P01584 (IL1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-1 beta
Short name=IL-1 beta

Alternative name(s):
Catabolin

Gene names

Name:	IL1B
Synonyms:	IL1F2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	Inflammatory response
Cellular component	Secreted
Molecular function	Cytokine Mitogen Pyrogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MAPK 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 cytokine-mediated signaling pathway Inferred from direct assay PubMed 10748004. Source: BHF-UCL embryo implantation Traceable author statement PubMed 16720713. Source: BHF-UCL 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: Compara 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 apoptotic process Inferred from direct assay PubMed 10748004. Source: BHF-UCL negative regulation of cell proliferation Inferred from direct assay Ref.5. 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 neutrophil chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of JNK cascade Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of fever generation Inferred from sequence or structural similarity. Source: BHF-UCL 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: Compara 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 transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent 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 cascade Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB regulation of insulin secretion Inferred from direct assay PubMed 8383325. Source: BHF-UCL response to ATP Inferred from electronic annotation. Source: Compara sequestering of triglyceride Inferred from direct assay PubMed 19032770. Source: BHF-UCL smooth muscle adaptation Non-traceable author statement PubMed 16477012. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 12483741. Source: BHF-UCL secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	cytokine activity Inferred from direct assay Ref.15. Source: BHF-UCL interleukin-1 receptor binding Non-traceable author statement Ref.15. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 116

116

PRO_0000015301

Chain

117 – 269

153

Interleukin-1 beta Ref.23

PRO_0000015302

Sites

Site

120

1

Involved in receptor binding

Experimental info

Sequence conflict

6

1

E → K in AAA36106. Ref.1

Sequence conflict

6

1

E → K in AAA59136. Ref.1

Sequence conflict

6

1

E → K in CAG28607. Ref.10

Sequence conflict

124

1

C → A AA sequence Ref.16

Sequence conflict

155

1

Q → D AA sequence Ref.16

Secondary structure

1

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269

Helix Strand Turn

Details...

Beta strand

121 – 128

8

Beta strand

133 – 140

8

Beta strand

142 – 145

4

Helix

149 – 154

6

Beta strand

158 – 162

5

Beta strand

172 – 178

7

Turn

179 – 181

3

Beta strand

183 – 190

8

Beta strand

193 – 200

8

Turn

203 – 205

3

Helix

213 – 215

3

Beta strand

217 – 222

6

Beta strand

225 – 233

9

Beta strand

237 – 240

4

Beta strand

242 – 247

6

Beta strand

249 – 252

4

Beta strand

254 – 259

6

Beta strand

262 – 266

5

Sequences

	Sequence		Length	Mass (Da)
	P01584 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 9BF73C3673C6FD66	FASTA	269	30,748
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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).
[20]	"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).
[21]	"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).
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.

IPI

IPI00307223.

PIR

A21851.
ICHU1B. A25542.

RefSeq

NP_000567.1. NM_000576.2.

UniGene

Hs.126256.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HIB	X-ray	2.40	A	117-269	[»]
1I1B	X-ray	2.00	A	117-269	[»]
1IOB	X-ray	2.00	A	117-269	[»]
1ITB	X-ray	2.50	A	117-269	[»]
1L2H	X-ray	1.54	A	117-269	[»]
1S0L	X-ray	2.34	A	117-269	[»]
1T4Q	X-ray	2.10	A	117-269	[»]
1TOO	X-ray	2.10	A	117-269	[»]
1TP0	X-ray	2.20	A	117-269	[»]
1TWE	X-ray	2.10	A	117-269	[»]
1TWM	X-ray	2.26	A	117-269	[»]
21BI	X-ray	2.00	A	117-269	[»]
2I1B	X-ray	2.00	A	117-269	[»]
2KH2	NMR	-	A	117-269	[»]
2NVH	X-ray	1.53	A	117-269	[»]
31BI	X-ray	2.00	A	117-269	[»]
3LTQ	X-ray	2.10	A	117-269	[»]
3O4O	X-ray	3.30	A	117-269	[»]
3POK	X-ray	1.70	A	117-269	[»]
41BI	X-ray	2.90	A	117-269	[»]
4DEP	X-ray	3.10	A/D	117-269	[»]
4G6J	X-ray	2.03	A	117-269	[»]
4G6M	X-ray	1.81	A	118-267	[»]
4GAF	X-ray	2.15	A	158-236	[»]
4GAI	X-ray	1.49	A/B	158-236	[»]
4I1B	X-ray	2.00	A	117-269	[»]
5I1B	X-ray	2.10	A	117-269	[»]
6I1B	NMR	-	A	117-269	[»]
7I1B	NMR	-	A	117-269	[»]
9ILB	X-ray	2.28	A	117-269	[»]

ProteinModelPortal

P01584.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-474N.

IntAct

P01584. 3 interactions.

MINT

MINT-189806.

STRING

9606.ENSP00000263341.

Polymorphism databases

DMDM

62906858.

Proteomic databases

PaxDb

P01584.

PRIDE

P01584.

Protocols and materials databases

DNASU

3553.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263341; ENSP00000263341; ENSG00000125538.

GeneID

3553.

KEGG

hsa:3553.

UCSC

uc002tih.1. human.

Organism-specific databases

CTD

3553.

GeneCards

GC02M113587.

HGNC

HGNC:5992. IL1B.

MIM

147720. gene.

neXtProt

NX_P01584.

PharmGKB

PA29808.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40099.

HOVERGEN

HBG007328.

InParanoid

P01584.

KO

K04519.

OMA

SNDKIPV.

OrthoDB

EOG4N30Q1.

PhylomeDB

P01584.

Enzyme and pathway databases

Pathway_Interaction_DB

anthraxpathway. Cellular roles of Anthrax toxin.
ifngpathway. IFN-gamma pathway.
il1pathway. IL1-mediated signaling events.
il12_2pathway. IL12-mediated signaling events.
il23pathway. IL23-mediated signaling events.
il27pathway. IL27-mediated signaling events.

Reactome

REACT_6900. Immune System.

SignaLink

P01584.

Gene expression databases

ArrayExpress

P01584.

Bgee

P01584.

CleanEx

HS_IL1B.

Genevestigator

P01584.

GermOnline

ENSG00000125538. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002348. IL1_HBGF.
IPR003502. IL1_propep.
IPR020877. Interleukin-1_CS.
IPR000975. Interleukin_1.
IPR003294. InterleukinIL1AB.
IPR003296. InterleukinIL1B.
[Graphical view]

Pfam

PF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]

PRINTS

PR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01359. INTRLEUKIN1B.
PR01357. INTRLEUKN1AB.

SMART

SM00125. IL1. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P01584.

ChEMBL

CHEMBL1909490.

ChiTaRS

IL1B. human.

DrugBank

DB00026. Anakinra.
DB01017. Minocycline.
DB01366. Procaterol.

EvolutionaryTrace

P01584.

GenomeRNAi

3553.

NextBio

13872.

PMAP-CutDB

P01584.

SOURCE

Search...

Entry information

Entry name

IL1B_HUMAN

Accession

Primary (citable) accession number: P01584
Secondary accession number(s): Q53X59 , Q53XX2, Q7M4S7, Q7RU01, Q96HE5, Q9UCT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 26, 2005
Last modified:	May 29, 2013
This is version 169 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.