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P49841

- GSK3B_HUMAN

UniProt

P49841 - GSK3B_HUMAN

Protein

Glycogen synthase kinase-3 beta

Gene

GSK3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    Functioni

    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.15 Publications

    Catalytic activityi

    ATP + [tau protein] = ADP + [tau protein] phosphate.
    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by phosphorylation at Tyr-216. In response to insulin, inhibited by phosphorylation at Ser-9 by PKB/AKT1 and RPS6KA3; phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. Inhibited by lithium.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851ATPPROSITE-ProRule annotation
    Active sitei181 – 1811Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi62 – 709ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. beta-catenin binding Source: BHF-UCL
    3. kinase activity Source: UniProtKB
    4. NF-kappaB binding Source: UniProtKB
    5. p53 binding Source: MGI
    6. protein binding Source: UniProtKB
    7. protein kinase A catalytic subunit binding Source: BHF-UCL
    8. protein kinase binding Source: UniProtKB
    9. protein serine/threonine kinase activity Source: UniProtKB
    10. RNA polymerase II transcription factor binding Source: UniProtKB
    11. tau-protein kinase activity Source: UniProtKB
    12. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. canonical Wnt signaling pathway Source: UniProtKB
    3. canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: Ensembl
    4. cell migration Source: Ensembl
    5. cellular response to interleukin-3 Source: UniProtKB
    6. cellular response to mechanical stimulus Source: Ensembl
    7. circadian rhythm Source: UniProtKB
    8. epidermal growth factor receptor signaling pathway Source: Reactome
    9. epithelial to mesenchymal transition Source: UniProtKB
    10. ER overload response Source: MGI
    11. establishment of cell polarity Source: Ensembl
    12. extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
    13. fat cell differentiation Source: Ensembl
    14. Fc-epsilon receptor signaling pathway Source: Reactome
    15. fibroblast growth factor receptor signaling pathway Source: Reactome
    16. glycogen metabolic process Source: BHF-UCL
    17. hippocampus development Source: BHF-UCL
    18. hypermethylation of CpG island Source: Ensembl
    19. innate immune response Source: Reactome
    20. intracellular signal transduction Source: MGI
    21. myoblast fusion Source: Ensembl
    22. negative regulation of apoptotic process Source: MGI
    23. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    24. negative regulation of cardiac muscle hypertrophy Source: Ensembl
    25. negative regulation of dendrite morphogenesis Source: Ensembl
    26. negative regulation of glycogen (starch) synthase activity Source: UniProtKB
    27. negative regulation of glycogen biosynthetic process Source: UniProtKB
    28. negative regulation of MAP kinase activity Source: Ensembl
    29. negative regulation of NFAT protein import into nucleus Source: UniProtKB
    30. negative regulation of protein binding Source: BHF-UCL
    31. negative regulation of protein complex assembly Source: BHF-UCL
    32. negative regulation of type B pancreatic cell development Source: UniProtKB
    33. neurotrophin TRK receptor signaling pathway Source: Reactome
    34. organ morphogenesis Source: Ensembl
    35. peptidyl-serine phosphorylation Source: BHF-UCL
    36. phosphatidylinositol-mediated signaling Source: Reactome
    37. positive regulation of cell-matrix adhesion Source: BHF-UCL
    38. positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
    39. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    40. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
    41. positive regulation of protein binding Source: UniProtKB
    42. positive regulation of protein catabolic process Source: BHF-UCL
    43. positive regulation of protein complex assembly Source: BHF-UCL
    44. positive regulation of protein export from nucleus Source: MGI
    45. positive regulation of Rac GTPase activity Source: BHF-UCL
    46. positive regulation of stem cell differentiation Source: Ensembl
    47. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    48. protein export from nucleus Source: Ensembl
    49. protein localization to microtubule Source: Ensembl
    50. protein phosphorylation Source: UniProtKB
    51. re-entry into mitotic cell cycle Source: Ensembl
    52. regulation of gene expression by genetic imprinting Source: Ensembl
    53. regulation of microtubule-based process Source: UniProtKB
    54. regulation of neuronal synaptic plasticity Source: Ensembl
    55. response to drug Source: Ensembl
    56. response to lithium ion Source: Ensembl
    57. superior temporal gyrus development Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Signal transduction inhibitor, Transferase

    Keywords - Biological processi

    Biological rhythms, Carbohydrate metabolism, Differentiation, Glycogen metabolism, Neurogenesis, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.26. 2681.
    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    SignaLinkiP49841.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen synthase kinase-3 beta (EC:2.7.11.26)
    Short name:
    GSK-3 beta
    Alternative name(s):
    Serine/threonine-protein kinase GSK3B (EC:2.7.11.1)
    Gene namesi
    Name:GSK3B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4617. GSK3B.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane
    Note: The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.

    GO - Cellular componenti

    1. beta-catenin destruction complex Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. dendritic shaft Source: Ensembl
    6. dendritic spine Source: Ensembl
    7. growth cone Source: Ensembl
    8. membrane raft Source: Ensembl
    9. neuronal cell body Source: Ensembl
    10. nucleus Source: UniProtKB
    11. perinuclear region of cytoplasm Source: Ensembl
    12. plasma membrane Source: UniProtKB
    13. ribonucleoprotein complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91S → A: Loss of phosphorylation; No inhibition of activity and constitutively active. 1 Publication
    Mutagenesisi96 – 961R → A: Prevents the phosphorylation of phosphate-primed glycogen synthase. 1 Publication
    Mutagenesisi128 – 1281L → A: Abolishes activity toward AXIN1. 1 Publication

    Keywords - Diseasei

    Alzheimer disease, Diabetes mellitus

    Organism-specific databases

    PharmGKBiPA29009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Glycogen synthase kinase-3 betaPRO_0000085980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK35 Publications
    Modified residuei216 – 2161Phosphotyrosine2 Publications
    Modified residuei389 – 3891PhosphoserineBy similarity
    Modified residuei390 – 3901Phosphothreonine2 Publications
    Modified residuei402 – 4021Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216.8 Publications
    Mono-ADP-ribosylation by PARP10 negatively regulates kinase activity.

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49841.
    PaxDbiP49841.
    PRIDEiP49841.

    PTM databases

    PhosphoSiteiP49841.

    Expressioni

    Tissue specificityi

    Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney. Colocalizes with EIF2AK2/PKR and TAU in the Alzheimer disease (AD) brain.1 Publication

    Gene expression databases

    ArrayExpressiP49841.
    BgeeiP49841.
    CleanExiHS_GSK3B.
    GenevestigatoriP49841.

    Organism-specific databases

    HPAiCAB016263.
    HPA028017.

    Interactioni

    Subunit structurei

    Monomer. Interacts with ARRB2, DISC1 and ZBED3 By similarity. Interacts with CABYR, MMP2, MUC1, NIN and PRUNE Interacts with AXIN1; the interaction mediates hyperphosphorylation of CTNNB1 leading to its ubiquitination and destruction. Interacts with and phosphorylates SNAI1. Interacts with DNM1L (via a C-terminal domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts with SGK3. Interacts with DAB2IP (via C2 domain); the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA. Interacts with the CLOCK-ARNTL/BMAL1 heterodimer. Interacts with the ARNTL/BMAL1.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317493EBI-373586,EBI-296087
    AKT2P317512EBI-373586,EBI-296058
    AXIN1O1516932EBI-373586,EBI-710484
    Axin1O356255EBI-373586,EBI-2365912From a different organism.
    Axin1Q14DJ82EBI-373586,EBI-4312125From a different organism.
    BICD1Q96G017EBI-373586,EBI-1104509
    CTNNB1P352229EBI-373586,EBI-491549
    DAB2IPQ5VWQ82EBI-373586,EBI-2871881
    DAB2IPQ5VWQ8-22EBI-373586,EBI-9543020
    DACT1Q9NYF03EBI-373586,EBI-3951744
    DEAF1O753982EBI-373586,EBI-718185
    Disc1Q811T94EBI-373586,EBI-2298259From a different organism.
    GYS1P138073EBI-373586,EBI-740553
    LRP6O755814EBI-373586,EBI-910915
    LRRK2Q5S0077EBI-373586,EBI-5323863
    Mapk1P630852EBI-373586,EBI-397697From a different organism.
    MAPTP106362EBI-373586,EBI-366182
    MAPTP10636-89EBI-373586,EBI-366233
    NINQ8N4C63EBI-373586,EBI-1164022
    PRKACAP176125EBI-373586,EBI-476586
    RELBQ012014EBI-373586,EBI-357837
    SMAD1Q157972EBI-373586,EBI-1567153
    SNAI1O958635EBI-373586,EBI-1045459
    SNCAP378402EBI-373586,EBI-985879
    STYK1Q6J9G02EBI-373586,EBI-6424915
    TP53P046373EBI-373586,EBI-366083
    TRIM29Q141342EBI-373586,EBI-702370
    YWHAZP631044EBI-373586,EBI-347088
    ZFPM1Q8IX072EBI-373586,EBI-3942619

    Protein-protein interaction databases

    BioGridi109187. 243 interactions.
    DIPiDIP-878N.
    IntActiP49841. 184 interactions.
    MINTiMINT-105006.
    STRINGi9606.ENSP00000324806.

    Structurei

    Secondary structure

    1
    420
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Beta strandi27 – 293
    Beta strandi32 – 343
    Beta strandi38 – 4811
    Beta strandi52 – 6413
    Beta strandi66 – 7510
    Turni76 – 783
    Beta strandi81 – 888
    Beta strandi91 – 933
    Helixi96 – 1027
    Beta strandi112 – 1209
    Turni121 – 1244
    Beta strandi125 – 1339
    Beta strandi136 – 1383
    Helixi139 – 14810
    Helixi155 – 17319
    Turni174 – 1763
    Helixi184 – 1863
    Beta strandi187 – 1904
    Turni191 – 1944
    Beta strandi195 – 1984
    Beta strandi209 – 2113
    Helixi220 – 2223
    Helixi225 – 2284
    Helixi237 – 25216
    Helixi262 – 27312
    Helixi278 – 2847
    Helixi286 – 2883
    Beta strandi289 – 2913
    Helixi301 – 3044
    Helixi311 – 32010
    Helixi325 – 3273
    Helixi331 – 3355
    Helixi338 – 3447
    Beta strandi345 – 3473
    Helixi364 – 3674
    Helixi371 – 3733
    Helixi374 – 3774
    Turni380 – 3834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GNGX-ray2.60A/B27-393[»]
    1H8FX-ray2.80A/B35-386[»]
    1I09X-ray2.70A/B1-420[»]
    1J1BX-ray1.80A/B1-420[»]
    1J1CX-ray2.10A/B1-420[»]
    1O6KX-ray1.70C3-12[»]
    1O6LX-ray1.60C3-12[»]
    1O9UX-ray2.40A35-384[»]
    1PYXX-ray2.40A/B1-420[»]
    1Q3DX-ray2.20A/B2-420[»]
    1Q3WX-ray2.30A/B2-420[»]
    1Q41X-ray2.10A/B2-420[»]
    1Q4LX-ray2.77A/B2-420[»]
    1Q5KX-ray1.94A/B7-420[»]
    1R0EX-ray2.25A/B35-420[»]
    1UV5X-ray2.80A35-384[»]
    2JDOX-ray1.80C3-12[»]
    2JDRX-ray2.30C3-12[»]
    2JLDX-ray2.35A/B1-420[»]
    2O5KX-ray3.20A29-393[»]
    2OW3X-ray2.80A/B35-386[»]
    2UW9X-ray2.10C3-12[»]
    2X39X-ray1.93C3-12[»]
    2XH5X-ray2.72C3-12[»]
    3CQUX-ray2.20C3-12[»]
    3CQWX-ray2.00C3-12[»]
    3DU8X-ray2.20A/B1-420[»]
    3E87X-ray2.30C/D3-12[»]
    3E88X-ray2.50C/D3-12[»]
    3E8DX-ray2.70C/D3-12[»]
    3F7ZX-ray2.40A/B35-383[»]
    3F88X-ray2.60A/B35-383[»]
    3GB2X-ray2.40A34-383[»]
    3I4BX-ray2.30A/B7-420[»]
    3L1SX-ray2.90A/B7-420[»]
    3M1SX-ray3.13A/B1-420[»]
    3MV5X-ray2.47C3-12[»]
    3OW4X-ray2.60C/D3-12[»]
    3PUPX-ray2.99A/B1-420[»]
    3Q3BX-ray2.70A/B2-420[»]
    3QKKX-ray2.30C3-12[»]
    3SAYX-ray2.23A/B1-420[»]
    3SD0X-ray2.70A/B35-384[»]
    3ZDIX-ray2.64A35-384[»]
    3ZRKX-ray2.37A/B23-393[»]
    3ZRLX-ray2.48A/B23-393[»]
    3ZRMX-ray2.49A/B23-393[»]
    4ACCX-ray2.21A/B1-420[»]
    4ACDX-ray2.60A/B1-420[»]
    4ACGX-ray2.60A/B1-420[»]
    4ACHX-ray2.60A/B1-420[»]
    4AFJX-ray1.98A/B27-393[»]
    4B7TX-ray2.77A35-384[»]
    4DITX-ray2.60A27-393[»]
    4EKKX-ray2.80C/D3-12[»]
    4IQ6X-ray3.12A/B1-420[»]
    4J1RX-ray2.70A/B/C/D1-420[»]
    4J71X-ray2.31A/B1-420[»]
    4NM0X-ray2.50A1-383[»]
    4NM3X-ray2.10A1-383[»]
    4NM5X-ray2.30A13-383[»]
    4NM7X-ray2.30A13-383[»]
    DisProtiDP00385.
    ProteinModelPortaliP49841.
    SMRiP49841. Positions 6-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49841.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 340285Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233017.
    HOVERGENiHBG014652.
    KOiK03083.
    OMAiNAGERVQ.
    OrthoDBiEOG7TF78V.
    PhylomeDBiP49841.
    TreeFamiTF101104.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49841-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR    50
    PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI 100
    MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK 150
    QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD 200
    FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL 250
    LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP 300
    WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL 350
    PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA 400
    NTGDRGQTNN AASASASNST 420
    Length:420
    Mass (Da):46,744
    Last modified:May 2, 2002 - v2
    Checksum:i4ACC24D00CDBB9C3
    GO
    Isoform 2 (identifier: P49841-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         303-303: K → KDSSGTGHFTSGVR

    Note: No experimental confirmation available.

    Show »
    Length:433
    Mass (Da):48,034
    Checksum:i540F853E1603A080
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281V → G in AAD48517. (PubMed:10486203)Curated
    Sequence conflicti350 – 3501L → H in AAA66475. (PubMed:7980435)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei303 – 3031K → KDSSGTGHFTSGVR in isoform 2. 1 PublicationVSP_004790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33801 mRNA. Translation: AAA66475.1.
    CH471052 Genomic DNA. Translation: EAW79533.1.
    CH471052 Genomic DNA. Translation: EAW79536.1.
    BC000251 mRNA. Translation: AAH00251.1.
    BC012760 mRNA. Translation: AAH12760.1.
    AF074333 Genomic DNA. Translation: AAD48517.1.
    AF098789 Genomic DNA. Translation: AAC69340.1.
    CCDSiCCDS2996.1. [P49841-2]
    CCDS54628.1. [P49841-1]
    PIRiS53324.
    RefSeqiNP_001139628.1. NM_001146156.1. [P49841-1]
    NP_002084.2. NM_002093.3. [P49841-2]
    UniGeneiHs.445733.

    Genome annotation databases

    EnsembliENST00000264235; ENSP00000264235; ENSG00000082701. [P49841-1]
    ENST00000316626; ENSP00000324806; ENSG00000082701. [P49841-2]
    GeneIDi2932.
    KEGGihsa:2932.
    UCSCiuc003edn.3. human. [P49841-2]
    uc003edo.3. human. [P49841-1]

    Polymorphism databases

    DMDMi20455502.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33801 mRNA. Translation: AAA66475.1 .
    CH471052 Genomic DNA. Translation: EAW79533.1 .
    CH471052 Genomic DNA. Translation: EAW79536.1 .
    BC000251 mRNA. Translation: AAH00251.1 .
    BC012760 mRNA. Translation: AAH12760.1 .
    AF074333 Genomic DNA. Translation: AAD48517.1 .
    AF098789 Genomic DNA. Translation: AAC69340.1 .
    CCDSi CCDS2996.1. [P49841-2 ]
    CCDS54628.1. [P49841-1 ]
    PIRi S53324.
    RefSeqi NP_001139628.1. NM_001146156.1. [P49841-1 ]
    NP_002084.2. NM_002093.3. [P49841-2 ]
    UniGenei Hs.445733.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GNG X-ray 2.60 A/B 27-393 [» ]
    1H8F X-ray 2.80 A/B 35-386 [» ]
    1I09 X-ray 2.70 A/B 1-420 [» ]
    1J1B X-ray 1.80 A/B 1-420 [» ]
    1J1C X-ray 2.10 A/B 1-420 [» ]
    1O6K X-ray 1.70 C 3-12 [» ]
    1O6L X-ray 1.60 C 3-12 [» ]
    1O9U X-ray 2.40 A 35-384 [» ]
    1PYX X-ray 2.40 A/B 1-420 [» ]
    1Q3D X-ray 2.20 A/B 2-420 [» ]
    1Q3W X-ray 2.30 A/B 2-420 [» ]
    1Q41 X-ray 2.10 A/B 2-420 [» ]
    1Q4L X-ray 2.77 A/B 2-420 [» ]
    1Q5K X-ray 1.94 A/B 7-420 [» ]
    1R0E X-ray 2.25 A/B 35-420 [» ]
    1UV5 X-ray 2.80 A 35-384 [» ]
    2JDO X-ray 1.80 C 3-12 [» ]
    2JDR X-ray 2.30 C 3-12 [» ]
    2JLD X-ray 2.35 A/B 1-420 [» ]
    2O5K X-ray 3.20 A 29-393 [» ]
    2OW3 X-ray 2.80 A/B 35-386 [» ]
    2UW9 X-ray 2.10 C 3-12 [» ]
    2X39 X-ray 1.93 C 3-12 [» ]
    2XH5 X-ray 2.72 C 3-12 [» ]
    3CQU X-ray 2.20 C 3-12 [» ]
    3CQW X-ray 2.00 C 3-12 [» ]
    3DU8 X-ray 2.20 A/B 1-420 [» ]
    3E87 X-ray 2.30 C/D 3-12 [» ]
    3E88 X-ray 2.50 C/D 3-12 [» ]
    3E8D X-ray 2.70 C/D 3-12 [» ]
    3F7Z X-ray 2.40 A/B 35-383 [» ]
    3F88 X-ray 2.60 A/B 35-383 [» ]
    3GB2 X-ray 2.40 A 34-383 [» ]
    3I4B X-ray 2.30 A/B 7-420 [» ]
    3L1S X-ray 2.90 A/B 7-420 [» ]
    3M1S X-ray 3.13 A/B 1-420 [» ]
    3MV5 X-ray 2.47 C 3-12 [» ]
    3OW4 X-ray 2.60 C/D 3-12 [» ]
    3PUP X-ray 2.99 A/B 1-420 [» ]
    3Q3B X-ray 2.70 A/B 2-420 [» ]
    3QKK X-ray 2.30 C 3-12 [» ]
    3SAY X-ray 2.23 A/B 1-420 [» ]
    3SD0 X-ray 2.70 A/B 35-384 [» ]
    3ZDI X-ray 2.64 A 35-384 [» ]
    3ZRK X-ray 2.37 A/B 23-393 [» ]
    3ZRL X-ray 2.48 A/B 23-393 [» ]
    3ZRM X-ray 2.49 A/B 23-393 [» ]
    4ACC X-ray 2.21 A/B 1-420 [» ]
    4ACD X-ray 2.60 A/B 1-420 [» ]
    4ACG X-ray 2.60 A/B 1-420 [» ]
    4ACH X-ray 2.60 A/B 1-420 [» ]
    4AFJ X-ray 1.98 A/B 27-393 [» ]
    4B7T X-ray 2.77 A 35-384 [» ]
    4DIT X-ray 2.60 A 27-393 [» ]
    4EKK X-ray 2.80 C/D 3-12 [» ]
    4IQ6 X-ray 3.12 A/B 1-420 [» ]
    4J1R X-ray 2.70 A/B/C/D 1-420 [» ]
    4J71 X-ray 2.31 A/B 1-420 [» ]
    4NM0 X-ray 2.50 A 1-383 [» ]
    4NM3 X-ray 2.10 A 1-383 [» ]
    4NM5 X-ray 2.30 A 13-383 [» ]
    4NM7 X-ray 2.30 A 13-383 [» ]
    DisProti DP00385.
    ProteinModelPortali P49841.
    SMRi P49841. Positions 6-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109187. 243 interactions.
    DIPi DIP-878N.
    IntActi P49841. 184 interactions.
    MINTi MINT-105006.
    STRINGi 9606.ENSP00000324806.

    Chemistry

    BindingDBi P49841.
    ChEMBLi CHEMBL2095188.
    DrugBanki DB01356. Lithium.
    GuidetoPHARMACOLOGYi 2030.

    PTM databases

    PhosphoSitei P49841.

    Polymorphism databases

    DMDMi 20455502.

    Proteomic databases

    MaxQBi P49841.
    PaxDbi P49841.
    PRIDEi P49841.

    Protocols and materials databases

    DNASUi 2932.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264235 ; ENSP00000264235 ; ENSG00000082701 . [P49841-1 ]
    ENST00000316626 ; ENSP00000324806 ; ENSG00000082701 . [P49841-2 ]
    GeneIDi 2932.
    KEGGi hsa:2932.
    UCSCi uc003edn.3. human. [P49841-2 ]
    uc003edo.3. human. [P49841-1 ]

    Organism-specific databases

    CTDi 2932.
    GeneCardsi GC03M119540.
    HGNCi HGNC:4617. GSK3B.
    HPAi CAB016263.
    HPA028017.
    MIMi 605004. gene.
    neXtProti NX_P49841.
    PharmGKBi PA29009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233017.
    HOVERGENi HBG014652.
    KOi K03083.
    OMAi NAGERVQ.
    OrthoDBi EOG7TF78V.
    PhylomeDBi P49841.
    TreeFami TF101104.

    Enzyme and pathway databases

    BRENDAi 2.7.11.26. 2681.
    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    SignaLinki P49841.

    Miscellaneous databases

    ChiTaRSi GSK3B. human.
    EvolutionaryTracei P49841.
    GeneWikii GSK3B.
    GenomeRNAii 2932.
    NextBioi 11619.
    PROi P49841.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49841.
    Bgeei P49841.
    CleanExi HS_GSK3B.
    Genevestigatori P49841.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation."
      Stambolic V., Woodgett J.R.
      Biochem. J. 303:701-704(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-9.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Eye and Placenta.
    4. "Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter."
      Lau K.F., Miller C.C.J., Anderton B.H., Shaw P.C.
      Genomics 60:121-128(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
    5. "Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway."
      Rhoads A.R., Karkera J.D., Detera-Wadleigh S.D.
      Mol. Psychiatry 4:437-442(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-202.
    6. "Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity."
      Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M., Hunter T.
      Cell 64:573-584(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF JUN.
    7. "Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B."
      Welsh G.I., Proud C.G.
      Biochem. J. 294:625-629(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF EIF2BE/EIF2B5.
    8. "Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling."
      Sutherland C., Leighton I.A., Cohen P.
      Biochem. J. 296:15-19(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-9.
    9. "Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B."
      Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., Hemmings B.A.
      Nature 378:785-789(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION BY AKT1.
    10. "Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3."
      Beals C.R., Sheridan C.M., Turck C.W., Gardner P., Crabtree G.R.
      Science 275:1930-1934(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NFATC1/NFATC.
    11. "Human dynamin-like protein interacts with the glycogen synthase kinase 3beta."
      Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.
      Biochem. Biophys. Res. Commun. 249:697-703(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNM1L.
      Tissue: Liver.
    12. "Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin."
      Li Y., Bharti A., Chen D., Gong J., Kufe D.
      Mol. Cell. Biol. 18:7216-7224(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MUC1, FUNCTION.
    13. "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase."
      Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.
      Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    14. "Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta."
      Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K., Howng S.-L.
      Biochim. Biophys. Acta 1492:513-516(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIN.
    15. "Potential role of glycogen synthase kinase-3 in skeletal muscle insulin resistance of type 2 diabetes."
      Nikoulina S.E., Ciaraldi T.P., Mudaliar S., Mohideen P., Carter L., Henry R.R.
      Diabetes 49:263-271(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH DIABETES MELLITUS.
    16. "A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation."
      Frame S., Cohen P., Biondi R.M.
      Mol. Cell 7:1321-1327(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-96 AND LEU-128.
    17. "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction."
      Dai F., Yu L., He H., Chen Y., Yu J., Yang Y., Xu Y., Ling W., Zhao S.
      Biochem. Biophys. Res. Commun. 293:1191-1196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-9 BY SGK3, INTERACTION WITH SGK3.
    18. "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."
      Cho J.H., Johnson G.V.
      J. Neurochem. 88:349-358(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT/TAU.
    19. "Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition."
      Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., Hung M.C.
      Nat. Cell Biol. 6:931-940(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNAI1, SUBCELLULAR LOCATION.
    20. "Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain."
      Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J., Hong Y.-R.
      Biochem. Biophys. Res. Commun. 329:1108-1117(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABYR.
    21. "Wnt-dependent regulation of the E-cadherin repressor snail."
      Yook J.I., Li X.Y., Ota I., Fearon E.R., Weiss S.J.
      J. Biol. Chem. 280:11740-11748(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNAI1.
    22. "Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions."
      Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A.
      Mol. Cell. Biol. 26:898-911(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRUNE.
    23. "Nuclear receptor Rev-erbalpha is a critical lithium-sensitive component of the circadian clock."
      Yin L., Wang J., Klein P.S., Lazar M.A.
      Science 311:1002-1005(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-9.
    24. "Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex."
      Luo W., Peterson A., Garcia B.A., Coombs G., Kofahl B., Heinrich R., Shabanowitz J., Hunt D.F., Yost H.J., Virshup D.M.
      EMBO J. 26:1511-1521(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1.
    25. "Importance of autophosphorylation at Ser186 in the A-loop of salt inducible kinase 1 for its sustained kinase activity."
      Hashimoto Y.K., Satoh T., Okamoto M., Takemori H.
      J. Cell. Biochem. 104:1724-1739(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SIK1.
    26. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts."
      Kandasamy A.D., Schulz R.
      Cardiovasc. Res. 83:698-706(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MMP2.
    29. "A serine cluster mediates BMAL1-dependent CLOCK phosphorylation and degradation."
      Spengler M.L., Kuropatwinski K.K., Schumer M., Antoch M.P.
      Cell Cycle 8:4138-4146(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CLOCK-ARNTL/BMAL1.
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    32. "Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing."
      Heyd F., Lynch K.W.
      Mol. Cell 40:126-137(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
      Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
      Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP AND PPP2CA.
    34. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
      Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
      Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-9.
    35. "Glycogen synthase kinase-3: properties, functions, and regulation."
      Ali A., Hoeflich K.P., Woodgett J.R.
      Chem. Rev. 101:2527-2540(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
    36. "The role of GSK3 in glucose homeostasis and the development of insulin resistance."
      Lee J., Kim M.S.
      Diabetes Res. Clin. Pract. 77:S49-S57(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    37. Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
    38. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Modulation of tau phosphorylation by the kinase PKR: implications in Alzheimer's disease."
      Bose A., Mouton-Liger F., Paquet C., Mazot P., Vigny M., Gray F., Hugon J.
      Brain Pathol. 21:189-200(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    41. "Glycogen synthase kinase 3? (GSK3?) modulates antiviral activity of zinc-finger antiviral protein (ZAP)."
      Sun L., Lv F., Guo X., Gao G.
      J. Biol. Chem. 287:22882-22888(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    42. "ARTD10 substrate identification on protein microarrays: regulation of GSK3beta by mono-ADP-ribosylation."
      Feijs K.L., Kleine H., Braczynski A., Forst A.H., Herzog N., Verheugd P., Linzen U., Kremmer E., Luscher B.
      Cell Commun. Signal. 11:5-5(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION BY PARP10.
    43. "Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition."
      Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H.
      Cell 105:721-732(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-386.
    44. "The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation."
      Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R., Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G., Reith A.D.
      Structure 9:1143-1152(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-393 OF PHOSPHORYLATED GSK3B.
    45. "Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex."
      Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H.
      EMBO J. 22:494-501(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-384 IN COMPLEX WITH AXIN1, INTERACTION WITH AXIN1 AND FRAT1, FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-216.

    Entry informationi

    Entry nameiGSK3B_HUMAN
    AccessioniPrimary (citable) accession number: P49841
    Secondary accession number(s): D3DN89, Q9BWH3, Q9UL47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 184 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Higher expression and activity of GSK3B are found in the skeletal muscle (vastus lateralis) of patients with type 2 diabetes (PubMed:10868943). Several potent GSK3 (GSK3A and GSK3B) inhibitors have been identified and characterized in preclinical models for treatments of type 2 diabetes (PubMed:19366350).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3