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P01584 (IL1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-1 beta

Short name=IL-1 beta
Alternative name(s):
Catabolin
Gene names
Name:IL1B
Synonyms:IL1F2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. Ref.16

Subunit structure

Monomer. Interacts with MEFV. Ref.19

Subcellular location

Secreted. Note: The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.

Domain

The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.

Sequence similarities

Belongs to the IL-1 family.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentSecreted
   Molecular functionCytokine
Mitogen
Pyrogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

activation of MAPK activity

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

apoptotic process

Traceable author statement PubMed 9218611. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.2. Source: ProtInc

cellular response to drug

Inferred from direct assay PubMed 19158679. Source: MGI

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cellular response to organic cyclic compound

Inferred from direct assay PubMed 21147091. Source: UniProtKB

cellular response to organic substance

Inferred from direct assay PubMed 19158679. Source: MGI

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Traceable author statement PubMed 16720713. Source: BHF-UCL

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

fever generation

Inferred from electronic annotation. Source: UniProtKB-KW

hyaluronan biosynthetic process

Inferred from direct assay PubMed 15100360. Source: UniProtKB

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory response

Inferred from direct assay PubMed 21147091. Source: UniProtKB

interleukin-1 beta production

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 21147091. Source: UniProtKB

monocyte aggregation

Inferred from direct assay PubMed 15100360. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

negative regulation of adiponectin secretion

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from direct assay Ref.5. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

negative regulation of glucose transport

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

negative regulation of insulin receptor signaling pathway

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

negative regulation of lipid catabolic process

Inferred from direct assay PubMed 19032770. Source: BHF-UCL

negative regulation of lipid metabolic process

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB import into nucleus

Inferred from direct assay PubMed 18390750. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 10383454PubMed 12958148. Source: BHF-UCL

positive regulation of T cell mediated immunity

Inferred by curator Ref.15. Source: BHF-UCL

positive regulation of T cell proliferation

Inferred from direct assay Ref.15. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of calcidiol 1-monooxygenase activity

Inferred from direct assay PubMed 16720713PubMed 17023519. Source: BHF-UCL

positive regulation of cell adhesion molecule production

Non-traceable author statement PubMed 19281832. Source: BHF-UCL

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of chemokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of fever generation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay PubMed 21559518. Source: AgBase

positive regulation of granulocyte macrophage colony-stimulating factor production

Inferred from direct assay PubMed 20027291. Source: BHF-UCL

positive regulation of heterotypic cell-cell adhesion

Inferred from direct assay PubMed 15100360. Source: UniProtKB

positive regulation of histone acetylation

Non-traceable author statement PubMed 20018936. Source: BHF-UCL

positive regulation of histone phosphorylation

Non-traceable author statement PubMed 20018936. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from direct assay PubMed 20027291. Source: BHF-UCL

positive regulation of interleukin-2 biosynthetic process

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

positive regulation of interleukin-6 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Traceable author statement PubMed 16865359. Source: BHF-UCL

positive regulation of interleukin-8 production

Inferred from direct assay PubMed 19524870. Source: UniProtKB

positive regulation of lipid catabolic process

Inferred from sequence or structural similarity PubMed 16865359. Source: BHF-UCL

positive regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 18373975. Source: BHF-UCL

positive regulation of mitosis

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

positive regulation of monocyte chemotactic protein-1 production

Inferred from direct assay PubMed 19524870. Source: UniProtKB

positive regulation of myosin light chain kinase activity

Inferred from direct assay PubMed 18390750. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay PubMed 8383325. Source: BHF-UCL

positive regulation of prostaglandin secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein export from nucleus

Non-traceable author statement PubMed 19281832. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15100360. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred by curator PubMed 12958148. Source: BHF-UCL

positive regulation vascular endothelial growth factor production

Inferred from direct assay PubMed 12958148. Source: BHF-UCL

protein kinase B signaling

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 10748004. Source: BHF-UCL

regulation of insulin secretion

Inferred from direct assay PubMed 8383325. Source: BHF-UCL

response to ATP

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

sequestering of triglyceride

Inferred from direct assay PubMed 19032770. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 10786823PubMed 9218611. Source: ProtInc

smooth muscle adaptation

Non-traceable author statement PubMed 16477012. Source: BHF-UCL

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement Ref.15. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 12483741. Source: BHF-UCL

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytokine activity

Inferred from direct assay Ref.15. Source: BHF-UCL

interleukin-1 receptor binding

Non-traceable author statement Ref.15. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 16575408. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 116116
PRO_0000015301
Chain117 – 269153Interleukin-1 beta Ref.24
PRO_0000015302

