human PSMC5 shRNA silencing AAV

26S protease regulatory subunit 8; 26S proteasome AAA-ATPase subunit RPT6; 26S proteasome regulatory subunit 8; MSUG1 protein; p45; p45/SUG; proteasome (prosome, macropain) 26S subunit, ATPase, 5; proteasome 26S ATPase subunit 5; Proteasome 26S subunit ATPase 5; proteasome subunit p45; S8; SUG1; SUG-1; Tat-binding protein homolog 10; TBP10; testicular tissue protein Li 149; thyroid hormone receptor-interacting protein 1; thyroid receptor interactor 1; TRIP1

Thyroid receptor interacting protein 1 (TRIP1) was originally identified as a protein that interacts with the thyroid receptor and is homologous to the yeast SUG1 protein, a transcriptional coactivator. It was later identified as an ATPase subunit of the 26S proteasome, a multicatalytic proteinase complex, and has also been shown to associate with nuclear receptors and transcription factors. TRIP1/SUG1 may function to regulate transcription factor abundance by targeting them for proteasome degradation.

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha. Two transcript variants encoding different isoforms have been found for this gene.

5705

proteasome 26S subunit, ATPase 5

proteasome 26S subunit, ATPase 5

PSMC5

HGNC:9552

9606.0

1221

1221 bp

26S protease regulatory subunit 8

NM_002805

NM_002805, NM_001199163, BC002367, BC001932,

Antigen Processing and Presentation,Apoptosis,B-cell Receptor Signaling,Cell Cycle,Complexome,DNA Damage/Repair,Gene Expression,Hedgehog Signaling,Host-Virus Interactions,Immunology,Interleukin Signaling,JAK-STAT Signaling,Metabolism/Metabolic Process,Neurobiology,Neurodegeneration,NF-kB Signaling,Notch Signaling,Parkinson's Disease,Parkin-Ubiquitin Proteasomal System,Proteasome,RNA Processing,Signal Transduction,T-cell Receptor Signaling,TGF-beta Signaling,TNF Signaling,Toll-like Receptor Signaling,Transcription Factor/Regulator,Ubiquitination,Wnt Signaling

signal_transduction,immunology,cell_biology,signal_transduction,immunology,cell_biology,cell_cycle,genetics,transcription_translation,signal_transduction,developmental_biology,infectious_disease,immunology,signal_transduction,metabolism,neurobiology,signal_transduction,immunology,developmental_biology,neurobiology,cell_biology,genetics,transcription_translation,signal_transduction,immunology,genetics,transcription_translation,developmental_biology

human

Thyroid receptor interacting protein 1 (TRIP1) was originally identified as a protein that interacts with the thyroid receptor and is homologous to the yeast SUG1 protein, a transcriptional coactivator. It was later identified as an ATPase subunit of the 26S proteasome, a multicatalytic proteinase complex, and has also been shown to associate with nuclear receptors and transcription factors. TRIP1/SUG1 may function to regulate transcription factor abundance by targeting them for proteasome degradation.

Hs.79387

P62195