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MGP002475

UniProt Annotations

Entry Information
Gene Nameproteasome (prosome, macropain) subunit, alpha type, 7
Protein EntryPSA7_HUMAN
UniProt IDO14818
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Comment=Experimental confirmation may be lacking for some isoforms.; Name=1; IsoId=O14818-1; Sequence=Displayed; Name=2; IsoId=O14818-2; Sequence=VSP_005281; Name=3; IsoId=O14818-4; Sequence=VSP_046556, VSP_046557;
Catalytic ActivityCleavage of peptide bonds with very broad specificity. {ECO:0000255|PROSITE-ProRule:PRU00808}.
FunctionThe 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. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229}.
InductionDown-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues. {ECO:0000269|PubMed:11574696, ECO:0000269|PubMed:18202793}.
InteractionSelf; NbExp=3; IntAct=EBI-603272, EBI-603272; P25786:PSMA1; NbExp=9; IntAct=EBI-603272, EBI-359352; P25787:PSMA2; NbExp=5; IntAct=EBI-603272, EBI-603262; P25788:PSMA3; NbExp=6; IntAct=EBI-603272, EBI-348380; P25789:PSMA4; NbExp=8; IntAct=EBI-603272, EBI-359310; P28066:PSMA5; NbExp=2; IntAct=EBI-603272, EBI-355475; P60900:PSMA6; NbExp=11; IntAct=EBI-603272, EBI-357793;
PtmPhosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks. {ECO:0000269|PubMed:16678104}.
SimilarityBelongs to the peptidase T1A family. {ECO:0000255|PROSITE-ProRule:PRU00808}.
Subcellular LocationCytoplasm. Nucleus.
SubunitThe 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. {ECO:0000269|PubMed:10748218, ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:14998988, ECO:0000269|PubMed:15987638, ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:19362550, ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:8764072}.
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