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:
37.52 – 37.57 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]

See also[edit]


IL2RB has been shown to interact with HGS,[2] Janus kinase 1,[3][4][5][6][7] CISH[8] and SHC1.[9][10]


  1. ^ a b "Entrez Gene: IL2RB interleukin 2 receptor, beta". 
  2. ^ Yamashita, Yuki; Kojima Katsuhiko; Tsukahara Tomonori; Agawa Hideyuki; Yamada Koichiro; Amano Yuji; Kurotori Naoki; Tanaka Nobuyuki; Sugamura Kazuo; Takeshita Toshikazu (May 2008). "Ubiquitin-independent binding of Hrs mediates endosomal sorting of the interleukin-2 receptor beta-chain". J. Cell. Sci. (England) 121 (Pt 10): 1727–38. doi:10.1242/jcs.024455. ISSN 0021-9533. PMID 18445679. 
  3. ^ Miyazaki, T; Kawahara A; Fujii H; Nakagawa Y; Minami Y; Liu Z J; Oishi I; Silvennoinen O; Witthuhn B A; Ihle J N (November 1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science (UNITED STATES) 266 (5187): 1045–7. doi:10.1126/science.7973659. ISSN 0036-8075. PMID 7973659. 
  4. ^ Russell, S M; Johnston J A; Noguchi M; Kawamura M; Bacon C M; Friedmann M; Berg M; McVicar D W; Witthuhn B A; Silvennoinen O (November 1994). "Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID". Science (UNITED STATES) 266 (5187): 1042–5. doi:10.1126/science.7973658. ISSN 0036-8075. PMID 7973658. 
  5. ^ Usacheva, Anna; Kotenko Sergei; Witte Michael M; Colamonici Oscar R (August 2002). "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. (United States) 169 (3): 1302–8. doi:10.4049/jimmunol.169.3.1302. ISSN 0022-1767. PMID 12133952. 
  6. ^ Zhu, M H; Berry J A; Russell S M; Leonard W J (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. (UNITED STATES) 273 (17): 10719–25. doi:10.1074/jbc.273.17.10719. ISSN 0021-9258. PMID 9553136. 
  7. ^ Migone, T S; Rodig S; Cacalano N A; Berg M; Schreiber R D; Leonard W J (November 1998). "Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation". Mol. Cell. Biol. (UNITED STATES) 18 (11): 6416–22. ISSN 0270-7306. PMC 109227. PMID 9774657. 
  8. ^ Aman, M J; Migone T S; Sasaki A; Ascherman D P; Zhu M h; Soldaini E; Imada K; Miyajima A; Yoshimura A; Leonard W J (October 1999). "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". J. Biol. Chem. (UNITED STATES) 274 (42): 30266–72. doi:10.1074/jbc.274.42.30266. ISSN 0021-9258. PMID 10514520. 
  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. (GERMANY) 30 (1): 59–68. doi:10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1. ISSN 0014-2980. PMID 10602027. 
  10. ^ Ravichandran, K S; Burakoff S J (January 1994). "The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation". J. Biol. Chem. (UNITED STATES) 269 (3): 1599–602. ISSN 0021-9258. PMID 8294403. 

Further reading[edit]

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