IL2RB

Interleukin-2 receptor subunit beta is a protein that in humans is encoded by the IL2RB gene.[5] Also known as CD122; IL15RB; P70-75.[5]

IL2RB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2B5I, 2ERJ, 3QAZ, 4GS7
Identifiers
Aliases	IL2RB, CD122, IL15RB, P70-75, interleukin 2 receptor subunit beta, IMD63
External IDs	OMIM: 146710 MGI: 96550 HomoloGene: 47955 GeneCards: IL2RB
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q12.3 Start 37,125,843 bp[1] End 37,175,054 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 E1|15 37.52 cM Start 78,479,256 bp[2] End 78,495,271 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • interleukin-2 binding • GO:0001948 protein binding • cytokine receptor activity • interleukin-2 receptor activity • Ras guanyl-nucleotide exchange factor activity • interleukin-15 receptor activity Cellular component • integral component of membrane • membrane • cell membrane • integral component of plasma membrane • external side of plasma membrane • endosome • cytosol • interleukin-2 receptor complex • cell surface Biological process • negative regulation of apoptotic process • MAPK cascade • interleukin-2-mediated signaling pathway • GO:0022415 viral process • signal transduction • cytokine-mediated signaling pathway • interleukin-15-mediated signaling pathway • regulation of molecular function • positive regulation of phagocytosis • macromolecular complex assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3560	16185
Ensembl	ENSG00000100385	ENSMUSG00000068227
UniProt	P14784	P16297
RefSeq (mRNA)	NM_000878 NM_001346222 NM_001346223	NM_008368
RefSeq (protein)	NP_000869 NP_001333151 NP_001333152	NP_032394
Location (UCSC)	Chr 22: 37.13 – 37.18 Mb	Chr 15: 78.48 – 78.5 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 (also called CD25) and is not involved in signal transduction. The intermediate affinity form consists of a gamma/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.[5]

This protein also forms one of the three subunits of the IL-15 receptor.

Activation of the receptor increases proliferation of CD8+ effector T cells.[6]

Interactions

IL2RB has been shown to interact with:

• CISH,[7]
• HGS,[8]
• Janus kinase 1,[9][10][11][12][13] and
• SHC1.[14][15]

See also

• IL-2 receptor
• IL-15 receptor

References

1. GRCh38: Ensembl release 89: ENSG00000100385 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000068227 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: IL2RB interleukin 2 receptor, beta".
6. Boyman O, Sprent J (February 17, 2012). "The role of interleukin-2 during homeostasis and activation of the immune system". Nat Rev Immunol. 12 (3): 180–190. doi:10.1038/nri3156. PMID 22343569.
7. 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.
8. 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.
9. 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.
10. 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" (PDF). Science. 266 (5187): 1042–5. doi:10.1126/science.7973658. PMID 7973658.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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

• Ellery JM, Nicholls PJ (2002). "Alternate signalling pathways from the interleukin-2 receptor". Cytokine Growth Factor Rev. 13 (1): 27–40. doi:10.1016/S1359-6101(01)00023-5. PMID 11750878.
• Purvis SF, Georges DL, Williams TM, Lederman MM (1992). "Suppression of interleukin-2 and interleukin-2 receptor expression in Jurkat cells stably expressing the human immunodeficiency virus Tat protein". Cell. Immunol. 144 (1): 32–42. doi:10.1016/0008-8749(92)90223-C. PMID 1394441.
• Torigoe T, Saragovi HU, Reed JC (1992). "Interleukin 2 regulates the activity of the lyn protein-tyrosine kinase in a B-cell line". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 2674–8. doi:10.1073/pnas.89.7.2674. PMC 48724. PMID 1557373.
• Maslinski W, Remillard B, Tsudo M, Strom TB (1992). "Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol". J. Biol. Chem. 267 (22): 15281–4. PMID 1639773.
• Miyazaki T, Maruyama M, Yamada G, Hatakeyama M, Taniguchi T (1991). "The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction". EMBO J. 10 (11): 3191–7. doi:10.1002/j.1460-2075.1991.tb04881.x. PMC 453042. PMID 1915291.
• Shibuya H, Yoneyama M, Nakamura Y, Harada H, Hatakeyama M, Minamoto S, Kono T, Doi T, White R, Taniguchi T (1990). "The human interleukin-2 receptor beta-chain gene: genomic organization, promoter analysis and chromosomal assignment". Nucleic Acids Res. 18 (13): 3697–703. doi:10.1093/nar/18.13.3697. PMC 331067. PMID 1973832.
• Hatakeyama M, Kono T, Kobayashi N, Kawahara A, Levin SD, Perlmutter RM, Taniguchi T (1991). "Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association". Science. 252 (5012): 1523–8. doi:10.1126/science.2047859. PMID 2047859.
• Mills GB, May C, McGill M, Fung M, Baker M, Sutherland R, Greene WC (1990). "Interleukin 2-induced tyrosine phosphorylation. Interleukin 2 receptor beta is tyrosine phosphorylated". J. Biol. Chem. 265 (6): 3561–7. PMID 2303462.
• Oyaizu N, Chirmule N, Kalyanaraman VS, Hall WW, Pahwa R, Shuster M, Pahwa S (1990). "Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA". Proc. Natl. Acad. Sci. U.S.A. 87 (6): 2379–83. doi:10.1073/pnas.87.6.2379. PMC 53690. PMID 2315327.
• Gnarra JR, Otani H, Wang MG, McBride OW, Sharon M, Leonard WJ (1990). "Human interleukin 2 receptor beta-chain gene: chromosomal localization and identification of 5' regulatory sequences". Proc. Natl. Acad. Sci. U.S.A. 87 (9): 3440–4. doi:10.1073/pnas.87.9.3440. PMC 53916. PMID 2333293.
• Tsudo M, Kitamura F, Miyasaka M (1989). "Characterization of the interleukin 2 receptor beta chain using three distinct monoclonal antibodies". Proc. Natl. Acad. Sci. U.S.A. 86 (6): 1982–6. doi:10.1073/pnas.86.6.1982. PMC 286829. PMID 2467293.
• Hatakeyama M, Tsudo M, Minamoto S, Kono T, Doi T, Miyata T, Miyasaka M, Taniguchi T (1989). "Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's". Science. 244 (4904): 551–6. doi:10.1126/science.2785715. PMID 2785715.
• Kornfeld H, Cruikshank WW, Pyle SW, Berman JS, Center DM (1988). "Lymphocyte activation by HIV-1 envelope glycoprotein". Nature. 335 (6189): 445–8. doi:10.1038/335445a0. PMID 2843775.
• Leonard WJ, Donlon TA, Lebo RV, Greene WC (1985). "Localization of the gene encoding the human interleukin-2 receptor on chromosome 10". Science. 228 (4707): 1547–9. doi:10.1126/science.3925551. PMID 3925551.
• Bamborough P, Hedgecock CJ, Richards WG (1994). "The interleukin-2 and interleukin-4 receptors studied by molecular modelling". Structure. 2 (9): 839–51. doi:10.1016/S0969-2126(94)00085-9. PMID 7529123.
• Minami Y, Nakagawa Y, Kawahara A, Miyazaki T, Sada K, Yamamura H, Taniguchi T (1995). "Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway". Immunity. 2 (1): 89–100. doi:10.1016/1074-7613(95)90081-0. PMID 7600304.
• Giri JG, Kumaki S, Ahdieh M, Friend DJ, Loomis A, Shanebeck K, DuBose R, Cosman D, Park LS, Anderson DM (1995). "Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor". EMBO J. 14 (15): 3654–63. doi:10.1002/j.1460-2075.1995.tb00035.x. PMC 394440. PMID 7641685.
• Kirken RA, Rui H, Evans GA, Farrar WL (1993). "Characterization of an interleukin-2 (IL-2)-induced tyrosine phosphorylated 116-kDa protein associated with the IL-2 receptor beta-subunit". J. Biol. Chem. 268 (30): 22765–70. PMID 7693677.
• Puri RK, Leland P, Aggarwal BB (1995). "Constitutive expression of human immunodeficiency virus type 1 tat gene inhibits interleukin 2 and interleukin 2 receptor expression in a human CD4+ T lymphoid (H9) cell line". AIDS Res. Hum. Retroviruses. 11 (1): 31–40. doi:10.1089/aid.1995.11.31. PMID 7734194.
• Miyazaki T, Liu ZJ, Kawahara A, Minami Y, Yamada K, Tsujimoto Y, Barsoumian EL, Permutter RM, Taniguchi T (1995). "Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation". Cell. 81 (2): 223–31. doi:10.1016/0092-8674(95)90332-1. PMID 7736574.

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