Tsc1
entrez
60445
canonical
uniprot
Q9Z136
canonical
ensembl
ENSRNOG00000011470
resolver
ensp
ENSRNOP00000016904
resolver
genesymbol
Tsc1
resolver
uniprot_entry
TSC1_RAT
resolver
amino_acid_sequence
MAQLANIGELLSMLDSSTLGVRDDVTTIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKMNEYVGKAATRLSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKTLETHDVVIECAKISLDPTEASYEDGDAVSHQLSACFPHRSADVTTSSYVDTQNSYGGATSTPSSTSRLMLFSTPGQLPQSLSSLSTRPLPEPLQASLWSPSAVCGMTTPPTSPGNVPADLSHPYSKAFGTTTGGKGTPSGTPATSPPPAPPCPQDDCAHGPASQASATPPRKEERADSSRPYLPRQQDVPSDRGLEDLPGSKGSVTLRNLPDFLGDLASEEDSIEKDKEEAAISKELSEITTAEADPVAPRGGFDSPFYRDSLSGSQRKTHSAASGTQGFSVNPEPLHSSLDKHGPDTPKQAFTPIDPPSGSADASPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTACHFVSKKTEELLKKAKGNPEEDCVPSTSPMEVLDRLLEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQQQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRSMIAELRVELKKANSKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLQKLEEDRAEAAEAAEERLDCCTDGCSDSLLGHNEEAAGHNGETRTSRPGGTRASCGGRVTGGSSSSSSELSTPEKPPNQRFSSRWEPTMGEPSSSIPTTVGSLPSSKSFLGMKTRELFRNKSESQCDEDGMTMSSFSETLKTELGKDSAGMENKTPPSLDAPHPSSPSSDSMGQLHIMDYNETHHEHS
uniprot
proteins
function
FUNCTION: Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (By similarity). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (By similarity). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (By similarity). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (By similarity). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:16707451). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (PubMed:16707451). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (By similarity). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (By similarity). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (By similarity). {ECO:0000250|UniProtKB:Q92574, ECO:0000269|PubMed:16707451}.
uniprot
proteins
mass_dalton
129022
uniprot
proteins
mutagenesis
MUTAGEN 287; /note="H->Q: In chemically induced renal carcinogenesis."; /evidence="ECO:0000269|PubMed:10029074"; MUTAGEN 674; /note="V->L: In chemically induced renal carcinogenesis."; /evidence="ECO:0000269|PubMed:10029074"; MUTAGEN 1027; /note="R->W: In chemically induced renal carcinogenesis."; /evidence="ECO:0000269|PubMed:10029074"; MUTAGEN 1106; /note="M->V: In chemically induced renal carcinogenesis."; /evidence="ECO:0000269|PubMed:10029074
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-505 does not affect interaction with TSC2. {ECO:0000250|UniProtKB:Q92574}.; PTM: 'Lys-63'-linked ubiquitinated at Lys-30 by PELI1; the ubiquitination promotes TSC1/TSC2 complex stability. {ECO:0000250|UniProtKB:Q92574}.
uniprot
proteins
pubmed
10029074
uniprot
proteins
pubmed
16707451
uniprot
proteins
pubmed
9809973
uniprot
proteins
sequence_length
1163
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q92574}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92574}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92574}. Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients. In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol. {ECO:0000250|UniProtKB:Q92574}.
uniprot
proteins