IL2_HUMAN
ID IL2_HUMAN Reviewed; 153 AA.
AC P60568; P01585;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Interleukin-2;
DE Short=IL-2;
DE AltName: Full=T-cell growth factor;
DE Short=TCGF;
DE AltName: INN=Aldesleukin;
DE Flags: Precursor;
GN Name=IL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6312994; DOI=10.1016/s0006-291x(83)80040-0;
RA Maeda S., Nishino N., Obaru K., Mita S., Nomiyama H., Shimada K.,
RA Fujimoto K., Teranishi T., Hirano T., Onoue K.;
RT "Cloning of interleukin 2 mRNAs from human tonsils.";
RL Biochem. Biophys. Res. Commun. 115:1040-1047(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=6403867; DOI=10.1038/302305a0;
RA Taniguchi T., Matsui H., Fujita T., Takaoka C., Kashima N., Yoshimoto R.,
RA Hamuro J.;
RT "Structure and expression of a cloned cDNA for human interleukin-2.";
RL Nature 302:305-310(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6306584; DOI=10.1093/nar/11.13.4307;
RA Devos R., Plaetinck G., Cheroutre H., Simons G., Degrave W., Tavernier J.,
RA Remaut E., Fiers W.;
RT "Molecular cloning of human interleukin 2 cDNA and its expression in E.
RT coli.";
RL Nucleic Acids Res. 11:4307-4323(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6324170; DOI=10.1073/pnas.80.24.7437;
RA Fujita T., Takaoka C., Matsui H., Taniguchi T.;
RT "Structure of the human interleukin 2 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7437-7441(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330695; DOI=10.1093/nar/12.12.5005;
RA Holbrook N.J., Lieber M., Crabtree G.R.;
RT "DNA sequence of the 5' flanking region of the human interleukin 2 gene:
RT homologies with adult T-cell leukemia virus.";
RL Nucleic Acids Res. 12:5005-5013(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=6608729; DOI=10.1073/pnas.81.6.1634;
RA Holbrook N.J., Smith K.A., Fornace A.J. Jr., Comeau C.M., Wiskocil R.L.,
RA Crabtree G.R.;
RT "T-cell growth factor: complete nucleotide sequence and organization of the
RT gene in normal and malignant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:1634-1638(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7722480; DOI=10.1046/j.1471-4159.1995.64051928.x;
RA Eizenberg O., Faber-Elman A., Lotan M., Schwartz M.;
RT "Interleukin-2 transcripts in human and rodent brains: possible expression
RT by astrocytes.";
RL J. Neurochem. 64:1928-1936(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8824916;
RX DOI=10.1002/(sici)1098-2795(199602)43:2<180::aid-mrd7>3.0.co;2-n;
RA Chernicky C.L., Tan H., Burfeind P., Ilan J., Ilan J.;
RT "Sequence of interleukin-2 isolated from human placental poly A+ RNA:
RT possible role in maintenance of fetal allograft.";
RL Mol. Reprod. Dev. 43:180-186(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RA Nishino N., Obaru K., Maeda S., Shimada K., Onoue K.;
RT "Organization of the DNA regions flanking the human interleukin 2 gene.";
RL Biomed. Res. 6:197-205(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=3491296; DOI=10.1128/mcb.6.9.3042-3049.1986;
RA Siebenlist U., Durand D.B., Bressler P., Holbrook N.J., Norris C.A.,
RA Kamoun M., Kant J.A., Crabtree G.R.;
RT "Promoter region of interleukin-2 gene undergoes chromatin structure
RT changes and confers inducibility on chloramphenicol acetyltransferase gene
RT during activation of T cells.";
RL Mol. Cell. Biol. 6:3042-3049(1986).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-153.
RX PubMed=3264184; DOI=10.1021/bi00418a034;
RA Weir M.P., Chaplin M.A., Wallace D.M., Dykes C.W., Hobden A.N.;
RT "Structure-activity relationships of recombinant human interleukin 2.";
RL Biochemistry 27:6883-6892(1988).
