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P60568 (IL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-2

Short name=IL-2
Alternative name(s):
T-cell growth factor
Short name=TCGF
INN=Aldesleukin
Gene names
Name:IL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells.

Subcellular location

Secreted.

Involvement in disease

A chromosomal aberration involving IL2 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with involves TNFRSF17.

Pharmaceutical use

Available under the name Proleukin (Chiron). Used in patients with renal cell carcinoma or metastatic melanoma.

Sequence similarities

Belongs to the IL-2 family.

Sequence caution

The sequence AAA59140.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentSecreted
   Coding sequence diversityChromosomal rearrangement
   DiseaseProto-oncogene
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation

Traceable author statement PubMed 8476561. Source: UniProtKB

cell adhesion

Traceable author statement PubMed 10929056. Source: UniProtKB

cell-cell signaling

Traceable author statement PubMed 8476561. Source: UniProtKB

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement PubMed 2342538. Source: UniProtKB

natural killer cell activation

Traceable author statement PubMed 8476561. Source: UniProtKB

negative regulation of B cell apoptotic process

Inferred from direct assay PubMed 9184696. Source: MGI

negative regulation of apoptotic process

Traceable author statement PubMed 8476561. Source: UniProtKB

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of lymphocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from direct assay PubMed 9184696. Source: MGI

positive regulation of activated T cell proliferation

Inferred from direct assay PubMed 10072077PubMed 1830926. Source: MGI

positive regulation of cell growth

Traceable author statement PubMed 8476561. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement PubMed 8476561. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendritic spine development

Inferred from electronic annotation. Source: Ensembl

positive regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred by curator PubMed 16482511. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-17 production

Inferred from direct assay PubMed 16482511. Source: BHF-UCL

positive regulation of isotype switching to IgG isotypes

Inferred from electronic annotation. Source: Ensembl

positive regulation of regulatory T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of tissue remodeling

Inferred by curator PubMed 16482511. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 19088061. Source: BHF-UCL

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of T cell homeostatic proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.6. Source: UniProtKB

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: Ensembl

cytokine activity

Inferred from direct assay PubMed 10072077PubMed 1830926. Source: MGI

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

growth factor activity

Traceable author statement PubMed 8476561. Source: UniProtKB

interleukin-2 receptor binding

Traceable author statement PubMed 3925347. Source: UniProtKB

kinase activator activity

Traceable author statement PubMed 8476561. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.14
Chain21 – 153133Interleukin-2
PRO_0000015484

Amino acid modifications

Glycosylation231O-linked (GalNAc...) Ref.14 Ref.15
CAR_000051
Disulfide bond78 ↔ 125 Ref.14 Ref.22

Natural variations

Natural variant211Missing in FT-IL2-A and FT-IL2-B.
VAR_003967
Natural variant221Missing in FT-IL2-B.
VAR_003968

Secondary structure

........................ 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60568 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 59E2F40F25860F84

FASTA15317,628
        10         20         30         40         50         60 
MYRMQLLSCI ALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN YKNPKLTRML 

        70         80         90        100        110        120 
TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL RPRDLISNIN VIVLELKGSE 

