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Janus kinase 1

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This is the current revision of this page, as edited by YuniToumei (talk | contribs) at 20:04, 16 October 2024 (Adding local short description: "Mammalian protein found in Homo sapiens", overriding Wikidata description "protein-coding gene"). The present address (URL) is a permanent link to this version.

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JAK1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesJAK1, JAK1A, JAK1B, JTK3, Janus kinase 1, AIIDE
External IDsOMIM: 147795; MGI: 96628; HomoloGene: 1678; GeneCards: JAK1; OMA:JAK1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3716

16451

Ensembl

ENSG00000162434

ENSMUSG00000028530

UniProt

P23458

P52332

RefSeq (mRNA)

NM_146145
NM_013567

RefSeq (protein)

n/a

Location (UCSC)Chr 1: 64.83 – 65.07 MbChr 4: 101.15 – 101.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

JAK1 is a human tyrosine kinase protein 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.[5] 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.[6] Expression of JAK1 in cancer cells enables individual cells to contract, potentially allowing them to escape their tumor and metastasize to other parts of the body.[7]

Interactions

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Janus kinase 1 has been shown to interact with:

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162434 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028530 – 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.
  5. ^ 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. doi:10.1016/S0952-7915(00)00228-4. PMID 11406370.
  6. ^ 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. doi:10.1016/S0092-8674(00)81166-6. PMID 9590172. S2CID 18684846.
  7. ^ Christian Nordqvist. "Protein JAK Makes Cancer Cells Contract, So They Can Squeeze Out Of A Tumor". Medical News Today.
  8. ^ Collum RG, Brutsaert S, Lee G, Schindler C (August 2000). "A Stat3-interacting protein (StIP1) regulates cytokine signal transduction". Proc. Natl. Acad. Sci. U.S.A. 97 (18): 10120–5. Bibcode:2000PNAS...9710120C. doi:10.1073/pnas.170192197. PMC 27739. PMID 10954736.
  9. ^ Usacheva A, Tian X, Sandoval R, Salvi D, Levy D, Colamonici OR (September 2003). "The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex". J. Immunol. 171 (6): 2989–94. doi:10.4049/jimmunol.171.6.2989. PMID 12960323.
  10. ^ Haan C, Is'harc H, Hermanns HM, Schmitz-Van De Leur H, Kerr IM, Heinrich PC, Grötzinger J, Behrmann I (October 2001). "Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction". J. Biol. Chem. 276 (40): 37451–8. doi:10.1074/jbc.M106135200. PMID 11468294.
  11. ^ Kim H, Baumann H (December 1997). "Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells". J. Biol. Chem. 272 (49): 30741–7. doi:10.1074/jbc.272.49.30741. PMID 9388212.
  12. ^ Haan C, Heinrich PC, Behrmann I (January 2002). "Structural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: the receptor is crucial for kinase activation". Biochem. J. 361 (Pt 1): 105–11. doi:10.1042/0264-6021:3610105. PMC 1222284. PMID 11742534.
  13. ^ Kim H, Lee YH, Won J, Yun Y (September 2001). "Through induction of juxtaposition and tyrosine kinase activity of Jak1, X-gene product of hepatitis B virus stimulates Ras and the transcriptional activation through AP-1, NF-kappaB, and SRE enhancers". Biochem. Biophys. Res. Commun. 286 (5): 886–94. doi:10.1006/bbrc.2001.5496. PMID 11527382.
  14. ^ Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (December 1995). "Involvement of Janus kinases in the insulin signaling pathway". Eur. J. Biochem. 234 (2): 656–60. doi:10.1111/j.1432-1033.1995.656_b.x. PMID 8536716.
  15. ^ a b 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.
  16. ^ 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.
  17. ^ 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.
  18. ^ 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.
  19. ^ 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.
  20. ^ Gual P, Baron V, Lequoy V, Van Obberghen E (March 1998). "Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor". Endocrinology. 139 (3): 884–93. doi:10.1210/endo.139.3.5829. PMID 9492017.
  21. ^ Johnston JA, Wang LM, Hanson EP, Sun XJ, White MF, Oakes SA, Pierce JH, O'Shea JJ (December 1995). "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. doi:10.1074/jbc.270.48.28527. PMID 7499365.
  22. ^ Usacheva A, Sandoval R, Domanski P, Kotenko SV, Nelms K, Goldsmith MA, Colamonici OR (December 2002). "Contribution of the Box 1 and Box 2 motifs of cytokine receptors to Jak1 association and activation". J. Biol. Chem. 277 (50): 48220–6. doi:10.1074/jbc.M205757200. PMID 12374810.
  23. ^ Yin T, Shen R, Feng GS, Yang YC (January 1997). "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases". J. Biol. Chem. 272 (2): 1032–7. doi:10.1074/jbc.272.2.1032. PMID 8995399.
  24. ^ Lehmann U, Schmitz J, Weissenbach M, Sobota RM, Hortner M, Friederichs K, Behrmann I, Tsiaris W, Sasaki A, Schneider-Mergener J, Yoshimura A, Neel BG, Heinrich PC, Schaper F (January 2003). "SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130". J. Biol. Chem. 278 (1): 661–71. doi:10.1074/jbc.M210552200. PMID 12403768.
  25. ^ Pandey A, Fernandez MM, Steen H, Blagoev B, Nielsen MM, Roche S, Mann M, Lodish HF (December 2000). "Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways". J. Biol. Chem. 275 (49): 38633–9. doi:10.1074/jbc.M007849200. PMID 10993906.
  26. ^ Endo K, Takeshita T, Kasai H, Sasaki Y, Tanaka N, Asao H, Kikuchi K, Yamada M, Chenb M, O'Shea JJ, Sugamura K (July 2000). "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Lett. 477 (1–2): 55–61. doi:10.1016/s0014-5793(00)01760-9. PMID 10899310.
  27. ^ Ueda T, Bruchovsky N, Sadar MD (March 2002). "Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways". J. Biol. Chem. 277 (9): 7076–85. doi:10.1074/jbc.M108255200. PMID 11751884.
  28. ^ Spiekermann K, Biethahn S, Wilde S, Hiddemann W, Alves F (August 2001). "Constitutive activation of STAT transcription factors in acute myelogenous leukemia". Eur. J. Haematol. 67 (2): 63–71. doi:10.1034/j.1600-0609.2001.t01-1-00385.x. PMID 11722592. S2CID 38074766.
  29. ^ a b Fujitani Y, Hibi M, Fukada T, Takahashi-Tezuka M, Yoshida H, Yamaguchi T, Sugiyama K, Yamanaka Y, Nakajima K, Hirano T (February 1997). "An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT". Oncogene. 14 (7): 751–61. doi:10.1038/sj.onc.1200907. PMID 9047382.
  30. ^ Guo D, Dunbar JD, Yang CH, Pfeffer LM, Donner DB (March 1998). "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". J. Immunol. 160 (6): 2742–50. doi:10.4049/jimmunol.160.6.2742. PMID 9510175.
  31. ^ Miscia S, Marchisio M, Grilli A, Di Valerio V, Centurione L, Sabatino G, Garaci F, Zauli G, Bonvini E, Di Baldassarre A (January 2002). "Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells". Cell Growth Differ. 13 (1): 13–8. PMID 11801527.

Further reading

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