[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=7980435 [NCBI, ExPASy, EBI, Israel, Japan] Stambolic V., Woodgett J.R.; "Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation."; Biochem. J. 303:701-704(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). TISSUE=Eye, and Placenta; 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).
[3]	NUCLEOTIDE SEQUENCE OF 185-202. DOI=10.1038/sj.mp.4000538; PubMed=10523816 [NCBI, ExPASy, EBI, Israel, Japan] Rhoads A.R., Karkera J.D., Detera-Wadleigh S.D.; "Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway."; Mol. Psychiatry 4:437-442(1999).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. DOI=10.1006/geno.1999.5875; PubMed=10486203 [NCBI, ExPASy, EBI, Israel, Japan] Lau K.F., Miller C.C.J., Anderton B.H., Shaw P.C.; "Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter."; Genomics 60:121-128(1999).
[5]	INTERACTION WITH MUC1, AND FUNCTION. PubMed=9819408 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Bharti A., Chen D., Gong J., Kufe D.; "Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin."; Mol. Cell. Biol. 18:7216-7224(1998).
[6]	CHARACTERIZATION. DOI=10.1073/pnas.95.19.11211; PubMed=9736715 [NCBI, ExPASy, EBI, Israel, Japan] Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.; "Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase."; Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998).
[7]	INTERACTION WITH NIN. DOI=10.1016/S0167-4781(00)00127-5; PubMed=11004522 [NCBI, ExPASy, EBI, Israel, Japan] Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K., Howng S.-L.; "Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta."; Biochim. Biophys. Acta 1492:513-516(2000).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[9]	INTERACTION WITH CABYR. DOI=10.1016/j.bbrc.2005.02.089; PubMed=15752768 [NCBI, ExPASy, EBI, Israel, Japan] Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J., Hong Y.-R.; "Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain."; Biochem. Biophys. Res. Commun. 329:1108-1117(2005).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.; "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."; Mol. Cell. Proteomics 4:1240-1250(2005).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, 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).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[14]	INTERACTION WITH PRUNE. DOI=10.1128/MCB.26.3.898-911.2006; PubMed=16428445 [NCBI, ExPASy, EBI, Israel, Japan] Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A.; "Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions."; Mol. Cell. Biol. 26:898-911(2006).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS SPECTROMETRY. 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).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216 AND THR-390, 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).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, 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).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216; SER-219; THR-275; THR-277; THR-390 AND THR-392, 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).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND THR-390, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[21]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-386. DOI=10.1016/S0092-8674(01)00374-9; PubMed=11440715 [NCBI, ExPASy, EBI, Israel, Japan] Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H.; "Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition."; Cell 105:721-732(2001).
[22]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-393 OF PHOSPHORYLATED GSK3B. DOI=10.1016/S0969-2126(01)00679-7; PubMed=11738041 [NCBI, ExPASy, EBI, Israel, Japan] Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R., Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G., Reith A.D.; "The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation."; Structure 9:1143-1152(2001).

