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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

  1. cytokine activity Source: BHF-UCL
  2. interleukin-1 receptor binding Source: UniProtKB
  3. protein domain specific binding Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: BHF-UCL
  2. apoptotic process Source: ProtInc
  3. cell-cell signaling Source: ProtInc
  4. cellular response to drug Source: MGI
  5. cellular response to mechanical stimulus Source: UniProtKB
  6. cellular response to organic cyclic compound Source: UniProtKB
  7. cellular response to organic substance Source: MGI
  8. cytokine-mediated signaling pathway Source: BHF-UCL
  9. ectopic germ cell programmed cell death Source: Ensembl
  10. embryo implantation Source: BHF-UCL
  11. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  12. fever generation Source: UniProtKB-KW
  13. hyaluronan biosynthetic process Source: UniProtKB
  14. immune response Source: InterPro
  15. inflammatory response Source: UniProtKB
  16. interleukin-1 beta production Source: Ensembl
  17. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  18. MAPK cascade Source: UniProtKB
  19. monocyte aggregation Source: UniProtKB
  20. negative regulation of adiponectin secretion Source: BHF-UCL
  21. negative regulation of cell proliferation Source: BHF-UCL
  22. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  23. negative regulation of glucose transport Source: BHF-UCL
  24. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  25. negative regulation of lipid catabolic process Source: BHF-UCL
  26. negative regulation of lipid metabolic process Source: BHF-UCL
  27. negative regulation of MAP kinase activity Source: BHF-UCL
  28. neutrophil chemotaxis Source: Ensembl
  29. positive regulation of angiogenesis Source: BHF-UCL
  30. positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  31. positive regulation of cell adhesion molecule production Source: BHF-UCL
  32. positive regulation of chemokine biosynthetic process Source: Ensembl
  33. positive regulation of fever generation Source: BHF-UCL
  34. positive regulation of gene expression Source: AgBase
  35. positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
  36. positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
  37. positive regulation of histone acetylation Source: BHF-UCL
  38. positive regulation of histone phosphorylation Source: BHF-UCL
  39. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: GO_Central
  40. positive regulation of interferon-gamma production Source: BHF-UCL
  41. positive regulation of interleukin-2 biosynthetic process Source: BHF-UCL
  42. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
  43. positive regulation of interleukin-6 production Source: BHF-UCL
  44. positive regulation of interleukin-8 production Source: UniProtKB
  45. positive regulation of JNK cascade Source: GO_Central
  46. positive regulation of lipid catabolic process Source: BHF-UCL
  47. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  48. positive regulation of mitotic nuclear division Source: BHF-UCL
  49. positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  50. positive regulation of myosin light chain kinase activity Source: BHF-UCL
  51. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  52. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  53. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  54. positive regulation of phagocytosis Source: AgBase
  55. positive regulation of prostaglandin secretion Source: BHF-UCL
  56. positive regulation of protein export from nucleus Source: BHF-UCL
  57. positive regulation of protein phosphorylation Source: BHF-UCL
  58. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  59. positive regulation of T cell mediated immunity Source: BHF-UCL
  60. positive regulation of T cell proliferation Source: BHF-UCL
  61. positive regulation of transcription, DNA-templated Source: UniProtKB
  62. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  63. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  64. positive regulation vascular endothelial growth factor production Source: BHF-UCL
  65. protein kinase B signaling Source: UniProtKB
  66. regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  67. regulation of insulin secretion Source: BHF-UCL
  68. response to ATP Source: Ensembl
  69. response to carbohydrate Source: Ensembl
  70. sequestering of triglyceride Source: BHF-UCL
  71. signal transduction Source: ProtInc
  72. smooth muscle adaptation Source: BHF-UCL
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.
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

  1. Secreted

  2. 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

  1. cytosol Source: Reactome
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. 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.
GenevestigatoriP01584.

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.

Polymorphism and mutation databases

BioMutaiIL1B.

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.
SignaLinkiP01584.

Miscellaneous databases

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

Gene expression databases

BgeeiP01584.
CleanExiHS_IL1B.
ExpressionAtlasiP01584. baseline and differential.
GenevestigatoriP01584.

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: April 29, 2015
This is version 189 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.