IL2RB

IL2RB
Identifiers
Aliases	IL2RB, CD122, IL15RB, P70-75, interleukin 2 receptor subunit beta, IMD63
External IDs	OMIM: 146710; MGI: 96550; GeneCards: IL2RB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2B5I, 2ERJ, 3QAZ, 4GS7
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
	granulocyte; ; decidua; ; mucosa of ileum; ; blood; ; lymph node; ; spleen; ; appendix; ; bone marrow cell; ; mucosa of urinary bladder; ; epithelium of nasopharynx;
	Top expressed in
	mesenteric lymph nodes; ; blood; ; decidua; ; spleen; ; secondary oocyte; ; gastrula; ; zygote; ; thymus; ; pharynx; ; lumbar subsegment of spinal cord;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	interleukin-2 binding; protein binding; cytokine receptor activity; interleukin-2 receptor activity; interleukin-15 receptor activity;
Cellular component	integral component of membrane; membrane; plasma 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; viral process; signal transduction; cytokine-mediated signaling pathway; interleukin-15-mediated signaling pathway; regulation of molecular function; positive regulation of phagocytosis; protein-containing complex assembly;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	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. Also known as CD122; IL15RB; P70-75.

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.

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.

Interactions

IL2RB has been shown to interact with:

Clinical significance

IL2RB-mediated interleukin-15 (IL-15) signaling has been implicated in the pathogenesis of celiac disease. Increased IL-15 signaling promotes activation of intraepithelial lymphocytes, epithelial injury, and persistent intestinal inflammation, including in some patients who remain symptomatic despite adherence to a gluten-free diet.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100385 – Ensembl, May 2017
1 2 3 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.
1 2 3 "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.
↑ Lee H, Park SH, Shin EC (2024-02-16). "IL-15 in T-Cell Responses and Immunopathogenesis". Immune Network. 24 (1): e11. doi:10.4110/in.2024.24.e11. PMID 38455459.

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] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100385 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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] 1 2 3 "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.

[16] Lee H, Park SH, Shin EC (2024-02-16). "IL-15 in T-Cell Responses and Immunopathogenesis". Immune Network. 24 (1): e11. doi:10.4110/in.2024.24.e11. PMID 38455459.

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	1 a-c 1A 1B 1D 1E 2 3 γ δ ε 4 5 6 7 8 a 9 10 11 a b c d 13 14 15 16 A B 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 A B 33 34 35 36 37 38 39 40 41 42 a b c d 43 44 45 46 47 48 49 a b c d e f 50
51–100	51 52 53 54 55 56 57 58 59 61 62 E L P 63 64 A B C 66 a b c d e f 68 69 70 71 72 73 74 78 79 a b 80 81 82 83 84 85 a d e h j k 86 87 88 89 90 91 92 93 94 95 96 97 98 99 100
101–150	101 102 103 104 105 106 107 a b 108 109 110 111 112 113 114 115 116 117 118 119 120 a b 121 a b 122 123 124 125 126 127 129 130 131 132 133 134 135 136 137 138 140b 141 142 143 144 146 147 148 150
151–200	151 152 153 154 155 156 a b c 157 158 (a d e i k) 159 a c 160 161 162 163 164 166 167 a b 168 169 170 171 172 a b g 174 177 178 179 a b 180 181 182 183 184 185 186 191 192 193 194 195 196 197 w198 w199 200
201–250	201 202b 204 205 206 207 208 209 w210 a b 212 213a 1 2 217 218 (a b) 220 221 222 223 224 225 226 227 228 229 230 233 234 235 a b 236 238 239 240CE 240D 241 243 244 246 247 248 249
251–300	252 253 254 256 257 258 261 262 263 264 265 266 267 268 269 271 272 273 274 275 276 278 279 280 281 282 283 284 286 288 289 290 292 w293 294 295 297 298 299
301–350	300A 301 302 303 304 305 306 307 309 312 314 315 316 317 318 320 321 322 324 325 326 327 328 329 331 332 333 334 335 336 337 338 339 340 344 349 350
351–371	351 352 353 354 355 357 358 360 361 362 363 364 365 366 367 368 369 370 371
Category Commons

IL2RB

Function

Interactions

Clinical significance

See also

References

Further reading