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P05112

- IL4_HUMAN

UniProt

P05112 - IL4_HUMAN

Protein

Interleukin-4

Gene

IL4

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

    Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes.

    GO - Molecular functioni

    1. growth factor activity Source: UniProtKB
    2. interleukin-4 receptor binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. B cell costimulation Source: Ensembl
    2. B cell differentiation Source: UniProtKB
    3. cellular defense response Source: ProtInc
    4. cellular response to mercury ion Source: Ensembl
    5. chemotaxis Source: ProtInc
    6. cholesterol metabolic process Source: UniProtKB
    7. connective tissue growth factor biosynthetic process Source: UniProtKB
    8. defense response to protozoan Source: Ensembl
    9. dendritic cell differentiation Source: DFLAT
    10. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    11. female pregnancy Source: Ensembl
    12. immune response Source: ProtInc
    13. innate immune response in mucosa Source: Ensembl
    14. negative regulation of acute inflammatory response Source: Ensembl
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of chronic inflammatory response Source: Ensembl
    17. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    18. negative regulation of macrophage activation Source: Ensembl
    19. negative regulation of nitric oxide biosynthetic process Source: Ensembl
    20. negative regulation of osteoclast differentiation Source: UniProtKB
    21. negative regulation of T-helper 17 cell differentiation Source: Ensembl
    22. negative regulation of transcription, DNA-templated Source: UniProtKB
    23. positive regulation of activated T cell proliferation Source: Ensembl
    24. positive regulation of B cell proliferation Source: UniProtKB
    25. positive regulation of chemokine biosynthetic process Source: Ensembl
    26. positive regulation of interleukin-10 production Source: Ensembl
    27. positive regulation of interleukin-13 production Source: UniProtKB
    28. positive regulation of isotype switching to IgE isotypes Source: UniProtKB
    29. positive regulation of isotype switching to IgG isotypes Source: UniProtKB
    30. positive regulation of MHC class II biosynthetic process Source: UniProtKB
    31. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    32. positive regulation of T cell differentiation Source: UniProtKB
    33. positive regulation of T cell proliferation Source: UniProtKB
    34. positive regulation of transcription, DNA-templated Source: UniProtKB
    35. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    36. positive regulation of tyrosine phosphorylation of Stat5 protein Source: Ensembl
    37. regulation of immune response Source: UniProtKB
    38. regulation of isotype switching Source: UniProtKB
    39. regulation of phosphorylation Source: UniProtKB
    40. regulation of proton transport Source: Ensembl
    41. response to cytokine Source: Ensembl
    42. response to drug Source: Ensembl
    43. response to ethanol Source: Ensembl
    44. response to nutrient Source: Ensembl
    45. response to organic cyclic compound Source: Ensembl
    46. T-helper 1 cell lineage commitment Source: Ensembl
    47. T-helper 2 cell cytokine production Source: UniProtKB
    48. T-helper 2 cell differentiation Source: Ensembl
    49. type 2 immune response Source: UniProtKB

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Keywords - Biological processi

    B-cell activation

    Enzyme and pathway databases

    SignaLinkiP05112.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-4
    Short name:
    IL-4
    Alternative name(s):
    B-cell stimulatory factor 1
    Short name:
    BSF-1
    Binetrakin
    Lymphocyte stimulatory factor 1
    Pitrakinra
    Gene namesi
    Name:IL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6014. IL4.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi601367. phenotype.
    PharmGKBiPA197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 153129Interleukin-4PRO_0000015532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 1511 Publication
    Disulfide bondi48 ↔ 891 Publication
    Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
    Disulfide bondi70 ↔ 123

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP05112.
    PRIDEiP05112.

    Expressioni

    Gene expression databases

    ArrayExpressiP05112.
    BgeeiP05112.
    CleanExiHS_IL4.
    GenevestigatoriP05112.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IL13RA1P785523EBI-367025,EBI-1391535
    IL4RP243947EBI-367025,EBI-367009

    Protein-protein interaction databases

    BioGridi109779. 4 interactions.
    DIPiDIP-3222N.
    IntActiP05112. 3 interactions.
    MINTiMINT-90320.
    STRINGi9606.ENSP00000231449.

    Structurei

    Secondary structure

    1
    153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni26 – 294
    Helixi30 – 4112
    Helixi48 – 503
    Beta strandi51 – 544
    Helixi56 – 583
    Turni60 – 623
    Helixi65 – 8319
    Turni87 – 893
    Helixi94 – 11825
    Beta strandi130 – 1323
    Helixi133 – 15119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BBNNMR-A25-153[»]
    1BCNNMR-A25-153[»]
    1CYLNMR-A25-153[»]
    1HIJX-ray3.00A25-153[»]
    1HIKX-ray2.60A25-153[»]
    1HZIX-ray2.05A25-153[»]
    1IARX-ray2.30A25-153[»]
    1ILLmodel-425-153[»]
    1ITEmodel-A25-153[»]
    1ITINMR-A25-153[»]
    1ITLNMR-A25-153[»]
    1ITMNMR-A25-153[»]
    1RCBX-ray2.25A25-153[»]
    2B8UX-ray1.80A25-153[»]
    2B8XX-ray1.70A25-153[»]
    2B8YX-ray1.80A25-153[»]
    2B8ZX-ray2.50A25-153[»]
    2B90X-ray2.10A25-153[»]
    2B91X-ray2.00A25-153[»]
    2CYKNMR-A25-153[»]
    2D48X-ray1.65A25-153[»]
    2INTX-ray2.35A25-153[»]
    3BPLX-ray2.93A25-153[»]
    3BPNX-ray3.02A25-153[»]
    3QB7X-ray3.24A/B25-153[»]
    ProteinModelPortaliP05112.
    SMRiP05112. Positions 25-153.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05112.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the IL-4/IL-13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG266404.
    HOGENOMiHOG000254781.
    HOVERGENiHBG000290.
    InParanoidiP05112.
    KOiK05430.
    OMAiKEKYSKC.
    OrthoDBiEOG7SJD75.
    PhylomeDBiP05112.
    TreeFamiTF336383.

    Family and domain databases

    Gene3Di1.20.1250.10. 1 hit.
    InterProiIPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR002354. IL-4.
    IPR001325. IL-4/IL-13.
    IPR018096. IL-4/IL-13_CS.
    [Graphical view]
    PANTHERiPTHR11456. PTHR11456. 1 hit.
    PfamiPF00727. IL4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001941. Interleukin_4. 1 hit.
    PRINTSiPR00431. INTERLEUKIN4.
    SMARTiSM00190. IL4_13. 1 hit.
    [Graphical view]
    SUPFAMiSSF47266. SSF47266. 1 hit.
    PROSITEiPS00838. INTERLEUKIN_4_13. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05112-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGLTSQLLPP LFFLLACAGN FVHGHKCDIT LQEIIKTLNS LTEQKTLCTE    50
    LTVTDIFAAS KNTTEKETFC RAATVLRQFY SHHEKDTRCL GATAQQFHRH 100
    KQLIRFLKRL DRNLWGLAGL NSCPVKEANQ STLENFLERL KTIMREKYSK 150
    CSS 153
    Length:153
    Mass (Da):17,492
    Last modified:August 13, 1987 - v1
    Checksum:i8725BF64B34D45F7
    GO
    Isoform 2 (identifier: P05112-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, IL-4delta2

    The sequence of this isoform differs from the canonical sequence as follows:
         46-61: Missing.

    Show »
    Length:137
    Mass (Da):15,797
    Checksum:i3B621F60D0F0D261
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271C → R.
    Corresponds to variant rs4986964 [ dbSNP | Ensembl ].
    VAR_020392

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei46 – 6116Missing in isoform 2. 1 PublicationVSP_002672Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13982 mRNA. Translation: AAA59149.1.
    M23442 Genomic DNA. Translation: AAA59150.1.
    X81851 mRNA. Translation: CAA57444.1.
    AF395008 Genomic DNA. Translation: AAK71324.1.
    BC066277 mRNA. Translation: AAH66277.1.
    BC067514 mRNA. Translation: AAH67514.1.
    BC070123 mRNA. Translation: AAH70123.1.
    X06750 Genomic DNA. Translation: CAA29925.1.
    CCDSiCCDS4158.1. [P05112-1]
    CCDS4159.1. [P05112-2]
    PIRiA30546. A25946.
    RefSeqiNP_000580.1. NM_000589.3. [P05112-1]
    NP_758858.1. NM_172348.2. [P05112-2]
    UniGeneiHs.73917.

