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P01584

- IL1B_HUMAN

UniProt

P01584 - IL1B_HUMAN

Protein

Interleukin-1 beta

Gene

IL1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
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    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 cell division Source: UniProtKB-KW
    33. positive regulation of chemokine biosynthetic process Source: Ensembl
    34. positive regulation of fever generation Source: BHF-UCL
    35. positive regulation of gene expression Source: AgBase
    36. positive regulation of granulocyte macrophage colony-stimulating factor production Source: BHF-UCL
    37. positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
    38. positive regulation of histone acetylation Source: BHF-UCL
    39. positive regulation of histone phosphorylation Source: BHF-UCL
    40. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    41. positive regulation of interferon-gamma production Source: BHF-UCL
    42. positive regulation of interleukin-2 biosynthetic process Source: BHF-UCL
    43. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
    44. positive regulation of interleukin-6 production Source: BHF-UCL
    45. positive regulation of interleukin-8 production Source: UniProtKB
    46. positive regulation of JNK cascade Source: Ensembl
    47. positive regulation of lipid catabolic process Source: BHF-UCL
    48. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    49. positive regulation of mitosis Source: BHF-UCL
    50. positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
    51. positive regulation of myosin light chain kinase activity Source: BHF-UCL
    52. positive regulation of NF-kappaB import into nucleus Source: BHF-UCL
    53. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    54. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
    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

    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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29808.

    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

    ArrayExpressiP01584.
    BgeeiP01584.
    CleanExiHS_IL1B.
    GenevestigatoriP01584.

    Interactioni

    Subunit structurei

    Monomer. Interacts with MEFV.2 Publications

    Protein-protein interaction databases

    BioGridi109769. 12 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 – 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.
    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.
    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

    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. 1 PublicationCurated
    Sequence conflicti124 – 1241C → A AA sequence (PubMed:3920526)Curated
    Sequence conflicti155 – 1551Q → D AA sequence (PubMed:3920526)Curated

    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. 6 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

    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: October 1, 2014
    This is version 182 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