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Reviewed, UniProtKB/Swiss-Prot Q9WV60 (GSK3B_MOUSE)

Last modified December 15, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen synthase kinase-3 beta
      Short name=GSK-3 beta
    EC=2.7.11.26
Gene names
Name: Gsk3b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. May phosphorylate MUC1 and decrease the interaction of MUC1 with CTNNB1/beta-catenin. Phosphorylates CTNNB1/beta-catenin By similarity.

Catalytic activity

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

Subunit structure

Monomer. Interacts with AXIN1, CABYR, MUC1, NIN and PRUNE By similarity. Interacts with ARRB2.

Post-translational modification

Phosphorylation on Tyr-216 is necessary for the activity By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Binary interactions

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 residue71Phosphothreonine Ref.11
Modified residue91Phosphoserine; by PKB/AKT1 By similarity
Modified residue2151Phosphoserine Ref.10 Ref.12
Modified residue2161Phosphotyrosine Ref.11 Ref.10 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Modified residue2191Phosphoserine Ref.11 Ref.7 Ref.9
Modified residue2751Phosphothreonine By similarity
Modified residue2771Phosphothreonine By similarity
Modified residue3891Phosphoserine Ref.10 Ref.3
Modified residue3951Phosphothreonine Ref.10

Sequences

Sequence LengthMass (Da)Tools
Q9WV60-1 [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
[3]"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: 15345747] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, MASS SPECTROMETRY.
Tissue: Brain.
[4]"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: 16051150] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
[6]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Brain.
[7]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND SER-219, MASS SPECTROMETRY.
Tissue: Mast cell.
[8]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND SER-219, MASS SPECTROMETRY.
Tissue: Brain.
[10]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; TYR-216; SER-389 AND THR-395, MASS SPECTROMETRY.
Tissue: Brain cortex.
[11]"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: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; TYR-216 AND SER-219, MASS SPECTROMETRY.
Tissue: Liver.
[12]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF156099 mRNA. Translation: AAD39258.2.
BC006936 mRNA. Translation: AAH06936.1.
BC060743 mRNA. Translation: AAH60743.1.
IPIIPI00125319.
RefSeqNP_062801.1.
UniGeneMm.394930

3D structure databases

SMRQ9WV60. Positions 23-386.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9WV60. 4 interactions.
STRINGQ9WV60.

PTM databases

PhosphoSiteQ9WV60.

Proteomic databases

PRIDEQ9WV60.

Genome annotation databases

EnsemblENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812; Mus musculus. [Genome view]
GeneID56637.
KEGGmmu:56637.
UCSCuc007zen.1. mouse.

Organism-specific databases

CTD56637.
MGIMGI:1861437. Gsk3b.

Phylogenomic databases

HOVERGENQ9WV60.
OrthoDBEOG9R52NK.

Enzyme and pathway databases

BRENDA2.7.11.26. 244.

Gene expression databases

ArrayExpressQ9WV60.
BgeeQ9WV60.
CleanExMM_GSK3B.
GenevestigatorQ9WV60.
GermOnlineENSMUSG00000022812. Mus musculus.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio313081.
PMAP-CutDBQ9WV60.
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: December 15, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents