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Protein

Interleukin-5

Gene

IL5

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

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

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
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_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 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6016. IL5.

Subcellular locationi

GO - Cellular componenti

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

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

BgeeiP05113.
CleanExiHS_IL5.
ExpressionAtlasiP05113. baseline and differential.
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 – 3914Combined sources
Helixi41 – 455Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 583Combined sources
Helixi60 – 623Combined sources
Helixi64 – 7512Combined sources
Helixi84 – 10320Combined sources
Beta strandi106 – 1116Combined sources
Helixi112 – 12817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HULX-ray2.40A/B24-131[»]
3QT2X-ray2.55C/D/E/F19-134[»]
3VA2X-ray2.70A/B23-134[»]
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.
GeneTreeiENSGT00390000016991.
HOGENOMiHOG000074049.
HOVERGENiHBG003865.
InParanoidiP05113.
KOiK05428.
OMAiGVINTEW.
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

        10         20         30         40         50
MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL
60 70 80 90 100
RIPVPVHKNH QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG
110 120 130
QKKKCGEERR RVNQFLDYLQ EFLGVMNTEW IIES
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 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP05113.
ChEMBLiCHEMBL1169600.
DrugBankiDB01411. Pranlukast.

Polymorphism databases

DMDMi124341.

Proteomic databases

PaxDbiP05113.
PeptideAtlasiP05113.
PRIDEiP05113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3567.
GeneCardsiGC05M131881.
HGNCiHGNC:6016. IL5.
HPAiCAB010304.
MIMi147850. gene.
neXtProtiNX_P05113.
PharmGKBiPA29833.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41650.
GeneTreeiENSGT00390000016991.
HOGENOMiHOG000074049.
HOVERGENiHBG003865.
InParanoidiP05113.
KOiK05428.
OMAiGVINTEW.
OrthoDBiEOG70PC0S.
PhylomeDBiP05113.
TreeFamiTF338422.

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinkiP05113.

Miscellaneous databases

ChiTaRSiIL5. human.
EvolutionaryTraceiP05113.
GeneWikiiInterleukin_5.
GenomeRNAii3567.
NextBioi13932.
PROiP05113.
SOURCEiSearch...

Gene expression databases

BgeeiP05113.
CleanExiHS_IL5.
ExpressionAtlasiP05113. baseline and differential.
GenevestigatoriP05113.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1985) [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(1986) [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(1986) [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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Honjo T., Takatsu K., Severinson E.
    Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  6. SeattleSNPs variation discovery resource
    Submitted (JAN-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(2003) [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(1989) [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(1990) [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(1992) [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(2010) [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: April 1, 2015
This is version 165 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

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.