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UniProtKB/Swiss-Prot entry P49840


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSK3A_HUMAN
Primary accession number P49840
Secondary accession number O14959
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 90)
Name and origin of the protein
Protein name Glycogen synthase kinase-3 alpha
Synonyms GSK-3 alpha
EC 2.7.11.26
Gene name
Name: GSK3A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Foreskin;
He X., Saint-Jeannet J.P., Woodgett J.R., Varmus H.E., Dawid I.B.;
"Glycogen synthase kinase 3 and dorsoventral patterning in Xenopus embryos.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Hoshino T., Kondo K., Ishiguro K., Takashima A., Imahori K.;
"Isolation of cDNA clones for human glycogen synthase kinase 3alpha.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-279, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-72, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[11]
VARIANT [LARGE SCALE ANALYSIS] PHE-461.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L40027; AAA62432.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D63424; BAA23608.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006486; AAD11986.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027984; AAH27984.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051865; AAH51865.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00292228; -.
RefSeq NP_063937.2; -.
UniGene Hs.466828
3D structure databases
PDB
2DFM; Model; -; A=98-449.[ExPASy / RCSB / EBI]
PDBsum 2DFM; -.
SMR P49840; 91-449.
ModBase P49840.
Protein-protein interaction databases
IntAct P49840; 8.
PTM databases
PhosphoSite P49840; -.
Enzyme and pathway databases
BRENDA 2.7.11.26; 247.
Pathway_Interaction_DB wnt_canonical_pathway; Canonical Wnt signaling pathway.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
foxm1pathway; FOXM1 transcription factor network.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC19M047426; -.
H-InvDB HIX0015173; -.
HGNC HGNC:4616; GSK3A.
GenAtlas GSK3A.
HPA CAB004422; -.
MIM 606784; gene. [NCBI / EBI]
PharmGKB PA29008; -.
Gene expression databases
ArrayExpress P49840; -.
Bgee P49840; -.
CleanEx HS_GSK3A; -.
GermOnline ENSG00000105723; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004696; Molecular function: glycogen synthase kinase 3 activity (inferred from direct assay from UniProtKB).
GO:0034236; Molecular function: protein kinase A catalytic subunit binding (inferred from physical interaction from UniProtKB).
GO:0050321; Molecular function: tau-protein kinase activity (inferred from electronic annotation from EC).
GO:0008286; Biological process: insulin receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0046325; Biological process: negative regulation of glucose import (inferred from mutant phenotype from UniProtKB).
GO:0046627; Biological process: negative regulation of insulin receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0051348; Biological process: negative regulation of transferase activity (inferred from mutant phenotype from UniProtKB).
GO:0010905; Biological process: negative regulation of UDP-glucose catabolic process (inferred by curator from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P49840; -.
PRIDE P49840; -.
Genome annotation databases
Ensembl ENSG00000105723; Homo sapiens. [Contig view]
GeneID 2931; -.
KEGG hsa:2931; -.
Phylogenomic databases
HOGENOM P49840; -.
HOVERGEN P49840; -.
OMA P49840; FQVERMA.
Other
NextBio 11615; -.
SOURCE GSK3A; Homo sapiens.
ProtoNet P49840.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   483  483     Glycogen synthase kinase-3 alpha. PRO_0000085978
DOMAIN   119   403  285     Protein kinase. 
NP_BIND   125   133  9     ATP (By similarity). 
COMPBIAS   1    83  83     Gly-rich. 
ACT_SITE   244   244        Proton acceptor (By similarity). 
BINDING   148   148        ATP (By similarity). 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   21    21        Phosphoserine. 
MOD_RES   72    72        Phosphoserine. 
MOD_RES   279   279        Phosphotyrosine. 
VARIANT   109   109  1     Q -> E (in dbSNP:rs35978177 [NCBI]). VAR_051625 [3D]
VARIANT   461   461  1     L -> F. VAR_040539 
CONFLICT   449   449        A -> S (in Ref. 1; AAA62432). 
Sequence information
Length: 483 AA [This is the length of the unprocessed precursor] Molecular weight: 50981 Da [This is the MW of the unprocessed precursor] CRC64: F18C012C03B7D786 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV 

        70         80         90        100        110        120 
GASSSGGGPG GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATLGQG PERSQEVAYT 

       130        140        150        160        170        180 
DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY 

       190        200        210        220        230        240 
SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLTIPILY VKVYMYQLFR SLAYIHSQGV 

       250        260        270        280        290        300 
CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS 

       310        320        330        340        350        360 
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK 

       370        380        390        400        410        420 
AHPWTKVFKS RTPPEAIALC SSLLEYTPSS RLSPLEACAH SFFDELRCLG TQLPNNRPLP 

       430        440        450        460        470        480 
PLFNFSAGEL SIQPSLNAIL IPPHLRSPAG TTTLTPSSQA LTETPTSSDW QSTDATPTLT 


NSS 

P49840 in FASTA format

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