Reviewed, UniProtKB/Swiss-Prot P49841 (GSK3B_HUMAN)

Names and origin

Protein names

Recommended name:
    Glycogen synthase kinase-3 beta
      Short name=GSK-3 beta
    EC=2.7.11.26

Gene names

Name:

GSK3B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Phosphorylates MUC1 in breast cancer cells, and decreases the interaction of MUC1 with CTNNB1/beta-catenin. Phosphorylates CTNNB1/beta-catenin. Ref.5 Ref.24
Catalytic activity	ATP + [tau protein] = ADP + [tau protein] phosphate.
Enzyme regulation	Activated by phosphorylation at Tyr-216. Inhibited when phosphorylated by AKT1. Ref.24
Subunit structure	Monomer By similarity. Interacts with AXIN1, CABYR, MUC1, NIN and PRUNE.
Tissue specificity	Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney.
Post-translational modification	Phosphorylated by AKT1 and ILK1. Activated by phosphorylation at Tyr-216. Ref.24 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ER overload response Inferred from direct assay. Source: MGI Wnt receptor signaling pathway through beta-catenin Inferred by curator. Source: UniProtKB glycogen metabolic process Inferred from direct assay. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of protein complex assembly Inferred from direct assay. Source: UniProtKB positive regulation of protein export from nucleus Inferred from direct assay. Source: MGI
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from direct assay. Source: UniProtKB beta-catenin destruction complex Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome nucleus Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NF-kappaB binding Inferred from physical interaction. Source: UniProtKB beta-catenin binding Inferred from physical interaction. Source: UniProtKB glycogen synthase kinase 3 activity Inferred from direct assay. Source: UniProtKB p53 binding Inferred from direct assay. Source: MGI protein kinase A catalytic subunit binding Inferred from physical interaction. Source: UniProtKB tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACLY	P53396	1	EBI-373586,EBI-1042794
AKT1	P31749	1	EBI-373586,EBI-296087
AKT2	P31751	1	EBI-373586,EBI-296058
AXIN1	O15169	1	EBI-373586,EBI-710484
BXDC1	Q9H7B2	1	EBI-373586,EBI-1051960
CCDC52	Q8N0Z3	1	EBI-373586,EBI-2361917
CTNNB1	P35222	1	EBI-373586,EBI-491549
DDX20	Q9UHI6	1	EBI-373586,EBI-347658
DEAF1	O75398	2	EBI-373586,EBI-718185
DHX36	Q9H2U1	1	EBI-373586,EBI-1047643
Disc1	Q811T9	3	EBI-373586,EBI-2298259	From a different organism.
EWSR1	Q01844	1	EBI-373586,EBI-739737
GEMIN4	P57678	1	EBI-373586,EBI-356700
GSKIP	Q9P0R6	1	EBI-373586,EBI-1052580
GYS1	P13807	1	EBI-373586,EBI-963094
IGF2BP1	Q9NZI8	1	EBI-373586,EBI-1053892
Mapk1	P63085	1	EBI-373586,EBI-397697	From a different organism.
NBR1	Q14596	1	EBI-373586,EBI-742698
NIN	Q8N4C6	1	EBI-373586,EBI-1164022
SF3B1	O75533	1	EBI-373586,EBI-876542
SMN1	Q16637	1	EBI-373586,EBI-395421
SMYD2	Q9NRG4	1	EBI-373586,EBI-1055671
SNRNP70	P08621	1	EBI-373586,EBI-1049228
STRAP	Q9Y3F4	1	EBI-373586,EBI-727414
Tsc2	P49816	1	EBI-373586,EBI-1104140	From a different organism.
UPF3A	Q9H1J1	1	EBI-373586,EBI-521530
VTA1	Q9NP79	1	EBI-373586,EBI-740160
XPO6	Q96QU8	1	EBI-373586,EBI-1022896

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49841-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P49841-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-303: K → KDSSGTGHFTSGVR

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 420

420

Glycogen synthase kinase-3 beta

PRO_0000085980

Regions

Domain

56 – 340

285

Protein kinase

Nucleotide binding

62 – 70

9

ATP By similarity

Sites

Active site

181

1

Proton acceptor

Binding site

85

1

ATP By similarity

Amino acid modifications

Modified residue

7

1

Phosphothreonine By similarity

Modified residue

9

1

Phosphoserine; by PKB/AKT1 Ref.16 Ref.18

Modified residue

215

1

Phosphoserine By similarity

Modified residue

216

1

Phosphotyrosine Ref.24 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

219

1

Phosphoserine Ref.18

Modified residue

275

1

Phosphothreonine Ref.18

Modified residue

277

1

Phosphothreonine Ref.18

Modified residue

389

1

Phosphoserine By similarity

Modified residue

390

1

Phosphothreonine Ref.8 Ref.16 Ref.18 Ref.19

Modified residue

392

1

Phosphothreonine Ref.18

Modified residue

395

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

303

1

K → KDSSGTGHFTSGVR in isoform 2.

VSP_004790

Experimental info

Mutagenesis

9

1

S → A: Loss of phosphorylation; insensitive to inhibitory phosphorylation.

Sequence conflict

28

1

V → G in AAD48517. Ref.4

Sequence conflict

350

1

L → H in AAA66475. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

420

Helix Strand Turn

Details...

Beta strand

26 – 30

5

Beta strand

38 – 48

11

Beta strand

52 – 64

13

Beta strand

66 – 75

10

Turn

76 – 78

3

Beta strand

81 – 88

8

Helix

96 – 102

7

Beta strand

112 – 120

9

Turn

121 – 124

4

Beta strand

125 – 133

9

Helix

139 – 148

10

Helix

155 – 173

19

Turn

174 – 176

3

Helix

184 – 186

3

Beta strand

187 – 190

4

Turn

191 – 194

4

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: 4ACC24D00CDBB9C3	FASTA	420	46,744
	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
	Isoform 2. Checksum: 540F853E1603A080	FASTA	433	48,034
	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 WTKDSSGTGH FTSGVRVFRP RTPPEAIALC SRLLEYTPTA RLTPLEACAH SFFDELRDPN 370 380 390 400 410 420 VKLPNGRDTP ALFNFTTQEL SSNPPLATIL IPPHARIQAA ASTPTNATAA SDANTGDRGQ 430 TNNAASASAS NST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation." Stambolic V., Woodgett J.R. Biochem. J. 303:701-704(1994) [PubMed: 7980435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORMS 1 AND 2). Tissue: Eye and Placenta.
[3]	"Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway." Rhoads A.R., Karkera J.D., Detera-Wadleigh S.D. Mol. Psychiatry 4:437-442(1999) [PubMed: 10523816] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 185-202.
[4]	"Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter." Lau K.F., Miller C.C.J., Anderton B.H., Shaw P.C. Genomics 60:121-128(1999) [PubMed: 10486203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[5]	"Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin." Li Y., Bharti A., Chen D., Gong J., Kufe D. Mol. Cell. Biol. 18:7216-7224(1998) [PubMed: 9819408] [Abstract] Cited for: INTERACTION WITH MUC1, FUNCTION.
[6]	"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase." Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S. Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed: 9736715] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta." Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K., Howng S.-L. Biochim. Biophys. Acta 1492:513-516(2000) [PubMed: 11004522] [Abstract] Cited for: INTERACTION WITH NIN.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain." Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J., Hong Y.-R. Biochem. Biophys. Res. Commun. 329:1108-1117(2005) [PubMed: 15752768] [Abstract] Cited for: INTERACTION WITH CABYR.
[10]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions." Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A. Mol. Cell. Biol. 26:898-911(2006) [PubMed: 16428445] [Abstract] Cited for: INTERACTION WITH PRUNE.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
[16]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216 AND THR-390, MASS SPECTROMETRY.
[17]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Platelet.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216; SER-219; THR-275; THR-277; THR-390 AND THR-392, MASS SPECTROMETRY.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND THR-390, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[22]	"Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition." Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H. Cell 105:721-732(2001) [PubMed: 11440715] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-386.
[23]	"The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation." 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. Structure 9:1143-1152(2001) [PubMed: 11738041] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-393 OF PHOSPHORYLATED GSK3B.
[24]	"Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex." Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H. EMBO J. 22:494-501(2003) [PubMed: 12554650] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-384 IN COMPLEX WITH AXIN1, INTERACTION WITH AXIN1 AND FRAT1, FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-216.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L33801 mRNA. Translation: AAA66475.1.
BC000251 mRNA. Translation: AAH00251.1.
BC012760 mRNA. Translation: AAH12760.1.
AF098789 Genomic DNA. Translation: AAC69340.1.
AF074333 Genomic DNA. Translation: AAD48517.1.

IPI

IPI00028570.
IPI00216190.

PIR

S53324.

RefSeq

NP_001139628.1.
NP_002084.2.

UniGene

Hs.445733

3D structure databases

PDBPDBe

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

DisProt

DP00385.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:878N.

IntAct

P49841. 72 interactions.

STRING

P49841.

PTM databases

PhosphoSite

P49841.

Proteomic databases

PRIDE

P49841.

Genome annotation databases

Ensembl

ENST00000264235; ENSP00000264235; ENSG00000082701; Homo sapiens. [Genome view]
ENST00000316626; ENSP00000324806; ENSG00000082701; Homo sapiens. [Genome view]

GeneID

2932.

KEGG

hsa:2932.

UCSC

uc003edn.1. human.
uc003edo.1. human.

Organism-specific databases

CTD

2932.

GeneCards

GC03M121028.

H-InvDB

HIX0003589.

HGNC

HGNC:4617. GSK3B.

HPA

CAB016263.

MIM

605004. gene.

PharmGKB

PA29009.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P49841.

OMA

DQQVEIS.

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.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P49841.

Bgee

P49841.

CleanEx

HS_GSK3B.

Genevestigator

P49841.

GermOnline

ENSG00000082701. Homo sapiens.

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]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01356. Lithium.

NextBio

11619.

SOURCE

Search...

Entry information

Entry name

GSK3B_HUMAN

Accession

Primary (citable) accession number: P49841
Secondary accession number(s): Q9BWH3, Q9UL47

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 2, 2002
Last modified:	November 3, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.