INT246793

Context Info Confidence 0.04 First Reported 2008 Last Reported 2008 Negated 0 Speculated 0 Reported most in Body Documents 1 Total Number 2 Disease Relevance 0.71 Pain Relevance 0.04

cytosol (Tsc2, Tsc1) protein complex (Tsc2, Tsc1) cytoplasm (Tsc2, Tsc1) signal transduction (Tsc2) Golgi apparatus (Tsc2) nucleus (Tsc2)

Tsc2 (Rattus norvegicus) Tsc1 (Rattus norvegicus)

Pain Link Frequency Relevance Heat agonist 2 72.88 anesthesia 2 5.00

Disease Link Frequency Relevance Heat Cancer 2 98.80 Adhesions 2 87.92 Targeted Disruption 2 81.36 Apoptosis 4 75.52 Injury 8 65.76 Diabetes Mellitus 78 65.36 Diabetes Complications 2 61.84 Albuminuria 2 60.36 Stress 14 35.48 Renal Disease 4 32.60

Sentences Mentioned In

Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

Tuberin normally exists in an active state physically bound to hamartin, the product of TSC-1 gene, to form a stable complex (22).

Tuberin Binding (bound) of hamartin

1) Confidence 0.04 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.57 Pain Relevance 0.04

Phosphorylation of tuberin by Akt affects its function through at least two mechanisms: first, phosphorylation decreases the activity of tuberin; second, phosphorylation destabilizes tuberin by disrupting the complex formation between hamartin and tuberin, resulting in ubiquitination of free tuberin and its degradation by the proteosome (27).

tuberin Binding (formation) of hamartin

2) Confidence 0.03 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.14 Pain Relevance 0

General Comments

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