General information | DisProt: | DP00385 | Name: | Glycogen synthase kinase-3 beta [Isoform 1] | Synonym(s): | GSK3B_HUMAN
GSK-3 beta
EC=2.7.11.26
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | P49841-1 | UniGene: | Hs.445733 | SwissProt: | GSK3B_HUMAN | TrEMBL: | | NCBI (GI): | 20455502 | Source organism: | Homo sapiens (Human) | Sequence length: | 420 | Percent disordered: | 21% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK - 60 VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG - 120 EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR - 180 DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV - 240 WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP - 300 WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF - 360 NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST - 420
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Functional narrative |
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.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 34 | Length: | 34 | Region sequence: |
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDG | Modification type: | Native
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Phosphorylation
Autoregulatory
| Detection methods:
- X-ray crystallography (100 K; DTT (pH 7.2) 1 mM; HEPES-NaOH 20 mM; MgCl2 2 mM; NaCl 500 mM; PEG 8000 6 %; Tris-HCl (pH 7.5) 100 mM)
| References:
- Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH. "Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition." Cell. 2001; 105(6): 721-32. PubMed: 11440715
| Comments:
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Region 2 | Type: | Disordered | Name: | | Location: | 387 - 420 | Length: | 34 | Region sequence: |
AASTPTNATAASDANTGDRGQTNNAASASASNST | Modification type: | Native
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (100 K; DTT (pH 7.2) 1 mM; HEPES-NaOH 20 mM; MgCl2 2 mM; NaCl 500 mM; PEG 8000 6 %; Tris-HCl (pH 7.5) 100 mM)
| References:
- Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH. "Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition." Cell. 2001; 105(6): 721-32. PubMed: 11440715
| Comments:
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Region 3 | Type: | Disordered | Name: | | Location: | 285 - 299 | Length: | 15 | Region sequence: |
NPNYTEFKFPQIKAH | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Phosphorylation
Substrate/ligand binding
| Detection methods:
- X-ray crystallography (100 K; )
| References:
- Dajani R, Fraser E, Roe SM, Yeo M, Good VM, Thompson V, Dale TC, Pearl LH. "Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex." EMBO J. 2003; 22(3): 494-501. PubMed: 12554650
| Comments:
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Region 4 | Type: | Disordered | Name: | | Location: | 120 - 126 | Length: | 7 | Region sequence: |
GEKKDEV | Modification type: | | PDB: | 1I09:A | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods: | References:
- ter Haar E, Coll JT, Austen DA, Hsiao HM, Swenson L, Jain J. "Structure of GSK3beta reveals a primed phosphorylation mechanism." Nat Struct Biol. 2001; 8(7): 593-6. PubMed: 11427888
| Comments:
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