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UniProtKB/Swiss-Prot entry P01584


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IL1B_HUMAN
Primary accession number P01584
Secondary accession numbers Q53X59 Q53XX2 Q7M4S7 Q7RU01 Q96HE5 Q9UCT6
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 117)
Name and origin of the protein
Protein name Interleukin-1 beta [Precursor]
Synonyms IL-1 beta
Catabolin
Gene name
Name: IL1B
Synonyms: IL1F2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6083565 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/315641a0; PubMed=2989698 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/nar/14.20.7897; PubMed=3490654 [NCBI, ExPASy, EBI, Israel, Japan]
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.
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1016/0378-1119(87)90398-2; PubMed=2954882 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/geno.2002.6751; PubMed=11991722 [NCBI, ExPASy, EBI, Israel, Japan]
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 program for genomic applications;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1084/jem.174.4.821; PubMed=1919436 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND FUNCTION.
DOI=10.1038/314266a0; PubMed=3920526 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0167-4838(91)90437-5; PubMed=1837236 [NCBI, ExPASy, EBI, Israel, Japan]
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]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3259176 [NCBI, ExPASy, EBI, Israel, Japan]
Priestle J.P., Schar H.-P., Grutter M.G.;
"Crystal structure of the cytokine interleukin-1 beta.";
EMBO J. 7:339-343(1988).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/0022-2836(89)90606-2; PubMed=2585509 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2602367 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
STRUCTURE BY NMR.
DOI=10.1021/bi00471a023; PubMed=2372550 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
STRUCTURE BY NMR.
DOI=10.1021/bi00223a005; PubMed=2001363 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
DOI=10.1038/386190a0; PubMed=9062193 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02770; AAA36106.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M54933; AAA59136.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02532; CAA26372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04500; CAA28185.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15330; AAA59135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15840; AAA74137.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56087; CAA39567.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BN000002; CAD29872.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007213; AAP35877.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407679; CAG28607.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY137079; AAM88883.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079753; AAX88888.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471217; EAW73605.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008678; AAH08678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A21851; A21851.
A25542; ICHU1B.
RefSeq NP_000567.1; -.
UniGene Hs.126256
3D structure databases
PDB
1HIB; X-ray; 2.40 A; A=117-269.[ExPASy / RCSB / EBI]
1I1B; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
1IOB; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
1ITB; X-ray; 2.50 A; A=117-269.[ExPASy / RCSB / EBI]
1L2H; X-ray; 1.54 A; A=117-269.[ExPASy / RCSB / EBI]
1S0L; X-ray; 2.34 A; A=117-269.[ExPASy / RCSB / EBI]
1T4Q; X-ray; 2.10 A; A=117-269.[ExPASy / RCSB / EBI]
1TOO; X-ray; 2.10 A; A=117-269.[ExPASy / RCSB / EBI]
1TP0; X-ray; 2.20 A; A=117-269.[ExPASy / RCSB / EBI]
1TWE; X-ray; 2.10 A; A=117-269.[ExPASy / RCSB / EBI]
1TWM; X-ray; 2.26 A; A=117-269.[ExPASy / RCSB / EBI]
21BI; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
2I1B; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
2NVH; X-ray; 1.53 A; A=117-269.[ExPASy / RCSB / EBI]
31BI; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
41BI; X-ray; 2.90 A; A=117-269.[ExPASy / RCSB / EBI]
4I1B; X-ray; 2.00 A; A=117-269.[ExPASy / RCSB / EBI]
5I1B; X-ray; 2.10 A; A=117-269.[ExPASy / RCSB / EBI]
6I1B; NMR; -; A=117-269.[ExPASy / RCSB / EBI]
7I1B; NMR; -; A=117-269.[ExPASy / RCSB / EBI]
9ILB; X-ray; 2.28 A; A=117-269.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HIB; -.
1I1B; -.
1IOB; -.
1ITB; -.
1L2H; -.
1S0L; -.
1T4Q; -.
1TOO; -.
1TP0; -.
1TWE; -.
1TWM; -.
21BI; -.
2I1B; -.
2NVH; -.
