| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-600998,
cpath:CPATH-LOCAL-600998,
cpath:CPATH-LOCAL-600999,
cpath:CPATH-LOCAL-600999,
cpath:CPATH-LOCAL-601000,
cpath:CPATH-LOCAL-601000,
cpath:CPATH-LOCAL-601001,
cpath:CPATH-LOCAL-601001,
cpath:CPATH-LOCAL-601002,
cpath:CPATH-LOCAL-601002,
cpath:CPATH-LOCAL-601003,
cpath:CPATH-LOCAL-601003,
cpath:CPATH-LOCAL-601004,
cpath:CPATH-LOCAL-601004,
cpath:CPATH-LOCAL-601005,
cpath:CPATH-LOCAL-601005,
cpath:CPATH-LOCAL-608393,
cpath:CPATH-LOCAL-608393
|
| http://www.biopax.org/relea... |
Glycogen synthase kinase-3 beta,
Glycogen synthase kinase-3 beta
|
| http://www.biopax.org/relea... |
GSK3B_HUMAN,
GSK3B_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
2.7.11.26,
2.7.11.26,
GSK-3 beta,
GSK-3 beta
|
| http://www.biopax.org/relea... |
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. 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. May be required for early embryo development and neuron differentiation (By similarity). CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein] phosphate. ENZYME REGULATION: Activated by phosphorylation at Tyr-216. Inhibited when phosphorylated by AKT1. SUBUNIT: Monomer (By similarity). Interacts with ARRB2 and DISC1 (By similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE Interacts with AXIN1; the interaction mediates hyperphosphorylates of CTNNB1 leading to its ubiquitination and destruction. Interacts with and phosphorylates SNAI1. Interacts with DNM1L (via a C- terminal domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=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. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49841-1; Sequence=Displayed; Name=2; IsoId=P49841-2; Sequence=VSP_004790; Note=No experimental confirmation available; TISSUE SPECIFICITY: Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney. PTM: Phosphorylated by AKT1 and ILK1. Activated by phosphorylation at Tyr-216. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily. SIMILARITY: Contains 1 protein kinase domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
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. 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. May be required for early embryo development and neuron differentiation (By similarity). CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein] phosphate. ENZYME REGULATION: Activated by phosphorylation at Tyr-216. Inhibited when phosphorylated by AKT1. SUBUNIT: Monomer (By similarity). Interacts with ARRB2 and DISC1 (By similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE Interacts with AXIN1; the interaction mediates hyperphosphorylates of CTNNB1 leading to its ubiquitination and destruction. Interacts with and phosphorylates SNAI1. Interacts with DNM1L (via a C- terminal domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=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. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49841-1; Sequence=Displayed; Name=2; IsoId=P49841-2; Sequence=VSP_004790; Note=No experimental confirmation available; TISSUE SPECIFICITY: Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney. PTM: Phosphorylated by AKT1 and ILK1. Activated by phosphorylation at Tyr-216. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily. SIMILARITY: Contains 1 protein kinase domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch | |
| skos:closeMatch |