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Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)

 IL2_HUMAN               Reviewed;         153 AA.
P60568; P01585;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
02-JUN-2021, entry version 184.
RecName: Full=Interleukin-2;
Short=IL-2;
AltName: Full=T-cell growth factor;
Short=TCGF;
AltName: INN=Aldesleukin;
Flags: Precursor;
Name=IL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6312994; DOI=10.1016/s0006-291x(83)80040-0;
Maeda S., Nishino N., Obaru K., Mita S., Nomiyama H., Shimada K.,
Fujimoto K., Teranishi T., Hirano T., Onoue K.;
"Cloning of interleukin 2 mRNAs from human tonsils.";
Biochem. Biophys. Res. Commun. 115:1040-1047(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6403867; DOI=10.1038/302305a0;
Taniguchi T., Matsui H., Fujita T., Takaoka C., Kashima N., Yoshimoto R.,
Hamuro J.;
"Structure and expression of a cloned cDNA for human interleukin-2.";
Nature 302:305-310(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6306584; DOI=10.1093/nar/11.13.4307;
Devos R., Plaetinck G., Cheroutre H., Simons G., Degrave W., Tavernier J.,
Remaut E., Fiers W.;
"Molecular cloning of human interleukin 2 cDNA and its expression in E.
coli.";
Nucleic Acids Res. 11:4307-4323(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6324170; DOI=10.1073/pnas.80.24.7437;
Fujita T., Takaoka C., Matsui H., Taniguchi T.;
"Structure of the human interleukin 2 gene.";
Proc. Natl. Acad. Sci. U.S.A. 80:7437-7441(1983).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6330695; DOI=10.1093/nar/12.12.5005;
Holbrook N.J., Lieber M., Crabtree G.R.;
"DNA sequence of the 5' flanking region of the human interleukin 2 gene:
homologies with adult T-cell leukemia virus.";
Nucleic Acids Res. 12:5005-5013(1984).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6608729; DOI=10.1073/pnas.81.6.1634;
Holbrook N.J., Smith K.A., Fornace A.J. Jr., Comeau C.M., Wiskocil R.L.,
Crabtree G.R.;
"T-cell growth factor: complete nucleotide sequence and organization of the
gene in normal and malignant cells.";
Proc. Natl. Acad. Sci. U.S.A. 81:1634-1638(1984).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7722480; DOI=10.1046/j.1471-4159.1995.64051928.x;
Eizenberg O., Faber-Elman A., Lotan M., Schwartz M.;
"Interleukin-2 transcripts in human and rodent brains: possible expression
by astrocytes.";
J. Neurochem. 64:1928-1936(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8824916;
DOI=10.1002/(sici)1098-2795(199602)43:2<180::aid-mrd7>3.0.co;2-n;
Chernicky C.L., Tan H., Burfeind P., Ilan J., Ilan J.;
"Sequence of interleukin-2 isolated from human placental poly A+ RNA:
possible role in maintenance of fetal allograft.";
Mol. Reprod. Dev. 43:180-186(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
Nishino N., Obaru K., Maeda S., Shimada K., Onoue K.;
"Organization of the DNA regions flanking the human interleukin 2 gene.";
Biomed. Res. 6:197-205(1985).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
PubMed=3491296; DOI=10.1128/mcb.6.9.3042;
Siebenlist U., Durand D.B., Bressler P., Holbrook N.J., Norris C.A.,
Kamoun M., Kant J.A., Crabtree G.R.;
"Promoter region of interleukin-2 gene undergoes chromatin structure
changes and confers inducibility on chloramphenicol acetyltransferase gene
during activation of T cells.";
Mol. Cell. Biol. 6:3042-3049(1986).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-153.
PubMed=3264184; DOI=10.1021/bi00418a034;
Weir M.P., Chaplin M.A., Wallace D.M., Dykes C.W., Hobden A.N.;
"Structure-activity relationships of recombinant human interleukin 2.";
Biochemistry 27:6883-6892(1988).
[14]
PROTEIN SEQUENCE OF 21-153, DISULFIDE BOND, AND GLYCOSYLATION AT THR-23.
PubMed=6333684; DOI=10.1073/pnas.81.20.6486;
Robb R.J., Kutny R.M., Panico M., Morris H.R., Chowdhry V.;
"Amino acid sequence and post-translational modification of human
interleukin 2.";
Proc. Natl. Acad. Sci. U.S.A. 81:6486-6490(1984).
[15]
GLYCOSYLATION AT THR-23.
PubMed=2793860;
Conradt H.S., Nimtz M., Dittmar K.E.J., Lindenmaier W., Hoppe J.,
Hauser H.;
"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.";
J. Biol. Chem. 264:17368-17373(1989).
[16]
CHROMOSOMAL TRANSLOCATION WITH TNFRSF17.
PubMed=1396583; DOI=10.1002/j.1460-2075.1992.tb05482.x;
Laabi Y., Gras M.P., Carbonnel F., Brouet J.C., Berger R., Larsen C.-J.,
Tsapis A.;
"A new gene, BCM, on chromosome 16 is fused to the interleukin 2 gene by a
t(4;16)(q26;p13) translocation in a malignant T cell lymphoma.";
EMBO J. 11:3897-3904(1992).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3500515; DOI=10.1126/science.3500515;
Brandhuber B.J., Boone T., Kenney W.C., McKay D.B.;
"Three-dimensional structure of interleukin-2.";
Science 238:1707-1709(1987).
[18]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1631562; DOI=10.1126/science.1631562;
Bazan J.F.;
"Unraveling the structure of IL-2.";
Science 257:410-412(1992).
[19]
RESPONSE TO PUBMED:1631562.
McKay D.B.;
Science 257:412-413(1992).
[20]
STRUCTURE BY NMR.
PubMed=1510960; DOI=10.1021/bi00148a040;
Mott H.R., Driscoll P.C., Boyd J., Cooke R.M., Weir M.P., Campbell I.D.;
"Secondary structure of human interleukin 2 from 3D heteronuclear NMR
experiments.";
Biochemistry 31:7741-7744(1992).
[21]
3D-STRUCTURE MODELING.
PubMed=7529123; DOI=10.1016/s0969-2126(94)00085-9;
Bamborough P., Hedgecock C.J., Richards W.G.;
"The interleukin-2 and interleukin-4 receptors studied by molecular
modelling.";
Structure 2:839-851(1994).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
IL2RB AND IL2RC.
PubMed=16293754; DOI=10.1126/science.1117893;
Wang X., Rickert M., Garcia K.C.;
"Structure of the quaternary complex of interleukin-2 with its alpha, beta,
and gammac receptors.";
Science 310:1159-1163(2005).
[23]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
IL2RB AND IL2RC, AND DISULFIDE BOND.
PubMed=16477002; DOI=10.1073/pnas.0511161103;
Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
"Crystal structure of the IL-2 signaling complex: paradigm for a
heterotrimeric cytokine receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
-!- 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.
-!- INTERACTION:
P60568; P01589: IL2RA; NbExp=3; IntAct=EBI-12508717, EBI-8614302;
P60568; P14784: IL2RB; NbExp=5; IntAct=EBI-12508717, EBI-2866779;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:1396583}.
-!- PHARMACEUTICAL: Available under the name Proleukin (Chiron). Used in
patients with renal cell carcinoma or metastatic melanoma.
-!- SIMILARITY: Belongs to the IL-2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-2 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_2";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il2/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL2";
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EMBL; X00695; CAA25292.1; -; Genomic_DNA.
EMBL; V00564; CAA23827.1; -; mRNA.
EMBL; X01586; CAA25742.1; -; mRNA.
EMBL; J00264; AAD48509.1; -; Genomic_DNA.
EMBL; K02056; AAA98792.1; -; Genomic_DNA.
EMBL; S77834; AAD14263.2; -; mRNA.
EMBL; S82692; AAB46883.1; -; mRNA.
EMBL; AF359939; AAK26665.1; -; Genomic_DNA.
EMBL; BC066255; AAH66255.1; -; mRNA.
EMBL; BC066257; AAH66257.1; -; mRNA.
EMBL; BC070338; AAH70338.1; -; mRNA.
EMBL; M33199; AAA59139.1; -; Genomic_DNA.
EMBL; M13879; AAA59141.1; -; Genomic_DNA.
EMBL; M22005; AAA59140.1; ALT_INIT; Genomic_DNA.
CCDS; CCDS3726.1; -.
PIR; A01849; ICHU2.
RefSeq; NP_000577.2; NM_000586.3.
