From Wikipedia, the free encyclopedia
Jump to: navigation, search
Interleukin 2 receptor, beta
Protein IL2RB PDB 2b5i.png
PDB rendering based on 2b5i.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols IL2RB ; CD122; IL15RB; P70-75
External IDs OMIM146710 MGI96550 HomoloGene47955 ChEMBL: 3276 GeneCards: IL2RB Gene
RNA expression pattern
PBB GE IL2RB 205291 at tn.png
More reference expression data
Species Human Mouse
Entrez 3560 16185
Ensembl ENSG00000100385 ENSMUSG00000068227
UniProt P14784 P16297
RefSeq (mRNA) NM_000878 NM_008368
RefSeq (protein) NP_000869 NP_032394
Location (UCSC) Chr 22:
37.13 – 37.18 Mb
Chr 15:
78.48 – 78.5 Mb
PubMed search [1] [2]

Interleukin-2 receptor subunit beta is a protein that in humans is encoded by the IL2RB gene.[1]


The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by this gene represents the beta subunit and is a type I membrane protein.[1]


IL2RB has been shown to interact with:

See also[edit]


  1. ^ a b "Entrez Gene: IL2RB interleukin 2 receptor, beta". 
  2. ^ Aman MJ, Migone TS, Sasaki A, Ascherman DP, Zhu Mh, Soldaini E, Imada K, Miyajima A, Yoshimura A, Leonard WJ (October 1999). "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". J. Biol. Chem. 274 (42): 30266–72. doi:10.1074/jbc.274.42.30266. PMID 10514520. 
  3. ^ Yamashita Y, Kojima K, Tsukahara T, Agawa H, Yamada K, Amano Y, Kurotori N, Tanaka N, Sugamura K, Takeshita T (May 2008). "Ubiquitin-independent binding of Hrs mediates endosomal sorting of the interleukin-2 receptor beta-chain". J. Cell. Sci. 121 (Pt 10): 1727–38. doi:10.1242/jcs.024455. PMID 18445679. 
  4. ^ Miyazaki T, Kawahara A, Fujii H, Nakagawa Y, Minami Y, Liu ZJ, Oishi I, Silvennoinen O, Witthuhn BA, Ihle JN (November 1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science 266 (5187): 1045–7. doi:10.1126/science.7973659. PMID 7973659. 
  5. ^ Russell SM, Johnston JA, Noguchi M, Kawamura M, Bacon CM, Friedmann M, Berg M, McVicar DW, Witthuhn BA, Silvennoinen O (November 1994). "Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID". Science 266 (5187): 1042–5. doi:10.1126/science.7973658. PMID 7973658. 
  6. ^ Usacheva A, Kotenko S, Witte MM, Colamonici OR (August 2002). "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. doi:10.4049/jimmunol.169.3.1302. PMID 12133952. 
  7. ^ Zhu MH, Berry JA, Russell SM, Leonard WJ (April 1998). "Delineation of the regions of interleukin-2 (IL-2) receptor beta chain important for association of Jak1 and Jak3. Jak1-independent functional recruitment of Jak3 to Il-2Rbeta". J. Biol. Chem. 273 (17): 10719–25. doi:10.1074/jbc.273.17.10719. PMID 9553136. 
  8. ^ Migone TS, Rodig S, Cacalano NA, Berg M, Schreiber RD, Leonard WJ (November 1998). "Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation". Mol. Cell. Biol. 18 (11): 6416–22. doi:10.1128/mcb.18.11.6416. PMC 109227. PMID 9774657. 
  9. ^ Delespine-Carmagnat M, Bouvier G, Bertoglio J (January 2000). "Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain". Eur. J. Immunol. 30 (1): 59–68. doi:10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1. PMID 10602027. 
  10. ^ Ravichandran KS, Burakoff SJ (January 1994). "The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation". J. Biol. Chem. 269 (3): 1599–602. PMID 8294403. 

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.