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UniProtKB/Swiss-Prot entry P60568


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IL2_HUMAN
Primary accession number P60568
Secondary accession number P01585
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 65)
Name and origin of the protein
Protein name Interleukin-2 [Precursor]
Synonyms IL-2
T-cell growth factor
TCGF
Aldesleukin
Gene name
Name: IL2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0006-291X(83)80040-0; PubMed=6312994 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/302305a0; PubMed=6403867 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1093/nar/11.13.4307; PubMed=6306584 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1093/nar/12.12.5005; PubMed=6330695 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1002/(SICI)1098-2795(199602)43:2<180::AID-MRD7>3.3.CO;2-D; PubMed=8824916 [NCBI, ExPASy, EBI, Israel, Japan]
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 program for genomic applications;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1021/bi00418a034; PubMed=3264184 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3500515 [NCBI, ExPASy, EBI, Israel, Japan]
Brandhuber B.J., Boone T., Kenney W.C., McKay D.B.;
"Three-dimensional structure of interleukin-2.";
Science 238:1707-1709(1987).
[17]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1631562 [NCBI, ExPASy, EBI, Israel, Japan]
Bazan J.F.;
"Unraveling the structure of IL-2.";
Science 257:410-412(1992).
[18]
RESPONSE TO ABOVE LETTER.
McKay D.B.;
Science 257:412-413(1992).
[19]
STRUCTURE BY NMR.
DOI=10.1021/bi00148a040; PubMed=1510960 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
3D-STRUCTURE MODELING.
DOI=10.1016/S0969-2126(94)00085-9; PubMed=7529123 [NCBI, ExPASy, EBI, Israel, Japan]
Bamborough P., Hedgecock C.J., Richards W.G.;
"The interleukin-2 and interleukin-4 receptors studied by molecular modelling.";
Structure 2:839-851(1994).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA; IL2RB AND IL2RC.
DOI=10.1126/science.1117893; PubMed=16293754 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA; IL2RB AND IL2RC, AND DISULFIDE BOND.
DOI=10.1073/pnas.0511161103; PubMed=16477002 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00695; CAA25292.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00564; CAA23827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01586; CAA25742.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00264; AAD48509.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02056; AAA98792.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S77834; AAD14263.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S82692; AAB46883.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF359939; AAK26665.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066255; AAH66255.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066257; AAH66257.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070338; AAH70338.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33199; AAA59139.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13879; AAA59141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22005; AAA59140.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01849; ICHU2.
RefSeq NP_000577.2; -.
UniGene Hs.89679
3D structure databases
PDB
1ILM; Model; -; 2=26-153.[ExPASy / RCSB / EBI]
1ILN; Model; -; 2=26-153.[ExPASy / RCSB / EBI]
1IRL; NMR; -; A=21-153.[ExPASy / RCSB / EBI]
1M47; X-ray; 1.99 A; A=21-153.[ExPASy / RCSB / EBI]
1M48; X-ray; 1.95 A; A/B=21-153.[ExPASy / RCSB / EBI]
1M49; X-ray; 2.00 A; A/B=21-153.[ExPASy / RCSB / EBI]
1M4A; X-ray; 2.18 A; A=21-153.[ExPASy / RCSB / EBI]
1M4B; X-ray; 2.15 A; A=21-153.[ExPASy / RCSB / EBI]
1M4C; X-ray; 2.40 A; A/B=21-153.[ExPASy / RCSB / EBI]
1NBP; X-ray; 2.20 A; A=21-153.[ExPASy / RCSB / EBI]
1PW6; X-ray; 2.60 A; A/B=21-153.[ExPASy / RCSB / EBI]
1PY2; X-ray; 2.80 A; A/B/C/D=21-152.[ExPASy / RCSB / EBI]
1QVN; X-ray; 2.70 A; A/B/C/D=21-152.[ExPASy / RCSB / EBI]
1Z92; X-ray; 2.80 A; A=21-153.[ExPASy / RCSB / EBI]
2B5I; X-ray; 2.30 A; A=21-153.[ExPASy / RCSB / EBI]
2ERJ; X-ray; 3.00 A; D/H=21-153.[ExPASy / RCSB / EBI]
3INK; X-ray; 2.50 A; C/D=21-153.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ILM; -.
1ILN; -.
1IRL; -.
1M47; -.
1M48; -.
1M49; -.
1M4A; -.
1M4B; -.
1M4C; -.
1NBP; -.
1PW6; -.
1PY2; -.
1QVN; -.
1Z92; -.
2B5I; -.
2ERJ; -.
3INK; -.
ModBase P60568.
PTM databases
GlycoSuiteDB P60568; -.
Organism-specific databases
H-InvDB HIX0031382; -.
HGNC HGNC:6001; IL2.
GenAtlas IL2.
HPA CAB010310; -.
MIM 147680; gene. [NCBI / EBI]
PharmGKB PA25405; -.
GeneCards P60568.
Gene expression databases
ArrayExpress P60568; -.
CleanEx HS_IL2; -.
GermOnline ENSG00000109471; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from UniProtKB).
GO:0005134; Molecular function: interleukin-2 receptor binding (traceable author statement from UniProtKB).
GO:0019209; Molecular function: kinase activator activity (traceable author statement from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0007155; Biological process: cell adhesion (traceable author statement from UniProtKB).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from UniProtKB).
GO:0006955; Biological process: immune response (traceable author statement from UniProtKB).
GO:0030101; Biological process: natural killer cell activation (traceable author statement from UniProtKB).
GO:0030307; Biological process: positive regulation of cell growth (traceable author statement from UniProtKB).
GO:0008284; Biological process: positive regulation of cell proliferation (traceable author statement from UniProtKB).
GO:0030217; Biological process: T cell differentiation (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR000779; Interleukin-2.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR11443; Interleukin-2; 1.
Pfam PF00715; IL2; 1.
Pfam graphical view of domain structure.
PRINTS PR00265; INTERLEUKIN2.
ProDom PD003649; Interleukin-2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00189; IL2; 1.
SMART graphical view of domain structure.
PROSITE PS00424; INTERLEUKIN_2; 1.
BLOCKS P60568.
Genome annotation databases
Ensembl ENSG00000109471; Homo sapiens. [Contig view]
GeneID 3558; -.
KEGG hsa:3558; -.
Phylogenomic databases
HOVERGEN P60568; -.
Other
LinkHub P60568; -.
SOURCE IL2; Homo sapiens.
ProtoNet P60568.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chromosomal rearrangement; Cytokine; Direct protein sequencing; Glycoprotein; Growth factor; Immune response; Pharmaceutical; Proto-oncogene; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   153  133     Interleukin-2. PRO_0000015484
CARBOHYD   23    23        O-linked (GalNAc...) [GlycoSuiteDB]. CAR_000051
DISULFID   78   125         
VARIANT   21    21  1     Missing (in FT-IL2-A and FT-IL2-B). VAR_003967
VARIANT   22    22  1     Missing (in FT-IL2-B). VAR_003968
HELIX   27    49  23      
HELIX   53    59  7      
HELIX   73    76  4      
HELIX   77    80  4      
HELIX   83    93  11      
HELIX   102   117  16      
HELIX   134   149  16      
TURN   150   152  3      
Sequence information
Length: 153 AA [This is the length of the unprocessed precursor] Molecular weight: 17628 Da [This is the MW of the unprocessed precursor] CRC64: 59E2F40F25860F84 [This is a checksum on the sequence]
        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 

P60568 in FASTA format

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