TSC1 In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1. Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1. Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney. Also expressed in embryonic kidney cells. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Tumor suppressor
Chromosomal Location of Human Ortholog: 3p12
Cellular Component:  actin filament; cell cortex; cell projection; chaperone complex; cytoplasm; cytoskeleton; cytosol; growth cone; intracellular membrane-bounded organelle; lamellipodium; lipid droplet; membrane; nucleus; perinuclear region of cytoplasm; postsynaptic density; protein-containing complex; TSC1-TSC2 complex
Molecular Function:  ATPase inhibitor activity; chaperone binding; GTPase activating protein binding; Hsp70 protein binding; Hsp90 protein binding; protein binding; protein N-terminus binding
Biological Process:  activation of GTPase activity; adaptive immune response; adult locomotory behavior; cardiac muscle cell differentiation; cell projection organization; cell-matrix adhesion; cellular response to oxygen-glucose deprivation; cerebral cortex development; glucose import; hippocampus development; kidney development; memory T cell differentiation; myelination; negative regulation of ATPase activity; negative regulation of cell proliferation; negative regulation of cell size; negative regulation of GTPase activity; negative regulation of insulin receptor signaling pathway; negative regulation of macroautophagy; negative regulation of neuron projection development; negative regulation of oxidative stress-induced neuron death; negative regulation of TOR signaling; negative regulation of translation; nervous system development; neural tube closure; positive regulation of focal adhesion assembly; positive regulation of macroautophagy; positive regulation of stress fiber assembly; potassium ion transport; protein heterooligomerization; protein stabilization; regulation of cell cycle; regulation of cell-matrix adhesion; regulation of focal adhesion assembly; regulation of neuron death; regulation of phosphoprotein phosphatase activity; regulation of protein kinase activity; regulation of stress fiber assembly; regulation of translation; response to insulin; rRNA export from nucleus; synapse organization
Reference #:  Q9Z136 (UniProtKB)
Alt. Names/Synonyms: Hamartin; Tsc1; tuberous sclerosis 1; Tuberous sclerosis 1 protein homolog
Gene Symbols: Tsc1
Molecular weight: 129,022 Da
Basal Isoelectric point: 5.9  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling  |  Insulin Receptor Signaling  |  mTOR Signaling  |  PI3K/Akt Signaling  |  Translation: eIF4E and p70S6K
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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TSC1

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene