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Reviewed, UniProtKB/Swiss-Prot P60568 (IL2_HUMAN)

Last modified July 22, 2008. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interleukin-2
      Short name(s)=IL-2
Alternative name(s):
    T-cell growth factor
      Short name(s)=TCGF
    INN=Aldesleukin
Gene names
Name: IL2
OrganismHomo sapiens (Human)
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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2020
Chain21 – 153133Interleukin-2

Amino acid modifications

Glycosylation231O-linked (GalNAc...)
Disulfide bond78 ↔ 125

Natural variations

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

Secondary structure

............... 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60568-1 [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: 6312994] [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: 6403867] [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: 6306584] [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: 6324170] [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: 6330695] [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: 6608729] [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: 7722480] [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: 8824916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[9]SeattleSNPs program for genomic applications
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: 15489334] [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: 3491296] [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: 3264184] [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: 6333684] [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: 2793860] [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: 3500515] [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: 1631562] [Abstract]
Cited for: COMPARISON OF X-RAY STRUCTURES.
[18]McKay D.B.
Science 257:412-413(1992)
Cited for: RESPONSE TO ABOVE LETTER.
[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: 1510960] [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: 7529123] [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: 16293754] [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: 16477002] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA; IL2RB AND IL2RC, DISULFIDE BOND.

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

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.
PIRICHU2. A01849.
RefSeqNP_000577.2.
UniGeneHs.89679

3D structure databases

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[»]
ModBaseSearch...

PTM databases

GlycoSuiteDBP60568.
PhosphoSiteP60568.

Genome annotation databases

EnsemblENSG00000109471. Homo sapiens. [Contig view]
GeneID3558.
KEGGhsa:3558.

Organism-specific databases

H-InvDBHIX0031382.
HGNCHGNC:6001. IL2.
HPACAB010310.
MIM147680. gene.
PharmGKBPA25405.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOVERGENP60568.

Gene expression databases

ArrayExpressP60568.
CleanExHS_IL2.
GermOnlineENSG00000109471. Homo sapiens.

Family and domain databases

InterProIPR012351. 4_helix_cytokine_core.
IPR000779. Interleukin-2.
[Graphical view]
Gene3DG3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.
PANTHERPTHR11443. Interleukin-2. 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]
PROSITEPS00424. INTERLEUKIN_2. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

LinkHubP60568.
SOURCESearch...
ProtoNetSearch...

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 22, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Forthcoming format changes (XML)

Announcements of forthcoming format changes in the XML format

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents