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Q9WV60 (GSK3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen synthase kinase-3 beta

Short name=GSK-3 beta
EC=2.7.11.26
Alternative name(s):
Serine/threonine-protein kinase GSK3B
EC=2.7.11.1
Gene names
Name:Gsk3b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. 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. 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 SFPQ at 'Thr-679' upon T-cell activation. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. 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. Ref.3 Ref.6 Ref.7 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Catalytic activity

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

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

Monomer. Interacts with DAB2IP (via C2 domain); the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA By similarity. Interacts with CABYR, MMP2, MUC1, NIN and PRUNE By similarity. 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) By similarity. Interacts with ARRB2 and DISC1. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts with SGK3. Interacts with the CLOCK-ARNTL/BMAL1 heterodimer By similarity. Interacts with AXIN1 and ZBED3. Interacts with the ARNTL/BMAL1. Ref.5 Ref.11 Ref.12 Ref.14

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. 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 By similarity.

Post-translational modification

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. Phosphorylation of Ser-9 in the hippocampus peaks at CT0, whereas in the liver it peaks at CT12. Ref.16 Ref.17

Mono-ADP-ribosylation by PARP10 negatively regulates kinase activity By similarity.

Disruption phenotype

Embryonic lethality at E16 due to hepatocyte apoptosis. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Differentiation
Glycogen metabolism
Neurogenesis
Wnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Signal transduction inhibitor
Transferase
   PTMADP-ribosylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from direct assay PubMed 14744935. Source: MGI

Wnt signaling pathway

Inferred from genetic interaction PubMed 16815997PubMed 23074275. Source: MGI

axonogenesis

Inferred from genetic interaction PubMed 18716223. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 15282335. Source: MGI

canonical Wnt signaling pathway involved in positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 12154096. Source: BHF-UCL

cell migration

Inferred from genetic interaction PubMed 17986005. Source: MGI

cell proliferation

Traceable author statement Ref.3. Source: MGI

cellular response to interleukin-3

Inferred from direct assay Ref.7. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from mutant phenotype Ref.13. Source: UniProtKB

cytoskeleton organization

Traceable author statement Ref.16. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay Ref.7. Source: UniProtKB

fat cell differentiation

Inferred from direct assay PubMed 12502791. Source: MGI

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from electronic annotation. Source: Ensembl

hypermethylation of CpG island

Inferred from mutant phenotype PubMed 21047779. Source: BHF-UCL

intracellular signal transduction

Inferred from sequence orthology PubMed 14749367. Source: MGI

myoblast fusion

Inferred from direct assay PubMed 15282335. Source: MGI

myotube differentiation

Inferred from genetic interaction PubMed 15282335. Source: MGI

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of NFAT protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.3. Source: MGI

negative regulation of cardiac muscle hypertrophy

Inferred from direct assay PubMed 11782539. Source: MGI

negative regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Inferred from mutant phenotype Ref.3. Source: MGI

peptidyl-serine phosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

phosphorylation

Inferred from mutant phenotype PubMed 17182001. Source: UniProtKB

positive regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 17986005. Source: MGI

positive regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 17986005. Source: MGI

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from genetic interaction PubMed 22660580. Source: MGI

positive regulation of protein binding

Inferred from direct assay Ref.12. Source: MGI

positive regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of stem cell differentiation

Inferred from mutant phenotype PubMed 22064483. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21047779. Source: BHF-UCL

protein export from nucleus

Inferred from direct assay PubMed 11782539. Source: MGI

protein localization to microtubule

Inferred from genetic interaction PubMed 18716223. Source: MGI

protein phosphorylation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

re-entry into mitotic cell cycle

Inferred from direct assay PubMed 12502791. Source: MGI

regulation of gene expression by genetic imprinting

Inferred from mutant phenotype PubMed 21047779. Source: BHF-UCL

regulation of microtubule-based process

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lithium ion

Inferred from electronic annotation. Source: Ensembl

superior temporal gyrus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbeta-catenin destruction complex

Inferred from direct assay PubMed 10318824. Source: MGI

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 12502791. Source: MGI

dendritic shaft

Inferred from direct assay PubMed 12805290. Source: MGI

dendritic spine

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from direct assay PubMed 12805290. Source: MGI

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

membrane-bounded organelle

Inferred from direct assay PubMed 12805290. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 12805290. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20890042. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 21709260. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

beta-catenin binding

Inferred from physical interaction PubMed 12874278. Source: MGI

kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 14730361. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay Ref.13Ref.16. Source: UniProtKB

tau-protein kinase activity

Inferred from direct assay PubMed 15192701. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Epm2aQ9WUA52EBI-400793,EBI-1040928

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Glycogen synthase kinase-3 beta
PRO_0000085981

Regions

Domain56 – 340285Protein kinase
Nucleotide binding62 – 709ATP By similarity

Sites

Active site1811Proton acceptor By similarity
Binding site851ATP By similarity

Amino acid modifications

Modified residue91Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 Ref.16 Ref.17
Modified residue2161Phosphotyrosine By similarity
Modified residue3891Phosphoserine Ref.4

