about
P688
Insulin like growth factor-1-induced phosphorylation and altered distribution of tuberous sclerosis complex (TSC)1/TSC2 in C2C12 myotubesLaforin, the most common protein mutated in Lafora disease, regulates autophagyHypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttlingReactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1IκB kinase complex (IKK) triggers detachment-induced autophagy in mammary epithelial cells independently of the PI3K-AKT-MTORC1 pathwayp53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signalingTSC2 missense mutations inhibit tuberin phosphorylation and prevent formation of the tuberin-hamartin complexInsulin inhibits lipolysis in adipocytes via the evolutionarily conserved mTORC1-Egr1-ATGL-mediated pathwayThe TSC1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteinsTsc2(+/-) mice develop tumors in multiple sites that express gelsolin and are influenced by genetic backgroundEnhanced cardiomyocyte DNA synthesis during myocardial hypertrophy in mice expressing a modified TSC2 transgeneFeedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2The tuberous sclerosis complex regulates trafficking of glucose transporters and glucose uptakeRegulation of neuronal morphology and function by the tumor suppressors Tsc1 and Tsc2Renal carcinogenesis, hepatic hemangiomatosis, and embryonic lethality caused by a germ-line Tsc2 mutation in miceGenetic analysis of Pten and Tsc2 functional interactions in the mouse reveals asymmetrical haploinsufficiency in tumor suppressionTuberous sclerosis complex tumor suppressor-mediated S6 kinase inhibition by phosphatidylinositide-3-OH kinase is mTOR independent
P921
Q24307579-40357740-6E3F-4449-9B91-5DA7CA1B213CQ24311181-459259AF-4CF1-4366-8D0E-4255ADAD993EQ24677061-88740DDB-5938-49A2-8B3A-CE439B53C296Q28115279-5CCD75DF-6224-42BE-B356-B4D2159A46A6Q28116229-43B0FBD8-E7F3-47C3-807B-865D0AA1E377Q28117922-27F53DE5-A6E6-4A39-AF98-5440B77201DAQ28210486-5518B3B2-4461-4601-8B65-CC56BD93F69DQ28505405-002843D6-DA45-4AB5-B537-F4A122BCDC61Q28507365-4EA175FA-454C-42D5-BB54-0B7DF4A8DEFBQ28507548-FB57C720-BDF7-45FA-A898-C63B9673B226Q28508426-494DF65F-449F-4BED-8E13-422C7B8D331AQ28509303-BEF4DB5B-E938-47CE-AB32-EC04AB01E4A6Q28512637-8554457C-2278-4096-92CC-E7479F59F3CDQ28578379-A176EA88-E771-4FC6-832D-D1D82F47E338Q28591496-A344AF38-ECBE-4EE2-B4E5-D730CCF35243Q28593244-8FD9F03C-4C68-4A19-BA3F-1E3497B0347BQ28593855-D4E3E597-C3B5-482F-8772-74E848B6A8EE
P921
description
mouse protein (annotated by UniProtKB/Swiss-Prot Q61037)
@en
proteinë
@sq
proteïne
@nl
بروتين في فأر المنازل
@ar
name
Tuberin
@en
type
label
Tuberin
@en
altLabel
Tuberous sclerosis 2 protein homolog
@en
prefLabel
Tuberin
@en
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SZCZSKMCTGEJKI-UHFFFAOYSA-N