:1919436};
AltName: Full=Catabolin;
Flags: Precursor;
Name=IL1B {ECO:0000312|HGNC:HGNC:5992}; Synonyms=IL1F2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6083565; DOI=10.1073/pnas.81.24.7907;
Auron P.E., Webb A.C., Rosenwasser L.J., Mucci S.F., Rich A., Wolff S.M.,
Dinarello C.A.;
"Nucleotide sequence of human monocyte interleukin 1 precursor cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:7907-7911(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2989698; DOI=10.1038/315641a0;
March C.J., Mosley B., Larsen A., Cerretti D.P., Braedt G., Price V.,
Gillis S., Henney C.S., Kronheim S.R., Grabstein K., Conlon P.J.,
Hopp T.P., Cosman D.;
"Cloning, sequence and expression of two distinct human interleukin-1
complementary DNAs.";
Nature 315:641-647(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=3490654; DOI=10.1093/nar/14.20.7897;
Clark B.D., Collins K.L., Gandy M.S., Webb A.C., Auron P.E.;
"Genomic sequence for human prointerleukin 1 beta: possible evolution from
a reverse transcribed prointerleukin 1 alpha gene.";
Nucleic Acids Res. 14:7897-7914(1986).
[4]
ERRATUM OF PUBMED:3490654.
Clark B.D., Collins K.L., Gandy M.S., Webb A.C., Auron P.E.;
Nucleic Acids Res. 15:868-868(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Histiocytic lymphoma;
PubMed=3493774; DOI=10.1016/0006-291x(87)90671-1;
Nishida T., Nishino N., Takano M., Kawai K., Bando K., Masui Y., Nakai S.,
Hirai Y.;
"cDNA cloning of IL-1 alpha and IL-1 beta from mRNA of U937 cell line.";
Biochem. Biophys. Res. Commun. 143:345-352(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2954882; DOI=10.1016/0378-1119(87)90398-2;
Bensi G., Raugei G., Palla E., Carinci V., Buonamassa D.T., Melli M.;
"Human interleukin-1 beta gene.";
Gene 52:95-101(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Monocyte;
PubMed=2635664;
Kotenko S.V., Bulenkov M.T., Veiko V.P., Epishin S.M., Lomakin I.B.,
Emel'Yanov A.V., Kozlov A.P., Konusova V.G., Kotov A.Y., Kurbatova T.V.,
Reshetnikov V.L., Simbirtsev A.S., Ketlinskii S.A., Vinetskii Y.P.;
"Cloning of the cDNA coding for human prointerleukin-1 alpha and
prointerleukin-1 beta.";
Dokl. Akad. Nauk SSSR 309:1005-1008(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11991722; DOI=10.1006/geno.2002.6751;
Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G.,
Kornman K.;
"A sequence-based map of the nine genes of the human interleukin-1
cluster.";
Genomics 79:718-725(2002).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
PROTEIN SEQUENCE OF 114-135.
TISSUE=Skin;
PubMed=1919436; DOI=10.1084/jem.174.4.821;
Mizutani H., Schechter N., Lazarus G., Black R.A., Kupper T.S.;
"Rapid and specific conversion of precursor interleukin 1 beta (IL-1 beta)
to an active IL-1 species by human mast cell chymase.";
J. Exp. Med. 174:821-825(1991).
[16]
PROTEIN SEQUENCE OF 117-155, VARIANT ASN-141, FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=3920526; DOI=10.1038/314266a0;
Van Damme J., De Ley M., Opdenakker G., Billiau A., De Somer P.,
Van Beeumen J.;
"Homogeneous interferon-inducing 22K factor is related to endogenous
pyrogen and interleukin-1.";
Nature 314:266-268(1985).
[17]
PROTEIN SEQUENCE OF 117-128.
PubMed=3281727;
Zsebo K.M., Wypych J., Yuschenkoff V.N., Lu H., Hunt P., Dukes P.P.,
Langley K.E.;
"Effects of hematopoietin-1 and interleukin 1 activities on early
hematopoietic cells of the bone marrow.";
Blood 71:962-968(1988).
[18]
RECEPTOR-BINDING.
PubMed=1837236; DOI=10.1016/0167-4838(91)90437-5;
Nanduri V.B., Hulmes J.D., Pan Y.C., Kilian P.L., Stern A.S.;
"The role of arginine residues in interleukin 1 receptor binding.";
Biochim. Biophys. Acta 1118:25-35(1991).
[19]
FUNCTION.
PubMed=10653850; DOI=10.1093/intimm/12.2.151;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K., Hada T.,
Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[20]
SUBCELLULAR LOCATION.
PubMed=11728343; DOI=10.1016/s1074-7613(01)00229-1;
MacKenzie A., Wilson H.L., Kiss-Toth E., Dower S.K., North R.A.,
Surprenant A.;
"Rapid secretion of interleukin-1beta by microvesicle shedding.";
Immunity 15:825-835(2001).
[21]
FUNCTION.
PubMed=12794819; DOI=10.1002/art.11143;
Nakahara H., Song J., Sugimoto M., Hagihara K., Kishimoto T., Yoshizaki K.,
Nishimoto N.;
"Anti-interleukin-6 receptor antibody therapy reduces vascular endothelial
growth factor production in rheumatoid arthritis.";
Arthritis Rheum. 48:1521-1529(2003).
[22]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY LPS, AND PROCESSING
BY THE INFLAMMASOME.
PubMed=15192144; DOI=10.1073/pnas.0308558101;
Andrei C., Margiocco P., Poggi A., Lotti L.V., Torrisi M.R., Rubartelli A.;
"Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion:
Implications for inflammatory processes.";
Proc. Natl. Acad. Sci. U.S.A. 101:9745-9750(2004).
[23]
INTERACTION WITH MEFV.
PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
Grutter C., Grutter M., Tschopp J.;
"The SPRY domain of Pyrin, mutated in familial Mediterranean fever
patients, interacts with inflammasome components and inhibits proIL-1beta
processing.";
Cell Death Differ. 14:1457-1466(2007).
[24]
INDUCTION BY M.TUBERCULOSIS.
TISSUE=Macrophage;
PubMed=20148899; DOI=10.1111/j.1462-5822.2010.01450.x;
Mishra B.B., Moura-Alves P., Sonawane A., Hacohen N., Griffiths G.,
Moita L.F., Anes E.;
"Mycobacterium tuberculosis protein ESAT-6 is a potent activator of the
NLRP3/ASC inflammasome.";
Cell. Microbiol. 12:1046-1063(2010).
[25]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE AND HIGH GLUCOSE.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J., Tam J.,
Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M., Czech M.P.,
Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
[26]
REVIEW ON SECRETION, AND SUBCELLULAR LOCATION.
PubMed=24201029; DOI=10.1016/j.smim.2013.10.007;
Piccioli P., Rubartelli A.;
"The secretion of IL-1beta and options for release.";
Semin. Immunol. 25:425-429(2013).
[27]
MUTAGENESIS OF ASP-27 AND ASP-116.
PubMed=24952504; DOI=10.1038/ni.2919;
Baroja-Mazo A., Martin-Sanchez F., Gomez A.I., Martinez C.M.,
Amores-Iniesta J., Compan V., Barbera-Cremades M., Yaguee J.,
Ruiz-Ortiz E., Anton J., Bujan S., Couillin I., Brough D., Arostegui J.I.,
Pelegrin P.;
"The NLRP3 inflammasome is released as a particulate danger signal that
amplifies the inflammatory response.";
Nat. Immunol. 15:738-748(2014).
[28]
INTERACTION WITH INTEGRINS ITGAV:ITGB3 AND ITGA5:ITGB1, SITES IMPORTANT FOR
INTEGRIN BINDING, AND MUTAGENESIS OF LYS-171; LYS-179; LYS-181; LYS-190;
LYS-204; GLU-221; PHE-233 AND GLU-244.
PubMed=29030430; DOI=10.1074/jbc.m117.818302;
Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.;
"Direct binding to integrins and loss of disulfide linkage in interleukin-
1beta (IL-1beta) are involved in the agonistic action of IL-1beta.";
J. Biol. Chem. 292:20067-20075(2017).
[29]
SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10; HSP90AB AND HSP90B1.
PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
Zhang D., Lv X., Zheng L., Ge L.;
"A Translocation Pathway for Vesicle-Mediated Unconventional Protein
Secretion.";
Cell 181:637-652(2020).
[30]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3259176; DOI=10.1002/j.1460-2075.1988.tb02818.x;
Priestle J.P., Schar H.-P., Grutter M.G.;
"Crystal structure of the cytokine interleukin-1 beta.";
EMBO J. 7:339-343(1988).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2585509; DOI=10.1016/0022-2836(89)90606-2;
Finzel B.C., Clancy L.L., Holland D.R., Muchmore S.W., Watenpaugh K.D.,
Einspahr H.M.;
"Crystal structure of recombinant human interleukin-1 beta at 2.0-A
resolution.";
J. Mol. Biol. 209:779-791(1989).
[32]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2602367; DOI=10.1073/pnas.86.24.9667;
Priestle J.P., Schar H.-P., Gruetter M.G.;
"Crystallographic refinement of interleukin 1 beta at 2.0-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 86:9667-9671(1989).
[33]
STRUCTURE BY NMR.
PubMed=2372550; DOI=10.1021/bi00471a023;
Driscoll P.C., Gronenborn A.M., Wingfield P.T., Clore G.M.;
"Determination of the secondary structure and molecular topology of
interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-
1H NMR spectroscopy.";
Biochemistry 29:4668-4682(1990).
[34]
STRUCTURE BY NMR.
PubMed=2001363; DOI=10.1021/bi00223a005;
Clore G.M., Wingfield P.T., Gronenborn A.M.;
"High-resolution three-dimensional structure of interleukin 1 beta in
solution by three- and four-dimensional nuclear magnetic resonance
spectroscopy.";
Biochemistry 30:2315-2323(1991).
[35]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
PubMed=9062193; DOI=10.1038/386190a0;
Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.;
"Crystal structure of the type-I interleukin-1 receptor complexed with
interleukin-1beta.";
Nature 386:190-194(1997).
[36]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 117-269 IN COMPLEX WITH IL1R2 AND
IL1RAP.
PubMed=20802483; DOI=10.1038/ni.1925;
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
"Structural insights into the assembly and activation of IL-1beta with its
receptors.";
Nat. Immunol. 11:905-911(2010).
-!- FUNCTION: Potent proinflammatory cytokine. 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. 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). {ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:3920526}.
-!- SUBUNIT: Monomer. In its precursor form, weakly interacts with full-
length MEFV; the mature cytokine does not interact at all
(PubMed:17431422). Interacts with integrins ITGAV:ITGBV and
ITGA5:ITGB1; integrin-binding is required for IL1B signaling
(PubMed:29030430). Interacts with cargo receptor TMED10; the
interaction is direct and is required for the secretion of IL1B mature
form (PubMed:32272059). Interacts with HSP90AB1; the interaction
facilitates cargo translocation into the ERGIC (PubMed:32272059).
Interacts with HSP90B1; the interaction facilitates cargo translocation
into the ERGIC (PubMed:32272059). {ECO:0000269|PubMed:17431422,
ECO:0000269|PubMed:20802483, ECO:0000269|PubMed:29030430,
ECO:0000269|PubMed:32272059}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15192144}.
Lysosome {ECO:0000269|PubMed:15192144}. Secreted, extracellular exosome
{ECO:0000250|UniProtKB:P10749}. Secreted {ECO:0000269|PubMed:11728343,
ECO:0000269|PubMed:15192144}. Note=The precursor is cytosolic. In
response to inflammasome-activating signals, such as ATP for NLRP3
inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and
secreted. IL1B lacks any known signal sequence and the pathway(s) of
its secretion is(are) not yet fully understood (PubMed:24201029). On
the basis of experimental results, several unconventional secretion
mechanisms have been proposed. 1. Secretion via secretory lysosomes: a
fraction of CASP1 and IL1B precursor may be incorporated, by a yet
undefined mechanism, into secretory lysosomes that undergo Ca(2+)-
dependent exocytosis with release of mature IL1B (PubMed:15192144). 2.
Secretory autophagy: IL1B-containing autophagosomes may fuse with
endosomes or multivesicular bodies (MVBs) and then merge with the
plasma membrane releasing soluble IL1B or IL1B-containing exosomes
(PubMed:24201029). However, autophagy impacts IL1B production at
several levels and its role in secretion is still controversial. 3.
Secretion via exosomes: ATP-activation of P2RX7 leads to the formation
of MVBs containing exosomes with entrapped IL1B, CASP1 and other
inflammasome components. These MVBs undergo exocytosis with the release
of exosomes. The release of soluble IL1B occurs after the lysis of
exosome membranes (By similarity). 4. Secretion by microvesicle
shedding: activation of the ATP receptor P2RX7 may induce an immediate
shedding of membrane-derived microvesicles containing IL1B and possibly
inflammasome components. The cytokine is then released in the
extracellular compartment after microvesicle lysis (PubMed:11728343).
5. Release by translocation through permeabilized plasma membrane. This
may occur in cells undergoing pyroptosis due to sustained activation of
the inflammasome (By similarity). 6. The secretion is dependent on
protein unfolding and facilitated by the cargo receptor TMED10; it
results in the protein translocation from the cytoplasm into the ERGIC
(endoplasmic reticulum-Golgi intermediate compartment) followed by
vesicle entry and secretion, and enhanced by chaperones HSP90AB1 and
HSP90B1/GRP9 (PubMed:32272059). These mechanisms may not be mutually
exclusive. {ECO:0000250|UniProtKB:P10749, ECO:0000269|PubMed:11728343,
ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:32272059,
ECO:0000305|PubMed:24201029}.
-!- TISSUE SPECIFICITY: Expressed in activated monocytes/macrophages (at
protein level). {ECO:0000269|PubMed:15192144}.
-!- INDUCTION: By LPS (PubMed:15192144). Transcription and translation
induced by M.tuberculosis and a number of different M.tuberculosis
components in macrophages; EsxA is the most potent activator tested (at
protein level) (PubMed:20148899). In pancreatic islets, release is
increased by high glucose treatment. In pancreatic islets and
macrophages, release is also increased by endocannabinoid
anandamide/AEA (PubMed:23955712). {ECO:0000269|PubMed:15192144,
ECO:0000269|PubMed:20148899, ECO:0000269|PubMed:23955712}.
-!- PTM: Activation of the IL1B precursor involves a CASP1-catalyzed
proteolytic cleavage. Processing and secretion are temporarily
associated. {ECO:0000269|PubMed:15192144}.
-!- MISCELLANEOUS: The IL1B production occurs in 2 steps, each being
controlled by different stimuli. First, inflammatory signals, such as
LPS, stimulate the synthesis and promote the accumulation of cytosolic
stores of pro-IL1B (priming). Then additional signals are required for
inflammasome assembly, leading to CASP1 activation, pro-IL1B processing
and eventually secretion of the active cytokine. IL1B processing and
secretion are temporarily associated. {ECO:0000269|PubMed:15192144}.
-!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IL1BID40950ch2q13.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_1";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il1b/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL1B";
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EMBL; K02770; AAA36106.1; -; mRNA.
EMBL; M54933; AAA59136.1; ALT_SEQ; mRNA.
EMBL; X02532; CAA26372.1; -; mRNA.
EMBL; X04500; CAA28185.1; -; Genomic_DNA.
EMBL; M15330; AAA59135.1; -; mRNA.
EMBL; M15840; AAA74137.1; -; Genomic_DNA.
EMBL; X56087; CAA39567.1; -; mRNA.
EMBL; BN000002; CAD29872.1; -; Genomic_DNA.
EMBL; BT007213; AAP35877.1; -; mRNA.
EMBL; CR407679; CAG28607.1; -; mRNA.
EMBL; AY137079; AAM88883.1; -; Genomic_DNA.
EMBL; AC079753; AAX88888.1; -; Genomic_DNA.
EMBL; CH471217; EAW73605.1; -; Genomic_DNA.
EMBL; BC008678; AAH08678.1; -; mRNA.
CCDS; CCDS2102.1; -.
PIR; A21851; A21851.
PIR; A25542; ICHU1B.
RefSeq; NP_000567.1; NM_000576.2.
PDB; 1HIB; X-ray; 2.40 A; A=117-269.
PDB; 1I1B; X-ray; 2.00 A; A=117-269.
PDB; 1IOB; X-ray; 2.00 A; A=117-269.
PDB; 1ITB; X-ray; 2.50 A; A=117-269.
PDB; 1L2H; X-ray; 1.54 A; A=117-269.
PDB; 1S0L; X-ray; 2.34 A; A=117-269.
PDB; 1T4Q; X-ray; 2.10 A; A=117-269.
PDB; 1TOO; X-ray; 2.10 A; A=117-269.
PDB; 1TP0; X-ray; 2.20 A; A=117-269.
PDB; 1TWE; X-ray; 2.10 A; A=117-269.
PDB; 1TWM; X-ray; 2.26 A; A=117-269.
PDB; 21BI; X-ray; 2.00 A; A=117-269.
PDB; 2I1B; X-ray; 2.00 A; A=117-269.
PDB; 2KH2; NMR; -; A=117-269.
PDB; 2NVH; X-ray; 1.53 A; A=117-269.
PDB; 31BI; X-ray; 2.00 A; A=117-269.
PDB; 3LTQ; X-ray; 2.10 A; A=117-269.
PDB; 3O4O; X-ray; 3.30 A; A=117-269.
PDB; 3POK; X-ray; 1.70 A; A=117-269.
PDB; 41BI; X-ray; 2.90 A; A=117-269.
PDB; 4DEP; X-ray; 3.10 A; A/D=117-269.
PDB; 4G6J; X-ray; 2.03 A; A=117-269.
PDB; 4G6M; X-ray; 1.81 A; A=118-267.
PDB; 4GAF; X-ray; 2.15 A; A=117-269.
PDB; 4GAI; X-ray; 1.49 A; A/B=117-269.
PDB; 4I1B; X-ray; 2.00 A; A=117-269.
PDB; 5BVP; X-ray; 2.20 A; I=117-269.
PDB; 5I1B; X-ray; 2.10 A; A=117-269.
PDB; 5MVZ; X-ray; 2.15 A; U/V=117-269.
