PSMD11 — Proteasome 26S subunit, non-ATPase 11
PSMD11 belongs to a gene co-expression module in 4 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.
PSMD11's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Proteasome/translation Protein processing & ER | ANP32E, CDC123, EIF4E, EIF5B, EMC8, MRPL20, NME7, PDXK +9 more | View in SCUBA |
| Innate lymphoid cells | Innate Immune Activation Inflammation | ANKRD11, ATP10D, CNOT2, COA4, DOCK10, IKZF2, NIFK, PRKDC +13 more | View in SCUBA |
| Lymphatic endothelial | NRF2 Oxidative Stress Stress | B4GALT1, CTTNBP2NL, DDX21, DRAM1, GCH1, HNRNPF, MSN, NFE2L2 +11 more | View in SCUBA |
| Macrophages | Osmotic Stress Response Stress | ANKRD28, BZW1, CD109, CXCL8, CYB5R4, CYTIP, DUSP4, EMP3 +25 more | View in SCUBA |
About the gene
| Synonyms | MGC3844, p44.5, Rpn6, S9 |
|---|---|
| Chromosome | 17: 32444379-32483319 |
| Predicted location | Intracellular |
| Essential gene | Yes |
| Protein class | Essential proteins, Plasma proteins, Predicted intracellular proteins |
Function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.