31BI; -.
41BI; -.
4I1B; -.
5I1B; -.
6I1B; -.
7I1B; -.
9ILB; -.
ModBase P01584.
Protein-protein interaction databases
DIP DIP:474N; -.
IntAct P01584; -.
Organism-specific databases
H-InvDB HIX0002386; -.
HGNC HGNC:5992; IL1B.
GenAtlas IL1B.
HPA HPA001410; -.
MIM 147720; gene. [NCBI / EBI]
PharmGKB PA29808; -.
GeneCards P01584.
Gene expression databases
ArrayExpress P01584; -.
CleanEx HS_IL1B; -.
GermOnline ENSG00000125538; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005149; Molecular function: interleukin-1 receptor binding (non-traceable author statement from UniProtKB).
GO:0004871; Molecular function: signal transducer activity (traceable author statement from ProtInc).
GO:0000187; Biological process: activation of MAPK activity (inferred from direct assay from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from direct assay from UniProtKB).
GO:0019221; Biological process: cytokine-mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0006954; Biological process: inflammatory response (non-traceable author statement from UniProtKB).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0045429; Biological process: positive regulation of nitric oxide biosynthetic process (inferred from direct assay from UniProtKB).
GO:0001934; Biological process: positive regulation of protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0051091; Biological process: positive regulation of transcription factor activity (inferred from direct assay from UniProtKB).
GO:0043122; Biological process: regulation of I-kappaB kinase/NF-kappaB cascade (inferred from direct assay from UniProtKB).
GO:0050796; Biological process: regulation of insulin secretion (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002348; IL1_HBGF.
IPR003502; IL1_propep.
IPR000975; Interleukin_1.
IPR003294; InterleukinIL1AB.
IPR003296; InterleukinIL1B.
Graphical view of domain structure.
Pfam PF00340; IL1; 1.
PF02394; IL1_propep; 1.
Pfam graphical view of domain structure.
PRINTS PR00262; IL1HBGF.
PR00264; INTERLEUKIN1.
PR01359; INTRLEUKIN1B.
PR01357; INTRLEUKN1AB.
ProDom PD002536; Interleukin_1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00125; IL1; 1.
SMART graphical view of domain structure.
PROSITE PS00253; INTERLEUKIN_1; 1.
BLOCKS P01584.
ProtoNet P01584.
Other
SWISS-3DIMAGE P01584.
Genome annotation databases
Ensembl ENSG00000125538; Homo sapiens. [Contig view]
GeneID 3553; -.
KEGG hsa:3553; -.
Phylogenomic databases
HOGENOM P01584; -.
HOVERGEN P01584; -.
Other
BindingDB P01584; -.
DrugBank DB00026; Anakinra.
DB01017; Minocycline.
DB01366; Procaterol.
LinkHub P01584; -.
NextBio 13872; -.
SOURCE IL1B; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytokine; Direct protein sequencing; Inflammatory response; Mitogen; Pyrogen; Secreted.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1   116  116      PRO_0000015301
CHAIN   117   269  153     Interleukin-1 beta. PRO_0000015302
SITE   120   120  1     Involved in receptor binding. 
CONFLICT   6     6        E -> K (in Ref. 1; AAA36106/AAA59136 and 10; CAG28607). 
CONFLICT   124   124        C -> A (in Ref. 16; AA sequence). 
CONFLICT   155   155        Q -> D (in Ref. 16; AA sequence). 
STRAND   121   128  8      
STRAND   131   138  8      
STRAND   141   147  7      
TURN   148   150  3      
STRAND   158   162  5      
STRAND   169   178  10      
TURN   179   181  3      
STRAND   183   190  8      
STRAND   193   200  8      
TURN   203   205  3      
HELIX   213   215  3      
STRAND   216   221  6      
STRAND   226   233  8      
STRAND   237   240  4      
STRAND   249   252  4      
STRAND   254   259  6      
STRAND   262   265  4      
Sequence information
Length: 269 AA [This is the length of the unprocessed precursor] Molecular weight: 30748 Da [This is the MW of the unprocessed precursor] CRC64: 9BF73C3673C6FD66 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEVPELASE MMAYYSGNED DLFFEADGPK QMKCSFQDLD LCPLDGGIQL RISDHHYSKG 

        70         80         90        100        110        120 
FRQAASVVVA MDKLRKMLVP CPQTFQENDL STFFPFIFEE EPIFFDTWDN EAYVHDAPVR 

       130        140        150        160        170        180 
SLNCTLRDSQ QKSLVMSGPY ELKALHLQGQ DMEQQVVFSM SFVQGEESND KIPVALGLKE 

       190        200        210        220        230        240 
KNLYLSCVLK DDKPTLQLES VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST 

       250        260 
SQAENMPVFL GGTKGGQDIT DFTMQFVSS 

P01584 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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