PDB; 5R7W; X-ray; 1.27 A; A=117-269.
PDB; 5R85; X-ray; 1.44 A; A=117-269.
PDB; 5R86; X-ray; 1.50 A; A=117-269.
PDB; 5R87; X-ray; 1.47 A; A=117-269.
PDB; 5R88; X-ray; 1.48 A; A=117-269.
PDB; 5R89; X-ray; 1.65 A; A=117-269.
PDB; 5R8A; X-ray; 1.47 A; A=117-269.
PDB; 5R8B; X-ray; 1.49 A; A=117-269.
PDB; 5R8C; X-ray; 1.54 A; A=117-269.
PDB; 5R8D; X-ray; 1.47 A; A=117-269.
PDB; 5R8E; X-ray; 1.35 A; A=117-269.
PDB; 5R8F; X-ray; 1.41 A; A=117-269.
PDB; 5R8G; X-ray; 1.43 A; A=117-269.
PDB; 5R8H; X-ray; 1.50 A; A=117-269.
PDB; 5R8I; X-ray; 1.47 A; A=117-269.
PDB; 5R8J; X-ray; 1.62 A; A=117-269.
PDB; 5R8K; X-ray; 1.47 A; A=117-269.
PDB; 5R8L; X-ray; 1.56 A; A=117-269.
PDB; 5R8M; X-ray; 1.39 A; A=117-269.
PDB; 5R8N; X-ray; 1.48 A; A=117-269.
PDB; 5R8O; X-ray; 1.42 A; A=117-269.
PDB; 5R8P; X-ray; 1.53 A; A=117-269.
PDB; 5R8Q; X-ray; 1.23 A; A=117-269.
PDB; 6I1B; NMR; -; A=117-269.
PDB; 6Y8I; X-ray; 1.46 A; A=117-269.
PDB; 6Y8M; X-ray; 1.90 A; A=117-269.
PDB; 7CHY; X-ray; 2.65 A; I=117-269.
PDB; 7CHZ; X-ray; 2.50 A; I=117-269.
PDB; 7I1B; NMR; -; A=117-269.
PDB; 9ILB; X-ray; 2.28 A; A=117-269.
PDBsum; 1HIB; -.
PDBsum; 1I1B; -.
PDBsum; 1IOB; -.
PDBsum; 1ITB; -.
PDBsum; 1L2H; -.
PDBsum; 1S0L; -.
PDBsum; 1T4Q; -.
PDBsum; 1TOO; -.
PDBsum; 1TP0; -.
PDBsum; 1TWE; -.
PDBsum; 1TWM; -.
PDBsum; 21BI; -.
PDBsum; 2I1B; -.
PDBsum; 2KH2; -.
PDBsum; 2NVH; -.
PDBsum; 31BI; -.
PDBsum; 3LTQ; -.
PDBsum; 3O4O; -.
PDBsum; 3POK; -.
PDBsum; 41BI; -.
PDBsum; 4DEP; -.
PDBsum; 4G6J; -.
PDBsum; 4G6M; -.
PDBsum; 4GAF; -.
PDBsum; 4GAI; -.
PDBsum; 4I1B; -.
PDBsum; 5BVP; -.
PDBsum; 5I1B; -.
PDBsum; 5MVZ; -.
PDBsum; 5R7W; -.
PDBsum; 5R85; -.
PDBsum; 5R86; -.
PDBsum; 5R87; -.
PDBsum; 5R88; -.
PDBsum; 5R89; -.
PDBsum; 5R8A; -.
PDBsum; 5R8B; -.
PDBsum; 5R8C; -.
PDBsum; 5R8D; -.
PDBsum; 5R8E; -.
PDBsum; 5R8F; -.
PDBsum; 5R8G; -.
PDBsum; 5R8H; -.
PDBsum; 5R8I; -.
PDBsum; 5R8J; -.
PDBsum; 5R8K; -.
PDBsum; 5R8L; -.
PDBsum; 5R8M; -.
PDBsum; 5R8N; -.
PDBsum; 5R8O; -.
PDBsum; 5R8P; -.
PDBsum; 5R8Q; -.
PDBsum; 6I1B; -.
PDBsum; 6Y8I; -.
PDBsum; 6Y8M; -.
PDBsum; 7CHY; -.
PDBsum; 7CHZ; -.
PDBsum; 7I1B; -.
PDBsum; 9ILB; -.
BMRB; P01584; -.
SMR; P01584; -.
BioGRID; 109769; 16.
DIP; DIP-474N; -.
IntAct; P01584; 8.
STRING; 9606.ENSP00000263341; -.
BindingDB; P01584; -.
ChEMBL; CHEMBL1909490; -.
DrugBank; DB05767; Andrographolide.
DrugBank; DB11967; Binimetinib.
DrugBank; DB06168; Canakinumab.
DrugBank; DB12140; Dilmapimod.
DrugBank; DB00843; Donepezil.
DrugBank; DB05442; Etiprednol dicloacetate.
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB05260; Gallium nitrate.
DrugBank; DB12119; Gevokizumab.
DrugBank; DB01017; Minocycline.
DrugBank; DB06372; Rilonacept.
DrugBank; DB05412; Talmapimod.
DrugBank; DB05133; VP025.
DrugBank; DB05470; VX-702.
DrugBank; DB05507; VX-765.
DrugCentral; P01584; -.
TCDB; 1.A.109.1.2; the interleukin 1 (il1) family.
iPTMnet; P01584; -.
PhosphoSitePlus; P01584; -.
SwissPalm; P01584; -.
BioMuta; IL1B; -.
DMDM; 62906858; -.
EPD; P01584; -.
MassIVE; P01584; -.
MaxQB; P01584; -.
PaxDb; P01584; -.
PeptideAtlas; P01584; -.
PRIDE; P01584; -.
ProteomicsDB; 51391; -.
ABCD; P01584; 5 sequenced antibodies.
Antibodypedia; 771; 2401 antibodies.
DNASU; 3553; -.
Ensembl; ENST00000263341; ENSP00000263341; ENSG00000125538.
GeneID; 3553; -.
KEGG; hsa:3553; -.
UCSC; uc002tii.2; human.
CTD; 3553; -.
DisGeNET; 3553; -.
GeneCards; IL1B; -.
HGNC; HGNC:5992; IL1B.
HPA; ENSG00000125538; Tissue enhanced (bone marrow, lymphoid tissue).
MalaCards; IL1B; -.
MIM; 147720; gene.
neXtProt; NX_P01584; -.
OpenTargets; ENSG00000125538; -.
PharmGKB; PA29808; -.
VEuPathDB; HostDB:ENSG00000125538.11; -.
eggNOG; ENOG502S3E9; Eukaryota.
GeneTree; ENSGT00950000182943; -.
HOGENOM; CLU_083639_0_0_1; -.
InParanoid; P01584; -.
OMA; RQPVGIT; -.
OrthoDB; 1243742at2759; -.
PhylomeDB; P01584; -.
TreeFam; TF300203; -.
PathwayCommons; P01584; -.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
SignaLink; P01584; -.
SIGNOR; P01584; -.
BioGRID-ORCS; 3553; 38 hits in 986 CRISPR screens.
ChiTaRS; IL1B; human.
EvolutionaryTrace; P01584; -.
GeneWiki; IL1B; -.
GenomeRNAi; 3553; -.
Pharos; P01584; Tclin.
PRO; PR:P01584; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; P01584; protein.
Bgee; ENSG00000125538; Expressed in smooth muscle tissue and 190 other tissues.
ExpressionAtlas; P01584; baseline and differential.
Genevisible; P01584; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0005149; F:interleukin-1 receptor binding; NAS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0035690; P:cellular response to drug; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0007566; P:embryo implantation; TAS:BHF-UCL.
GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
GO; GO:0030213; P:hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0070487; P:monocyte aggregation; IDA:UniProtKB.
GO; GO:0070164; P:negative regulation of adiponectin secretion; ISS:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
GO; GO:1903597; P:negative regulation of gap junction assembly; IDA:ARUK-UCL.
GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
GO; GO:0045833; P:negative regulation of lipid metabolic process; ISS:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:BHF-UCL.
GO; GO:0050768; P:negative regulation of neurogenesis; TAS:ARUK-UCL.
GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:ARUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0060355; P:positive regulation of cell adhesion molecule production; NAS:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0045917; P:positive regulation of complement activation; IGI:ARUK-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IGI:ARUK-UCL.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; NAS:BHF-UCL.
GO; GO:0033129; P:positive regulation of histone phosphorylation; NAS:BHF-UCL.
GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IBA:GO_Central.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:ARUK-UCL.
GO; GO:0050996; P:positive regulation of lipid catabolic process; ISS:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IDA:UniProtKB.
GO; GO:0035505; P:positive regulation of myosin light chain kinase activity; IDA:BHF-UCL.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; TAS:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:ARUK-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IGI:ARUK-UCL.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISS:BHF-UCL.
GO; GO:0046827; P:positive regulation of protein export from nucleus; NAS:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:1902680; P:positive regulation of RNA biosynthetic process; IDA:ARUK-UCL.
GO; GO:0002711; P:positive regulation of T cell mediated immunity; IC:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IC:BHF-UCL.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; TAS:Reactome.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; IDA:BHF-UCL.
GO; GO:0050767; P:regulation of neurogenesis; ISS:ARUK-UCL.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; IDA:ARUK-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:ARUK-UCL.
GO; GO:0030730; P:sequestering of triglyceride; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0014805; P:smooth muscle adaptation; NAS:BHF-UCL.
GO; GO:0010573; P:vascular endothelial growth factor production; IDA:UniProtKB.
InterPro; IPR003296; IL-1_beta.
InterPro; IPR020877; IL-1_CS.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR003502; IL-1_propep.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR10078; PTHR10078; 1.
PANTHER; PTHR10078:SF30; PTHR10078:SF30; 1.
Pfam; PF00340; IL1; 1.
Pfam; PF02394; IL1_propep; 1.
PRINTS; PR00264; INTERLEUKIN1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00253; INTERLEUKIN_1; 1.
1: Evidence at protein level;
3D-structure; Cytokine; Cytoplasm; Direct protein sequencing;
Inflammatory response; Lysosome; Mitogen; Pyrogen; Reference proteome;
Secreted.
PROPEP 1..116
/note="Removed in mature form; by CASP1"
/evidence="ECO:0000269|PubMed:3281727,
ECO:0000269|PubMed:3920526"
/id="PRO_0000015301"
CHAIN 117..269
/note="Interleukin-1 beta"
/evidence="ECO:0000269|PubMed:2001363"
/id="PRO_0000015302"
MOTIF 228..241
/note="Involved in interaction with TMED10 C-terminus"
/evidence="ECO:0000269|PubMed:32272059"
SITE 120
/note="Involved in receptor binding"
SITE 171
/note="Important for interaction with integrin"
/evidence="ECO:0000269|PubMed:29030430"
SITE 179
/note="Important for interaction with integrin"
/evidence="ECO:0000269|PubMed:29030430"
SITE 181
/note="Important for interaction with integrin"
/evidence="ECO:0000269|PubMed:29030430"
SITE 190
/note="Important for interaction with integrin"
/evidence="ECO:0000269|PubMed:29030430"
SITE 204
/note="Important for interaction with integrin"
/evidence="ECO:0000269|PubMed:29030430"
VARIANT 141
/note="E -> N (requires 2 nucleotide substitutions;
dbSNP:rs144640380)"
/evidence="ECO:0000269|PubMed:3920526"
/id="VAR_073951"
MUTAGEN 27
/note="D->A: Loss of activation by CASP1; when associated
with A-116."
/evidence="ECO:0000269|PubMed:24952504"
MUTAGEN 116
/note="D->A: Loss of activation by CASP1; when associated
with A-27."
/evidence="ECO:0000269|PubMed:24952504"
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"
CONFLICT 6
/note="E -> K (in Ref. 1; AAA36106/AAA59136 and 10;
CAG28607)"
/evidence="ECO:0000305"
CONFLICT 124
/note="C -> A (in Ref. 16; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 155
/note="Q -> D (in Ref. 16; AA sequence)"
/evidence="ECO:0000305"
STRAND 120..128
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 133..138
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 141..145
/evidence="ECO:0007829|PDB:5R8Q"
HELIX 149..154
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 158..162
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 171..178
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 181..190
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 193..200
/evidence="ECO:0007829|PDB:5R8Q"
TURN 203..205
/evidence="ECO:0007829|PDB:5R8Q"
HELIX 213..215
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 217..222
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 225..233
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 237..240
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 242..247
/evidence="ECO:0007829|PDB:5R8F"
STRAND 249..252
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 254..259
/evidence="ECO:0007829|PDB:5R8Q"
STRAND 262..266
/evidence="ECO:0007829|PDB:5R8Q"
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


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E0563h ELISA kit Catabolin,Homo sapiens,Human,IL-1 beta,IL1B,IL1F2,Interleukin-1 beta 96T
E0046h ELISA CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 13 96T
E0046h ELISA kit CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprote 96T
U0046h CLIA CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130 96T
U0046m CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncost 96T
E0046m ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncos 96T
E0046r ELISA kit gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M recept 96T
E0046m ELISA kit gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus, 96T
E0046r ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor su 96T
U0046r CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor sub 96T
U1592h CLIA CASP1,CASP-1,Caspase-1,Homo sapiens,Human,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,IL1BCE,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45 96T
E1592h ELISA CASP1,CASP-1,Caspase-1,Homo sapiens,Human,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,IL1BCE,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45 96T
E1592h ELISA kit CASP1,CASP-1,Caspase-1,Homo sapiens,Human,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,IL1BCE,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45 96T
U1592r CLIA Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Il1bce,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Rat,Rattus norvegicus 96T
E1592r ELISA kit Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Il1bce,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Rat,Rattus norvegicus 96T
E1592r ELISA Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Il1bce,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Rat,Rattus norvegicus 96T
E1592m ELISA kit Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,Mouse,Mus musculus,p45 96T
U1592m CLIA Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,Mouse,Mus musculus,p45 96T
E1592m ELISA Casp1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,Il1bc,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,Mouse,Mus musculus,p45 96T
U1592p CLIA CASP1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Pig,Sus scrofa 96T
E1592p ELISA kit CASP1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Pig,Sus scrofa 96T
E1592p ELISA CASP1,CASP-1,Caspase-1,ICE,IL-1 beta-converting enzyme,IL1BC,IL-1BC,Interleukin-1 beta convertase,Interleukin-1 beta-converting enzyme,p45,Pig,Sus scrofa 96T
E0066h ELISA kit CD121 antigen-like family member B,CDw121b,Homo sapiens,Human,IL1R2,IL-1R-2,IL1RB,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 recepto 96T
Pathways :
WP1045: TGF-beta Receptor Signaling Pathway
WP418: Beta Oxidation of Unsaturated Fatty Acids
WP126: Fatty Acid Beta Oxidation 1
WP237: Glucocorticoid & Mineralcorticoid Metabolism
WP615: Senescence and Autophagy
WP1367: TGF-beta Receptor Signaling Pathway
WP25: Fatty Acid Beta Oxidation 3
WP809: TGF-beta Receptor Signaling Pathway
WP1058: Senescence and Autophagy
WP187: Fatty Acid Beta Oxidation 2
WP443: Beta Oxidation Meta MAPP
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1941: Peroxisomal beta-oxidation of tetracosanoyl-CoA
WP495: Glucocorticoid & Mineralcorticoid Metabolism
WP1434: Osteopontin Signaling
WP3: Keap1-Nrf2 Pathway
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1571: EBV LMP1 signaling
WP362: TGF-beta Receptor Signaling Pathway
WP943: Fatty Acid Beta Oxidation
WP1164: TGF Beta Signaling Pathway
WP209: Fatty Acid Beta Oxidation Meta
WP505: TGF Beta Signaling Pathway
WP1224: EBV LMP1 signaling
WP219: Cytoplasmic tRNA Synthetases

Related Genes :
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[IL36B IL1F8 IL1H2] Interleukin-36 beta (FIL1 eta) (Interleukin-1 eta) (IL-1 eta) (Interleukin-1 family member 8) (IL-1F8) (Interleukin-1 homolog 2) (IL-1H2)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[Il1b] Interleukin-1 beta (IL-1 beta)
[Il1b] Interleukin-1 beta (IL-1 beta)
[IL1B] Interleukin-1 beta (IL-1 beta)
[IL1B] Interleukin-1 beta (IL-1 beta)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL1B E5288_WYG009670 M91_19273] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[Il36b Fil1e Il1f8] Interleukin-36 beta (Interleukin-1 family member 8) (IL-1F8)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[OSMR OSMRB] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[CARD16 COP COP1] Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme)
[IL6 IFNB2] Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
[IL1b IL1B] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[IL1b IL1B] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[Il1b IL1B rCG_27107] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[Il1b IL1B] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[Il1b IL1B] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[Cebpb Crp2 Nf-il6 Sfb] CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)

Bibliography :
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[34687713] Crystal structure of NLRP3 NACHT domain with an inhibitor defines mechanism of inflammasome inhibition.
[34686198] WEE1 promotes endometriosis via the Wnt/β-catenin signaling pathway.
[34684576] Astaxanthin Inhibits Diabetes-Triggered Periodontal Destruction, Ameliorates Oxidative Complications in STZ-Injected Mice, and Recovers Nrf2-Dependent Antioxidant System.
[34684537] Anti-Inflammatory Effect of 4,5-Dicaffeoylquinic Acid on RAW264.7 Cells and a Rat Model of Inflammation.
[34684325] Eggshell Membrane Ameliorates Hyperuricemia by Increasing Urate Excretion in Potassium Oxonate-Injected Rats.
[34681367] Cell Types Used for Cultured Meat Production and the Importance of Myokines.
[34681254] Brain Perivascular Macrophages Do Not Mediate Interleukin-1-Induced Sickness Behavior in Rats.
[34681074] Flower Extract Attenuates Postprandial Lipemia and Increases Plasma Antioxidant Status Responses to a High-Fat Meal Challenge in Overweight and Obese Participants.
[34680549] Lobeglitazone Exerts Anti-Inflammatory Effect in Lipopolysaccharide-Induced Bone-Marrow Derived Macrophages.