Interleukin-2 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P60568 (IL2_HUMAN)

Last modified June 16, 2009. Version 74. History...

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

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Names and origin

Protein names

Recommended name:
    Interleukin-2
      Short name=IL-2
Alternative name(s):
    T-cell growth factor
      Short name=TCGF
    INN=Aldesleukin

Gene names

Name:

IL2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Immune response
Cellular component	Secreted
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	T cell differentiation Traceable author statement. Source: UniProtKB anti-apoptosis Traceable author statement. Source: UniProtKB cell adhesion Traceable author statement. Source: UniProtKB cell-cell signaling Traceable author statement. Source: UniProtKB immune response Traceable author statement. Source: UniProtKB natural killer cell activation Traceable author statement. Source: UniProtKB negative regulation of B cell apoptosis Inferred from direct assay. Source: MGI positive regulation of B cell proliferation Inferred from direct assay. Source: MGI positive regulation of activated T cell proliferation Inferred from direct assay. Source: MGI positive regulation of cell growth Traceable author statement. Source: UniProtKB
Cellular component	extracellular space Ref.6 Traceable author statement. Source: UniProtKB
Molecular function	cytokine activity Inferred from direct assay. Source: MGI interleukin-2 receptor binding Traceable author statement. Source: UniProtKB kinase activator activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.14

Chain

21 – 153

133

Interleukin-2

PRO_0000015484

Amino acid modifications

Glycosylation

O-linked (GalNAc...) Ref.14 Ref.15

CAR_000051

Disulfide bond

78 ↔ 125

Ref.14 Ref.22

Natural variations

Natural variant

Missing in FT-IL2-A and FT-IL2-B.

VAR_003967

Natural variant

Missing in FT-IL2-B.

VAR_003968

Secondary structure

153

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P60568-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 59E2F40F25860F84
Show »

FASTA

153

17,628

        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

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References

	« Hide 'large scale' referencesShow '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 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: 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.
+	Additional computationally mapped references.

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Web resources

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

Wikipedia

Interleukin-2 entry

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

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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.

IPI

IPI00003099.

PIR

ICHU2. A01849.

RefSeq

NP_000577.2.

UniGene

Hs.89679

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILM	model	-	2	26-153	[»]
1ILN	model	-	2	26-153	[»]
1IRL	NMR	-	A	21-153	[»]
1M47	X-ray	1.99	A	21-153	[»]
1M48	X-ray	1.95	A/B	21-153	[»]
1M49	X-ray	2.00	A/B	21-153	[»]
1M4A	X-ray	2.18	A	21-153	[»]
1M4B	X-ray	2.15	A	21-153	[»]
1M4C	X-ray	2.40	A/B	21-153	[»]
1NBP	X-ray	2.20	A	21-153	[»]
1PW6	X-ray	2.60	A/B	21-153	[»]
1PY2	X-ray	2.80	A/B/C/D	21-152	[»]
1QVN	X-ray	2.70	A/B/C/D	21-152	[»]
1Z92	X-ray	2.80	A	21-153	[»]
2B5I	X-ray	2.30	A	21-153	[»]
2ERJ	X-ray	3.00	D/H	21-153	[»]
3INK	X-ray	2.50	C/D	21-153	[»]

ModBase

Search...

PTM databases

GlycoSuiteDB

P60568.

Genome annotation databases

Ensembl

ENSG00000109471. Homo sapiens. [Contig view]

GeneID

3558.

KEGG

hsa:3558.

Organism-specific databases

GeneCards

GC04M123652.

H-InvDB

HIX0031382.

HGNC

HGNC:6001. IL2.

HPA

CAB010310.

MIM

147680. gene.

Orphanet

101972. Combined T and B cell immunodeficiency.

PharmGKB

PA25405.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P60568.

OMA

P60568. NINVTVL.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il12_2pathway. IL12-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
il23pathway. IL23-mediated signaling events.
il27pathway. IL27-mediated signaling events.
telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

P60568.

Bgee

P60568.

CleanEx

HS_IL2.

GermOnline

ENSG00000109471. Homo sapiens.

Family and domain databases

InterPro

IPR012351. 4_helix_cytokine_core.
IPR000779. Interleukin-2.
[Graphical view]

Gene3D

G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.

PANTHER

PTHR11443. Interleukin-2. 1 hit.

Pfam

PF00715. IL2. 1 hit.
[Graphical view]

PRINTS

PR00265. INTERLEUKIN2.

ProDom

PD003649. Interleukin-2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00189. IL2. 1 hit.
[Graphical view]

PROSITE

PS00424. INTERLEUKIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13896.

SOURCE

Search...

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Entry information

Entry name

IL2_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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