Sites

Site1201Involved in receptor binding

Experimental info

Sequence conflict61E → K in AAA36106. Ref.1
Sequence conflict61E → K in AAA59136. Ref.1
Sequence conflict61E → K in CAG28607. Ref.10
Sequence conflict1241C → A AA sequence Ref.16
Sequence conflict1551Q → D AA sequence Ref.16

Secondary structure

.................................... 269
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01584 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 9BF73C3673C6FD66

FASTA26930,748
        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 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human monocyte interleukin 1 precursor cDNA."
Auron P.E., Webb A.C., Rosenwasser L.J., Mucci S.F., Rich A., Wolff S.M., Dinarello C.A.
Proc. Natl. Acad. Sci. U.S.A. 81:7907-7911(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs."
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.
Nature 315:641-647(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic sequence for human prointerleukin 1 beta: possible evolution from a reverse transcribed prointerleukin 1 alpha gene."
Clark B.D., Collins K.L., Gandy M.S., Webb A.C., Auron P.E.
Nucleic Acids Res. 14:7897-7914(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[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]"cDNA cloning of IL-1 alpha and IL-1 beta from mRNA of U937 cell line."
Nishida T., Nishino N., Takano M., Kawai K., Bando K., Masui Y., Nakai S., Hirai Y.
Biochem. Biophys. Res. Commun. 143:345-352(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Histiocytic lymphoma.
[6]"Human interleukin-1 beta gene."
Bensi G., Raugei G., Palla E., Carinci V., Buonamassa D.T., Melli M.
Gene 52:95-101(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Cloning of the cDNA coding for human prointerleukin-1 alpha and prointerleukin-1 beta."
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.
Dokl. Akad. Nauk SSSR 309:1005-1008(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Monocyte.
[8]"A sequence-based map of the nine genes of the human interleukin-1 cluster."
Nicklin M.J.H., Barton J.L., Nguyen M., Fitzgerald M.G., Duff W.G., Kornman K.
Genomics 79:718-725(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]SeattleSNPs variation discovery resource
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[12]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[15]"Rapid and specific conversion of precursor interleukin 1 beta (IL-1 beta) to an active IL-1 species by human mast cell chymase."
Mizutani H., Schechter N., Lazarus G., Black R.A., Kupper T.S.
J. Exp. Med. 174:821-825(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-135.
Tissue: Skin.
[16]"Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1."
Van Damme J., De Ley M., Opdenakker G., Billiau A., De Somer P., Van Beeumen J.
Nature 314:266-268(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 117-155, FUNCTION.
[17]"Effects of hematopoietin-1 and interleukin 1 activities on early hematopoietic cells of the bone marrow."
Zsebo K.M., Wypych J., Yuschenkoff V.N., Lu H., Hunt P., Dukes P.P., Langley K.E.
Blood 71:962-968(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 117-128.
[18]"The role of arginine residues in interleukin 1 receptor binding."
Nanduri V.B., Hulmes J.D., Pan Y.C., Kilian P.L., Stern A.S.
Biochim. Biophys. Acta 1118:25-35(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR-BINDING.
[19]"The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing."
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D., Grutter C., Grutter M., Tschopp J.
Cell Death Differ. 14:1457-1466(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEFV.
[20]"Crystal structure of the cytokine interleukin-1 beta."
Priestle J.P., Schar H.-P., Grutter M.G.
EMBO J. 7:339-343(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[21]"Crystal structure of recombinant human interleukin-1 beta at 2.0-A resolution."
Finzel B.C., Clancy L.L., Holland D.R., Muchmore S.W., Watenpaugh K.D., Einspahr H.M.
J. Mol. Biol. 209:779-791(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[22]"Crystallographic refinement of interleukin 1 beta at 2.0-A resolution."
Priestle J.P., Schar H.-P., Gruetter M.G.
Proc. Natl. Acad. Sci. U.S.A. 86:9667-9671(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[23]"Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy."
Driscoll P.C., Gronenborn A.M., Wingfield P.T., Clore G.M.
Biochemistry 29:4668-4682(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[24]"High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy."
Clore G.M., Wingfield P.T., Gronenborn A.M.
Biochemistry 30:2315-2323(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[25]"Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta."
Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.
Nature 386:190-194(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
[26]"Structural insights into the assembly and activation of IL-1beta with its receptors."
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.
Nat. Immunol. 11:905-911(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 117-269 IN COMPLEX WITH IL1R2 AND IL1RAP.
+Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Interleukin-1 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02770 mRNA. Translation: AAA36106.1.
M54933 mRNA. Translation: AAA59136.1. Sequence problems.
X02532 mRNA. Translation: CAA26372.1.
X04500 Genomic DNA. Translation: CAA28185.1.
M15330 mRNA. Translation: AAA59135.1.
M15840 Genomic DNA. Translation: AAA74137.1.
X56087 mRNA. Translation: CAA39567.1.
BN000002 Genomic DNA. Translation: CAD29872.1.
BT007213 mRNA. Translation: AAP35877.1.
CR407679 mRNA. Translation: CAG28607.1.
AY137079 Genomic DNA. Translation: AAM88883.1.
AC079753 Genomic DNA. Translation: AAX88888.1.
CH471217 Genomic DNA. Translation: EAW73605.1.
BC008678 mRNA. Translation: AAH08678.1.
CCDSCCDS2102.1.
PIRA21851.
ICHU1B. A25542.
RefSeqNP_000567.1. NM_000576.2.
UniGeneHs.126256.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HIBX-ray2.40A117-269[»]
1I1BX-ray2.00A117-269[»]
1IOBX-ray2.00A117-269[»]
1ITBX-ray2.50A117-269[»]
1L2HX-ray1.54A117-269[»]
1S0LX-ray2.34A117-269[»]
1T4QX-ray2.10A117-269[»]
1TOOX-ray2.10A117-269[»]
1TP0X-ray2.20A117-269[»]
1TWEX-ray2.10A117-269[»]
1TWMX-ray2.26A117-269[»]
21BIX-ray2.00A117-269[»]
2I1BX-ray2.00A117-269[»]
2KH2NMR-A117-269[»]
2NVHX-ray1.53A117-269[»]
31BIX-ray2.00A117-269[»]
3LTQX-ray2.10A117-269[»]
3O4OX-ray3.30A117-269[»]
3POKX-ray1.70A117-269[»]
41BIX-ray2.90A117-269[»]
4DEPX-ray3.10A/D117-269[»]
4G6JX-ray2.03A117-269[»]
4G6MX-ray1.81A118-267[»]
4GAFX-ray2.15A117-269[»]
4GAIX-ray1.49A/B117-269[»]
4I1BX-ray2.00A117-269[»]
5I1BX-ray2.10A117-269[»]
6I1BNMR-A117-269[»]
7I1BNMR-A117-269[»]
9ILBX-ray2.28A117-269[»]
ProteinModelPortalP01584.
SMRP01584. Positions 117-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109769. 12 interactions.
DIPDIP-474N.
IntActP01584. 4 interactions.
MINTMINT-189806.
STRING9606.ENSP00000263341.

