ID:PSA7_HUMAN DESCRIPTION: RecName: Full=Proteasome subunit alpha type-7; EC=3.4.25.1; AltName: Full=Proteasome subunit RC6-1; AltName: Full=Proteasome subunit XAPC7; FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. 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. CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad specificity. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Interacts with HIV-1 TAT protein. Interacts with hepatitis B virus X protein (HBX). Interacts with HIF1A. Interacts with RAB7A. Interacts with PARK2. Interacts with ABL1 and ABL2. Interacts with EMAP2. Interacts with MAVS. INTERACTION: Self; NbExp=2; IntAct=EBI-603272, EBI-603272; P25786:PSMA1; NbExp=7; IntAct=EBI-603272, EBI-359352; P25787:PSMA2; NbExp=2; IntAct=EBI-603272, EBI-603262; P25788:PSMA3; NbExp=4; IntAct=EBI-603272, EBI-348380; P25789:PSMA4; NbExp=6; IntAct=EBI-603272, EBI-359310; P60900:PSMA6; NbExp=6; IntAct=EBI-603272, EBI-357793; SUBCELLULAR LOCATION: Cytoplasm. Nucleus. INDUCTION: Down-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues. PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks. SIMILARITY: Belongs to the peptidase T1A family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O14818
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006508 proteolysis GO:0006511 ubiquitin-dependent protein catabolic process GO:0016032 viral process GO:0016579 protein deubiquitination GO:0043687 post-translational protein modification GO:0051603 proteolysis involved in cellular protein catabolic process