Janus kinase 1

From Wikipedia, the free encyclopedia


Janus kinase 1 (a protein tyrosine kinase)
Identifiers
Symbol(s) JAK1; JAK1A; JAK1B
External IDs OMIM: 147795 MGI: 96628 HomoloGene: 1678
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3716 16451
Ensembl ENSG00000162434 ENSMUSG00000028530
Uniprot P23458 Q3TI10
Refseq NM_002227 (mRNA)
NP_002218 (protein)		 NM_146145 (mRNA)
NP_666257 (protein)
Location Chr 1: 65.07 - 65.2 Mb Chr 4: 100.65 - 100.76 Mb
Pubmed search [1] [2]

JAK1 is essential for signaling for certain type I and type II cytokines. It interacts with the common gamma chain (γc) of type I cytokine receptors, to elicit signals from the IL-2 receptor family (e.g. IL-2R, IL-7R, IL-9R and IL-15R), the IL-4 receptor family (e.g. IL-4R and IL-13R), the gp130 receptor family (e.g. IL-6R, IL-11R, LIF-R, OSM-R, cardiotrophin-1 receptor (CT-1R), ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It is also important for transducing a signal by type I (IFN-α/β) and type II (IFN-γ) interferons, and members of the IL-10 family via type II cytokine receptors.[1] Jak1 plays a critical role in initiating responses to multiple major cytokine receptor families. Loss of Jak1 is lethal in neonatal mice, possibly due to difficulties suckling.[2]

[edit] References

  1. ^ Gadina M, Hilton D, Johnston JA, Morinobu A, Lighvani A, Zhou YJ, Visconti R, O'Shea JJ (2001). "Signaling by type I and II cytokine receptors: ten years after". Curr. Opin. Immunol. 13 (3): 363–73. PMID 11406370. 
  2. ^ Rodig SJ, Meraz MA, White JM, Lampe PA, Riley JK, Arthur CD, King KL, Sheehan KC, Yin L, Pennica D, Johnson EM, Schreiber RD (1998). "Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses". Cell 93 (3): 373–83. PMID 9590172. 

[edit] Further reading

  • Donnelly RP, Dickensheets H, Finbloom DS (1999). "The interleukin-10 signal transduction pathway and regulation of gene expression in mononuclear phagocytes.". J. Interferon Cytokine Res. 19 (6): 563–73. doi:10.1089/107999099313695. PMID 10433356. 
  • Carter-Su C, Rui L, Stofega MR (2000). "SH2-B and SIRP: JAK2 binding proteins that modulate the actions of growth hormone.". Recent Prog. Horm. Res. 55: 293–311. PMID 11036942. 
  • Kostrodymova GM (1976). "[An experimental study of the possible sensitizing properties of triethanolamine contained in chemical compounds used at home]". Gigiena i sanitariia (6): 10–2. PMID 1213395. 
  • Howard OM, Dean M, Young H, et al. (1992). "Characterization of a class 3 tyrosine kinase.". Oncogene 7 (5): 895–900. PMID 1373877. 
  • Pritchard MA, Baker E, Callen DF, et al. (1992). "Two members of the JAK family of protein tyrosine kinases map to chromosomes 1p31.3 and 9p24.". Mamm. Genome 3 (1): 36–8. PMID 1581631. 
  • Wilks AF, Harpur AG, Kurban RR, et al. (1991). "Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase.". Mol. Cell. Biol. 11 (4): 2057–65. PMID 1848670. 
  • Johnston JA, Wang LM, Hanson EP, et al. (1996). "Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases.". J. Biol. Chem. 270 (48): 28527–30. PMID 7499365. 
  • Nicholson SE, Oates AC, Harpur AG, et al. (1994). "Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation.". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 2985–8. PMID 7512720. 
  • Domanski P, Yan H, Witte MM, et al. (1995). "Homodimerization and intermolecular tyrosine phosphorylation of the Tyk-2 tyrosine kinase.". FEBS Lett. 374 (3): 317–22. PMID 7589562. 
  • Modi WS, Farrar WL, Howard OM (1995). "Confirmed assignment of a novel human tyrosine kinase gene (JAK1A) to 1p32.3-->p31.3 by nonisotopic in situ hybridization.". Cytogenet. Cell Genet. 69 (3-4): 232–4. PMID 7698020. 
  • Miyazaki T, Kawahara A, Fujii H, et al. (1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits.". Science 266 (5187): 1045–7. PMID 7973659. 
  • Müller M, Briscoe J, Laxton C, et al. (1993). "The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction.". Nature 366 (6451): 129–35. doi:10.1038/366129a0. PMID 8232552. 
  • Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes.". Oncogene 8 (12): 3403–10. PMID 8247543. 
  • Lütticken C, Wegenka UM, Yuan J, et al. (1994). "Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130.". Science 263 (5143): 89–92. PMID 8272872. 
  • Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (1996). "Involvement of Janus kinases in the insulin signaling pathway.". Eur. J. Biochem. 234 (2): 656–60. PMID 8536716. 
  • Friedmann MC, Migone TS, Russell SM, Leonard WJ (1996). "Different interleukin 2 receptor beta-chain tyrosines couple to at least two signaling pathways and synergistically mediate interleukin 2-induced proliferation.". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 2077–82. PMID 8700888. 
  • Gauzzi MC, Velazquez L, McKendry R, et al. (1996). "Interferon-alpha-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase.". J. Biol. Chem. 271 (34): 20494–500. PMID 8702790. 
  • Demoulin JB, Uyttenhove C, Van Roost E, et al. (1996). "A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9.". Mol. Cell. Biol. 16 (9): 4710–6. PMID 8756628. 
  • Yin T, Shen R, Feng GS, Yang YC (1997). "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases.". J. Biol. Chem. 272 (2): 1032–7. PMID 8995399. 
  • Bluyssen HA, Levy DE (1997). "Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA.". J. Biol. Chem. 272 (7): 4600–5. PMID 9020188. 

[edit] External links


v • d • e
Kinases: tyrosine kinases (EC 2.7.10)
2.7.10.1
2.7.10.2