Chemistry

BindingDBP01584.
ChEMBLCHEMBL1909490.
DrugBankDB00026. Anakinra.
DB01017. Minocycline.
DB01366. Procaterol.
GuidetoPHARMACOLOGY2623.

Polymorphism databases

DMDM62906858.

Proteomic databases

MaxQBP01584.
PaxDbP01584.
PRIDEP01584.

Protocols and materials databases

DNASU3553.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263341; ENSP00000263341; ENSG00000125538.
GeneID3553.
KEGGhsa:3553.
UCSCuc002tih.1. human.

Organism-specific databases

CTD3553.
GeneCardsGC02M113587.
HGNCHGNC:5992. IL1B.
MIM147720. gene.
neXtProtNX_P01584.
PharmGKBPA29808.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40099.
HOVERGENHBG007328.
InParanoidP01584.
KOK04519.
OMASNDKIPV.
OrthoDBEOG71P2BQ.
PhylomeDBP01584.
TreeFamTF300203.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP01584.

Gene expression databases

ArrayExpressP01584.
BgeeP01584.
CleanExHS_IL1B.
GenevestigatorP01584.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR003294. IL-1_alpha/beta.
IPR003296. IL-1_beta.
IPR020877. IL-1_CS.
IPR000975. IL-1_fam.
IPR028142. IL-1_fam/FGF_fam.
IPR003502. IL-1_propep.
[Graphical view]
PANTHERPTHR10078:SF20. PTHR10078:SF20. 1 hit.
PfamPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSPR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01357. INTRLEUKN1AB.
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL1B. human.
EvolutionaryTraceP01584.
GeneWikiIL1B.
GenomeRNAi3553.
NextBio13872.
PMAP-CutDBP01584.
PROP01584.
SOURCESearch...

Entry information

Entry nameIL1B_HUMAN
AccessionPrimary (citable) accession number: P01584
Secondary accession number(s): Q53X59 expand/collapse secondary AC list , Q53XX2, Q7M4S7, Q7RU01, Q96HE5, Q9UCT6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM