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P01584

- IL1B_HUMAN

UniProt

P01584 - IL1B_HUMAN

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Protein
Interleukin-1 beta
Gene
IL1B, IL1F2
Organism
Homo sapiens (Human)
Status
Reviewed - 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. MAPK cascade Source: UniProtKB
  2. activation of MAPK activity Source: BHF-UCL
  3. apoptotic process Source: ProtInc
  4. cell-cell signaling Source: ProtInc
  5. cellular response to drug Source: MGI
  6. cellular response to mechanical stimulus Source: UniProtKB
  7. cellular response to organic cyclic compound Source: UniProtKB
  8. cellular response to organic substance Source: MGI
  9. cytokine-mediated signaling pathway Source: BHF-UCL
  10. ectopic germ cell programmed cell death Source: Ensembl
  11. embryo implantation Source: BHF-UCL
  12. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  13. fever generation Source: UniProtKB-KW
  14. hyaluronan biosynthetic process Source: UniProtKB
  15. immune response Source: InterPro
  16. inflammatory response Source: UniProtKB
  17. interleukin-1 beta production Source: Ensembl
  18. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  19. monocyte aggregation Source: UniProtKB
  20. negative regulation of MAP kinase activity Source: BHF-UCL
  21. negative regulation of adiponectin secretion Source: BHF-UCL
  22. negative regulation of cell proliferation Source: BHF-UCL
  23. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  24. negative regulation of glucose transport Source: BHF-UCL
  25. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  26. negative regulation of lipid catabolic process Source: BHF-UCL
  27. negative regulation of lipid metabolic process Source: BHF-UCL
  28. neutrophil chemotaxis Source: Ensembl
  29. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  30. positive regulation of JNK cascade Source: Ensembl
  31. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
  32. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  33. positive regulation of T cell mediated immunity Source: BHF-UCL
  34. positive regulation of T cell proliferation Source: BHF-UCL
  35. positive regulation of angiogenesis Source: BHF-UCL
  36. positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  37. positive regulation of cell adhesion molecule production Source: BHF-UCL
  38. positive regulation of cell division Source: UniProtKB-KW
  39. positive regulation of chemokine biosynthetic process Source: Ensembl
  40. positive regulation of fever generation Source: BHF-UCL
  41. positive regulation of gene expression Source: AgBase
  42. positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
  43. positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
  44. positive regulation of histone acetylation Source: BHF-UCL
  45. positive regulation of histone phosphorylation Source: BHF-UCL
  46. positive regulation of interferon-gamma production Source: BHF-UCL
  47. positive regulation of interleukin-2 biosynthetic process Source: BHF-UCL
  48. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
  49. positive regulation of interleukin-6 production Source: BHF-UCL
  50. positive regulation of interleukin-8 production Source: UniProtKB
  51. positive regulation of lipid catabolic process Source: BHF-UCL
  52. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  53. positive regulation of mitosis Source: BHF-UCL
  54. positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  55. positive regulation of myosin light chain kinase activity Source: BHF-UCL
  56. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  57. positive regulation of prostaglandin secretion Source: BHF-UCL
  58. positive regulation of protein export from nucleus Source: BHF-UCL
  59. positive regulation of protein phosphorylation Source: BHF-UCL
  60. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  61. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  62. positive regulation of transcription, DNA-templated Source: UniProtKB
  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: 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

  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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 116116
PRO_0000015301Add
BLAST
Chaini117 – 269153Interleukin-1 beta1 Publication
PRO_0000015302Add
BLAST

Proteomic databases

MaxQBiP01584.
PaxDbiP01584.
PRIDEiP01584.

Miscellaneous databases

PMAP-CutDBP01584.

Expressioni

Gene expression databases

ArrayExpressiP01584.
BgeeiP01584.
CleanExiHS_IL1B.
GenevestigatoriP01584.

Interactioni

Subunit structurei

Monomer. Interacts with MEFV.1 Publication

Protein-protein interaction databases

BioGridi109769. 12 interactions.
DIPiDIP-474N.
IntActiP01584. 4 interactions.
MINTiMINT-189806.
STRINGi9606.ENSP00000263341.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.

