Interleukin 12 receptor, beta 1 subunit

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IL12RB1
Identifiers
AliasesIL12RB1, CD212, IL-12R-BETA1, IL12RB, IMD30, Interleukin 12 receptor beta 1 subunit, IL12 receptor beta 1 subunit, interleukin 12 receptor subunit beta 1
External IDsMGI: 104579 HomoloGene: 4042 GeneCards: IL12RB1
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for IL12RB1
Genomic location for IL12RB1
Band19p13.11Start18,058,995 bp[1]
End18,098,944 bp[1]
RNA expression pattern
PBB GE IL12RB1 206890 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001290023
NM_001290024
NM_005535
NM_153701

NM_008353

RefSeq (protein)

NP_001276952
NP_001276953
NP_005526
NP_714912

NP_032379

Location (UCSC)Chr 19: 18.06 – 18.1 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Interleukin-12 receptor, beta 1, or IL-12Rβ1 in short, is a subunit of the interleukin 12 receptor. IL12RB1, is the name of its human gene.[4] IL-12Rβ1 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 (IL-12) with a low affinity, and is part of the IL-12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL-12 binding activity. The coexpression of this and IL-12Rβ2 protein was shown to lead to the formation of high-affinity IL-12 binding sites and reconstitution of IL-12 dependent signaling. IL-12Rβ1 can also bind interleukin-23 (IL-23) as part of the IL-23 receptor complex. This complex forms a disulfide-linked oligomer, which is required for its IL-23 binding activity. The coexpression of this and IL-23R protein was shown to lead to the formation of IL-23 binding sites.

Various mutations in this gene were found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections.[5] Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.[4] All mutations known in the IL12RB1 gene, as well as many polymorphisms, have been collected in a mutation database [6][7]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000096996 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ a b "Entrez Gene: IL12RB1 interleukin 12 receptor, beta 1". 
  5. ^ "OMIM Entry - # 614891 - IMMUNODEFICIENCY 30; IMD30". omim.org. 
  6. ^ http://www.lovd.nl/IL12RB1
  7. ^ Van De Vosse, Esther; Haverkamp, Margje H; Ramirez-Alejo, Noe; Martinez-Gallo, Mónica; Blancas-Galicia, Lizbeth; Metin, Ayşe; Garty, Ben Zion; Sun-Tan, Çağman; Broides, Arnon; De Paus, Roelof A; Keskin, Özlem; Çağdaş, Deniz; Tezcan, Ilhan; Lopez-Ruzafa, Encarna; Aróstegui, Juan I; Levy, Jacov; Espinosa-Rosales, Francisco J; Sanal, Özden; Santos-Argumedo, Leopoldo; Casanova, Jean-Laurent; Boisson-Dupuis, Stephanie; Van Dissel, Jaap T; Bustamante, Jacinta (2013). "IL-12Rβ1 Deficiency: Mutation Update and Description of theIL12RB1Variation Database". Human Mutation. 34 (10): 1329–1339. doi:10.1002/humu.22380. PMC 4104692Freely accessible. PMID 23864330. 

Further reading[edit]

  • 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 19484Freely accessible. 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 139241Freely accessible. 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[edit]

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