PDB; 1ILM; Model; -; 2=26-153.
PDB; 1ILN; Model; -; 2=26-153.
PDB; 1IRL; NMR; -; A=21-153.
PDB; 1M47; X-ray; 1.99 A; A=21-153.
PDB; 1M48; X-ray; 1.95 A; A/B=21-153.
PDB; 1M49; X-ray; 2.00 A; A/B=21-153.
PDB; 1M4A; X-ray; 2.18 A; A=21-153.
PDB; 1M4B; X-ray; 2.15 A; A=21-153.
PDB; 1M4C; X-ray; 2.40 A; A/B=21-153.
PDB; 1NBP; X-ray; 2.20 A; A=21-153.
PDB; 1PW6; X-ray; 2.60 A; A/B=21-153.
PDB; 1PY2; X-ray; 2.80 A; A/B/C/D=21-152.
PDB; 1QVN; X-ray; 2.70 A; A/B/C/D=21-152.
PDB; 1Z92; X-ray; 2.80 A; A=21-153.
PDB; 2B5I; X-ray; 2.30 A; A=21-153.
PDB; 2ERJ; X-ray; 3.00 A; D/H=21-153.
PDB; 3INK; X-ray; 2.50 A; C/D=21-153.
PDB; 3QAZ; X-ray; 3.80 A; A/D/G/J/M/P/S/V/Y/b/e/h=21-153.
PDB; 3QB1; X-ray; 3.10 A; A/B/C/D/E/F/G/H=21-153.
PDB; 4NEJ; X-ray; 1.92 A; A=24-153.
PDB; 4NEM; X-ray; 1.93 A; A=24-153.
PDB; 5LQB; X-ray; 1.95 A; A=22-153.
PDB; 5M5E; X-ray; 2.30 A; D=8-153.
PDB; 5UTZ; X-ray; 2.75 A; A/D/E/I=21-153.
PDB; 6LX3; EM; 3.15 A; A/B/C/D=1-21.
PDB; 6LXW; EM; 3.27 A; A/B/C/D=1-21.
PDB; 6VWU; X-ray; 3.40 A; A=10-21, A=90-94.
PDB; 6YE3; X-ray; 2.89 A; C/F/I=21-153.
PDBsum; 1ILM; -.
PDBsum; 1ILN; -.
PDBsum; 1IRL; -.
PDBsum; 1M47; -.
PDBsum; 1M48; -.
PDBsum; 1M49; -.
PDBsum; 1M4A; -.
PDBsum; 1M4B; -.
PDBsum; 1M4C; -.
PDBsum; 1NBP; -.
PDBsum; 1PW6; -.
PDBsum; 1PY2; -.
PDBsum; 1QVN; -.
PDBsum; 1Z92; -.
PDBsum; 2B5I; -.
PDBsum; 2ERJ; -.
PDBsum; 3INK; -.
PDBsum; 3QAZ; -.
PDBsum; 3QB1; -.
PDBsum; 4NEJ; -.
PDBsum; 4NEM; -.
PDBsum; 5LQB; -.
PDBsum; 5M5E; -.
PDBsum; 5UTZ; -.
PDBsum; 6LX3; -.
PDBsum; 6LXW; -.
PDBsum; 6VWU; -.
PDBsum; 6YE3; -.
SMR; P60568; -.
BioGRID; 109773; 2.
CORUM; P60568; -.
DIP; DIP-475N; -.
IntAct; P60568; 4.
STRING; 9606.ENSP00000226730; -.
BindingDB; P60568; -.
ChEMBL; CHEMBL5880; -.
DrugBank; DB03455; (1H-indol-3-yl)-(2-mercapto-ethoxyimino)-acetic acid.
DrugBank; DB04278; 2-[2-(2-Cyclohexyl-2-guanidino-acetylamino)-acetylamino]-N-(3-mercapto-propyl)-propionamide.
DrugBank; DB03372; 3-Mercapto-1-(1,3,4,9-Tetrahydro-B-Carbolin-2-Yl)-Propan-1-One.
DrugBank; DB01327; Cefazolin.
DrugBank; DB05304; Girentuximab.
DrugBank; DB05299; keyhole limpet hemocyanin.
DrugBank; DB03453; Methyl (2S)-2-[[2-[(3R)-1-carbamimidoylpiperidin-3-yl]acetyl]amino]-3-[4-(2-phenylethynyl)phenyl]propanoate.
DrugBank; DB02581; N(2)-carbamimidoyl-N-{2-[4-(3-{4-[(5-carboxyfuran-2-yl)methoxy]-2,3-dichlorophenyl}-1-methyl-1H-pyrazol-5-yl)piperidin-1-yl]-2-oxoethyl}-D-leucinamide.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB03957; SP2456.
DrugBank; DB02555; SP4160.
DrugBank; DB06083; Tapinarof.
DrugBank; DB06584; TG4010.
DrugCentral; P60568; -.
GlyConnect; 225; 6 N-Linked glycans, 2 O-Linked glycans.
GlyConnect; 297; 3 O-Linked glycans (1 site).
GlyConnect; 298; 2 O-Linked glycans.
GlyConnect; 299; 2 O-Linked glycans.
GlyConnect; 300; 2 N-Linked glycans.
GlyGen; P60568; 1 site, 3 O-linked glycans (1 site).
iPTMnet; P60568; -.
MetOSite; P60568; -.
PhosphoSitePlus; P60568; -.
BioMuta; IL2; -.
DMDM; 45593462; -.
MassIVE; P60568; -.
PaxDb; P60568; -.
PeptideAtlas; P60568; -.
PRIDE; P60568; -.
ProteomicsDB; 57215; -.
ABCD; P60568; 4 sequenced antibodies.
Antibodypedia; 4147; 2084 antibodies.
DNASU; 3558; -.
Ensembl; ENST00000226730; ENSP00000226730; ENSG00000109471.
GeneID; 3558; -.
KEGG; hsa:3558; -.
CTD; 3558; -.
DisGeNET; 3558; -.
GeneCards; IL2; -.
HGNC; HGNC:6001; IL2.
HPA; ENSG00000109471; Tissue enhanced (blood, intestine, lymphoid tissue).
MIM; 147680; gene.
neXtProt; NX_P60568; -.
OpenTargets; ENSG00000109471; -.
PharmGKB; PA195; -.
VEuPathDB; HostDB:ENSG00000109471.4; -.
eggNOG; ENOG502RVR5; Eukaryota.
GeneTree; ENSGT00390000003555; -.
HOGENOM; CLU_124210_0_0_1; -.
InParanoid; P60568; -.
OMA; FCQSIFS; -.
OrthoDB; 1491449at2759; -.
PhylomeDB; P60568; -.
TreeFam; TF338200; -.
PathwayCommons; P60568; -.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-HSA-9020558; Interleukin-2 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P60568; -.
SIGNOR; P60568; -.
BioGRID-ORCS; 3558; 3 hits in 981 CRISPR screens.
ChiTaRS; IL2; human.
EvolutionaryTrace; P60568; -.
GeneWiki; Interleukin_2; -.
GenomeRNAi; 3558; -.
Pharos; P60568; Tchem.
PRO; PR:P60568; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; P60568; protein.
Bgee; ENSG00000109471; Expressed in small intestine Peyer's patch and 76 other tissues.
ExpressionAtlas; P60568; baseline and differential.
Genevisible; P60568; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IDA:MGI.
GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
GO; GO:0005134; F:interleukin-2 receptor binding; IDA:MGI.
GO; GO:0031851; F:kappa-type opioid receptor binding; IEA:Ensembl.
GO; GO:0019209; F:kinase activator activity; TAS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0010467; P:gene expression; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:UniProtKB.
GO; GO:0038110; P:interleukin-2-mediated signaling pathway; TAS:Reactome.
GO; GO:0002366; P:leukocyte activation involved in immune response; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0030101; P:natural killer cell activation; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IGI:ARUK-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:1900100; P:positive regulation of plasma cell differentiation; IGI:ARUK-UCL.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0046013; P:regulation of T cell homeostatic proliferation; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000779; IL-2.
InterPro; IPR030477; IL-2_CS.
Pfam; PF00715; IL2; 1.
PRINTS; PR00265; INTERLEUKIN2.
SMART; SM00189; IL2; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00424; INTERLEUKIN_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Chromosomal rearrangement; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
Immunity; Pharmaceutical; Proto-oncogene; Reference proteome; Secreted;
Signal.