       130        140        150 
TTFMCEYADE TATIVEFLNR WITFCQSIIS TLT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of interleukin 2 mRNAs from human tonsils."
Maeda S., Nishino N., Obaru K., Mita S., Nomiyama H., Shimada K., Fujimoto K., Teranishi T., Hirano T., Onoue K.
Biochem. Biophys. Res. Commun. 115:1040-1047(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and expression of a cloned cDNA for human interleukin-2."
Taniguchi T., Matsui H., Fujita T., Takaoka C., Kashima N., Yoshimoto R., Hamuro J.
Nature 302:305-310(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Molecular cloning of human interleukin 2 cDNA and its expression in E. coli."
Devos R., Plaetinck G., Cheroutre H., Simons G., Degrave W., Tavernier J., Remaut E., Fiers W.
Nucleic Acids Res. 11:4307-4323(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure of the human interleukin 2 gene."
Fujita T., Takaoka C., Matsui H., Taniguchi T.
Proc. Natl. Acad. Sci. U.S.A. 80:7437-7441(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence of the 5' flanking region of the human interleukin 2 gene: homologies with adult T-cell leukemia virus."
Holbrook N.J., Lieber M., Crabtree G.R.
Nucleic Acids Res. 12:5005-5013(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"T-cell growth factor: complete nucleotide sequence and organization of the gene in normal and malignant cells."
Holbrook N.J., Smith K.A., Fornace A.J. Jr., Comeau C.M., Wiskocil R.L., Crabtree G.R.
Proc. Natl. Acad. Sci. U.S.A. 81:1634-1638(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Interleukin-2 transcripts in human and rodent brains: possible expression by astrocytes."
Eizenberg O., Faber-Elman A., Lotan M., Schwartz M.
J. Neurochem. 64:1928-1936(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]"Sequence of interleukin-2 isolated from human placental poly A+ RNA: possible role in maintenance of fetal allograft."
Chernicky C.L., Tan H., Burfeind P., Ilan J., Ilan J.
Mol. Reprod. Dev. 43:180-186(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[9]SeattleSNPs variation discovery resource
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"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].
Tissue: Blood.
[11]"Organization of the DNA regions flanking the human interleukin 2 gene."
Nishino N., Obaru K., Maeda S., Shimada K., Onoue K.
Biomed. Res. 6:197-205(1985)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
[12]"Promoter region of interleukin-2 gene undergoes chromatin structure changes and confers inducibility on chloramphenicol acetyltransferase gene during activation of T cells."
Siebenlist U., Durand D.B., Bressler P., Holbrook N.J., Norris C.A., Kamoun M., Kant J.A., Crabtree G.R.
Mol. Cell. Biol. 6:3042-3049(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
[13]"Structure-activity relationships of recombinant human interleukin 2."
Weir M.P., Chaplin M.A., Wallace D.M., Dykes C.W., Hobden A.N.
Biochemistry 27:6883-6892(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-153.
[14]"Amino acid sequence and post-translational modification of human interleukin 2."
Robb R.J., Kutny R.M., Panico M., Morris H.R., Chowdhry V.
Proc. Natl. Acad. Sci. U.S.A. 81:6486-6490(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-153, DISULFIDE BOND, GLYCOSYLATION AT THR-23.
[15]"Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their location within the polypeptide."
Conradt H.S., Nimtz M., Dittmar K.E.J., Lindenmaier W., Hoppe J., Hauser H.
J. Biol. Chem. 264:17368-17373(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-23.
[16]"Three-dimensional structure of interleukin-2."
Brandhuber B.J., Boone T., Kenney W.C., McKay D.B.
Science 238:1707-1709(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[17]"Unraveling the structure of IL-2."
Bazan J.F.
Science 257:410-412(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPARISON OF X-RAY STRUCTURES.
[18]McKay D.B.
Science 257:412-413(1992)
Cited for: RESPONSE TO PUBMED:1631562.
[19]"Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments."
Mott H.R., Driscoll P.C., Boyd J., Cooke R.M., Weir M.P., Campbell I.D.
Biochemistry 31:7741-7744(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[20]"The interleukin-2 and interleukin-4 receptors studied by molecular modelling."
Bamborough P., Hedgecock C.J., Richards W.G.
Structure 2:839-851(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[21]"Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors."
Wang X., Rickert M., Garcia K.C.
Science 310:1159-1163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA; IL2RB AND IL2RC.
[22]"Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor."
Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.
Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA; IL2RB AND IL2RC, DISULFIDE BOND.
+Additional computationally mapped references.

Web resources

R&D Systems' cytokine source book: IL-2
Wikipedia

Interleukin-2 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00695 Genomic DNA. Translation: CAA25292.1.
V00564 mRNA. Translation: CAA23827.1.
X01586 mRNA. Translation: CAA25742.1.
J00264 Genomic DNA. Translation: AAD48509.1.
K02056 Genomic DNA. Translation: AAA98792.1.
S77834 mRNA. Translation: AAD14263.2.
S82692 mRNA. Translation: AAB46883.1.
AF359939 Genomic DNA. Translation: AAK26665.1.
BC066255 mRNA. Translation: AAH66255.1.
BC066257 mRNA. Translation: AAH66257.1.
BC070338 mRNA. Translation: AAH70338.1.
M33199 Genomic DNA. Translation: AAA59139.1.
M13879 Genomic DNA. Translation: AAA59141.1.
M22005 Genomic DNA. Translation: AAA59140.1. Different initiation.
CCDSCCDS3726.1.
PIRICHU2. A01849.
RefSeqNP_000577.2. NM_000586.3.
UniGeneHs.89679.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILMmodel-226-153[»]
1ILNmodel-226-153[»]
1IRLNMR-A21-153[»]
1M47X-ray1.99A21-153[»]
1M48X-ray1.95A/B21-153[»]
1M49X-ray2.00A/B21-153[»]
1M4AX-ray2.18A21-153[»]
1M4BX-ray2.15A21-153[»]
1M4CX-ray2.40A/B21-153[»]
1NBPX-ray2.20A21-153[»]
1PW6X-ray2.60A/B21-153[»]
1PY2X-ray2.80A/B/C/D21-152[»]
1QVNX-ray2.70A/B/C/D21-152[»]
1Z92X-ray2.80A21-153[»]
2B5IX-ray2.30A21-153[»]
2ERJX-ray3.00D/H21-153[»]
3INKX-ray2.50C/D21-153[»]
3QAZX-ray3.80A/D/G/J/M/P/S/V/Y/b/e/h21-153[»]
3QB1X-ray3.10A/B/C/D/E/F/G/H21-153[»]
ProteinModelPortalP60568.
SMRP60568. Positions 25-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109773. 2 interactions.
DIPDIP-475N.
MINTMINT-1522299.
STRING9606.ENSP00000226730.

Chemistry

ChEMBLCHEMBL5880.

PTM databases

PhosphoSiteP60568.
UniCarbKBP60568.

Polymorphism databases

DMDM45593462.

Proteomic databases

PaxDbP60568.
PRIDEP60568.

Protocols and materials databases

DNASU3558.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226730; ENSP00000226730; ENSG00000109471.
GeneID3558.
KEGGhsa:3558.
UCSCuc003ier.3. human.

Organism-specific databases

CTD3558.
GeneCardsGC04M123372.
HGNCHGNC:6001. IL2.
HPACAB010310.
MIM147680. gene.
neXtProtNX_P60568.
PharmGKBPA195.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41211.
HOVERGENHBG007496.
InParanoidP60568.
KOK05429.
OMAYEVIANT.
OrthoDBEOG72RN13.
PhylomeDBP60568.
TreeFamTF338200.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP60568.

Gene expression databases

ArrayExpressP60568.
BgeeP60568.
CleanExHS_IL2.
GenevestigatorP60568.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000779. IL-2.
[Graphical view]
PANTHERPTHR11443. PTHR11443. 1 hit.
PfamPF00715. IL2. 1 hit.
[Graphical view]
PRINTSPR00265. INTERLEUKIN2.
ProDomPD003649. Interleukin-2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00189. IL2. 1 hit.
[Graphical view]
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00424. INTERLEUKIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL2. human.
EvolutionaryTraceP60568.
GeneWikiInterleukin_2.
GenomeRNAi3558.
NextBio13896.
PROP60568.
SOURCESearch...

Entry information

Entry nameIL2_HUMAN
AccessionPrimary (citable) accession number: P60568
Secondary accession number(s): P01585
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 126 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 entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM