Laboratory demand management strategies: An overview

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; OMA:IL2RB - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	37,175,054 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	78,379,471 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	3560
	16185
	ENSG00000100385
	ENSMUSG00000068227
	P14784
	P16297
	NM_000878; NM_001346222; NM_001346223
	NM_008368
	NP_000869; NP_001333151; NP_001333152
	NP_032394
	Wikidata
View/Edit Human	View/Edit Mouse

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]

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100385 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000068227 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c "Entrez Gene: IL2RB interleukin 2 receptor, beta".
^ 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. S2CID 22680847.
^ 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.
^ 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.
^ 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. Bibcode:1994Sci...266.1045M. doi:10.1126/science.7973659. PMID 7973659.
^ 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. Bibcode:1994Sci...266.1042R. doi:10.1126/science.7973658. PMID 7973658.
^ 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.
^ 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.
^ 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.
^ 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. S2CID 40742391.
^ 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. doi:10.1016/S0021-9258(17)42066-7. PMID 8294403.

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. Bibcode:1992PNAS...89.2674T. 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. doi:10.1016/S0021-9258(19)49530-6. 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. Bibcode:1991Sci...252.1523H. doi:10.1126/science.2047859. PMID 2047859. S2CID 41503548.
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. doi:10.1016/S0021-9258(19)39806-0. 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. Bibcode:1990PNAS...87.2379O. 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. Bibcode:1990PNAS...87.3440G. 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. Bibcode:1989PNAS...86.1982T. 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. Bibcode:1989Sci...244..551H. 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. Bibcode:1988Natur.335..445K. doi:10.1038/335445a0. PMID 2843775. S2CID 4326650.
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. Bibcode:1985Sci...228.1547L. 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. doi:10.1016/S0021-9258(18)41592-X. 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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100385 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-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. S2CID 22680847.

[pmid10514520-7] 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.

[pmid18445679-8] 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.

[pmid7973659-9] 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. Bibcode:1994Sci...266.1045M. doi:10.1126/science.7973659. PMID 7973659.

[pmid7973658-10] 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". Science. 266 (5187): 1042–5. Bibcode:1994Sci...266.1042R. doi:10.1126/science.7973658. PMID 7973658.

[pmid12133952-11] 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.

[pmid9553136-12] 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.

[pmid9774657-13] 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.

[pmid10602027-14] 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. S2CID 40742391.

[pmid8294403-15] 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. doi:10.1016/S0021-9258(17)42066-7. PMID 8294403.

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Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Laboratory demand management strategies: An overview

Function

Interactions

See also

References

Further reading