SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49840

- GSK3A_HUMAN

UniProt

P49840 - GSK3A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glycogen synthase kinase-3 alpha
Gene
GSK3A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by phosphorylation at Tyr-279. In response to insulin, inhibited by phosphorylation at Ser-21 by PKB/AKT1; phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. Inhibited by lithium.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481ATP By similarity
Active sitei244 – 2441Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi125 – 1339ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. protein kinase A catalytic subunit binding Source: BHF-UCL
  4. protein serine/threonine kinase activity Source: BHF-UCL
  5. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. Wnt signaling pathway Source: UniProtKB-KW
  3. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  4. cardiac left ventricle morphogenesis Source: BHF-UCL
  5. cellular protein metabolic process Source: Reactome
  6. cellular response to insulin stimulus Source: BHF-UCL
  7. cellular response to interleukin-3 Source: UniProtKB
  8. endoplasmic reticulum unfolded protein response Source: Reactome
  9. epidermal growth factor receptor signaling pathway Source: Reactome
  10. extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  11. fibroblast growth factor receptor signaling pathway Source: Reactome
  12. glycogen metabolic process Source: UniProtKB-KW
  13. innate immune response Source: Reactome
  14. insulin receptor signaling pathway Source: BHF-UCL
  15. negative regulation of TOR signaling Source: BHF-UCL
  16. negative regulation of UDP-glucose catabolic process Source: UniProtKB
  17. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  18. negative regulation of cell growth involved in cardiac muscle cell development Source: BHF-UCL
  19. negative regulation of glucose import Source: BHF-UCL
  20. negative regulation of glycogen (starch) synthase activity Source: UniProtKB
  21. negative regulation of glycogen biosynthetic process Source: UniProtKB
  22. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  23. negative regulation of transferase activity Source: BHF-UCL
  24. negative regulation of type B pancreatic cell development Source: UniProtKB
  25. nervous system development Source: UniProtKB-KW
  26. neurotrophin TRK receptor signaling pathway Source: Reactome
  27. phosphatidylinositol-mediated signaling Source: Reactome
  28. positive regulation of adrenergic receptor signaling pathway Source: BHF-UCL
  29. positive regulation of cAMP biosynthetic process Source: BHF-UCL
  30. positive regulation of glycogen (starch) synthase activity Source: BHF-UCL
  31. positive regulation of heart contraction Source: BHF-UCL
  32. positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
  33. positive regulation of protein catabolic process Source: BHF-UCL
  34. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  35. protein phosphorylation Source: BHF-UCL
  36. regulation of systemic arterial blood pressure Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Signal transduction inhibitor, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism, Neurogenesis, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_18273. XBP1(S) activates chaperone genes.
SignaLinkiP49840.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen synthase kinase-3 alpha (EC:2.7.11.26)
Short name:
GSK-3 alpha
Alternative name(s):
Serine/threonine-protein kinase GSK3A (EC:2.7.11.1)
Gene namesi
Name:GSK3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4616. GSK3A.

Subcellular locationi

GO - Cellular componenti

  1. beta-catenin destruction complex Source: UniProtKB
  2. cytosol Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Alzheimer disease, Diabetes mellitus

Organism-specific databases

PharmGKBiPA29008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 483482Glycogen synthase kinase-3 alpha
PRO_0000085978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine2 Publications
Modified residuei21 – 211Phosphoserine; by PKB/AKT1 By similarity
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei279 – 2791Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49840.
PaxDbiP49840.
PeptideAtlasiP49840.
PRIDEiP49840.

PTM databases

PhosphoSiteiP49840.

Expressioni

Gene expression databases

ArrayExpressiP49840.
BgeeiP49840.
CleanExiHS_GSK3A.
GenevestigatoriP49840.

Organism-specific databases

HPAiCAB004422.
HPA028423.

Interactioni

Subunit structurei

Monomer. Interacts with ARRB2 By similarity. Interacts with AXIN1 and CTNNB1/beta-catenin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AXIN1O151692EBI-1044067,EBI-710484
DEAF1O753982EBI-1044067,EBI-718185
HSP90AB1P082382EBI-1044067,EBI-352572
LRP6O755812EBI-1044067,EBI-910915
ZDHHC17Q8IUH53EBI-1044067,EBI-524753

Protein-protein interaction databases

BioGridi109186. 50 interactions.
IntActiP49840. 35 interactions.
MINTiMINT-1688290.
STRINGi9606.ENSP00000222330.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DFMmodel-A98-449[»]
ProteinModelPortaliP49840.
SMRiP49840. Positions 99-446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 403285Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 8381Gly-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233017.
HOVERGENiHBG014652.
InParanoidiP49840.
KOiK08822.
OMAiFDELRCP.
OrthoDBiEOG7TF78V.
PhylomeDBiP49840.
TreeFamiTF101104.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49840-1 [UniParc]FASTAAdd to Basket

« Hide

MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK    50
ASVGAMGGGV GASSSGGGPG GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV 100
TTVVATLGQG PERSQEVAYT DIKVIGNGSF GVVYQARLAE TRELVAIKKV 150
LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY SSGEKKDELY LNLVLEYVPE 200
TVYRVARHFT KAKLTIPILY VKVYMYQLFR SLAYIHSQGV CHRDIKPQNL 250
LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS 300
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN 350
YTEFKFPQIK AHPWTKVFKS RTPPEAIALC SSLLEYTPSS RLSPLEACAH 400
SFFDELRCLG TQLPNNRPLP PLFNFSAGEL SIQPSLNAIL IPPHLRSPAG 450
TTTLTPSSQA LTETPTSSDW QSTDATPTLT NSS 483
Length:483
Mass (Da):50,981
Last modified:December 1, 2000 - v2
Checksum:iF18C012C03B7D786
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091Q → E.
Corresponds to variant rs35978177 [ dbSNP | Ensembl ].
VAR_051625
Natural varianti461 – 4611L → F.1 Publication
Corresponds to variant rs35454502 [ dbSNP | Ensembl ].
VAR_040539

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti449 – 4491A → S in AAA62432. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40027 mRNA. Translation: AAA62432.1.
D63424 mRNA. Translation: BAA23608.1.
AC006486 Genomic DNA. Translation: AAD11986.1.
BC027984 mRNA. Translation: AAH27984.1.
BC051865 mRNA. Translation: AAH51865.1.
CCDSiCCDS12599.1.
RefSeqiNP_063937.2. NM_019884.2.
UniGeneiHs.466828.

Genome annotation databases

EnsembliENST00000222330; ENSP00000222330; ENSG00000105723.
ENST00000453535; ENSP00000412663; ENSG00000105723.
GeneIDi2931.
KEGGihsa:2931.
UCSCiuc002otb.1. human.

Polymorphism databases

DMDMi12644292.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40027 mRNA. Translation: AAA62432.1 .
D63424 mRNA. Translation: BAA23608.1 .
AC006486 Genomic DNA. Translation: AAD11986.1 .
BC027984 mRNA. Translation: AAH27984.1 .
BC051865 mRNA. Translation: AAH51865.1 .
CCDSi CCDS12599.1.
RefSeqi NP_063937.2. NM_019884.2.
UniGenei Hs.466828.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DFM model - A 98-449 [» ]
ProteinModelPortali P49840.
SMRi P49840. Positions 99-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109186. 50 interactions.
IntActi P49840. 35 interactions.
MINTi MINT-1688290.
STRINGi 9606.ENSP00000222330.

Chemistry

BindingDBi P49840.
ChEMBLi CHEMBL2850.
GuidetoPHARMACOLOGYi 2029.

PTM databases

PhosphoSitei P49840.

Polymorphism databases

DMDMi 12644292.

Proteomic databases

MaxQBi P49840.
PaxDbi P49840.
PeptideAtlasi P49840.
PRIDEi P49840.

Protocols and materials databases

DNASUi 2931.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222330 ; ENSP00000222330 ; ENSG00000105723 .
ENST00000453535 ; ENSP00000412663 ; ENSG00000105723 .
GeneIDi 2931.
KEGGi hsa:2931.
UCSCi uc002otb.1. human.

Organism-specific databases

CTDi 2931.
GeneCardsi GC19M042734.
HGNCi HGNC:4616. GSK3A.
HPAi CAB004422.
HPA028423.
MIMi 606784. gene.
neXtProti NX_P49840.
PharmGKBi PA29008.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233017.
HOVERGENi HBG014652.
InParanoidi P49840.
KOi K08822.
OMAi FDELRCP.
OrthoDBi EOG7TF78V.
PhylomeDBi P49840.
TreeFami TF101104.

Enzyme and pathway databases

Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_18273. XBP1(S) activates chaperone genes.
SignaLinki P49840.

Miscellaneous databases

ChiTaRSi GSK3A. human.
GeneWikii GSK3A.
GenomeRNAii 2931.
NextBioi 11615.
PROi P49840.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49840.
Bgeei P49840.
CleanExi HS_GSK3A.
Genevestigatori P49840.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Glycogen synthase kinase 3 and dorsoventral patterning in Xenopus embryos."
    He X., Saint-Jeannet J.P., Woodgett J.R., Varmus H.E., Dawid I.B.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Foreskin.
  2. "Isolation of cDNA clones for human glycogen synthase kinase 3alpha."
    Hoshino T., Kondo K., Ishiguro K., Takashima A., Imahori K.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Eye and Pancreas.
  5. "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.
  6. "GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides."
    Phiel C.J., Wilson C.A., Lee V.M., Klein P.S.
    Nature 423:435-439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH ALZHEIMER DISEASE, FUNCTION.
  7. "GSK3alpha exhibits beta-catenin and tau directed kinase activities that are modulated by Wnt."
    Asuni A.A., Hooper C., Reynolds C.H., Lovestone S., Anderton B.H., Killick R.
    Eur. J. Neurosci. 24:3387-3392(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH AXIN1 AND CTNNB1/BETA-CATENIN.
  8. "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.
  9. "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.
  10. "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 SER-2 AND SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-77 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-461.

Entry informationi

Entry nameiGSK3A_HUMAN
AccessioniPrimary (citable) accession number: P49840
Secondary accession number(s): O14959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: September 3, 2014
This is version 146 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 GSK3A are found in the skeletal muscle (vastus lateralis) of patients with type 2 diabetes (1 Publication). Several potent GSK3 (GSK3A and GSK3B) inhibitors have been identified and characterized in preclinical models for treatments of type 2 diabetes (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi