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P49841

- GSK3B_HUMAN

UniProt

P49841 - GSK3B_HUMAN

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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

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 – 851ATP By similarity
Active sitei181 – 1811Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 709ATP By similarity

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
Complete GO annotation...

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.3 Publications

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
Complete GO annotation...

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 SGK34 Publications
Modified residuei216 – 2161Phosphotyrosine1 Publication
Modified residuei389 – 3891Phosphoserine By similarity
Modified residuei390 – 3901Phosphothreonine1 Publication
Modified residuei402 – 4021Phosphothreonine1 Publication

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-216.6 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/BMAL1.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317493EBI-373586,EBI-296087
AKT2P317512EBI-373586,EBI-296058
AXIN1O1516931EBI-373586,EBI-710484
Axin1O356254EBI-373586,EBI-2365912From a different organism.
Axin1Q14DJ82EBI-373586,EBI-4312125From a different organism.
BICD1Q96G017EBI-373586,EBI-1104509
CTNNB1P352228EBI-373586,EBI-491549
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
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. 241 interactions.
DIPiDIP-878N.
IntActiP49841. 174 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.

Miscellaneous databases

EvolutionaryTraceiP49841.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 340285Protein kinaseAdd
BLAST

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei303 – 3031K → KDSSGTGHFTSGVR in isoform 2. VSP_004790

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281V → G in AAD48517. 1 Publication
Sequence conflicti350 – 3501L → H in AAA66475. 1 Publication

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. 241 interactions.
DIPi DIP-878N.
IntActi P49841. 174 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 183 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 (1 Publication). Several potent GSK3 (GSK3A and GSK3B) inhibitors have been identified and characterized in preclinical models for treatments of type 2 diabetes (1 Publication).

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

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