SIGNAL 1..20
/evidence="ECO:0000269|PubMed:6333684"
CHAIN 21..153
/note="Interleukin-2"
/id="PRO_0000015484"
CARBOHYD 23
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:2793860,
ECO:0000269|PubMed:6333684"
/id="CAR_000051"
DISULFID 78..125
/evidence="ECO:0000269|PubMed:16477002,
ECO:0000269|PubMed:6333684"
VARIANT 21
/note="Missing (in FT-IL2-A and FT-IL2-B)"
/id="VAR_003967"
VARIANT 22
/note="Missing (in FT-IL2-B)"
/id="VAR_003968"
HELIX 10..18
/evidence="ECO:0007829|PDB:6VWU"
HELIX 25..49
/evidence="ECO:0007829|PDB:4NEJ"
HELIX 53..59
/evidence="ECO:0007829|PDB:4NEJ"
HELIX 60..62
/evidence="ECO:0007829|PDB:1IRL"
STRAND 64..68
/evidence="ECO:0007829|PDB:3INK"
HELIX 73..76
/evidence="ECO:0007829|PDB:4NEJ"
HELIX 77..93
/evidence="ECO:0007829|PDB:4NEJ"
TURN 95..97
/evidence="ECO:0007829|PDB:1M48"
STRAND 98..100
/evidence="ECO:0007829|PDB:3INK"
HELIX 105..117
/evidence="ECO:0007829|PDB:4NEJ"
HELIX 120..122
/evidence="ECO:0007829|PDB:5LQB"
STRAND 127..132
/evidence="ECO:0007829|PDB:3INK"
HELIX 134..149
/evidence="ECO:0007829|PDB:4NEJ"
TURN 150..152
/evidence="ECO:0007829|PDB:4NEJ"
SEQUENCE 153 AA; 17628 MW; 59E2F40F25860F84 CRC64;
MYRMQLLSCI ALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN YKNPKLTRML
TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL RPRDLISNIN VIVLELKGSE
TTFMCEYADE TATIVEFLNR WITFCQSIIS TLT


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Pathways :
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
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WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP2005: Muscle cell TarBase
WP413: G1 to S cell cycle control
WP1011: T Cell Receptor Signaling Pathway
WP1793: Cell junction organization
WP2328: Allograft rejection
WP1833: Integrin cell surface interactions
WP2377: Integrated Pancreatic Cancer Pathway
WP840: G1 to S cell cycle control
WP1308: Endochondral Ossification
WP2023: Cell Differentiation - meta
WP1365: Calcium Regulation in the Cardiac Cell
WP2082: Cell Differentiation - Index
WP474: Endochondral Ossification

Related Genes :
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL6 IFNB2] Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
[IL2 IL-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2 IL-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[ITK EMT LYK] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[IL27RA CRL1 TCCR WSX1 UNQ296/PRO336] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Cytokine receptor WSX-1) (Cytokine receptor-like 1) (Type I T-cell cytokine receptor) (TCCR) (ZcytoR1)
[Il27ra Tccr Wsx1] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1)
[Il1r1 Il-1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]

Bibliography :
[33193321] Humanized Mouse as a Tool to Predict Immunotoxicity of Human Biologics.
[33027905] The Impact of a New Interleukin-2-Based Immunotherapy Candidate on Urothelial Cells to Support Use for Intravesical Drug Delivery.
[32651161] Repeated 5-day cycles of low dose aldesleukin in amyotrophic lateral sclerosis (IMODALS): A phase 2a randomised, double-blind, placebo-controlled trial.
[32399500] Interleukin-2 Therapy of Autoimmunity in Diabetes (ITAD): a phase 2, multicentre, double-blind, randomized, placebo-controlled trial.
[31466582] Systemic Therapies for Advanced Melanoma.
[31108244] High-dose interleukin-2 and interferon as first-line immunotherapy for metastatic melanoma: long-term follow-up in a large unselected Danish patient cohort.
[30947425] GOF/LOF knowledge inference with tensor decomposition in support of high order link discovery for gene, mutation and disease.
[30917871] Overall survival by clinical risk category for high dose interleukin-2 (HD IL-2) treated patients with metastatic renal cell cancer (mRCC): data from the PROCLAIM registry.
[30282826] The DILfrequency study is an adaptive trial to identify optimal IL-2 dosing in patients with type 1 diabetes.