Glycogen synthase kinase-3 beta

Details

Name
Glycogen synthase kinase-3 beta
Synonyms
  • 2.7.11.26
  • GSK-3 beta
  • Serine/threonine-protein kinase GSK3B
Gene Name
GSK3B
Organism
Humans
Amino acid sequence
>lcl|BSEQ0002121|Glycogen synthase kinase-3 beta
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK
VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG
EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR
DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV
WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP
WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF
NFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST
Number of residues
420
Molecular Weight
46743.865
Theoretical pI
8.97
GO Classification
Functions
ATP binding / beta-catenin binding / kinase activity / NF-kappaB binding / p53 binding / protein kinase A catalytic subunit binding / protein kinase binding / protein serine/threonine kinase activity / RNA polymerase II transcription factor binding / tau-protein kinase activity / ubiquitin protein ligase binding
Processes
axon guidance / canonical Wnt signaling pathway / canonical Wnt signaling pathway involved in positive regulation of apoptotic process / cell migration / cellular response to heat / cellular response to interleukin-3 / circadian rhythm / epidermal growth factor receptor signaling pathway / epithelial to mesenchymal transition / ER overload response / extrinsic apoptotic signaling pathway in absence of ligand / fat cell differentiation / Fc-epsilon receptor signaling pathway / fibroblast growth factor receptor signaling pathway / glycogen metabolic process / hippocampus development / hypermethylation of CpG island / innate immune response / intracellular signal transduction / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / myoblast fusion / negative regulation of apoptotic process / negative regulation of canonical Wnt signaling pathway / negative regulation of cardiac muscle hypertrophy / negative regulation of glycogen (starch) synthase activity / negative regulation of glycogen biosynthetic process / negative regulation of neuron maturation / negative regulation of neuron projection development / negative regulation of NFAT protein import into nucleus / negative regulation of protein binding / negative regulation of protein complex assembly / negative regulation of protein localization to nucleus / negative regulation of type B pancreatic cell development / neurotrophin TRK receptor signaling pathway / organ morphogenesis / peptidyl-serine phosphorylation / phosphatidylinositol-mediated signaling / positive regulation of axon extension / positive regulation of canonical Wnt signaling pathway / positive regulation of cell-matrix adhesion / positive regulation of GTPase activity / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of peptidyl-serine phosphorylation / positive regulation of peptidyl-threonine phosphorylation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of protein binding / positive regulation of protein catabolic process / positive regulation of protein complex assembly / positive regulation of protein export from nucleus / positive regulation of stem cell differentiation / positive regulation of transcription from RNA polymerase II promoter / protein autophosphorylation / protein export from nucleus / protein localization to microtubule / protein phosphorylation / re-entry into mitotic cell cycle / regulation of cellular response to heat / regulation of gene expression by genetic imprinting / regulation of microtubule-based process / superior temporal gyrus development
Components
beta-catenin destruction complex / centrosome / cytoplasm / cytosol / dendritic shaft / growth cone / neuronal cell body / neuronal postsynaptic density / nucleus / perinuclear region of cytoplasm / plasma membrane / ribonucleoprotein complex
General Function
Ubiquitin protein ligase binding
Specific Function
Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021658|Glycogen synthase kinase-3 beta (GSK3B)
ATGTCAGGGCGGCCCAGAACCACCTCCTTTGCGGAGAGCTGCAAGCCGGTGCAGCAGCCT
TCAGCTTTTGGCAGCATGAAAGTTAGCAGAGACAAGGACGGCAGCAAGGTGACAACAGTG
GTGGCAACTCCTGGGCAGGGTCCAGACAGGCCACAAGAAGTCAGCTATACAGACACTAAA
GTGATTGGAAATGGATCATTTGGTGTGGTATATCAAGCCAAACTTTGTGATTCAGGAGAA
CTGGTCGCCATCAAGAAAGTATTGCAGGACAAGAGATTTAAGAATCGAGAGCTCCAGATC
ATGAGAAAGCTAGATCACTGTAACATAGTCCGATTGCGTTATTTCTTCTACTCCAGTGGT
GAGAAGAAAGATGAGGTCTATCTTAATCTGGTGCTGGACTATGTTCCGGAAACAGTATAC
AGAGTTGCCAGACACTATAGTCGAGCCAAACAGACGCTCCCTGTGATTTATGTCAAGTTG
TATATGTATCAGCTGTTCCGAAGTTTAGCCTATATCCATTCCTTTGGAATCTGCCATCGG
GATATTAAACCGCAGAACCTCTTGTTGGATCCTGATACTGCTGTATTAAAACTCTGTGAC
TTTGGAAGTGCAAAGCAGCTGGTCCGAGGAGAACCCAATGTTTCGTATATCTGTTCTCGG
TACTATAGGGCACCAGAGTTGATCTTTGGAGCCACTGATTATACCTCTAGTATAGATGTA
TGGTCTGCTGGCTGTGTGTTGGCTGAGCTGTTACTAGGACAACCAATATTTCCAGGGGAT
AGTGGTGTGGATCAGTTGGTAGAAATAATCAAGGTCCTGGGAACTCCAACAAGGGAGCAA
ATCAGAGAAATGAACCCAAACTACACAGAATTTAAATTCCCTCAAATTAAGGCACATCCT
TGGACTAAGGTCTTCCGACCCCGAACTCCACCGGAGGCAATTGCACTGTGTAGCCGTCTG
CTGGAGTATACACCAACTGCCCGACTAACACCACTGGAAGCTTGTGCACATTCATTTTTT
GATGAATTACGGGACCCAAATGTCAAACTACCAAATGGGCGAGACACACCTGCACTCTTC
AACTTCACCACTCAAGAACTGTCAAGTAATCCACCTCTGGCTACCATCCTTATTCCTCCT
CATGCTCGGATTCAAGCAGCTGCTTCAACCCCCACAAATGCCACAGCAGCGTCAGATGCT
AATACTGGAGACCGTGGACAGACCAATAATGCTGCTTCTGCATCAGCTTCCAACTCCACC
TGA
Chromosome Location
3
Locus
3q13.3
External Identifiers
ResourceLink
UniProtKB IDP49841
UniProtKB Entry NameGSK3B_HUMAN
GenBank Protein ID529237
GenBank Gene IDL33801
GenAtlas IDGSK3B
HGNC IDHGNC:4617
General References
  1. Stambolic V, Woodgett JR: Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem J. 1994 Nov 1;303 ( Pt 3):701-4. [Article]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  3. Lau KF, Miller CC, Anderton BH, Shaw PC: Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter. Genomics. 1999 Sep 1;60(2):121-8. [Article]
  4. Rhoads AR, Karkera JD, Detera-Wadleigh SD: Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway. Mol Psychiatry. 1999 Sep;4(5):437-42. [Article]
  5. Boyle WJ, Smeal T, Defize LH, Angel P, Woodgett JR, Karin M, Hunter T: Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell. 1991 Feb 8;64(3):573-84. [Article]
  6. Welsh GI, Proud CG: Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem J. 1993 Sep 15;294 ( Pt 3):625-9. [Article]
  7. Sutherland C, Leighton IA, Cohen P: Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem J. 1993 Nov 15;296 ( Pt 1):15-9. [Article]
  8. Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA: Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature. 1995 Dec 21-28;378(6559):785-9. [Article]
  9. Beals CR, Sheridan CM, Turck CW, Gardner P, Crabtree GR: Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3. Science. 1997 Mar 28;275(5308):1930-4. [Article]
  10. Hong YR, Chen CH, Cheng DS, Howng SL, Chow CC: Human dynamin-like protein interacts with the glycogen synthase kinase 3beta. Biochem Biophys Res Commun. 1998 Aug 28;249(3):697-703. [Article]
  11. Li Y, Bharti A, Chen D, Gong J, Kufe D: Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin. Mol Cell Biol. 1998 Dec;18(12):7216-24. [Article]
  12. Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S: Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11211-6. [Article]
  13. Hong YR, Chen CH, Chang JH, Wang S, Sy WD, Chou CK, Howng SL: Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):513-6. [Article]
  14. Nikoulina SE, Ciaraldi TP, Mudaliar S, Mohideen P, Carter L, Henry RR: Potential role of glycogen synthase kinase-3 in skeletal muscle insulin resistance of type 2 diabetes. Diabetes. 2000 Feb;49(2):263-71. [Article]
  15. Frame S, Cohen P, Biondi RM: A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol Cell. 2001 Jun;7(6):1321-7. [Article]
  16. Dai F, Yu L, He H, Chen Y, Yu J, Yang Y, Xu Y, Ling W, Zhao S: Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction. Biochem Biophys Res Commun. 2002 May 17;293(4):1191-6. [Article]
  17. Cho JH, Johnson GV: Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J Neurochem. 2004 Jan;88(2):349-58. [Article]
  18. Zhou BP, Deng J, Xia W, Xu J, Li YM, Gunduz M, Hung MC: Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat Cell Biol. 2004 Oct;6(10):931-40. Epub 2004 Sep 26. [Article]
  19. Hsu HC, Lee YL, Cheng TS, Howng SL, Chang LK, Lu PJ, Hong YR: Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain. Biochem Biophys Res Commun. 2005 Apr 15;329(3):1108-17. [Article]
  20. Yook JI, Li XY, Ota I, Fearon ER, Weiss SJ: Wnt-dependent regulation of the E-cadherin repressor snail. J Biol Chem. 2005 Mar 25;280(12):11740-8. Epub 2005 Jan 11. [Article]
  21. Kobayashi T, Hino S, Oue N, Asahara T, Zollo M, Yasui W, Kikuchi A: Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions. Mol Cell Biol. 2006 Feb;26(3):898-911. [Article]
  22. Yin L, Wang J, Klein PS, Lazar MA: Nuclear receptor Rev-erbalpha is a critical lithium-sensitive component of the circadian clock. Science. 2006 Feb 17;311(5763):1002-5. [Article]
  23. Luo W, Peterson A, Garcia BA, Coombs G, Kofahl B, Heinrich R, Shabanowitz J, Hunt DF, Yost HJ, Virshup DM: Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex. EMBO J. 2007 Mar 21;26(6):1511-21. Epub 2007 Feb 22. [Article]
  24. Hashimoto YK, Satoh T, Okamoto M, Takemori H: Importance of autophosphorylation at Ser186 in the A-loop of salt inducible kinase 1 for its sustained kinase activity. J Cell Biochem. 2008 Aug 1;104(5):1724-39. doi: 10.1002/jcb.21737. [Article]
  25. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [Article]
  26. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  27. Kandasamy AD, Schulz R: Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts. Cardiovasc Res. 2009 Sep 1;83(4):698-706. doi: 10.1093/cvr/cvp175. Epub 2009 Jun 3. [Article]
  28. Spengler ML, Kuropatwinski KK, Schumer M, Antoch MP: A serine cluster mediates BMAL1-dependent CLOCK phosphorylation and degradation. Cell Cycle. 2009 Dec 15;8(24):4138-46. Epub 2009 Dec 8. [Article]
  29. Oh M, Kim H, Yang I, Park JH, Cong WT, Baek MC, Bareiss S, Ki H, Lu Q, No J, Kwon I, Choi JK, Kim K: GSK-3 phosphorylates delta-catenin and negatively regulates its stability via ubiquitination/proteosome-mediated proteolysis. J Biol Chem. 2009 Oct 16;284(42):28579-89. doi: 10.1074/jbc.M109.002659. Epub 2009 Aug 25. [Article]
  30. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [Article]
  31. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  32. Castano Z, Gordon-Weeks PR, Kypta RM: The neuron-specific isoform of glycogen synthase kinase-3beta is required for axon growth. J Neurochem. 2010 Apr;113(1):117-30. doi: 10.1111/j.1471-4159.2010.06581.x. Epub 2010 Jan 12. [Article]
  33. Heyd F, Lynch KW: Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing. Mol Cell. 2010 Oct 8;40(1):126-37. doi: 10.1016/j.molcel.2010.09.013. [Article]
  34. Xie D, Gore C, Liu J, Pong RC, Mason R, Hao G, Long M, Kabbani W, Yu L, Zhang H, Chen H, Sun X, Boothman DA, Min W, Hsieh JT: Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis. Proc Natl Acad Sci U S A. 2010 Feb 9;107(6):2485-90. doi: 10.1073/pnas.0908133107. Epub 2010 Jan 13. [Article]
  35. Zaoui K, Benseddik K, Daou P, Salaun D, Badache A: ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18517-22. doi: 10.1073/pnas.1000975107. Epub 2010 Oct 11. [Article]
  36. Ali A, Hoeflich KP, Woodgett JR: Glycogen synthase kinase-3: properties, functions, and regulation. Chem Rev. 2001 Aug;101(8):2527-40. [Article]
  37. Lee J, Kim MS: The role of GSK3 in glucose homeostasis and the development of insulin resistance. Diabetes Res Clin Pract. 2007 Sep;77 Suppl 1:S49-57. Epub 2007 May 2. [Article]
  38. Rayasam GV, Tulasi VK, Sodhi R, Davis JA, Ray A: Glycogen synthase kinase 3: more than a namesake. Br J Pharmacol. 2009 Mar;156(6):885-98. doi: 10.1111/j.1476-5381.2008.00085.x. Epub 2009 Mar 4. [Article]
  39. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  40. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  41. Bose A, Mouton-Liger F, Paquet C, Mazot P, Vigny M, Gray F, Hugon J: Modulation of tau phosphorylation by the kinase PKR: implications in Alzheimer's disease. Brain Pathol. 2011 Mar;21(2):189-200. doi: 10.1111/j.1750-3639.2010.00437.x. Epub 2010 Oct 3. [Article]
  42. Sun L, Lv F, Guo X, Gao G: Glycogen synthase kinase 3beta (GSK3beta) modulates antiviral activity of zinc-finger antiviral protein (ZAP). J Biol Chem. 2012 Jun 29;287(27):22882-8. doi: 10.1074/jbc.M111.306373. Epub 2012 Apr 18. [Article]
  43. Feijs KL, Kleine H, Braczynski A, Forst AH, Herzog N, Verheugd P, Linzen U, Kremmer E, Luscher B: ARTD10 substrate identification on protein microarrays: regulation of GSK3beta by mono-ADP-ribosylation. Cell Commun Signal. 2013 Jan 19;11(1):5. doi: 10.1186/1478-811X-11-5. [Article]
  44. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  45. Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A: NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3beta resulting in the stabilization of MYCN in human neuroblastomas. PLoS Genet. 2014 Jan;10(1):e1003996. doi: 10.1371/journal.pgen.1003996. Epub 2014 Jan 2. [Article]
  46. Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH: Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 2001 Jun 15;105(6):721-32. [Article]
  47. Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD: The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. Structure. 2001 Dec;9(12):1143-52. [Article]
  48. Dajani R, Fraser E, Roe SM, Yeo M, Good VM, Thompson V, Dale TC, Pearl LH: Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex. EMBO J. 2003 Feb 3;22(3):494-501. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01356Lithium cationexperimentalunknowninhibitorDetails
DB017723-[3-(2,3-Dihydroxy-Propylamino)-Phenyl]-4-(5-Fluoro-1-Methyl-1h-Indol-3-Yl)-Pyrrole-2,5-DioneexperimentalunknownDetails
DB01793SB-409513experimentalunknownDetails
DB01950AR-AO-14418experimentalunknownDetails
DB02010StaurosporineexperimentalunknownDetails
DB02052Indirubin-3'-monoximeexperimentalunknownDetails
DB04014AlsterpaulloneexperimentalunknownDetails
DB04395Phosphoaminophosphonic Acid-Adenylate EsterexperimentalunknownDetails
DB070142-(1,3-benzodioxol-5-yl)-5-[(3-fluoro-4-methoxybenzyl)sulfanyl]-1,3,4-oxadiazoleexperimentalunknownDetails
DB070585-[1-(4-methoxyphenyl)-1H-benzimidazol-6-yl]-1,3,4-oxadiazole-2(3H)-thioneexperimentalunknownDetails
DB07149(7S)-2-(2-aminopyrimidin-4-yl)-7-(2-fluoroethyl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-oneexperimentalunknownDetails
DB034446-bromoindirubin-3'-oximeexperimentalunknownDetails
DB07584N-[2-(5-methyl-4H-1,2,4-triazol-3-yl)phenyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amineexperimentalunknownDetails
DB075855-(5-chloro-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-4,5,6,7-tetrahydro-1H-imidazo[4,5-c]pyridineexperimentalunknownDetails
DB076763-({[(3S)-3,4-dihydroxybutyl]oxy}amino)-1H,2'H-2,3'-biindol-2'-oneexperimentalunknownDetails
DB07812N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamideexperimentalunknownDetails
DB078594-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINEexperimentalunknownDetails
DB07947ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDEexperimentalunknownDetails
DB08073(2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINEexperimentalunknownDetails
DB12129Tideglusibinvestigational, withdrawnyesantagonistDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails
DB14507Lithium citrateapprovedunknownDetails
DB14508Lithium succinateexperimentalunknownDetails
DB14509Lithium carbonateapprovedunknownDetails