Interleukin 12 receptor, beta 1 subunit

IL12RB1
Identifiers
Aliases	IL12RB1, CD212, IL-12R-BETA1, IL12RB, IMD30, Interleukin 12 receptor beta 1 subunit, IL12 receptor beta 1 subunit, interleukin 12 receptor subunit beta 1
External IDs	MGI: 104579 HomoloGene: 4042 GeneCards: IL12RB1
Gene ontology Molecular function • interleukin-23 receptor activity • interleukin-12 receptor activity • interleukin-12 receptor binding • cytokine receptor activity • interleukin-23 binding • cytokine binding Cellular component • integral component of membrane • interleukin-23 receptor complex • interleukin-12 receptor complex • membrane • external side of plasma membrane • plasma membrane Biological process • cytokine-mediated signaling pathway • positive regulation of T cell mediated cytotoxicity • positive regulation of interferon-gamma production • positive regulation of T-helper 17 cell lineage commitment • positive regulation of T-helper 17 type immune response • positive regulation of T-helper 1 type immune response • positive regulation of memory T cell differentiation • cellular response to interferon-gamma • peptidyl-tyrosine phosphorylation • signal transduction • positive regulation of activated T cell proliferation • positive regulation of defense response to virus by host • interleukin-12-mediated signaling pathway • interleukin-23-mediated signaling pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3594	16161
Ensembl	ENSG00000096996	ENSMUSG00000000791
UniProt	P42701	Q60837
RefSeq (mRNA)	NM_001290023 NM_001290024 NM_005535 NM_153701	NM_008353
RefSeq (protein)	NP_001276952.1 NP_005526.1 NP_714912.1	NP_032379.2
Location (UCSC)	Chr 19: 18.06 – 18.1 Mb	Chr 8: 70.81 – 70.82 Mb
PubMed search	[1]	[2]
Wikidata

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Interleukin 12 receptor, beta 1 is a subunit of the interleukin 12 receptor. IL12RB1, is its human gene.^[3] IL12RB1 is also known as CD212 (cluster of differentiation 212).

The protein encoded by this gene is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukin 12 (IL12) with a low affinity, and is thought to be a part of IL12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL12 binding activity. The coexpression of this and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. The lack of expression of this gene was found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: IL12RB1 interleukin 12 receptor, beta 1".

Further reading

• van de Vosse E, Lichtenauer-Kaligis EG, van Dissel JT, Ottenhoff TH (2003). "Genetic variations in the interleukin-12/interleukin-23 receptor (beta1) chain, and implications for IL-12 and IL-23 receptor structure and function.". Immunogenetics. 54 (12): 817–29. doi:10.1007/s00251-002-0534-9. PMID 12671732.
• Ling P, Gately MK, Gubler U, et al. (1995). "Human IL-12 p40 homodimer binds to the IL-12 receptor but does not mediate biologic activity.". J. Immunol. 154 (1): 116–27. PMID 7527811.
• Gillessen S, Carvajal D, Ling P, et al. (1995). "Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12 antagonist.". Eur. J. Immunol. 25 (1): 200–6. doi:10.1002/eji.1830250133. PMID 7843232.
• Chua AO, Chizzonite R, Desai BB, et al. (1994). "Expression cloning of a human IL-12 receptor component. A new member of the cytokine receptor superfamily with strong homology to gp130.". J. Immunol. 153 (1): 128–36. PMID 7911493.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Presky DH, Yang H, Minetti LJ, et al. (1997). "A functional interleukin 12 receptor complex is composed of two beta-type cytokine receptor subunits". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 14002–7. doi:10.1073/pnas.93.24.14002. PMC 19484. PMID 8943050.
• Gubler U, Presky DH (1997). "Molecular biology of interleukin-12 receptors". Ann. N. Y. Acad. Sci. 795: 36–40. doi:10.1111/j.1749-6632.1996.tb52653.x. PMID 8958915.
• Zou J, Presky DH, Wu CY, Gubler U (1997). "Differential associations between the cytoplasmic regions of the interleukin-12 receptor subunits beta1 and beta2 and JAK kinases". J. Biol. Chem. 272 (9): 6073–7. doi:10.1074/jbc.272.9.6073. PMID 9038232.
• Yamamoto K, Kobayashi H, Miura O, et al. (1997). "Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1 and beta 2 chains, to human chromosome 19 band p13.1 and chromosome 1 band p31.2, respectively, by in situ hybridization". Cytogenet. Cell Genet. 77 (3–4): 257–8. doi:10.1159/000134589. PMID 9284929.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Igarashi O, Yamane H, Imajoh-Ohmi S, Nariuchi H (1998). "IL-12 receptor (IL-12R) expression and accumulation of IL-12R beta 1 and IL-12R beta 2 mRNAs in CD4+ T cells by costimulation with B7-2 molecules". J. Immunol. 160 (4): 1638–46. PMID 9469420.
• de Jong R, Altare F, Haagen IA, et al. (1998). "Severe mycobacterial and Salmonella infections in interleukin-12 receptor-deficient patients". Science. 280 (5368): 1435–8. doi:10.1126/science.280.5368.1435. PMID 9603733.
• Kawashima T, Kawasaki H, Kitamura T, et al. (1998). "Interleukin-12 induces tyrosine phosphorylation of an 85-kDa protein associated with the interleukin-12 receptor beta 1 subunit". Cell. Immunol. 186 (1): 39–44. doi:10.1006/cimm.1998.1294. PMID 9637763.
• Yao BB, Niu P, Surowy CS, Faltynek CR (1999). "Direct interaction of STAT4 with the IL-12 receptor". Arch. Biochem. Biophys. 368 (1): 147–55. doi:10.1006/abbi.1999.1302. PMID 10415122.
• Oppmann B, Lesley R, Blom B, et al. (2001). "Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12". Immunity. 13 (5): 715–25. doi:10.1016/S1074-7613(00)00070-4. PMID 11114383.
• Altare F, Ensser A, Breiman A, et al. (2001). "Interleukin-12 receptor beta1 deficiency in a patient with abdominal tuberculosis". J. Infect. Dis. 184 (2): 231–6. doi:10.1086/321999. PMID 11424023.
• Losana G, Rigamonti L, Borghi I, et al. (2002). "Requirement for both IL-12 and IFN-gamma signaling pathways in optimal IFN-gamma production by human T cells". Eur. J. Immunol. 32 (3): 693–700. doi:10.1002/1521-4141(200203)32:3<693::AID-IMMU693>3.0.CO;2-Q. PMID 11857344.
• Parham C, Chirica M, Timans J, et al. (2002). "A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R". J. Immunol. 168 (11): 5699–708. doi:10.4049/jimmunol.168.11.5699. PMID 12023369.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cleary AM, Tu W, Enright A, et al. (2003). "Impaired accumulation and function of memory CD4 T cells in human IL-12 receptor beta 1 deficiency". J. Immunol. 170 (1): 597–603. doi:10.4049/jimmunol.170.1.597. PMID 12496448.

External links

• IL12RB1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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