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P01589 (IL2RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-2 receptor subunit alpha

Short name=IL-2 receptor subunit alpha
Short name=IL-2-RA
Short name=IL-2R subunit alpha
Short name=IL2-RA
Alternative name(s):
TAC antigen
p55
CD_antigen=CD25
Gene names
Name:IL2RA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for interleukin-2.

Subunit structure

Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit.

Subcellular location

Membrane; Single-pass type I membrane protein.

Involvement in disease

Diabetes mellitus, insulin-dependent, 10 (IDDM10) [MIM:601942]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.13

Sequence similarities

Contains 2 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDiabetes mellitus
   DomainRepeat
Signal
Sushi
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation-induced cell death of T cells

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement PubMed 9096364. Source: ProtInc

cell proliferation

Traceable author statement PubMed 2983318. Source: ProtInc

cell surface receptor signaling pathway

Traceable author statement PubMed 2983318. Source: ProtInc

immune response

Traceable author statement PubMed 9096364. Source: ProtInc

inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of defense response to virus

Inferred from electronic annotation. Source: Ensembl

negative regulation of immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of T cell homeostatic proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functiondrug binding

Inferred from electronic annotation. Source: Ensembl

interleukin-2 receptor activity

Traceable author statement PubMed 9096364. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 272251Interleukin-2 receptor subunit alpha
PRO_0000011024

Regions

Topological domain22 – 240219Extracellular Potential
Transmembrane241 – 25919Helical; Potential
Topological domain260 – 27213Cytoplasmic Potential
Domain22 – 8463Sushi 1
Domain123 – 18664Sushi 2

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Ref.9
Glycosylation891N-linked (GlcNAc...) Ref.9
Glycosylation2181O-linked (GalNAc...) Ref.9
Glycosylation2241O-linked (GalNAc...) Ref.9
Glycosylation2291O-linked (GalNAc...) Ref.9
Glycosylation2371O-linked (GalNAc...) Ref.9
Disulfide bond24 ↔ 168 Ref.9 Ref.11 Ref.12
Disulfide bond49 ↔ 80 Ref.9 Ref.11 Ref.12
Disulfide bond51 ↔ 82 Ref.9 Ref.11 Ref.12
Disulfide bond67 ↔ 125 Ref.9 Ref.11 Ref.12
Disulfide bond152 ↔ 184 Ref.9 Ref.11 Ref.12

Natural variations

Natural variant2721I → T. Ref.5
Corresponds to variant rs12722712 [ dbSNP | Ensembl ].
VAR_019280

Secondary structure

.............................. 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01589 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 83D907C8C81D2C0E

FASTA27230,819
        10         20         30         40         50         60 
MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE CKRGFRRIKS 

        70         80         90        100        110        120 
GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE QKERKTTEMQ SPMQPVDQAS 

       130        140        150        160        170        180 
LPGHCREPPP WENEATERIY HFVVGQMVYY QCVQGYRALH RGPAESVCKM THGKTRWTQP 

       190        200        210        220        230        240 
QLICTGEMET SQFPGEEKPQ ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ 

       250        260        270 
VAVAGCVFLL ISVLLLSGLT WQRRQRKSRR TI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNA encoding human interleukin-2 receptor."
Nikaido T., Shimizu A., Ishida N., Sabe H., Teshigawara K., Maeda M., Uchiyama T., Yodoi J., Honjo T.
Nature 311:631-635(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and expression of cDNAs for the human interleukin-2 receptor."
Leonard W.J., Depper J.M., Crabtree G.R., Rudikoff S., Pumphrey J., Robb R.J., Kroenke M., Svetlik P.B., Peffer N.J., Waldmann T.A., Greene W.C.
Nature 311:626-631(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning and structure of the human interleukin 2 receptor gene."
Ishida N., Kanamori H., Noma T., Nikaido T., Sabe H., Suzuki N., Shimizu A., Honjo T.
Nucleic Acids Res. 13:7579-7589(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure of the human interleukin-2 receptor gene."
Leonard W.J., Depper J.M., Kanehisa M., Kroenke M., Peffer N.J., Svetlik P.B., Sullivan M., Greene W.C.
Science 230:633-639(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]SeattleSNPs variation discovery resource
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-272.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a nonfunctional promoter by the transactivator gene of HTLV-I."
Cross S.L., Feinberg M.B., Wolf J.B., Holbrook N.J., Wong-Stall F., Leonard W.J.
Cell 49:47-56(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[9]"Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure."
Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.
Biochem. Biophys. Res. Commun. 154:372-379(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-89; THR-218; THR-224; THR-229 AND THR-237.
[10]"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] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 23-83.
[11]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-238 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
[12]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-233 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
[13]"Large-scale genetic fine mapping and genotype-phenotype associations implicate polymorphism in the IL2RA region in type 1 diabetes."
Lowe C.E., Cooper J.D., Brusko T., Walker N.M., Smyth D.J., Bailey R., Bourget K., Plagnol V., Field S., Atkinson M., Clayton D.G., Wicker L.S., Todd J.A.
Nat. Genet. 39:1074-1082(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IDDM10.
+Additional computationally mapped references.

Web resources

IL2RAbase

IL2RA mutation db

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01057 mRNA. Translation: CAA25525.1.
X03131 expand/collapse EMBL AC list , X03132, X03133, X03134, X03135, X03136, X03137, X03138 Genomic DNA. Translation: CAA26906.1.
K03122 mRNA. Translation: AAB59535.1. Sequence problems.
M11066 expand/collapse EMBL AC list , M10322, M11060, M11061, M11062, M11063, M11064, M11065 Genomic DNA. Translation: AAA67527.1.
AY563103 Genomic DNA. Translation: AAS55572.1.
AL157395, AL137186 Genomic DNA. Translation: CAH73595.1.
AL137186, AL157395 Genomic DNA. Translation: CAI41069.1.
CH471072 Genomic DNA. Translation: EAW86414.1.
M15864 Genomic DNA. Translation: AAA59162.1.
BN000945 Genomic DNA. Translation: CAK26553.1.
PIRUHHU2. A44186.
RefSeqNP_000408.1. NM_000417.2.
UniGeneHs.231367.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILMmodel-A23-83[»]
1ILNmodel-A23-83[»]
1Z92X-ray2.80B22-238[»]
2B5IX-ray2.30D22-238[»]
2ERJX-ray3.00A/E22-233[»]
3IU3X-ray2.90I/J/K22-238[»]
3NFPX-ray2.86I/K22-238[»]
ProteinModelPortalP01589.
SMRP01589. Positions 22-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109774. 4 interactions.
DIPDIP-1080N.
IntActP01589. 1 interaction.
MINTMINT-8146732.
STRING9606.ENSP00000369293.

Chemistry

BindingDBP01589.
ChEMBLCHEMBL2364167.
DrugBankDB00041. Aldesleukin.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00004. Denileukin diftitox.
GuidetoPHARMACOLOGY1695.

PTM databases

PhosphoSiteP01589.

Polymorphism databases

DMDM124317.

Proteomic databases

PaxDbP01589.
PRIDEP01589.

Protocols and materials databases

DNASU3559.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379959; ENSP00000369293; ENSG00000134460.
GeneID3559.
KEGGhsa:3559.
UCSCuc001iiz.2. human.

Organism-specific databases

CTD3559.
GeneCardsGC10M006041.
HGNCHGNC:6008. IL2RA.
HPACAB002419.
MIM147730. gene.
601942. phenotype.
606367. phenotype.
neXtProtNX_P01589.
Orphanet169100. Immunodeficiency due to CD25 deficiency.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
PharmGKBPA29828.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47154.
HOGENOMHOG000113044.
HOVERGENHBG052109.
InParanoidP01589.
KOK05068.
OMACQAELCD.
OrthoDBEOG7S21ZH.
PhylomeDBP01589.
TreeFamTF337408.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP01589.
BgeeP01589.
CleanExHS_IL2RA.
GenevestigatorP01589.

Family and domain databases

InterProIPR015486. IL-2_rcpt_alpha.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PANTHERPTHR10573. PTHR10573. 1 hit.
PfamPF00084. Sushi. 2 hits.
[Graphical view]
SMARTSM00032. CCP. 2 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 2 hits.
PROSITEPS50923. SUSHI. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01589.
GeneWikiIL2RA.
GenomeRNAi3559.
NextBio13900.
PROP01589.
SOURCESearch...

Entry information

Entry nameIL2RA_HUMAN
AccessionPrimary (citable) accession number: P01589
Secondary accession number(s): Q5W007
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries