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Protein

Interleukin-4

Gene

IL4

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

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. cytokine activity Source: GO_Central
  2. growth factor activity Source: UniProtKB
  3. interleukin-4 receptor binding Source: UniProtKB

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Ischemic stroke1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:601367

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

BgeeiP05112.
CleanExiHS_IL4.
ExpressionAtlasiP05112. baseline and differential.
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 – 294Combined sources
Helixi30 – 4112Combined sources
Helixi48 – 503Combined sources
Beta strandi51 – 544Combined sources
Helixi56 – 583Combined sources
Turni60 – 623Combined sources
Helixi65 – 8319Combined sources
Turni87 – 893Combined sources
Helixi94 – 11825Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 15119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000013108.
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

        10         20         30         40         50
MGLTSQLLPP LFFLLACAGN FVHGHKCDIT LQEIIKTLNS LTEQKTLCTE
60 70 80 90 100
LTVTDIFAAS KNTTEKETFC RAATVLRQFY SHHEKDTRCL GATAQQFHRH
110 120 130 140 150
KQLIRFLKRL DRNLWGLAGL NSCPVKEANQ STLENFLERL KTIMREKYSK

CSS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Polymorphism databases

DMDMi124337.

Proteomic databases

PaxDbiP05112.
PRIDEiP05112.

Protocols and materials databases

DNASUi3565.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3565.
GeneCardsiGC05P132009.
H-InvDBHIX0164435.
HGNCiHGNC:6014. IL4.
MIMi147780. gene.
601367. phenotype.
neXtProtiNX_P05112.
PharmGKBiPA197.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266404.
GeneTreeiENSGT00390000013108.
HOGENOMiHOG000254781.
HOVERGENiHBG000290.
InParanoidiP05112.
KOiK05430.
OMAiKEKYSKC.
OrthoDBiEOG7SJD75.
PhylomeDBiP05112.
TreeFamiTF336383.

Enzyme and pathway databases

SignaLinkiP05112.

Miscellaneous databases

EvolutionaryTraceiP05112.
GeneWikiiInterleukin_4.
GenomeRNAii3565.
NextBioi13920.
PROiP05112.
SOURCEiSearch...

Gene expression databases

BgeeiP05112.
CleanExiHS_IL4.
ExpressionAtlasiP05112. baseline and differential.
GenevestigatoriP05112.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.