PSMD10 — Proteasome 26S subunit, non-ATPase 10
PSMD10 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
PSMD10's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Endothelial | Actin Cytoskeletal Remodeling Cytoskeletal | ACTR2, ANKRD11, ARPC4, CAP1, EIF4G1, FYTTD1, G3BP1, GSPT1 +8 more | View in SCUBA |
About the gene
| Synonyms | p28 |
|---|---|
| Chromosome | X: 108084207-108091549 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins |
| Molecular function | Chaperone |
| Biological process | Apoptosis |
Function
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.