Reviewed, UniProtKB/Swiss-Prot P01584 (IL1B_HUMAN)

Names and origin

Protein names

Recommended name:
    Interleukin-1 beta
      Short name(s)=IL-1 beta
Alternative name(s):
    Catabolin

Gene names

Name:	IL1B
Synonyms:	IL1F2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	activation of MAPK activity Inferred from direct assay. Source: UniProtKB anti-apoptosis Inferred from direct assay. Source: UniProtKB cell-cell signaling Ref.2 Traceable author statement. Source: ProtInc cytokine and chemokine mediated signaling pathway Inferred from direct assay. Source: UniProtKB inflammatory response Ref.15 Non-traceable author statement. Source: UniProtKB negative regulation of cell proliferation Ref.5 Traceable author statement. Source: ProtInc positive regulation of protein amino acid phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of transcription factor activity Inferred from direct assay. Source: UniProtKB regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Ref.5 Traceable author statement. Source: ProtInc
Molecular function	interleukin-1 receptor binding Ref.15 Non-traceable author statement. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL1R1	P14778	1	EBI-1026290,EBI-525905

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Propeptide

1 – 116

116

Chain

117 – 269

153

Interleukin-1 beta

Sites

Site

120

1

Involved in receptor binding

Experimental info

Sequence conflict

6

1

E → K in AAA36106 and 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

120 – 128

9

Beta strand

133 – 136

4

Beta strand

142 – 145

4

Helix

150 – 154

5

Beta strand

158 – 162

5

Beta strand

169 – 178

10

Beta strand

181 – 200

20

Turn

203 – 205

3

Helix

213 – 215

3

Beta strand

216 – 222

7

Beta strand

225 – 233

9

Beta strand

237 – 240

4

Beta strand

249 – 252

4

Beta strand

255 – 259

5

Beta strand

262 – 266

5

Sequences

	Sequence		Length	Mass (Da)
	P01584-1 [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: 6083565] [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: 2989698] [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: 3490654] [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: 3493774] [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: 2954882] [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: 2635664] [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: 11991722] [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 program for genomic applications 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: 15815621] [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: 15489334] [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: 1919436] [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: 3920526] [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: 3281727] [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: 1837236] [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: 3259176] [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: 2585509] [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: 2602367] [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: 2372550] [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: 2001363] [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: 9062193] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH RECEPTOR.

Web resources

Wikipedia

Interleukin-1 entry

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

A21851.
ICHU1B. A25542.

RefSeq

NP_000567.1.

UniGene

Hs.126256

3D structure databases

PDBMSD

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	[»]
2NVH	X-ray	1.53	A	117-269	[»]
31BI	X-ray	2.00	A	117-269	[»]
41BI	X-ray	2.90	A	117-269	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:474N.

IntAct

P01584.

Genome annotation databases

Ensembl

ENSG00000125538. Homo sapiens. [Contig view]

GeneID

3553.

KEGG

hsa:3553.

Organism-specific databases

H-InvDB

HIX0002386.

HGNC

HGNC:5992. IL1B.

HPA

HPA001410.

MIM

147720. gene.

PharmGKB

PA29808.

GenAtlas

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