Phylogenomic databases

eggNOGiNOG40099.
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

MAEVPELASE MMAYYSGNED DLFFEADGPK QMKCSFQDLD LCPLDGGIQL    50
RISDHHYSKG FRQAASVVVA MDKLRKMLVP CPQTFQENDL STFFPFIFEE 100
EPIFFDTWDN EAYVHDAPVR SLNCTLRDSQ QKSLVMSGPY ELKALHLQGQ 150
DMEQQVVFSM SFVQGEESND KIPVALGLKE KNLYLSCVLK DDKPTLQLES 200
VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST SQAENMPVFL 250
GGTKGGQDIT DFTMQFVSS 269
Length:269
Mass (Da):30,748
Last modified:April 26, 2005 - v2
Checksum:i9BF73C3673C6FD66
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61E → K in AAA36106. 1 Publication
Sequence conflicti6 – 61E → K in AAA59136. 1 Publication
Sequence conflicti6 – 61E → K in CAG28607. 1 Publication
Sequence conflicti124 – 1241C → A AA sequence 1 Publication
Sequence conflicti155 – 1551Q → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi62906858.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2102.1.
PIRi A21851.
A25542. ICHU1B.
RefSeqi NP_000567.1. NM_000576.2.
UniGenei Hs.126256.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HIB X-ray 2.40 A 117-269 [» ]
1I1B X-ray 2.00 A 117-269 [» ]
1IOB X-ray 2.00 A 117-269 [» ]
1ITB X-ray 2.50 A 117-269 [» ]
1L2H X-ray 1.54 A 117-269 [» ]
1S0L X-ray 2.34 A 117-269 [» ]
1T4Q X-ray 2.10 A 117-269 [» ]
1TOO X-ray 2.10 A 117-269 [» ]
1TP0 X-ray 2.20 A 117-269 [» ]
1TWE X-ray 2.10 A 117-269 [» ]
1TWM X-ray 2.26 A 117-269 [» ]
21BI X-ray 2.00 A 117-269 [» ]
2I1B X-ray 2.00 A 117-269 [» ]
2KH2 NMR - A 117-269 [» ]
2NVH X-ray 1.53 A 117-269 [» ]
31BI X-ray 2.00 A 117-269 [» ]
3LTQ X-ray 2.10 A 117-269 [» ]
3O4O X-ray 3.30 A 117-269 [» ]
3POK X-ray 1.70 A 117-269 [» ]
41BI X-ray 2.90 A 117-269 [» ]
4DEP X-ray 3.10 A/D 117-269 [» ]
4G6J X-ray 2.03 A 117-269 [» ]
4G6M X-ray 1.81 A 118-267 [» ]
4GAF X-ray 2.15 A 117-269 [» ]
4GAI X-ray 1.49 A/B 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 [» ]
ProteinModelPortali P01584.
SMRi P01584. Positions 117-268.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109769. 12 interactions.
DIPi DIP-474N.
IntActi P01584. 4 interactions.
MINTi MINT-189806.
STRINGi 9606.ENSP00000263341.

Chemistry

BindingDBi P01584.
ChEMBLi CHEMBL1909490.
DrugBanki DB00026. Anakinra.
DB01017. Minocycline.
DB01366. Procaterol.
GuidetoPHARMACOLOGYi 2623.

Polymorphism databases

DMDMi 62906858.

Proteomic databases

MaxQBi P01584.
PaxDbi P01584.
PRIDEi P01584.

Protocols and materials databases

DNASUi 3553.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263341 ; ENSP00000263341 ; ENSG00000125538 .
GeneIDi 3553.
KEGGi hsa:3553.
UCSCi uc002tih.1. human.

Organism-specific databases

CTDi 3553.
GeneCardsi GC02M113587.
HGNCi HGNC:5992. IL1B.
MIMi 147720. gene.
neXtProti NX_P01584.
PharmGKBi PA29808.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40099.
HOVERGENi HBG007328.
InParanoidi P01584.
KOi K04519.
OMAi SNDKIPV.
OrthoDBi EOG71P2BQ.
PhylomeDBi P01584.
TreeFami TF300203.

Enzyme and pathway databases

Reactomei REACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
SignaLinki P01584.

Miscellaneous databases

ChiTaRSi IL1B. human.
EvolutionaryTracei P01584.
GeneWikii IL1B.
GenomeRNAii 3553.
NextBioi 13872.
PMAP-CutDB P01584.
PROi P01584.
SOURCEi Search...

Gene expression databases

ArrayExpressi P01584.
Bgeei P01584.
CleanExi HS_IL1B.
Genevestigatori P01584.

Family and domain databases

InterProi IPR008996. 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 ]
PANTHERi PTHR10078:SF20. PTHR10078:SF20. 1 hit.
Pfami PF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view ]
PRINTSi PR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01357. INTRLEUKN1AB.
SUPFAMi SSF50353. SSF50353. 1 hit.
PROSITEi PS00253. INTERLEUKIN_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 181 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

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