RN [14]
RP PROTEIN SEQUENCE OF 21-153, DISULFIDE BOND, AND GLYCOSYLATION AT THR-23.
RX PubMed=6333684; DOI=10.1073/pnas.81.20.6486;
RA Robb R.J., Kutny R.M., Panico M., Morris H.R., Chowdhry V.;
RT "Amino acid sequence and post-translational modification of human
RT interleukin 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6486-6490(1984).
RN [15]
RP FUNCTION.
RX PubMed=6438535; DOI=10.1038/312641a0;
RA Mingari M.C., Gerosa F., Carra G., Accolla R.S., Moretta A., Zubler R.H.,
RA Waldmann T.A., Moretta L.;
RT "Human interleukin-2 promotes proliferation of activated B cells via
RT surface receptors similar to those of activated T cells.";
RL Nature 312:641-643(1984).
RN [16]
RP GLYCOSYLATION AT THR-23.
RX PubMed=2793860; DOI=10.1016/s0021-9258(18)71502-0;
RA Conradt H.S., Nimtz M., Dittmar K.E.J., Lindenmaier W., Hoppe J.,
RA Hauser H.;
RT "Expression of human interleukin-2 in recombinant baby hamster kidney,
RT Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate
RT chains and their location within the polypeptide.";
RL J. Biol. Chem. 264:17368-17373(1989).
RN [17]
RP CHROMOSOMAL TRANSLOCATION WITH TNFRSF17.
RX PubMed=1396583; DOI=10.1002/j.1460-2075.1992.tb05482.x;
RA Laabi Y., Gras M.P., Carbonnel F., Brouet J.C., Berger R., Larsen C.-J.,
RA Tsapis A.;
RT "A new gene, BCM, on chromosome 16 is fused to the interleukin 2 gene by a
RT t(4;16)(q26;p13) translocation in a malignant T cell lymphoma.";
RL EMBO J. 11:3897-3904(1992).
RN [18]
RP FUNCTION.
RX PubMed=7973659; DOI=10.1126/science.7973659;
RA Miyazaki T., Kawahara A., Fujii H., Nakagawa Y., Minami Y., Liu Z.J.,
RA Oishi I., Silvennoinen O., Witthuhn B.A., Ihle J.N.;
RT "Functional activation of Jak1 and Jak3 by selective association with IL-2
RT receptor subunits.";
RL Science 266:1045-1047(1994).
RN [19]
RP FUNCTION.
RX PubMed=8580378; DOI=10.1006/cyto.1995.0081;
RA Kirken R.A., Rui H., Malabarba M.G., Howard O.M., Kawamura M., O'Shea J.J.,
RA Farrar W.L.;
RT "Activation of JAK3, but not JAK1, is critical for IL-2-induced
RT proliferation and STAT5 recruitment by a COOH-terminal region of the IL-2
RT receptor beta-chain.";
RL Cytokine 7:689-700(1995).
RN [20]
RP FUNCTION.
RX PubMed=25142963; DOI=10.1002/pmic.201400194;
RA Osinalde N., Sanchez-Quiles V., Akimov V., Guerra B., Blagoev B.,
RA Kratchmarova I.;
RT "Simultaneous dissection and comparison of IL-2 and IL-15 signaling
RT pathways by global quantitative phosphoproteomics.";
RL Proteomics 15:520-531(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=3500515; DOI=10.1126/science.3500515;
RA Brandhuber B.J., Boone T., Kenney W.C., McKay D.B.;
RT "Three-dimensional structure of interleukin-2.";
RL Science 238:1707-1709(1987).
RN [22]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=1631562; DOI=10.1126/science.1631562;
RA Bazan J.F.;
RT "Unraveling the structure of IL-2.";
RL Science 257:410-412(1992).
RN [23]
RP RESPONSE TO PUBMED:1631562.
RA McKay D.B.;
RL Science 257:412-413(1992).
RN [24]
RP STRUCTURE BY NMR.
RX PubMed=1510960; DOI=10.1021/bi00148a040;
RA Mott H.R., Driscoll P.C., Boyd J., Cooke R.M., Weir M.P., Campbell I.D.;
RT "Secondary structure of human interleukin 2 from 3D heteronuclear NMR
RT experiments.";
RL Biochemistry 31:7741-7744(1992).
RN [25]
RP 3D-STRUCTURE MODELING.
RX PubMed=7529123; DOI=10.1016/s0969-2126(94)00085-9;
RA Bamborough P., Hedgecock C.J., Richards W.G.;
RT "The interleukin-2 and interleukin-4 receptors studied by molecular
RT modelling.";
RL Structure 2:839-851(1994).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
RP IL2RB AND IL2RG, AND FUNCTION.
RX PubMed=16293754; DOI=10.1126/science.1117893;
RA Wang X., Rickert M., Garcia K.C.;
RT "Structure of the quaternary complex of interleukin-2 with its alpha, beta,
RT and gammac receptors.";
RL Science 310:1159-1163(2005).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
RP IL2RB AND IL2RG, DISULFIDE BOND, AND FUNCTION.
RX PubMed=16477002; DOI=10.1073/pnas.0511161103;
RA Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
RT "Crystal structure of the IL-2 signaling complex: paradigm for a
RT heterotrimeric cytokine receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
CC -!- FUNCTION: Cytokine produced by activated CD4-positive helper T-cells
CC and to a lesser extend activated CD8-positive T-cells and natural
CC killer (NK) cells that plays pivotal roles in the immune response and
CC tolerance (PubMed:6438535). Binds to a receptor complex composed of
CC either the high-affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and
CC IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG)
CC (PubMed:16293754, PubMed:16477002). Interaction with the receptor leads
CC to oligomerization and conformation changes in the IL-2R subunits
CC resulting in downstream signaling starting with phosphorylation of JAK1
CC and JAK3 (PubMed:7973659). In turn, JAK1 and JAK3 phosphorylate the
CC receptor to form a docking site leading to the phosphorylation of
CC several substrates including STAT5 (PubMed:8580378). This process leads
CC to activation of several pathways including STAT, phosphoinositide-3-
CC kinase/PI3K and mitogen-activated protein kinase/MAPK pathways
CC (PubMed:25142963). Functions as a T-cell growth factor and can increase
CC NK-cell cytolytic activity as well (PubMed:6608729). Promotes strong
CC proliferation of activated B-cells and subsequently immunoglobulin
CC production (PubMed:6438535). Plays a pivotal role in regulating the
CC adaptive immune system by controlling the survival and proliferation of
CC regulatory T-cells, which are required for the maintenance of immune
CC tolerance. Moreover, participates in the differentiation and
CC homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as
CC well as memory CD8-positive T-cells. {ECO:0000269|PubMed:16293754,
CC ECO:0000269|PubMed:16477002, ECO:0000269|PubMed:25142963,
CC ECO:0000269|PubMed:6438535, ECO:0000269|PubMed:6608729,
CC ECO:0000269|PubMed:7973659, ECO:0000269|PubMed:8580378}.
CC -!- INTERACTION:
CC P60568; P01589: IL2RA; NbExp=3; IntAct=EBI-12508717, EBI-8614302;
CC P60568; P14784: IL2RB; NbExp=5; IntAct=EBI-12508717, EBI-2866779;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISEASE: Note=A chromosomal aberration involving IL2 is found in a form
CC of T-cell acute lymphoblastic leukemia (T-ALL). Translocation
CC t(4;16)(q26;p13) with involves TNFRSF17. {ECO:0000269|PubMed:1396583}.
CC -!- PHARMACEUTICAL: Available under the name Proleukin (Chiron). Used in
CC patients with renal cell carcinoma or metastatic melanoma.
CC -!- SIMILARITY: Belongs to the IL-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-2 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_2";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il2/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X00695; CAA25292.1; -; Genomic_DNA.
DR EMBL; V00564; CAA23827.1; -; mRNA.
DR EMBL; X01586; CAA25742.1; -; mRNA.
DR EMBL; J00264; AAD48509.1; -; Genomic_DNA.
DR EMBL; K02056; AAA98792.1; -; Genomic_DNA.
DR EMBL; S77834; AAD14263.2; -; mRNA.
DR EMBL; S82692; AAB46883.1; -; mRNA.
DR EMBL; AF359939; AAK26665.1; -; Genomic_DNA.
DR EMBL; BC066255; AAH66255.1; -; mRNA.
DR EMBL; BC066257; AAH66257.1; -; mRNA.
DR EMBL; BC070338; AAH70338.1; -; mRNA.
DR EMBL; M33199; AAA59139.1; -; Genomic_DNA.
DR EMBL; M13879; AAA59141.1; -; Genomic_DNA.
DR EMBL; M22005; AAA59140.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS3726.1; -.
DR PIR; A01849; ICHU2.
DR RefSeq; NP_000577.2; NM_000586.3.
DR PDB; 1IRL; NMR; -; A=21-153.
DR PDB; 1M47; X-ray; 1.99 A; A=21-153.
DR PDB; 1M48; X-ray; 1.95 A; A/B=21-153.
DR PDB; 1M49; X-ray; 2.00 A; A/B=21-153.
DR PDB; 1M4A; X-ray; 2.18 A; A=21-153.
DR PDB; 1M4B; X-ray; 2.15 A; A=21-153.
DR PDB; 1M4C; X-ray; 2.40 A; A/B=21-153.
DR PDB; 1NBP; X-ray; 2.20 A; A=21-153.
DR PDB; 1PW6; X-ray; 2.60 A; A/B=21-153.
DR PDB; 1PY2; X-ray; 2.80 A; A/B/C/D=21-152.
DR PDB; 1QVN; X-ray; 2.70 A; A/B/C/D=21-152.
DR PDB; 1Z92; X-ray; 2.80 A; A=21-153.
DR PDB; 2B5I; X-ray; 2.30 A; A=21-153.
DR PDB; 2ERJ; X-ray; 3.00 A; D/H=21-153.
DR PDB; 3INK; X-ray; 2.50 A; C/D=21-153.
DR PDB; 3QAZ; X-ray; 3.80 A; A/D/G/J/M/P/S/V/Y/b/e/h=21-153.
DR PDB; 3QB1; X-ray; 3.10 A; A/B/C/D/E/F/G/H=21-153.
DR PDB; 4NEJ; X-ray; 1.92 A; A=24-153.
DR PDB; 4NEM; X-ray; 1.93 A; A=24-153.
DR PDB; 5LQB; X-ray; 1.95 A; A=22-153.
DR PDB; 5M5E; X-ray; 2.30 A; D=8-153.
DR PDB; 5UTZ; X-ray; 2.75 A; A/D/E/I=21-153.
DR PDB; 6LX3; EM; 3.15 A; A/B/C/D=1-21.
DR PDB; 6LXW; EM; 3.27 A; A/B/C/D=1-21.
DR PDB; 6VWU; X-ray; 3.40 A; A=10-21, A=90-94.
DR PDB; 6YE3; X-ray; 2.89 A; C/F/I=21-153.
DR PDB; 7DR4; X-ray; 2.49 A; G/I/J/K=21-153.
DR PDB; 7M2G; X-ray; 1.79 A; A=21-153.
DR PDB; 7RA9; X-ray; 2.20 A; A=21-153.
DR PDB; 7RAA; X-ray; 2.69 A; A/B/C/D=21-153.
DR PDBsum; 1IRL; -.
DR PDBsum; 1M47; -.
DR PDBsum; 1M48; -.
DR PDBsum; 1M49; -.
DR PDBsum; 1M4A; -.
DR PDBsum; 1M4B; -.
DR PDBsum; 1M4C; -.
DR PDBsum; 1NBP; -.
DR PDBsum; 1PW6; -.
DR PDBsum; 1PY2; -.
DR PDBsum; 1QVN; -.
DR PDBsum; 1Z92; -.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3INK; -.
DR PDBsum; 3QAZ; -.
DR PDBsum; 3QB1; -.
DR PDBsum; 4NEJ; -.
DR PDBsum; 4NEM; -.
DR PDBsum; 5LQB; -.
DR PDBsum; 5M5E; -.
DR PDBsum; 5UTZ; -.
DR PDBsum; 6LX3; -.
DR PDBsum; 6LXW; -.
DR PDBsum; 6VWU; -.
DR PDBsum; 6YE3; -.
DR PDBsum; 7DR4; -.
DR PDBsum; 7M2G; -.
DR PDBsum; 7RA9; -.
DR PDBsum; 7RAA; -.
DR AlphaFoldDB; P60568; -.
DR SMR; P60568; -.
DR BioGRID; 109773; 2.
DR CORUM; P60568; -.
DR DIP; DIP-475N; -.
DR IntAct; P60568; 4.
DR STRING; 9606.ENSP00000226730; -.
DR BindingDB; P60568; -.
DR ChEMBL; CHEMBL5880; -.
DR DrugBank; DB03455; (1H-indol-3-yl)-(2-mercapto-ethoxyimino)-acetic acid.
DR DrugBank; DB04278; 2-[2-(2-Cyclohexyl-2-guanidino-acetylamino)-acetylamino]-N-(3-mercapto-propyl)-propionamide.
DR DrugBank; DB03372; 3-Mercapto-1-(1,3,4,9-Tetrahydro-B-Carbolin-2-Yl)-Propan-1-One.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB05304; Girentuximab.
DR DrugBank; DB05299; Keyhole limpet hemocyanin.
DR DrugBank; DB03453; Methyl (2S)-2-[[2-[(3R)-1-carbamimidoylpiperidin-3-yl]acetyl]amino]-3-[4-(2-phenylethynyl)phenyl]propanoate.
DR 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.
DR DrugBank; DB00852; Pseudoephedrine.
DR DrugBank; DB03957; SP2456.
DR DrugBank; DB02555; SP4160.
DR DrugBank; DB06083; Tapinarof.
DR DrugBank; DB06584; TG4010.
DR DrugCentral; P60568; -.
DR GlyConnect; 225; 6 N-Linked glycans, 2 O-Linked glycans.
DR GlyConnect; 297; 3 O-Linked glycans (1 site).
DR GlyConnect; 298; 2 O-Linked glycans.
DR GlyConnect; 299; 2 O-Linked glycans.
DR GlyConnect; 300; 2 N-Linked glycans.
DR GlyGen; P60568; 2 sites, 11 N-linked glycans (1 site), 9 O-linked glycans (2 sites).
DR iPTMnet; P60568; -.
DR MetOSite; P60568; -.
DR PhosphoSitePlus; P60568; -.
DR BioMuta; IL2; -.
DR DMDM; 45593462; -.
DR MassIVE; P60568; -.
DR PaxDb; P60568; -.
DR PeptideAtlas; P60568; -.
DR PRIDE; P60568; -.
DR ABCD; P60568; 6 sequenced antibodies.
DR Antibodypedia; 4147; 2022 antibodies from 47 providers.
DR DNASU; 3558; -.
DR Ensembl; ENST00000226730.5; ENSP00000226730.5; ENSG00000109471.5.
DR GeneID; 3558; -.
DR KEGG; hsa:3558; -.
DR MANE-Select; ENST00000226730.5; ENSP00000226730.5; NM_000586.4; NP_000577.2.
DR CTD; 3558; -.
DR DisGeNET; 3558; -.
DR GeneCards; IL2; -.
DR HGNC; HGNC:6001; IL2.
DR HPA; ENSG00000109471; Not detected.
DR MIM; 147680; gene.
DR neXtProt; NX_P60568; -.
DR OpenTargets; ENSG00000109471; -.
DR PharmGKB; PA195; -.
DR VEuPathDB; HostDB:ENSG00000109471; -.
DR eggNOG; ENOG502RVR5; Eukaryota.
DR GeneTree; ENSGT00390000003555; -.
DR HOGENOM; CLU_124210_0_0_1; -.
DR InParanoid; P60568; -.
DR OMA; NGVNNYE; -.
DR OrthoDB; 1491449at2759; -.
DR PhylomeDB; P60568; -.
DR TreeFam; TF338200; -.
DR PathwayCommons; P60568; -.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR SignaLink; P60568; -.
DR SIGNOR; P60568; -.
DR BioGRID-ORCS; 3558; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; IL2; human.
DR EvolutionaryTrace; P60568; -.
DR GeneWiki; Interleukin_2; -.
DR GenomeRNAi; 3558; -.
DR Pharos; P60568; Tchem.
DR PRO; PR:P60568; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P60568; protein.
DR Bgee; ENSG00000109471; Expressed in lymph node and 77 other tissues.
DR ExpressionAtlas; P60568; baseline and differential.
DR Genevisible; P60568; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
DR GO; GO:0005134; F:interleukin-2 receptor binding; IDA:MGI.
DR GO; GO:0031851; F:kappa-type opioid receptor binding; IEA:Ensembl.
DR GO; GO:0019209; F:kinase activator activity; TAS:UniProtKB.
DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:UniProtKB.
DR GO; GO:0002366; P:leukocyte activation involved in immune response; IDA:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; TAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:MGI.
DR GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IGI:ARUK-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
DR GO; GO:1900100; P:positive regulation of plasma cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2000561; P:regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0046013; P:regulation of T cell homeostatic proliferation; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000779; IL-2.
DR InterPro; IPR030477; IL-2_CS.
DR Pfam; PF00715; IL2; 1.
DR PRINTS; PR00265; INTERLEUKIN2.
DR SMART; SM00189; IL2; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00424; INTERLEUKIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Chromosomal rearrangement; Cytokine;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW Immunity; Pharmaceutical; Proto-oncogene; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:6333684"
FT CHAIN 21..153
FT /note="Interleukin-2"
FT /id="PRO_0000015484"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:2793860,
FT ECO:0000269|PubMed:6333684"
FT /id="CAR_000051"
FT DISULFID 78..125
FT /evidence="ECO:0000269|PubMed:16477002,
FT ECO:0000269|PubMed:6333684"
FT VARIANT 21
FT /note="Missing (in FT-IL2-A and FT-IL2-B)"
FT /id="VAR_003967"
FT VARIANT 22
FT /note="Missing (in FT-IL2-B)"
FT /id="VAR_003968"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:6VWU"
FT HELIX 25..48
FT /evidence="ECO:0007829|PDB:7M2G"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2B5I"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7M2G"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1IRL"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7DR4"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:7M2G"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:7M2G"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:7M2G"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6YE3"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:7M2G"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3INK"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:7M2G"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5LQB"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:7DR4"
FT HELIX 134..151
FT /evidence="ECO:0007829|PDB:7M2G"
SQ SEQUENCE 153 AA; 17628 MW; 59E2F40F25860F84 CRC64;
MYRMQLLSCI ALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN YKNPKLTRML
TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL RPRDLISNIN VIVLELKGSE
TTFMCEYADE TATIVEFLNR WITFCQSIIS TLT
