lmmol · Proteins

Proteasome subunit alpha type-7

UniProt O14818 Organism Homo sapiens Gene HSPC, PSMA7

Also known as: HSPC, PSMA7

Function

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.

Classification

Family (Pfam)
PF00227 Proteasome, PF10584 Proteasome_A_N
InterPro
Ntn_hydrolases_N, Proteasome_alpha, Proteasome_alpha-type, Proteasome_asu_N, Proteasome_sua/b
Functional cluster
Small GTPases (Ras/Rab) & related

Experimental structures · PDB · 126

A predicted model is available from AlphaFold.

Gene Ontology · 33

Drugs targeting this protein · 7

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

Literature · 37 cited papers

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