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P05113

- IL5_HUMAN

UniProt

P05113 - IL5_HUMAN

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Protein

Interleukin-5

Gene
IL5
Organism
Homo sapiens (Human)
Status
Reviewed - 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
  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
Complete GO annotation...

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
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...) Inferred1 Publication
Glycosylationi47 – 471N-linked (GlcNAc...) Inferred
Disulfide bondi63 – 63Interchain (with C-105)4 Publications
Disulfide bondi105 – 105Interchain (with C-63)4 Publications

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.

Miscellaneous databases

EvolutionaryTraceiP05113.

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-5 family.

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

Sequence conflict

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

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

« 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(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: September 3, 2014
This is version 160 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

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