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Protein

Glycogen synthase kinase-3 beta

Gene

Gsk3b

Organism
Mus musculus (Mouse)
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. 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.10 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.

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  • aging Source: Ensembl
  • axonogenesis Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: BHF-UCL
  • cell migration Source: MGI
  • cell proliferation Source: MGI
  • cellular response to dopamine Source: Ensembl
  • cellular response to erythropoietin Source: Ensembl
  • cellular response to hepatocyte growth factor stimulus Source: MGI
  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to interleukin-3 Source: UniProtKB
  • cellular response to iron(II) ion Source: Ensembl
  • cellular response to lithium ion Source: Ensembl
  • cellular response to mechanical stimulus Source: Ensembl
  • circadian rhythm Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • epithelial to mesenchymal transition Source: UniProtKB
  • ER overload response Source: MGI
  • establishment of cell polarity Source: Ensembl
  • extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  • fat cell differentiation Source: MGI
  • glycogen metabolic process Source: MGI
  • hippocampus development Source: MGI
  • hypermethylation of CpG island Source: BHF-UCL
  • intracellular signal transduction Source: MGI
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: CACAO
  • myoblast fusion Source: MGI
  • myotube differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cardiac muscle hypertrophy Source: MGI
  • negative regulation of dendrite morphogenesis Source: Ensembl
  • negative regulation of dopaminergic neuron differentiation Source: Ensembl
  • negative regulation of MAP kinase activity Source: Ensembl
  • negative regulation of neuron maturation Source: MGI
  • negative regulation of neuron migration Source: Ensembl
  • negative regulation of neuron projection development Source: MGI
  • negative regulation of NFAT protein import into nucleus Source: UniProtKB
  • negative regulation of nitric-oxide synthase activity Source: Ensembl
  • negative regulation of protein binding Source: MGI
  • negative regulation of protein complex assembly Source: MGI
  • negative regulation of smooth muscle cell apoptotic process Source: Ensembl
  • organ morphogenesis Source: MGI
  • peptidyl-serine phosphorylation Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: MGI
  • phosphorylation Source: UniProtKB
  • positive regulation of axon extension Source: MGI
  • positive regulation of cell-matrix adhesion Source: MGI
  • positive regulation of DNA biosynthetic process Source: Ensembl
  • positive regulation of excitatory postsynaptic potential Source: Ensembl
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of mitochondrial membrane potential Source: Ensembl
  • positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: Ensembl
  • positive regulation of neuron death Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of peptidyl-threonine phosphorylation Source: MGI
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of protein complex assembly Source: MGI
  • positive regulation of protein export from nucleus Source: MGI
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of stem cell differentiation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein autophosphorylation Source: MGI
  • protein export from nucleus Source: MGI
  • protein localization to microtubule Source: MGI
  • protein phosphorylation Source: UniProtKB
  • re-entry into mitotic cell cycle Source: MGI
  • regulation of gene expression by genetic imprinting Source: BHF-UCL
  • regulation of microtubule-based process Source: UniProtKB
  • regulation of neuronal synaptic plasticity Source: Ensembl
  • regulation of neuron projection development Source: MGI
  • response to activity Source: Ensembl
  • response to angiotensin Source: Ensembl
  • response to drug Source: Ensembl
  • response to epinephrine Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to insulin Source: Ensembl
  • response to insulin-like growth factor stimulus Source: Ensembl
  • response to L-glutamate Source: Ensembl
  • response to ultrasound Source: Ensembl
  • superior temporal gyrus development Source: MGI
  • Wnt signaling pathway Source: MGI
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. 3474.
ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1861437. Gsk3b.

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

  • axon Source: Ensembl
  • beta-catenin destruction complex Source: MGI
  • cell body Source: MGI
  • centrosome Source: MGI
  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • dendritic shaft Source: MGI
  • dendritic spine Source: Ensembl
  • growth cone Source: MGI
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • membrane-bounded organelle Source: MGI
  • membrane raft Source: Ensembl
  • mitochondrion Source: Ensembl
  • neuronal cell body Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • Wnt signalosome Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at E16 due to hepatocyte apoptosis.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91S → A: Loss of phosphorylation; No inhibition of activity and constitutively active. 2 Publications
Mutagenesisi85 – 851K → R: Inhibits interaction with AXIN1 and ZBED3. 1 Publication

Chemistry

ChEMBLiCHEMBL1075321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Glycogen synthase kinase-3 betaPRO_0000085981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK32 Publications
Modified residuei216 – 2161PhosphotyrosineBy similarity
Modified residuei389 – 3891PhosphoserineCombined sources

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. Phosphorylation of Ser-9 in the hippocampus peaks at CT0, whereas in the liver it peaks at CT12.2 Publications
Mono-ADP-ribosylation by PARP10 negatively regulates kinase activity.By similarity

Keywords - PTMi

ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDiQ9WV60.
MaxQBiQ9WV60.
PaxDbiQ9WV60.
PRIDEiQ9WV60.

PTM databases

iPTMnetiQ9WV60.
PhosphoSiteiQ9WV60.

Miscellaneous databases

PMAP-CutDBQ9WV60.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022812.
CleanExiMM_GSK3B.
ExpressionAtlasiQ9WV60. baseline and differential.
GenevisibleiQ9WV60. MM.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ctnnb1Q022482EBI-400793,EBI-397872
Epm2aQ9WUA52EBI-400793,EBI-1040928

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208115. 59 interactions.
DIPiDIP-32446N.
IntActiQ9WV60. 46 interactions.
MINTiMINT-4096935.
STRINGi10090.ENSMUSP00000023507.

Chemistry

BindingDBiQ9WV60.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293Combined sources
Beta strandi38 – 4811Combined sources
Beta strandi52 – 6413Combined sources
Beta strandi69 – 757Combined sources
Turni76 – 783Combined sources
Beta strandi81 – 888Combined sources
Helixi97 – 1015Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi127 – 1337Combined sources
Helixi139 – 14810Combined sources
Helixi155 – 17319Combined sources
Turni174 – 1763Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1904Combined sources
Turni191 – 1944Combined sources
Beta strandi195 – 1984Combined sources
Helixi201 – 2033Combined sources
Helixi220 – 2223Combined sources
Helixi225 – 2284Combined sources
Helixi237 – 25216Combined sources
Helixi262 – 27312Combined sources
Helixi278 – 2847Combined sources
Helixi286 – 2883Combined sources
Helixi301 – 3044Combined sources
Helixi311 – 32010Combined sources
Helixi325 – 3273Combined sources
Helixi331 – 3355Combined sources
Helixi338 – 3403Combined sources
Helixi341 – 3444Combined sources
Turni364 – 3674Combined sources
Helixi371 – 3733Combined sources
Helixi374 – 3774Combined sources
Helixi380 – 3823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NU1X-ray2.50A1-383[»]
5AIRX-ray2.53A/B4-420[»]
ProteinModelPortaliQ9WV60.
SMRiQ9WV60. Positions 6-386.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
HOVERGENiHBG014652.
InParanoidiQ9WV60.
KOiK03083.
PhylomeDBiQ9WV60.
TreeFamiTF101104.

Family and domain databases

InterProiIPR033573. GSK3B.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24057:SF8. PTHR24057:SF8. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

Q9WV60-1 [UniParc]FASTAAdd to basket

« 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 HARIQAAASP PANATAASDT
410 420
NAGDRGQTNN AASASASNST
Length:420
Mass (Da):46,710
Last modified:May 1, 2000 - v2
Checksum:i200C3FD1B38B4883
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156099 mRNA. Translation: AAD39258.2.
BC006936 mRNA. Translation: AAH06936.1.
BC060743 mRNA. Translation: AAH60743.1.
CCDSiCCDS28163.1.
RefSeqiNP_062801.1. NM_019827.6.
UniGeneiMm.394930.

Genome annotation databases

EnsembliENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
GeneIDi56637.
KEGGimmu:56637.
UCSCiuc007zen.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156099 mRNA. Translation: AAD39258.2.
BC006936 mRNA. Translation: AAH06936.1.
BC060743 mRNA. Translation: AAH60743.1.
CCDSiCCDS28163.1.
RefSeqiNP_062801.1. NM_019827.6.
UniGeneiMm.394930.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NU1X-ray2.50A1-383[»]
5AIRX-ray2.53A/B4-420[»]
ProteinModelPortaliQ9WV60.
SMRiQ9WV60. Positions 6-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208115. 59 interactions.
DIPiDIP-32446N.
IntActiQ9WV60. 46 interactions.
MINTiMINT-4096935.
STRINGi10090.ENSMUSP00000023507.

Chemistry

BindingDBiQ9WV60.
ChEMBLiCHEMBL1075321.

PTM databases

iPTMnetiQ9WV60.
PhosphoSiteiQ9WV60.

Proteomic databases

EPDiQ9WV60.
MaxQBiQ9WV60.
PaxDbiQ9WV60.
PRIDEiQ9WV60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
GeneIDi56637.
KEGGimmu:56637.
UCSCiuc007zen.1. mouse.

Organism-specific databases

CTDi2932.
MGIiMGI:1861437. Gsk3b.

Phylogenomic databases

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00520000055635.
HOGENOMiHOG000233017.
HOVERGENiHBG014652.
InParanoidiQ9WV60.
KOiK03083.
PhylomeDBiQ9WV60.
TreeFamiTF101104.

Enzyme and pathway databases

BRENDAi2.7.11.26. 3474.
ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.

Miscellaneous databases

ChiTaRSiGsk3b. mouse.
PMAP-CutDBQ9WV60.
PROiQ9WV60.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022812.
CleanExiMM_GSK3B.
ExpressionAtlasiQ9WV60. baseline and differential.
GenevisibleiQ9WV60. MM.

Family and domain databases

InterProiIPR033573. GSK3B.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24057:SF8. PTHR24057:SF8. 1 hit.
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...

Entry informationi

Entry nameiGSK3B_MOUSE
AccessioniPrimary (citable) accession number: Q9WV60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.