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Open Access Articles- Top Results for IL2RB

IL2RB

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Identifiers
SymbolsIL2RB ; CD122; IL15RB; P70-75
External IDsOMIM146710 MGI96550 HomoloGene47955 IUPHAR: 1696 ChEMBL: 3276 GeneCards: IL2RB Gene
RNA expression pattern
File:PBB GE IL2RB 205291 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez356016185
EnsemblENSG00000100385ENSMUSG00000068227
UniProtP14784P16297
RefSeq (mRNA)NM_000878NM_008368
RefSeq (protein)NP_000869NP_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]

Function

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]

Interactions

IL2RB has been shown to interact with:

See also

References

  1. ^ a b "Entrez Gene: IL2RB interleukin 2 receptor, beta". 
  2. ^ Aman MJ, Migone TS, Sasaki A, Ascherman DP, Zhu M, Soldaini E et al. (October 1999). "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". J. Biol. Chem. 274 (42): 30266–72. PMID 10514520. doi:10.1074/jbc.274.42.30266. 
  3. ^ Yamashita Y, Kojima K, Tsukahara T, Agawa H, Yamada K, Amano Y et al. (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. PMID 18445679. doi:10.1242/jcs.024455. 
  4. ^ Miyazaki T, Kawahara A, Fujii H, Nakagawa Y, Minami Y, Liu ZJ et al. (November 1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science 266 (5187): 1045–7. PMID 7973659. doi:10.1126/science.7973659. 
  5. ^ Russell SM, Johnston JA, Noguchi M, Kawamura M, Bacon CM, Friedmann M et al. (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. PMID 7973658. doi:10.1126/science.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. PMID 12133952. doi:10.4049/jimmunol.169.3.1302. 
  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. PMID 9553136. doi:10.1074/jbc.273.17.10719. 
  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. 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. PMID 10602027. doi:10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1. 
  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

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


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