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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

Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Involved in receptor binding1

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
  • apoptotic process Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • cellular response to drug Source: MGI
  • cellular response to mechanical stimulus Source: UniProtKB
  • cellular response to organic cyclic compound Source: UniProtKB
  • cellular response to organic substance Source: MGI
  • cytokine-mediated signaling pathway Source: BHF-UCL
  • ectopic germ cell programmed cell death Source: Ensembl
  • embryo implantation Source: BHF-UCL
  • extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • fever generation Source: UniProtKB-KW
  • hyaluronan biosynthetic process Source: UniProtKB
  • immune response Source: InterPro
  • inflammatory response Source: UniProtKB
  • interleukin-1 beta production Source: Ensembl
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • monocyte aggregation Source: UniProtKB
  • negative regulation of adiponectin secretion Source: BHF-UCL
  • 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 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
  • neutrophil chemotaxis Source: Ensembl
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  • positive regulation of cell adhesion molecule production Source: BHF-UCL
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of chemokine biosynthetic process Source: Ensembl
  • positive regulation of fever generation Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • 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 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-6 secretion Source: Ensembl
  • positive regulation of interleukin-8 production Source: UniProtKB
  • positive regulation of JNK cascade Source: GO_Central
  • 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 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
  • regulation of establishment of endothelial barrier Source: UniProtKB
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • regulation of insulin secretion Source: BHF-UCL
  • regulation of nitric-oxide synthase activity Source: UniProtKB
  • response to ATP Source: Ensembl
  • response to carbohydrate Source: Ensembl
  • sequestering of triglyceride Source: BHF-UCL
  • signal transduction Source: ProtInc
  • smooth muscle adaptation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Mitogen, Pyrogen

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125538-MONOMER.
ReactomeiR-HSA-446652. Interleukin-1 signaling.
R-HSA-448706. Interleukin-1 processing.
R-HSA-5660668. CLEC7A/inflammasome pathway.
SignaLinkiP01584.
SIGNORiP01584.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5992. IL1B.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Lysosome 1 Publication
  • Secretedexosome By similarity
  • Cytoplasmic vesicleautophagosome 1 Publication
  • Secreted 2 Publications

  • Note: The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. IL1B lacks any known signal sequence and the pathway(s) of its secretion is(are) not yet fully understood (PubMed:24201029). On the basis of experimental results, several unconventional secretion mechanisms have been proposed. 1. Secretion via secretory lysosomes: a fraction of CASP1 and IL1B precursor may be incorporated, by a yet undefined mechanism, into secretory lysosomes that undergo Ca2+-dependent exocytosis with release of mature IL1B (PubMed:15192144). 2. Secretory autophagy: IL1B-containing autophagosomes may fuse with endosomes or multivesicular bodies (MVBs) and then merge with the plasma membrane releasing soluble IL1B or IL1B-containing exosomes (PubMed:24201029). However, autophagy impacts IL1B production at several levels and its role in secretion is still controversial. 3. Secretion via exosomes: ATP-activation of P2RX7 leads to the formation of MVBs containing exosomes with entrapped IL1B, CASP1 and other inflammasome components. These MVBs undergo exocytosis with the release of exosomes. The release of soluble IL1B occurs after the lysis of exosome membranes (By similarity). 4. Secretion by microvesicle shedding: activation of the ATP receptor P2RX7 may induce an immediate shedding of membrane-derived microvesicles containing IL1B and possibly inflammasome components. The cytokine is then released in the extracellular compartment after microvesicle lysis (PubMed:11728343). 5. Release by translocation through permeabilized plasma membrane. This may occur in cells undergoing pyroptosis due to sustained activation of the inflammasome (By similarity). These mechanisms may not be not mutually exclusive.By similarity1 Publication2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27D → A: Loss of activation by CASP1; when associated with A-116. 1 Publication1
Mutagenesisi116D → A: Loss of activation by CASP1; when associated with A-27. 1 Publication1

Organism-specific databases

DisGeNETi3553.
MalaCardsiIL1B.
OpenTargetsiENSG00000125538.
PharmGKBiPA29808.

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiIL1B.
DMDMi62906858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000153011 – 116Removed in mature form; by CASP12 PublicationsAdd BLAST116
ChainiPRO_0000015302117 – 269Interleukin-1 beta1 PublicationAdd BLAST153

Post-translational modificationi

Activation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated.1 Publication

Proteomic databases

EPDiP01584.
MaxQBiP01584.
PaxDbiP01584.
PeptideAtlasiP01584.
PRIDEiP01584.

PTM databases

iPTMnetiP01584.
PhosphoSitePlusiP01584.

Miscellaneous databases

PMAP-CutDBP01584.

Expressioni

Tissue specificityi

Expressed in activated monocytes/macrophages (at protein level).1 Publication

Inductioni

By LPS (PubMed:15192144). Transcription and translation induced by M.tuberculosis and a number of different M.tuberculosis components in macrophages; EsxA is the most potent activator tested (at protein level) (PubMed:20148899).2 Publications

Gene expression databases

BgeeiENSG00000125538.
CleanExiHS_IL1B.
ExpressionAtlasiP01584. baseline and differential.
GenevisibleiP01584. HS.

Interactioni

Subunit structurei

Monomer. In its precursor form, weakly interacts with full-length MEFV; the mature cytokine does not interact at all (PubMed:17431422).2 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi109769. 15 interactors.
DIPiDIP-474N.
IntActiP01584. 6 interactors.
MINTiMINT-189806.
STRINGi9606.ENSP00000263341.

Chemistry databases

BindingDBiP01584.

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi121 – 128Combined sources8
Beta strandi133 – 137Combined sources5
Beta strandi138 – 140Combined sources3
Beta strandi141 – 145Combined sources5
Helixi149 – 154Combined sources6
Beta strandi158 – 162Combined sources5
Beta strandi172 – 178Combined sources7
Turni179 – 181Combined sources3
Beta strandi183 – 190Combined sources8
Beta strandi193 – 200Combined sources8
Turni203 – 205Combined sources3
Helixi213 – 215Combined sources3
Beta strandi217 – 222Combined sources6
Beta strandi225 – 233Combined sources9
Beta strandi237 – 240Combined sources4
Beta strandi242 – 247Combined sources6
Beta strandi249 – 252Combined sources4
Turni254 – 257Combined sources4
Beta strandi262 – 266Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BVPX-ray2.20I117-269[»]
5I1BX-ray2.10A117-269[»]
6I1BNMR-A117-269[»]
7I1BNMR-A117-269[»]
9ILBX-ray2.28A117-269[»]
ProteinModelPortaliP01584.
SMRiP01584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01584.

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-1 family.Curated

Phylogenomic databases

eggNOGiENOG410IGSZ. Eukaryota.
ENOG410XU2E. LUCA.
GeneTreeiENSGT00510000048687.
HOVERGENiHBG007328.
InParanoidiP01584.
KOiK04519.
OMAiSNDKIPV.
OrthoDBiEOG091G0GR9.
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)DescriptionActionsGraphical viewLength
Sequence conflicti6E → K in AAA36106 (PubMed:6083565).Curated1
Sequence conflicti6E → K in AAA59136 (PubMed:6083565).Curated1
Sequence conflicti6E → K in CAG28607 (Ref. 9) Curated1
Sequence conflicti124C → A AA sequence (PubMed:3920526).Curated1
Sequence conflicti155Q → D AA sequence (PubMed:3920526).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073951141E → N Requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant rs144640380dbSNPEnsembl.1

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.
UCSCiuc002tii.2. human.

Keywords - Coding sequence diversityi

Polymorphism

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
PDB 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[»]
5BVPX-ray2.20I117-269[»]
5I1BX-ray2.10A117-269[»]
6I1BNMR-A117-269[»]
7I1BNMR-A117-269[»]
9ILBX-ray2.28A117-269[»]
ProteinModelPortaliP01584.
SMRiP01584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109769. 15 interactors.
DIPiDIP-474N.
IntActiP01584. 6 interactors.
MINTiMINT-189806.
STRINGi9606.ENSP00000263341.

Chemistry databases

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

PTM databases

iPTMnetiP01584.
PhosphoSitePlusiP01584.

Polymorphism and mutation databases

BioMutaiIL1B.
DMDMi62906858.

Proteomic databases

EPDiP01584.
MaxQBiP01584.
PaxDbiP01584.
PeptideAtlasiP01584.
PRIDEiP01584.

Protocols and materials databases

DNASUi3553.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263341; ENSP00000263341; ENSG00000125538.
GeneIDi3553.
KEGGihsa:3553.
UCSCiuc002tii.2. human.

Organism-specific databases

CTDi3553.
DisGeNETi3553.
GeneCardsiIL1B.
HGNCiHGNC:5992. IL1B.
MalaCardsiIL1B.
MIMi147720. gene.
neXtProtiNX_P01584.
OpenTargetsiENSG00000125538.
PharmGKBiPA29808.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGSZ. Eukaryota.
ENOG410XU2E. LUCA.
GeneTreeiENSGT00510000048687.
HOVERGENiHBG007328.
InParanoidiP01584.
KOiK04519.
OMAiSNDKIPV.
OrthoDBiEOG091G0GR9.
PhylomeDBiP01584.
TreeFamiTF300203.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125538-MONOMER.
ReactomeiR-HSA-446652. Interleukin-1 signaling.
R-HSA-448706. Interleukin-1 processing.
R-HSA-5660668. CLEC7A/inflammasome pathway.
SignaLinkiP01584.
SIGNORiP01584.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000125538.
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...

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: November 30, 2016
This is version 206 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

Miscellaneous

The IL1B production occurs in 2 steps, each being controlled by different stimuli. First, inflammatory signals, such as LPS, stimulate the synthesis and promote the accumulation of cytosolic stores of pro-IL1B (priming). Then additional signals are required for inflammasome assembly, leading to CASP1 activation, pro-IL1B processing and eventually secretion of the active cytokine. IL1B processing and secretion are temporarily associated.1 Publication

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.