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Protein

Glycogen synthase kinase-3 beta

Gene

GSK3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 851ATPPROSITE-ProRule annotation
Active sitei181 – 1811Proton acceptor

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • beta-catenin binding Source: BHF-UCL
  • kinase activity Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • p53 binding Source: MGI
  • protein kinase A catalytic subunit binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: UniProtKB
  • tau-protein kinase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

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_19199. CRMPs in Sema3A signaling.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_355468. Constitutive Signaling by AKT1 E17K in Cancer.
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 Componenti: 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

  • beta-catenin destruction complex Source: UniProtKB
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic shaft Source: Ensembl
  • dendritic spine Source: Ensembl
  • growth cone Source: Ensembl
  • membrane raft Source: Ensembl
  • neuronal cell body Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: UniProtKB
  • 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.

Chemistry

DrugBankiDB01356. Lithium.

Polymorphism and mutation databases

BioMutaiGSK3B.
DMDMi20455502.

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 – 3891PhosphoserineBy 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

BgeeiP49841.
CleanExiHS_GSK3B.
ExpressionAtlasiP49841. baseline and differential.
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
AXIN1O1516942EBI-373586,EBI-710484
Axin1O356255EBI-373586,EBI-2365912From a different organism.
Axin1Q14DJ82EBI-373586,EBI-4312125From a different organism.
BICD1Q96G017EBI-373586,EBI-1104509
CTNNB1P3522215EBI-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
UBR5O950718EBI-373586,EBI-358329
YWHAZP631044EBI-373586,EBI-347088
ZFPM1Q8IX072EBI-373586,EBI-3942619

Protein-protein interaction databases

BioGridi109187. 255 interactions.
DIPiDIP-878N.
IntActiP49841. 188 interactions.
MINTiMINT-105006.
STRINGi9606.ENSP00000324806.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
HOVERGENiHBG014652.
InParanoidiP49841.
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.
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. AlignAdd to basket

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

Also known as: GSK-3beta1

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

        10         20         30         40         50
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR
60 70 80 90 100
PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI
110 120 130 140 150
MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK
160 170 180 190 200
QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD
210 220 230 240 250
FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL
260 270 280 290 300
LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP
310 320 330 340 350
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL
360 370 380 390 400
PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA
410 420
NTGDRGQTNN AASASASNST
Length:420
Mass (Da):46,744
Last modified:May 2, 2002 - v2
Checksum:i4ACC24D00CDBB9C3
GO
Isoform 2 (identifier: P49841-2) [UniParc]FASTAAdd to basket

Also known as: GSK-3beta2, neuron-specific

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

Note: May play a specific role in axon growth and neurite outgrowth. Reduced binding to AXIN1, reduced ability to phosphorylate MAPT/TAU.1 Publication

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:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi109187. 255 interactions.
DIPiDIP-878N.
IntActiP49841. 188 interactions.
MINTiMINT-105006.
STRINGi9606.ENSP00000324806.

Chemistry

BindingDBiP49841.
ChEMBLiCHEMBL2095188.
DrugBankiDB01356. Lithium.
GuidetoPHARMACOLOGYi2030.

PTM databases

PhosphoSiteiP49841.

Polymorphism and mutation databases

BioMutaiGSK3B.
DMDMi20455502.

Proteomic databases

MaxQBiP49841.
PaxDbiP49841.
PRIDEiP49841.

Protocols and materials databases

DNASUi2932.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi2932.
GeneCardsiGC03M119540.
HGNCiHGNC:4617. GSK3B.
HPAiCAB016263.
HPA028017.
MIMi605004. gene.
neXtProtiNX_P49841.
PharmGKBiPA29009.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
HOVERGENiHBG014652.
InParanoidiP49841.
KOiK03083.
OMAiNAGERVQ.
OrthoDBiEOG7TF78V.
PhylomeDBiP49841.
TreeFamiTF101104.

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_19199. CRMPs in Sema3A signaling.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_355468. Constitutive Signaling by AKT1 E17K in Cancer.
SignaLinkiP49841.

Miscellaneous databases

ChiTaRSiGSK3B. human.
EvolutionaryTraceiP49841.
GeneWikiiGSK3B.
GenomeRNAii2932.
NextBioi11619.
PROiP49841.
SOURCEiSearch...

Gene expression databases

BgeeiP49841.
CleanExiHS_GSK3B.
ExpressionAtlasiP49841. baseline and differential.
GenevestigatoriP49841.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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]
ProtoNetiSearch...

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. "The neuron-specific isoform of glycogen synthase kinase-3beta is required for axon growth."
    Castano Z., Gordon-Weeks P.R., Kypta R.M.
    J. Neurochem. 113:117-130(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
  39. "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.
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "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.
  42. "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.
  43. "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.
  44. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  45. "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.
  46. "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.
  47. "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: May 27, 2015
This is version 192 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.