| Tbio | 26S proteasome regulatory subunit 6A |
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. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases that have chaperone-like activity. This subunit may compete with PSMC2 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex. A pseudogene has been identified on chromosome 9. [provided by RefSeq, Jul 2008]
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases that have chaperone-like activity. This subunit may compete with PSMC2 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex. A pseudogene has been identified on chromosome 9. [provided by RefSeq, Jul 2008]
Comments
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| HIV Infections | 102 | 0.0 | 0.0 |
| Disease | Target Count | P-value |
|---|---|---|
| Multiple myeloma | 1332 | 1.1e-03 |
| ovarian cancer | 8520 | 1.6e-03 |
| lung cancer | 4740 | 1.9e-03 |
| subependymal giant cell astrocytoma | 2287 | 4.9e-02 |
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| Acquired metabolic disease | 336 | 0.0 | 3.0 |
| Disease | log2 FC | p |
|---|---|---|
| lung cancer | 1.100 | 1.9e-03 |
| Multiple myeloma | 1.182 | 1.1e-03 |
| ovarian cancer | 1.300 | 1.6e-03 |
| subependymal giant cell astrocytoma | -1.255 | 4.9e-02 |
PSMD1
RAI14
KAT14
ZZZ3
PSMC4
YEATS2
KIF1A
KIF1B
TAB1
FLYWCH2
PSMC6
PSMD2
NFRKB
PSMD10
TPD52L1
FBXO28
FAM117B
LIN54
RPL23
PHF19
PSMD12
LRIF1
MGA
PSMD6
MBIP
GTF2F1
MPRIP
TBC1D2B
SLMAP
CHD8
PARD3
TADA2A
GARS
TRAF4
EIF2D
EIF2AK4
L3MBTL2
STKLD1
PEX6
ELF2
TSEN15
NEDD1
SPATS2
FAM83D
KXD1
ATG16L1
MAVS
UBXN1
SCML1
RNASEH2C
TSR3
ARHGEF1
E2F6
CXXC1
MEX3D
MAP3K7
MARK4
TRMO
MNLLPNIESPVTRQEKMATVWDEAEQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVLRVTHELQAMK 1 - 70 DKIKENSEKIKVNKTLPYLVSNVIELLDVDPNDQEEDGANIDLDSQRKGKCAVIKTSTRQTYFLPVIGLV 71 - 140 DAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKE 141 - 210 KFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAP 211 - 280 SIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDR 281 - 350 KIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDY 351 - 420 MEGILEVQAKKKANLQYYA 421 - 439 //
