Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05113 (IL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IL5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer; disulfide-linked. Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Secreted.

Sequence similarities

Belongs to the IL-5 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory response

Traceable author statement Ref.3. Source: ProtInc

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of eosinophil differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of podosome assembly

Inferred from direct assay PubMed 15220135. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from direct assay PubMed 20041150. Source: BHF-UCL

extracellular space

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functioninterleukin-5 receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8
Chain20 – 134115Interleukin-5
PRO_0000015560

Sites

Site901Not glycosylated

Amino acid modifications

Glycosylation221O-linked (GalNAc...) Probable Ref.8
Glycosylation471N-linked (GlcNAc...) Probable
Disulfide bond63Interchain (with C-105) Ref.8 Ref.9 Ref.10 Ref.11
Disulfide bond105Interchain (with C-63) Ref.8 Ref.9 Ref.10 Ref.11

Experimental info

Sequence conflict881F → L in CAA31210. Ref.5

Secondary structure

.................. 134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05113 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: DC984467179556A3

FASTA13415,238
        10         20         30         40         50         60 
MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL RIPVPVHKNH 

        70         80         90        100        110        120 
QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG QKKKCGEERR RVNQFLDYLQ 

       130 
EFLGVMNTEW IIES 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA28477.
RefSeqNP_000870.1. NM_000879.2.
UniGeneHs.2247.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HULX-ray2.40A/B24-131[»]
3QT2X-ray2.55C/D/E/F19-134[»]
3VA2X-ray2.70A/B23-134[»]
ProteinModelPortalP05113.
SMRP05113. Positions 24-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109781. 3 interactions.
DIPDIP-28N.
IntActP05113. 2 interactions.
STRING9606.ENSP00000231454.

Chemistry

BindingDBP05113.
ChEMBLCHEMBL1169600.
DrugBankDB01411. Pranlukast.

Polymorphism databases

DMDM124341.

Proteomic databases

PaxDbP05113.
PeptideAtlasP05113.
PRIDEP05113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231454; ENSP00000231454; ENSG00000113525.
GeneID3567.
KEGGhsa:3567.
UCSCuc003kxe.1. human.

Organism-specific databases

CTD3567.
GeneCardsGC05M131881.
HGNCHGNC:6016. IL5.
HPACAB010304.
MIM147850. gene.
neXtProtNX_P05113.
PharmGKBPA29833.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41650.
HOGENOMHOG000074049.
HOVERGENHBG003865.
InParanoidP05113.
KOK05428.
OMAGVINTEW.
OrthoDBEOG70PC0S.
PhylomeDBP05113.
TreeFamTF338422.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP05113.

Gene expression databases

ArrayExpressP05113.
BgeeP05113.
CleanExHS_IL5.
GenevestigatorP05113.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000186. IL-5.
[Graphical view]
PANTHERPTHR10525. PTHR10525. 1 hit.
PfamPF02025. IL5. 1 hit.
[Graphical view]
PRINTSPR00432. INTERLEUKIN5.
ProDomPD006721. Interleukin_5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47266. SSF47266. 1 hit.
ProtoNetSearch...

Other

ChiTaRSIL5. human.
EvolutionaryTraceP05113.
GeneWikiInterleukin_5.
GenomeRNAi3567.
NextBio13932.
PROP05113.
SOURCESearch...

Entry information

Entry nameIL5_HUMAN
AccessionPrimary (citable) accession number: P05113
Secondary accession number(s): Q13840
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM