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P05113

- IL5_HUMAN

UniProt

P05113 - IL5_HUMAN

Protein

Interleukin-5

Gene

IL5

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

    Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei90 – 901Not glycosylated

    GO - Molecular functioni

    1. interleukin-5 receptor binding Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Ensembl
    2. immune response Source: InterPro
    3. inflammatory response Source: ProtInc
    4. positive regulation of B cell proliferation Source: Ensembl
    5. positive regulation of eosinophil differentiation Source: Ensembl
    6. positive regulation of immunoglobulin secretion Source: Ensembl
    7. positive regulation of JAK-STAT cascade Source: Ensembl
    8. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    9. positive regulation of podosome assembly Source: BHF-UCL
    10. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    11. positive regulation of transcription, DNA-templated Source: Ensembl

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Enzyme and pathway databases

    ReactomeiREACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinkiP05113.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-5
    Short name:
    IL-5
    Alternative name(s):
    B-cell differentiation factor I
    Eosinophil differentiation factor
    T-cell replacing factor
    Short name:
    TRF
    Gene namesi
    Name:IL5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6016. IL5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: BHF-UCL
    2. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29833.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 134115Interleukin-5PRO_0000015560Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi22 – 221O-linked (GalNAc...)1 Publication
    Glycosylationi47 – 471N-linked (GlcNAc...)1 Publication
    Disulfide bondi63 – 63Interchain (with C-105)1 Publication
    Disulfide bondi105 – 105Interchain (with C-63)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP05113.
    PeptideAtlasiP05113.
    PRIDEiP05113.

    Expressioni

    Gene expression databases

    ArrayExpressiP05113.
    BgeeiP05113.
    CleanExiHS_IL5.
    GenevestigatoriP05113.

    Organism-specific databases

    HPAiCAB010304.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSF2RBP329272EBI-2435811,EBI-1809771
    IL5RAQ013442EBI-2435811,EBI-1759442

    Protein-protein interaction databases

    BioGridi109781. 3 interactions.
    DIPiDIP-28N.
    IntActiP05113. 2 interactions.
    STRINGi9606.ENSP00000231454.

    Structurei

    Secondary structure

    1
    134
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 3914
    Helixi41 – 455
    Beta strandi51 – 544
    Beta strandi56 – 583
    Helixi60 – 623
    Helixi64 – 7512
    Helixi84 – 10320
    Beta strandi106 – 1116
    Helixi112 – 12817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HULX-ray2.40A/B24-131[»]
    3QT2X-ray2.55C/D/E/F19-134[»]
    3VA2X-ray2.70A/B23-134[»]
    ProteinModelPortaliP05113.
    SMRiP05113. Positions 24-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05113.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the IL-5 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG41650.
    HOGENOMiHOG000074049.
    HOVERGENiHBG003865.
    InParanoidiP05113.
    KOiK05428.
    OMAiQLCIEEV.
    OrthoDBiEOG70PC0S.
    PhylomeDBiP05113.
    TreeFamiTF338422.

    Family and domain databases

    Gene3Di1.20.1250.10. 1 hit.
    InterProiIPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR000186. IL-5.
    [Graphical view]
    PANTHERiPTHR10525. PTHR10525. 1 hit.
    PfamiPF02025. IL5. 1 hit.
    [Graphical view]
    PRINTSiPR00432. INTERLEUKIN5.
    ProDomiPD006721. Interleukin_5. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF47266. SSF47266. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P05113-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL    50
    RIPVPVHKNH QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG 100
    QKKKCGEERR RVNQFLDYLQ EFLGVMNTEW IIES 134
    Length:134
    Mass (Da):15,238
    Last modified:August 13, 1987 - v1
    Checksum:iDC984467179556A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881F → L in CAA31210. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04688 mRNA. Translation: CAA28390.1.
    J03478 Genomic DNA. Translation: AAA74469.1.
    J02971 Genomic DNA. Translation: AAA98620.1.
    X12705 mRNA. Translation: CAA31210.1.
    X12706 Genomic DNA. Translation: CAA31211.1.
    AF353265 Genomic DNA. Translation: AAK19759.1.
    BC066282 mRNA. Translation: AAH66282.1.
    CCDSiCCDS4156.1.
    PIRiA28477.
    RefSeqiNP_000870.1. NM_000879.2.
    UniGeneiHs.2247.

    Genome annotation databases

    EnsembliENST00000231454; ENSP00000231454; ENSG00000113525.
    GeneIDi3567.
    KEGGihsa:3567.
    UCSCiuc003kxe.1. human.

    Polymorphism databases

    DMDMi124341.

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine mini-reviews: IL-5
    Wikipedia

    Interleukin-5 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04688 mRNA. Translation: CAA28390.1 .
    J03478 Genomic DNA. Translation: AAA74469.1 .
    J02971 Genomic DNA. Translation: AAA98620.1 .
    X12705 mRNA. Translation: CAA31210.1 .
    X12706 Genomic DNA. Translation: CAA31211.1 .
    AF353265 Genomic DNA. Translation: AAK19759.1 .
    BC066282 mRNA. Translation: AAH66282.1 .
    CCDSi CCDS4156.1.
    PIRi A28477.
    RefSeqi NP_000870.1. NM_000879.2.
    UniGenei Hs.2247.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HUL X-ray 2.40 A/B 24-131 [» ]
    3QT2 X-ray 2.55 C/D/E/F 19-134 [» ]
    3VA2 X-ray 2.70 A/B 23-134 [» ]
    ProteinModelPortali P05113.
    SMRi P05113. Positions 24-131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109781. 3 interactions.
    DIPi DIP-28N.
    IntActi P05113. 2 interactions.
    STRINGi 9606.ENSP00000231454.

    Chemistry

    BindingDBi P05113.
    ChEMBLi CHEMBL1169600.
    DrugBanki DB01411. Pranlukast.

    Polymorphism databases

    DMDMi 124341.

    Proteomic databases

    PaxDbi P05113.
    PeptideAtlasi P05113.
    PRIDEi P05113.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231454 ; ENSP00000231454 ; ENSG00000113525 .
    GeneIDi 3567.
    KEGGi hsa:3567.
    UCSCi uc003kxe.1. human.

    Organism-specific databases

    CTDi 3567.
    GeneCardsi GC05M131881.
    HGNCi HGNC:6016. IL5.
    HPAi CAB010304.
    MIMi 147850. gene.
    neXtProti NX_P05113.
    PharmGKBi PA29833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41650.
    HOGENOMi HOG000074049.
    HOVERGENi HBG003865.
    InParanoidi P05113.
    KOi K05428.
    OMAi QLCIEEV.
    OrthoDBi EOG70PC0S.
    PhylomeDBi P05113.
    TreeFami TF338422.

    Enzyme and pathway databases

    Reactomei REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinki P05113.

    Miscellaneous databases

    ChiTaRSi IL5. human.
    EvolutionaryTracei P05113.
    GeneWikii Interleukin_5.
    GenomeRNAii 3567.
    NextBioi 13932.
    PROi P05113.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05113.
    Bgeei P05113.
    CleanExi HS_IL5.
    Genevestigatori P05113.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR000186. IL-5.
    [Graphical view ]
    PANTHERi PTHR10525. PTHR10525. 1 hit.
    Pfami PF02025. IL5. 1 hit.
    [Graphical view ]
    PRINTSi PR00432. INTERLEUKIN5.
    ProDomi PD006721. Interleukin_5. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF47266. SSF47266. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNA for human T-cell replacing factor (interleukin-5) and comparison with the murine homologue."
      Azuma C., Tanabe T., Konishi M., Kinashi T., Noma T., Matsuda F., Yaoita Y., Takatsu K., Hammarstroem L., Smith C.I.E., Severinson E., Honjo T.
      Nucleic Acids Res. 14:9149-9158(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and structure of the human interleukin-5 gene."
      Tanabe T., Konishi M., Mizuta T., Noma T., Honjo T.
      J. Biol. Chem. 262:16580-16584(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning, nucleotide sequence, and expression of the gene encoding human eosinophil differentiation factor (interleukin 5)."
      Campbell H.D., Tucker W.Q.J., Hort Y., Martinson M.E., Mayo G., Clutterbuck E.J., Sanderson C.J., Young I.G.
      Proc. Natl. Acad. Sci. U.S.A. 84:6629-6633(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Isolation and characterization of lymphokine cDNA clones encoding mouse and human IgA-enhancing factor and eosinophil colony-stimulating factor activities: relationship to interleukin 5."
      Yokota T., Coffman R.L., Hagiwara H., Rennick D.M., Takebe Y., Yokota K., Gemmell L., Shrader B., Yang G., Meyerson P., Luh J., Hoy P., Pene J., Briere F., Spits H., Banchereau J., de Vries J., Lee F.D., Arai N., Arai K.
      Proc. Natl. Acad. Sci. U.S.A. 84:7388-7392(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Honjo T., Takatsu K., Severinson E.
      Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    6. SeattleSNPs variation discovery resource
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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].
    8. "Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells."
      Minamitake Y., Kodama S., Katayama T., Adachi H., Tanaka S., Tsujimoto M.
      J. Biochem. 107:292-297(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-134, DISULFIDE BONDS, GLYCOSYLATION AT THR-22 AND ASN-47, LACK OF GLYCOSYLATION AT ASN-90.
    9. "Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein."
      Proudfoot A.E.I., Davies J.G., Turcatti G., Wingfield P.T.
      FEBS Lett. 283:61-64(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    10. "A novel dimer configuration revealed by the crystal structure at 2.4-A resolution of human interleukin-5."
      Milburn M.V., Hassell A.M., Lambert M.H., Jordan S.R., Proudfoot A.E.I., Graber P., Wells T.N.C.
      Nature 363:172-176(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.
    11. "Structure analysis of the IL-5 ligand-receptor complex reveals a wrench-like architecture for IL-5Ralpha."
      Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W., Mueller T.D.
      Structure 19:1864-1875(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 19-134 IN COMPLEX WITH IL5RA, DISULFIDE BONDS.

    Entry informationi

    Entry nameiIL5_HUMAN
    AccessioniPrimary (citable) accession number: P05113
    Secondary accession number(s): Q13840
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 161 of the entry and version 1 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 5
      Human chromosome 5: 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