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. Phosphorylates MUC1 in breast cancer cells, and decreases the interaction of MUC1 with CTNNB1/beta-catenin.
CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein] phosphate.
ENZYME REGULATION: Inhibited when phosphorylated by AKT1.
SUBUNIT: Monomer (By similarity). Interacts with CABYR, MUC1, NIN and PRUNE.
INTERACTION:
P53396:ACLY; NbExp=1; IntAct=EBI-373586, EBI-1042794;
P31749:AKT1; NbExp=1; IntAct=EBI-373586, EBI-296087;
P31751:AKT2; NbExp=1; IntAct=EBI-373586, EBI-296058;
O15169:AXIN1; NbExp=1; IntAct=EBI-373586, EBI-710484;
Q9H7B2:BXDC1; NbExp=1; IntAct=EBI-373586, EBI-1051960;
P35222:CTNNB1; NbExp=1; IntAct=EBI-373586, EBI-491549;
Q9UHI6:DDX20; NbExp=1; IntAct=EBI-373586, EBI-347658;
Q9H2U1:DHX36; NbExp=1; IntAct=EBI-373586, EBI-1047643;
Q811T9:Disc1 (xeno); NbExp=3; IntAct=EBI-373586, EBI-2298259;
Q01844:EWSR1; NbExp=1; IntAct=EBI-373586, EBI-739737;
P57678:GEMIN4; NbExp=1; IntAct=EBI-373586, EBI-356700;
Q9P0R6:GSKIP; NbExp=1; IntAct=EBI-373586, EBI-1052580;
P13807:GYS1; NbExp=1; IntAct=EBI-373586, EBI-963094;
Q9NZI8:IGF2BP1; NbExp=1; IntAct=EBI-373586, EBI-1053892;
P63085:Mapk1 (xeno); NbExp=1; IntAct=EBI-373586, EBI-397697;
Q8N4C6:NIN; NbExp=1; IntAct=EBI-373586, EBI-1164022;
O75533:SF3B1; NbExp=1; IntAct=EBI-373586, EBI-876542;
Q16637:SMN1; NbExp=1; IntAct=EBI-373586, EBI-395421;
Q9NRG4:SMYD2; NbExp=1; IntAct=EBI-373586, EBI-1055671;
P08621:SNRNP70; NbExp=1; IntAct=EBI-373586, EBI-1049228;
Q9Y3F4:STRAP; NbExp=1; IntAct=EBI-373586, EBI-727414;
P49816:Tsc2 (xeno); NbExp=1; IntAct=EBI-373586, EBI-1104140;
Q9H1J1:UPF3A; NbExp=1; IntAct=EBI-373586, EBI-521530;
Q96QU8:XPO6; NbExp=1; IntAct=EBI-373586, EBI-1022896;

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P49841-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P49841-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_004790.

TISSUE SPECIFICITY: Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney.
PTM: Phosphorylated by AKT1 and ILK1.
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
SIMILARITY: Contains 1 protein kinase domain.

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

L33801; AAA66475.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000251; AAH00251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012760; AAH12760.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF098789; AAC69340.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF074333; AAD48517.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00028570; -.
IPI00216190; -.

S53324; S53324.

NP_001139628.1; -.

3D structure databases

PDB

1GNG; X-ray; 2.60 A; A/B=27-393.	[ExPASy / RCSB / EBI]
1H8F; X-ray; 2.80 A; A/B=35-386.	[ExPASy / RCSB / EBI]
1I09; X-ray; 2.70 A; A/B=1-420.	[ExPASy / RCSB / EBI]
1J1B; X-ray; 1.80 A; A/B=1-420.	[ExPASy / RCSB / EBI]
1J1C; X-ray; 2.10 A; A/B=1-420.	[ExPASy / RCSB / EBI]
1O9U; X-ray; 2.40 A; A=35-384.	[ExPASy / RCSB / EBI]
1PYX; X-ray; 2.40 A; A/B=1-420.	[ExPASy / RCSB / EBI]
1Q3D; X-ray; 2.20 A; A/B=2-420.	[ExPASy / RCSB / EBI]
1Q3W; X-ray; 2.30 A; A/B=2-420.	[ExPASy / RCSB / EBI]
1Q41; X-ray; 2.10 A; A/B=2-420.	[ExPASy / RCSB / EBI]
1Q4L; X-ray; 2.77 A; A/B=2-420.	[ExPASy / RCSB / EBI]
1Q5K; X-ray; 1.94 A; A/B=7-420.	[ExPASy / RCSB / EBI]
1R0E; X-ray; 2.25 A; A/B=35-420.	[ExPASy / RCSB / EBI]
1UV5; X-ray; 2.80 A; A=35-384.	[ExPASy / RCSB / EBI]
2JDO; X-ray; 1.80 A; C=3-12.	[ExPASy / RCSB / EBI]
2JDR; X-ray; 2.30 A; C=3-12.	[ExPASy / RCSB / EBI]
2JLD; X-ray; 2.35 A; A/B=1-420.	[ExPASy / RCSB / EBI]
2O5K; X-ray; 3.20 A; A=29-393.	[ExPASy / RCSB / EBI]
2OW3; X-ray; 2.80 A; A/B=35-386.	[ExPASy / RCSB / EBI]
2UW9; X-ray; 2.10 A; C=3-12.	[ExPASy / RCSB / EBI]
3CQU; X-ray; 2.20 A; C=3-12.	[ExPASy / RCSB / EBI]
3CQW; X-ray; 2.00 A; C=3-12.	[ExPASy / RCSB / EBI]
3DU8; X-ray; 2.20 A; A/B=1-420.	[ExPASy / RCSB / EBI]
3E87; X-ray; 2.30 A; C/D=3-12.	[ExPASy / RCSB / EBI]
3E88; X-ray; 2.50 A; C/D=3-12.	[ExPASy / RCSB / EBI]
3E8D; X-ray; 2.70 A; C/D=3-12.	[ExPASy / RCSB / EBI]
3F7Z; X-ray; 2.40 A; A/B=35-383.	[ExPASy / RCSB / EBI]
3F88; X-ray; 2.60 A; A/B=35-383.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GNG; -.
1H8F; -.
1I09; -.
1J1B; -.
1J1C; -.
1O9U; -.
1PYX; -.
1Q3D; -.
1Q3W; -.
1Q41; -.
1Q4L; -.
1Q5K; -.
1R0E; -.
1UV5; -.
2JDO; -.
2JDR; -.
2JLD; -.
2O5K; -.
2OW3; -.
2UW9; -.
3CQU; -.
3CQW; -.
3DU8; -.
3E87; -.
3E88; -.
3E8D; -.
3F7Z; -.
3F88; -.

DisProt

DP00385; -.

ModBase

P49841.

Protein-protein interaction databases

DIP

DIP:878N; -.

IntAct

P49841; 46.

PTM databases

PhosphoSite

P49841; -.

Enzyme and pathway databases

BRENDA

2.7.11.26; 247.

Pathway_Interaction_DB

aurora_a_pathway; Aurora A signaling.
bmppathway; BMP receptor signaling.
wnt_canonical_pathway; Canonical Wnt signaling pathway.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
hedgehog_glipathway; Hedgehog signaling events mediated by Gli proteins.
insulin_glucose_pathway; Insulin-mediated glucose transport.
lysophospholipid_pathway; LPA receptor mediated events.
ps1pathway; Presenilin action in Notch and Wnt signaling.
reelinpathway; Reelin signaling pathway.
ar_tf_pathway; Regulation of Androgen receptor activity.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.

Reactome

REACT_11045; Signaling by Wnt.
REACT_11061; Signalling by NGF.

Organism-specific databases

GC03M121028; -.

HIX0003589; -.

HGNC:4617; GSK3B.

CAB016263; -.

605004; gene. [NCBI / EBI]

PharmGKB

PA29009; -.

Gene expression databases

P49841; -.

P49841; -.

HS_GSK3B; -.

ENSG00000082701; Homo sapiens.

Ontologies

GO:0034747;	Cellular component: Axin-APC-beta-catenin-GSK3B complex (inferred from direct assay from UniProtKB).
GO:0030877;	Cellular component: beta-catenin destruction complex (inferred from direct assay from UniProtKB).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008013;	Molecular function: beta-catenin binding (inferred from physical interaction from UniProtKB).
GO:0004696;	Molecular function: glycogen synthase kinase 3 activity (inferred from direct assay from UniProtKB).
GO:0051059;	Molecular function: NF-kappaB binding (inferred from physical interaction from UniProtKB).
GO:0002039;	Molecular function: p53 binding (inferred from direct assay from MGI).
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:0006983;	Biological process: ER overload response (inferred from direct assay from MGI).
GO:0005977;	Biological process: glycogen metabolic process (inferred from direct assay from UniProtKB).
GO:0018105;	Biological process: peptidyl-serine phosphorylation (inferred from direct assay from UniProtKB).
GO:0031334;	Biological process: positive regulation of protein complex assembly (inferred from direct assay from UniProtKB).
GO:0046827;	Biological process: positive regulation of protein export from nucleus (inferred from direct assay from MGI).
GO:0060070;	Biological process: Wnt receptor signaling pathway through beta-catenin (inferred by curator 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

PRIDE

P49841; -.

Genome annotation databases

Ensembl

ENSG00000082701; Homo sapiens. [Contig view]

GeneID

2932; -.

KEGG

hsa:2932; -.

Phylogenomic databases

HOVERGEN

P49841; -.

OMA

P49841; DQQVEIS.

Other

DB01356; Lithium.

11619; -.

GSK3B; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 420`	`420`	`Glycogen synthase kinase-3 beta.`	`PRO_0000085980`
`DOMAIN`	`56 340`	`285`	`Protein kinase.`
`NP_BIND`	`62 70`	`9`	`ATP (By similarity).`
`ACT_SITE`	`181 181`		`Proton acceptor.`
`BINDING`	`85 85`		`ATP (By similarity).`
`MOD_RES`	`7 7`		`Phosphothreonine (By similarity).`
`MOD_RES`	`9 9`		`Phosphoserine; by PKB/AKT1.`
`MOD_RES`	`215 215`		`Phosphoserine (By similarity).`
`MOD_RES`	`216 216`		`Phosphotyrosine.`
`MOD_RES`	`219 219`		`Phosphoserine.`
`MOD_RES`	`275 275`		`Phosphothreonine.`
`MOD_RES`	`277 277`		`Phosphothreonine.`
`MOD_RES`	`389 389`		`Phosphoserine (By similarity).`
`MOD_RES`	`390 390`		`Phosphothreonine.`
`MOD_RES`	`392 392`		`Phosphothreonine.`
`MOD_RES`	`395 395`		`Phosphothreonine (By similarity).`
`VAR_SEQ`	`303 303`		`K -> KDSSGTGHFTSGVR (in isoform 2).`	`VSP_004790`
`MUTAGEN`	`9 9`		`S->A: Loss of phosphorylation; insensitive to inhibitory phosphorylation.`
`CONFLICT`	`28 28`		`V -> G (in Ref. 4; AAD48517).`
`CONFLICT`	`350 350`		`L -> H (in Ref. 1; AAA66475).`
`STRAND`	`26 30`	`5`
`STRAND`	`38 48`	`11`
`STRAND`	`52 64`	`13`
`STRAND`	`66 75`	`10`
`TURN`	`76 78`	`3`
`STRAND`	`81 88`	`8`
`HELIX`	`96 102`	`7`
`STRAND`	`112 120`	`9`
`TURN`	`121 124`	`4`
`STRAND`	`125 133`	`9`
`HELIX`	`139 148`	`10`
`HELIX`	`155 173`	`19`
`TURN`	`174 176`	`3`
`HELIX`	`184 186`	`3`
`STRAND`	`187 190`	`4`
`TURN`	`191 194`	`4`
`STRAND`	`195 198`	`4`
`HELIX`	`225 228`	`4`
`HELIX`	`237 252`	`16`
`HELIX`	`262 273`	`12`
`HELIX`	`278 284`	`7`
`HELIX`	`301 304`	`4`
`HELIX`	`311 320`	`10`
`HELIX`	`325 327`	`3`
`HELIX`	`331 335`	`5`
`HELIX`	`338 344`	`7`
`HELIX`	`364 367`	`4`
`HELIX`	`371 373`	`3`
`HELIX`	`374 377`	`4`
`TURN`	`380 383`	`4`

Sequence information

Length: 420 AA [This is the length of the unprocessed precursor]

Molecular weight: 46744 Da [This is the MW of the unprocessed precursor]

CRC64: 4ACC24D00CDBB9C3 [This is a checksum on the sequence]

        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 HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST

P49841 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools