• Glycogen Synthase Kinase 3 Beta
• Glycogen synthase kinase-3 beta
• GSK 3 beta

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. Phosphorylates SNAI1. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Prevents the phosphorylation of APC ａnd CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture ａnd stabilization. Phosphorylates MACF1 ａnd this phosphorylation inhibits the binding of MACF1 to microtubules which is critical for its role in bulge stem cell migration ａnd skin wound repair.

Expressed in testis, thymus, prostate ａnd ovary ａnd weakly expressed in lung, brain ａnd kidney.

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Contains 1 protein kinase domain.

Phosphorylated by AKT1 ａnd ILK1. Activated by phosphorylation at Tyr-216.

Cytoplasm. Nucleus. Cell membrane. The phosphorylated form shows localization to cytoplasm ａnd cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.

Target information above from: UniProt accession  P49841The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .