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Protein

Interleukin-1 beta

Gene

IL1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Involved in receptor binding

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • interleukin-1 receptor binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • activation of MAPK activity Source: BHF-UCL
  • aging Source: Ensembl
  • apoptotic process Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • cellular response to antibiotic Source: Ensembl
  • cellular response to drug Source: MGI
  • cellular response to fatty acid Source: Ensembl
  • cellular response to glucose stimulus Source: Ensembl
  • cellular response to mechanical stimulus Source: UniProtKB
  • cellular response to methotrexate Source: Ensembl
  • cellular response to organic cyclic compound Source: UniProtKB
  • cellular response to organic substance Source: MGI
  • chronic inflammatory response to antigenic stimulus Source: Ensembl
  • cytokine-mediated signaling pathway Source: BHF-UCL
  • ectopic germ cell programmed cell death Source: Ensembl
  • embryo implantation Source: BHF-UCL
  • estrogen metabolic process Source: Ensembl
  • extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • fever generation Source: UniProtKB-KW
  • glycoprotein metabolic process Source: Ensembl
  • hyaluronan biosynthetic process Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • innate immune response Source: Reactome
  • interleukin-1 beta production Source: Ensembl
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • memory Source: Ensembl
  • monocyte aggregation Source: UniProtKB
  • negative regulation of adiponectin secretion Source: BHF-UCL
  • negative regulation of branching morphogenesis of a nerve Source: Ensembl
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • negative regulation of glucose transport Source: BHF-UCL
  • negative regulation of glutamate secretion Source: Ensembl
  • negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of lipid metabolic process Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: BHF-UCL
  • negative regulation of neural precursor cell proliferation Source: Ensembl
  • negative regulation of neuron differentiation Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • neutrophil chemotaxis Source: Ensembl
  • ovulation Source: Ensembl
  • pentacyclic triterpenoid metabolic process Source: Ensembl
  • polyketide metabolic process Source: Ensembl
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of astrocyte differentiation Source: Ensembl
  • positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  • positive regulation of cell adhesion molecule production Source: BHF-UCL
  • positive regulation of chemokine biosynthetic process Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • positive regulation of fever generation Source: BHF-UCL
  • positive regulation of gene expression Source: AgBase
  • positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
  • positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
  • positive regulation of histone acetylation Source: BHF-UCL
  • positive regulation of histone phosphorylation Source: BHF-UCL
  • positive regulation of immature T cell proliferation in thymus Source: Ensembl
  • positive regulation of interferon-gamma production Source: BHF-UCL
  • positive regulation of interleukin-2 biosynthetic process Source: BHF-UCL
  • positive regulation of interleukin-6 biosynthetic process Source: Ensembl
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of interleukin-8 production Source: UniProtKB
  • positive regulation of JNK cascade Source: GO_Central
  • positive regulation of JUN kinase activity Source: Ensembl
  • positive regulation of lipid catabolic process Source: BHF-UCL
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of mitotic nuclear division Source: BHF-UCL
  • positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  • positive regulation of myosin light chain kinase activity Source: BHF-UCL
  • positive regulation of neutrophil chemotaxis Source: Ensembl
  • positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • positive regulation of phagocytosis Source: AgBase
  • positive regulation of prostaglandin secretion Source: BHF-UCL
  • positive regulation of protein export from nucleus Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of T cell mediated immunity Source: BHF-UCL
  • positive regulation of T cell proliferation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of vascular endothelial growth factor production Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • protein kinase B signaling Source: UniProtKB
  • purine nucleobase metabolic process Source: Ensembl
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • regulation of insulin secretion Source: BHF-UCL
  • response to ATP Source: Ensembl
  • response to dexamethasone Source: Ensembl
  • response to diuretic Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to gamma radiation Source: Ensembl
  • response to heat Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to L-ascorbic acid Source: Ensembl
  • response to morphine Source: Ensembl
  • response to ozone Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • response to statin Source: Ensembl
  • response to stilbenoid Source: Ensembl
  • response to vitamin D Source: Ensembl
  • sequestering of triglyceride Source: BHF-UCL
  • signal transduction Source: ProtInc
  • smooth muscle adaptation Source: BHF-UCL
  • social behavior Source: Ensembl
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Mitogen, Pyrogen

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
REACT_355550. CLEC7A/inflammasome pathway.
SignaLinkiP01584.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 beta
Short name:
IL-1 beta
Alternative name(s):
Catabolin
Gene namesi
Name:IL1B
Synonyms:IL1F2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5992. IL1B.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular region Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • secretory granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29808.

Chemistry

DrugBankiDB06168. Canakinumab.
DB05260. Gallium nitrate.
DB01017. Minocycline.
DB06372. Rilonacept.

Polymorphism and mutation databases

BioMutaiIL1B.
DMDMi62906858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1161162 PublicationsPRO_0000015301Add
BLAST
Chaini117 – 269153Interleukin-1 beta1 PublicationPRO_0000015302Add
BLAST

Proteomic databases

MaxQBiP01584.
PaxDbiP01584.
PRIDEiP01584.

Miscellaneous databases

PMAP-CutDBP01584.

Expressioni

Gene expression databases

BgeeiP01584.
CleanExiHS_IL1B.
ExpressionAtlasiP01584. baseline and differential.
GenevisibleiP01584. HS.

Interactioni

Subunit structurei

Monomer. Interacts with MEFV.2 Publications

Protein-protein interaction databases

BioGridi109769. 13 interactions.
DIPiDIP-474N.
IntActiP01584. 6 interactions.
MINTiMINT-189806.
STRINGi9606.ENSP00000263341.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi121 – 1288Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi141 – 1455Combined sources
Helixi149 – 1546Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi172 – 1787Combined sources
Turni179 – 1813Combined sources
Beta strandi183 – 1908Combined sources
Beta strandi193 – 2008Combined sources
Turni203 – 2053Combined sources
Helixi213 – 2153Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi225 – 2339Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi242 – 2476Combined sources
Beta strandi249 – 2524Combined sources
Turni254 – 2574Combined sources
Beta strandi262 – 2665Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP01584.
SMRiP01584. Positions 117-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01584.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the IL-1 family.Curated

Phylogenomic databases

eggNOGiNOG40099.
GeneTreeiENSGT00510000048687.
HOVERGENiHBG007328.
InParanoidiP01584.
KOiK04519.
OMAiSNDKIPV.
OrthoDBiEOG71P2BQ.
PhylomeDBiP01584.
TreeFamiTF300203.

Family and domain databases

InterProiIPR008996. 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]
PANTHERiPTHR10078:SF20. PTHR10078:SF20. 1 hit.
PfamiPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSiPR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01357. INTRLEUKN1AB.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVPELASE MMAYYSGNED DLFFEADGPK QMKCSFQDLD LCPLDGGIQL
60 70 80 90 100
RISDHHYSKG FRQAASVVVA MDKLRKMLVP CPQTFQENDL STFFPFIFEE
110 120 130 140 150
EPIFFDTWDN EAYVHDAPVR SLNCTLRDSQ QKSLVMSGPY ELKALHLQGQ
160 170 180 190 200
DMEQQVVFSM SFVQGEESND KIPVALGLKE KNLYLSCVLK DDKPTLQLES
210 220 230 240 250
VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST SQAENMPVFL
260
GGTKGGQDIT DFTMQFVSS
Length:269
Mass (Da):30,748
Last modified:April 26, 2005 - v2
Checksum:i9BF73C3673C6FD66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61E → K in AAA36106 (PubMed:6083565).Curated
Sequence conflicti6 – 61E → K in AAA59136 (PubMed:6083565).Curated
Sequence conflicti6 – 61E → K in CAG28607 (Ref. 9) Curated
Sequence conflicti124 – 1241C → A AA sequence (PubMed:3920526).Curated
Sequence conflicti155 – 1551Q → D AA sequence (PubMed:3920526).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2102.1.
PIRiA21851.
A25542. ICHU1B.
RefSeqiNP_000567.1. NM_000576.2.
UniGeneiHs.126256.

Genome annotation databases

EnsembliENST00000263341; ENSP00000263341; ENSG00000125538.
GeneIDi3553.
KEGGihsa:3553.
UCSCiuc002tih.1. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Interleukin-1 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2102.1.
PIRiA21851.
A25542. ICHU1B.
RefSeqiNP_000567.1. NM_000576.2.
UniGeneiHs.126256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP01584.
SMRiP01584. Positions 117-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109769. 13 interactions.
DIPiDIP-474N.
IntActiP01584. 6 interactions.
MINTiMINT-189806.
STRINGi9606.ENSP00000263341.

Chemistry

BindingDBiP01584.
ChEMBLiCHEMBL1909490.
DrugBankiDB06168. Canakinumab.
DB05260. Gallium nitrate.
DB01017. Minocycline.
DB06372. Rilonacept.
GuidetoPHARMACOLOGYi2623.

Polymorphism and mutation databases

BioMutaiIL1B.
DMDMi62906858.

Proteomic databases

MaxQBiP01584.
PaxDbiP01584.
PRIDEiP01584.

Protocols and materials databases

DNASUi3553.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263341; ENSP00000263341; ENSG00000125538.
GeneIDi3553.
KEGGihsa:3553.
UCSCiuc002tih.1. human.

Organism-specific databases

CTDi3553.
GeneCardsiGC02M113587.
HGNCiHGNC:5992. IL1B.
MIMi147720. gene.
neXtProtiNX_P01584.
PharmGKBiPA29808.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40099.
GeneTreeiENSGT00510000048687.
HOVERGENiHBG007328.
InParanoidiP01584.
KOiK04519.
OMAiSNDKIPV.
OrthoDBiEOG71P2BQ.
PhylomeDBiP01584.
TreeFamiTF300203.

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
REACT_355550. CLEC7A/inflammasome pathway.
SignaLinkiP01584.

Miscellaneous databases

ChiTaRSiIL1B. human.
EvolutionaryTraceiP01584.
GeneWikiiIL1B.
GenomeRNAii3553.
NextBioi13872.
PMAP-CutDBP01584.
PROiP01584.
SOURCEiSearch...

Gene expression databases

BgeeiP01584.
CleanExiHS_IL1B.
ExpressionAtlasiP01584. baseline and differential.
GenevisibleiP01584. HS.

Family and domain databases

InterProiIPR008996. 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]
PANTHERiPTHR10078:SF20. PTHR10078:SF20. 1 hit.
PfamiPF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]
PRINTSiPR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01357. INTRLEUKN1AB.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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.

Entry informationi

Entry nameiIL1B_HUMAN
AccessioniPrimary (citable) accession number: P01584
Secondary accession number(s): Q53X59
, Q53XX2, Q7M4S7, Q7RU01, Q96HE5, Q9UCT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 26, 2005
Last modified: July 22, 2015
This is version 192 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.