Experimental info

Mutagenesis91S → A: Loss of phosphorylation; No inhibition of activity and constitutively active. Ref.6 Ref.16
Mutagenesis851K → R: Inhibits interaction with AXIN1 and ZBED3. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q9WV60 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 200C3FD1B38B4883

FASTA42046,710
        10         20         30         40         50         60 
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK 

        70         80         90        100        110        120 
VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG 

       130        140        150        160        170        180 
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR 

       190        200        210        220        230        240 
DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV 

       250        260        270        280        290        300 
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP 

       310        320        330        340        350        360 
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF 

       370        380        390        400        410        420 
NFTTQELSSN PPLATILIPP HARIQAAASP PANATAASDT NAGDRGQTNN AASASASNST 

« Hide

References

« Hide 'large scale' references
[1]"Testicular expression and hormonal control of glycogen synthase kinase 3, a homologue of yeast RIM11."
Salameh W.A., Guo T.B., Chan K.C., Mitchell A.P.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
[3]"Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation."
Hoeflich K.P., Luo J., Rubie E.A., Tsao M.S., Jin O., Woodgett J.R.
Nature 406:86-90(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior."
Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J., Gainetdinov R.R., Caron M.G.
Cell 122:261-273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[6]"Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis."
McManus E.J., Sakamoto K., Armit L.J., Ronaldson L., Shpiro N., Marquez R., Alessi D.R.
EMBO J. 24:1571-1583(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-9.
[7]"Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1."
Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.
Mol. Cell 21:749-760(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MCL1 PHOSPHORYLATION.
[8]"GSK3 alpha and GSK3 beta are necessary for axon formation."
Garrido J.J., Simon D., Varea O., Wandosell F.
FEBS Lett. 581:1579-1586(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AXON FORMATION.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Genetic deficiency of glycogen synthase kinase-3beta corrects diabetes in mouse models of insulin resistance."
Tanabe K., Liu Z., Patel S., Doble B.W., Li L., Cras-Meneur C., Martinez S.C., Welling C.M., White M.F., Bernal-Mizrachi E., Woodgett J.R., Permutt M.A.
PLoS Biol. 6:E37-E37(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF PANCREATIC BETA-CELLS.
[11]"Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3beta/beta-catenin signaling."
Mao Y., Ge X., Frank C.L., Madison J.M., Koehler A.N., Doud M.K., Tassa C., Berry E.M., Soda T., Singh K.K., Biechele T., Petryshen T.L., Moon R.T., Haggarty S.J., Tsai L.H.
Cell 136:1017-1031(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DISC1.
[12]"Identification of zinc-finger BED domain-containing 3 (Zbed3) as a novel Axin-interacting protein that activates Wnt/beta-catenin signaling."
Chen T., Li M., Ding Y., Zhang L.S., Xi Y., Pan W.J., Tao D.L., Wang J.Y., Li L.
J. Biol. Chem. 284:6683-6689(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1 AND ZBED3, MUTAGENESIS OF LYS-85.
[13]"DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping."
Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.
Mol. Cell. Biol. 30:1757-1768(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Regulation of BMAL1 protein stability and circadian function by GSK3beta-mediated phosphorylation."
Sahar S., Zocchi L., Kinoshita C., Borrelli E., Sassone-Corsi P.
PLoS ONE 5:E8561-E8561(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARNTL/BMAL1.
[15]"Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3beta."
Wu X., Shen Q.T., Oristian D.S., Lu C.P., Zheng Q., Wang H.W., Fuchs E.
Cell 144:341-352(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation."
Wakatsuki S., Saitoh F., Araki T.
Nat. Cell Biol. 13:1415-1423(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2, PHOSPHORYLATION AT SER-9, MUTAGENESIS OF SER-9.
[17]"Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock."
Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K., Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.
Cell Metab. 17:291-302(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-9.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156099 mRNA. Translation: AAD39258.2.
BC006936 mRNA. Translation: AAH06936.1.
BC060743 mRNA. Translation: AAH60743.1.
RefSeqNP_062801.1. NM_019827.6.
UniGeneMm.394930.

3D structure databases

ProteinModelPortalQ9WV60.
SMRQ9WV60. Positions 23-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208115. 20 interactions.
IntActQ9WV60. 17 interactions.
MINTMINT-4096935.
STRING10090.ENSMUSP00000110398.

Chemistry

BindingDBQ9WV60.
ChEMBLCHEMBL1075321.

PTM databases

PhosphoSiteQ9WV60.

Proteomic databases

PaxDbQ9WV60.
PRIDEQ9WV60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
GeneID56637.
KEGGmmu:56637.
UCSCuc007zen.1. mouse.

Organism-specific databases

CTD2932.
MGIMGI:1861437. Gsk3b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00520000055635.
HOGENOMHOG000233017.
HOVERGENHBG014652.
KOK03083.
OrthoDBEOG7TF78V.
PhylomeDBQ9WV60.
TreeFamTF101104.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.

Gene expression databases

ArrayExpressQ9WV60.
BgeeQ9WV60.
CleanExMM_GSK3B.
GenevestigatorQ9WV60.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSK3B. mouse.
NextBio313081.
PMAP-CutDBQ9WV60.
PROQ9WV60.
SOURCESearch...

Entry information

Entry nameGSK3B_MOUSE
AccessionPrimary (citable) accession number: Q9WV60
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot