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Protein

Interleukin-2

Gene

IL2

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

Functioni

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.

GO - Molecular functioni

  • carbohydrate binding Source: Ensembl
  • cytokine activity Source: MGI
  • glycosphingolipid binding Source: Ensembl
  • growth factor activity Source: UniProtKB
  • interleukin-2 receptor binding Source: UniProtKB
  • kinase activator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
REACT_27283. Interleukin-2 signaling.
SignaLinkiP60568.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-2
Short name:
IL-2
Alternative name(s):
T-cell growth factor
Short name:
TCGF
INN: Aldesleukin
Gene namesi
Name:IL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6001. IL2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GOC
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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 usei

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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA195.

Chemistry

DrugBankiDB00852. Pseudoephedrine.

Polymorphism and mutation databases

BioMutaiIL2.
DMDMi45593462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 153133Interleukin-2PRO_0000015484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231O-linked (GalNAc...)2 PublicationsCAR_000051
Disulfide bondi78 ↔ 1252 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP60568.
PRIDEiP60568.

PTM databases

PhosphoSiteiP60568.
UniCarbKBiP60568.

Expressioni

Gene expression databases

BgeeiP60568.
CleanExiHS_IL2.
ExpressionAtlasiP60568. baseline and differential.
GenevisibleiP60568. HS.

Organism-specific databases

HPAiCAB010310.

Interactioni

Protein-protein interaction databases

BioGridi109773. 3 interactions.
DIPiDIP-475N.
MINTiMINT-1522299.
STRINGi9606.ENSP00000226730.

Structurei

Secondary structure

1
153
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 4925Combined sources
Helixi53 – 597Combined sources
Helixi60 – 623Combined sources
Beta strandi64 – 685Combined sources
Helixi73 – 764Combined sources
Helixi77 – 9317Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 1003Combined sources
Helixi105 – 11713Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi127 – 1326Combined sources
Helixi134 – 14916Combined sources
Turni150 – 1523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4NEJX-ray1.92A24-153[»]
4NEMX-ray1.93A24-153[»]
ProteinModelPortaliP60568.
SMRiP60568. Positions 25-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60568.

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41211.
GeneTreeiENSGT00390000003555.
HOVERGENiHBG007496.
InParanoidiP60568.
KOiK05429.
OMAiLMSNINV.
OrthoDBiEOG72RN13.
PhylomeDBiP60568.
TreeFamiTF338200.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000779. IL-2.
IPR030477. IL-2_CS.
[Graphical view]
PANTHERiPTHR11443. PTHR11443. 1 hit.
PfamiPF00715. IL2. 1 hit.
[Graphical view]
PRINTSiPR00265. INTERLEUKIN2.
ProDomiPD003649. Interleukin-2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00189. IL2. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00424. INTERLEUKIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRMQLLSCI ALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN
60 70 80 90 100
YKNPKLTRML TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL
110 120 130 140 150
RPRDLISNIN VIVLELKGSE TTFMCEYADE TATIVEFLNR WITFCQSIIS

TLT
Length:153
Mass (Da):17,628
Last modified:July 21, 1986 - v1
Checksum:i59E2F40F25860F84
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211Missing in FT-IL2-A and FT-IL2-B.
VAR_003967
Natural varianti22 – 221Missing in FT-IL2-B.
VAR_003968

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3726.1.
PIRiA01849. ICHU2.
RefSeqiNP_000577.2. NM_000586.3.
UniGeneiHs.89679.

Genome annotation databases

EnsembliENST00000226730; ENSP00000226730; ENSG00000109471.
GeneIDi3558.
KEGGihsa:3558.
UCSCiuc003ier.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

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

Interleukin-2 entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3726.1.
PIRiA01849. ICHU2.
RefSeqiNP_000577.2. NM_000586.3.
UniGeneiHs.89679.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4NEJX-ray1.92A24-153[»]
4NEMX-ray1.93A24-153[»]
ProteinModelPortaliP60568.
SMRiP60568. Positions 25-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109773. 3 interactions.
DIPiDIP-475N.
MINTiMINT-1522299.
STRINGi9606.ENSP00000226730.

Chemistry

BindingDBiP60568.
ChEMBLiCHEMBL5880.
DrugBankiDB00852. Pseudoephedrine.

PTM databases

PhosphoSiteiP60568.
UniCarbKBiP60568.

Polymorphism and mutation databases

BioMutaiIL2.
DMDMi45593462.

Proteomic databases

PaxDbiP60568.
PRIDEiP60568.

Protocols and materials databases

DNASUi3558.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226730; ENSP00000226730; ENSG00000109471.
GeneIDi3558.
KEGGihsa:3558.
UCSCiuc003ier.3. human.

Organism-specific databases

CTDi3558.
GeneCardsiGC04M123372.
HGNCiHGNC:6001. IL2.
HPAiCAB010310.
MIMi147680. gene.
neXtProtiNX_P60568.
PharmGKBiPA195.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41211.
GeneTreeiENSGT00390000003555.
HOVERGENiHBG007496.
InParanoidiP60568.
KOiK05429.
OMAiLMSNINV.
OrthoDBiEOG72RN13.
PhylomeDBiP60568.
TreeFamiTF338200.

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
REACT_27283. Interleukin-2 signaling.
SignaLinkiP60568.

Miscellaneous databases

ChiTaRSiIL2. human.
EvolutionaryTraceiP60568.
GeneWikiiInterleukin_2.
GenomeRNAii3558.
NextBioi13896.
PROiP60568.
SOURCEiSearch...

Gene expression databases

BgeeiP60568.
CleanExiHS_IL2.
ExpressionAtlasiP60568. baseline and differential.
GenevisibleiP60568. HS.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000779. IL-2.
IPR030477. IL-2_CS.
[Graphical view]
PANTHERiPTHR11443. PTHR11443. 1 hit.
PfamiPF00715. IL2. 1 hit.
[Graphical view]
PRINTSiPR00265. INTERLEUKIN2.
ProDomiPD003649. Interleukin-2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00189. IL2. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00424. INTERLEUKIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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.

Entry informationi

Entry nameiIL2_HUMAN
AccessioniPrimary (citable) accession number: P60568
Secondary accession number(s): P01585
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 137 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, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.