    Genome annotation databases

    EnsembliENST00000231449; ENSP00000231449; ENSG00000113520. [P05112-1]
    ENST00000350025; ENSP00000325190; ENSG00000113520. [P05112-2]
    GeneIDi3565.
    KEGGihsa:3565.
    UCSCiuc003kxk.2. human. [P05112-1]

    Polymorphism databases

    DMDMi124337.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13982 mRNA. Translation: AAA59149.1 .
    M23442 Genomic DNA. Translation: AAA59150.1 .
    X81851 mRNA. Translation: CAA57444.1 .
    AF395008 Genomic DNA. Translation: AAK71324.1 .
    BC066277 mRNA. Translation: AAH66277.1 .
    BC067514 mRNA. Translation: AAH67514.1 .
    BC070123 mRNA. Translation: AAH70123.1 .
    X06750 Genomic DNA. Translation: CAA29925.1 .
    CCDSi CCDS4158.1. [P05112-1 ]
    CCDS4159.1. [P05112-2 ]
    PIRi A30546. A25946.
    RefSeqi NP_000580.1. NM_000589.3. [P05112-1 ]
    NP_758858.1. NM_172348.2. [P05112-2 ]
    UniGenei Hs.73917.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BBN NMR - A 25-153 [» ]
    1BCN NMR - A 25-153 [» ]
    1CYL NMR - A 25-153 [» ]
    1HIJ X-ray 3.00 A 25-153 [» ]
    1HIK X-ray 2.60 A 25-153 [» ]
    1HZI X-ray 2.05 A 25-153 [» ]
    1IAR X-ray 2.30 A 25-153 [» ]
    1ILL model - 4 25-153 [» ]
    1ITE model - A 25-153 [» ]
    1ITI NMR - A 25-153 [» ]
    1ITL NMR - A 25-153 [» ]
    1ITM NMR - A 25-153 [» ]
    1RCB X-ray 2.25 A 25-153 [» ]
    2B8U X-ray 1.80 A 25-153 [» ]
    2B8X X-ray 1.70 A 25-153 [» ]
    2B8Y X-ray 1.80 A 25-153 [» ]
    2B8Z X-ray 2.50 A 25-153 [» ]
    2B90 X-ray 2.10 A 25-153 [» ]
    2B91 X-ray 2.00 A 25-153 [» ]
    2CYK NMR - A 25-153 [» ]
    2D48 X-ray 1.65 A 25-153 [» ]
    2INT X-ray 2.35 A 25-153 [» ]
    3BPL X-ray 2.93 A 25-153 [» ]
    3BPN X-ray 3.02 A 25-153 [» ]
    3QB7 X-ray 3.24 A/B 25-153 [» ]
    ProteinModelPortali P05112.
    SMRi P05112. Positions 25-153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109779. 4 interactions.
    DIPi DIP-3222N.
    IntActi P05112. 3 interactions.
    MINTi MINT-90320.
    STRINGi 9606.ENSP00000231449.

    Polymorphism databases

    DMDMi 124337.

    Proteomic databases

    PaxDbi P05112.
    PRIDEi P05112.

    Protocols and materials databases

    DNASUi 3565.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231449 ; ENSP00000231449 ; ENSG00000113520 . [P05112-1 ]
    ENST00000350025 ; ENSP00000325190 ; ENSG00000113520 . [P05112-2 ]
    GeneIDi 3565.
    KEGGi hsa:3565.
    UCSCi uc003kxk.2. human. [P05112-1 ]

    Organism-specific databases

    CTDi 3565.
    GeneCardsi GC05P132009.
    H-InvDB HIX0164435.
    HGNCi HGNC:6014. IL4.
    MIMi 147780. gene.
    601367. phenotype.
    neXtProti NX_P05112.
    PharmGKBi PA197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266404.
    HOGENOMi HOG000254781.
    HOVERGENi HBG000290.
    InParanoidi P05112.
    KOi K05430.
    OMAi KEKYSKC.
    OrthoDBi EOG7SJD75.
    PhylomeDBi P05112.
    TreeFami TF336383.

    Enzyme and pathway databases

    SignaLinki P05112.

    Miscellaneous databases

    EvolutionaryTracei P05112.
    GeneWikii Interleukin_4.
    GenomeRNAii 3565.
    NextBioi 13920.
    PROi P05112.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05112.
    Bgeei P05112.
    CleanExi HS_IL4.
    Genevestigatori P05112.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR002354. IL-4.
    IPR001325. IL-4/IL-13.
    IPR018096. IL-4/IL-13_CS.
    [Graphical view ]
    PANTHERi PTHR11456. PTHR11456. 1 hit.
    Pfami PF00727. IL4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001941. Interleukin_4. 1 hit.
    PRINTSi PR00431. INTERLEUKIN4.
    SMARTi SM00190. IL4_13. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47266. SSF47266. 1 hit.
    PROSITEi PS00838. INTERLEUKIN_4_13. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a human interleukin cDNA clone, homologous to mouse B-cell stimulatory factor 1, that expresses B-cell- and T-cell-stimulating activities."
      Yokota T., Otsuka T., Mosmann T., Banchereau J., Defrance T., Blanchard D., de Vries J.E., Lee F., Arai K.
      Proc. Natl. Acad. Sci. U.S.A. 83:5894-5898(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete nucleotide sequence of the chromosomal gene for human IL-4 and its expression."
      Arai N., Nomura D., Villaret D., Malefijt R.D., Seiki M., Yoshida M., Minoshima S., Fukuyama R., Maekawa M., Kudoh J., Shimizu N., Yokota K., Abe E., Yokota T., Takebe Y., Arai K.
      J. Immunol. 142:274-282(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "An alternatively spliced interleukin 4 form in lymphoid cells."
      Klein S.C., Golverdingen J., Bouwens A.G.M., Tilanus M.G.J.
      Immunogenetics 41:57-57(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Blood.
    6. "The 5' region of the human interleukin 4 gene: structure and potential regulatory elements."
      Eder A., Krafft-Czepa H., Krammer P.H.
      Nucleic Acids Res. 16:772-772(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
    7. "Disulfide assignments in recombinant mouse and human interleukin 4."
      Carr C., Aykent S., Kimack N.M., Levine A.D.
      Biochemistry 30:1515-1523(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-62, DISULFIDE BONDS.
    8. "Crystal structure of recombinant human interleukin-4."
      Walter M.R., Cook W.J., Zhao B.G., Cameron R.P. Jr., Ealick S.E., Walter R.L. Jr., Reichert P., Nagabhushan T.L., Trotta P.P., Bugg C.E.
      J. Biol. Chem. 267:20371-20376(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    9. "Crystal structure of human recombinant interleukin-4 at 2.25-A resolution."
      Wlodaver A., Pavlovsky A., Gustchina A.
      FEBS Lett. 309:59-64(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    10. "Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface."
      Hage T., Sebald W., Reinemer P.
      Cell 97:271-281(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-153 IN COMPLEX WITH IL4RALPHA.
    11. "Secondary structure and topology of human interleukin 4 in solution."
      Redfield C., Smith L.J., Boyd J., Lawrence G.M.P., Edwards R.G., Smith R.A.G., Dobson C.M.
      Biochemistry 30:11029-11035(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    12. "Human interleukin 4. The solution structure of a four-helix bundle protein."
      Smith L.J., Redfield C., Boyd J., Lawrence G.M.P., Edwards R.G., Smith R.A.G., Dobson C.M.
      J. Mol. Biol. 224:899-904(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    13. "1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy."
      Powers R., Garret D.S., March C.J., Frieden E.A., Gronenborn A.M., Clore G.M.
      Biochemistry 31:4334-4346(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    14. "Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy."
      Garret D.S., Powers R., March C.J., Frieden E.A., Clore G.M., Gronenborn A.M.
      Biochemistry 31:4347-4353(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    15. "Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy."
      Powers R., Garret D.S., March C.J., Frieden E.A., Gronenborn A.M., Clore G.M.
      Science 256:1673-1677(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    16. "Experimental and theoretical studies of the three-dimensional structure of human interleukin-4."
      Curtis B.M., Presnell S.R., Srinivasan S., Sassenfeld H., Klinke R., Jeffery E., Cosman D., March C.J., Cohen F.E.
      Proteins 11:111-119(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS, 3D-STRUCTURE MODELING.
    17. "Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy."
      Mueller T., Dieckmann T., Sebald W., Oschkinat H.
      J. Mol. Biol. 237:423-436(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, STRUCTURE BY NMR.
    18. "Comparison of four independently determined structures of human recombinant interleukin-4."
      Smith L.J., Redfield C., Smith R.A.G., Dobson C.M., Clore G.M., Gronenborn A.M., Walter M.R., Naganbushan T.L., Wlodawer A.
      Nat. Struct. Biol. 1:301-310(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPARISON OF STRUCTURES.
    19. "Polymorphism in the P-selectin and interleukin-4 genes as determinants of stroke: a population-based, prospective genetic analysis."
      Zee R.Y.L., Cook N.R., Cheng S., Reynolds R., Erlich H.A., Lindpaintner K., Ridker P.M.
      Hum. Mol. Genet. 13:389-396(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.

    Entry informationi

    Entry nameiIL4_HUMAN
    AccessioniPrimary (citable) accession number: P05112
    Secondary accession number(s): Q14630, Q6NZ77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 177 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3