P46471
PR
Gene name |
Psmc2 (Mss1) |
Protein name |
26S proteasome regulatory subunit 7 |
Names |
26S proteasome AAA-ATPase subunit RPT1, Proteasome 26S subunit ATPase 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:19181 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P46471
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P46471-F1 | Predicted | AlphaFoldDB |
15 variants for P46471
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388731329 | 12 | T>S | No | EVA | |
| rs3388743200 | 46 | K>E | No | EVA | |
| rs3388738841 | 81 | A>S | No | EVA | |
| rs3388743169 | 99 | T>M | No | EVA | |
| rs3388745428 | 143 | D>E | No | EVA | |
| rs3388718020 | 271 | L>I | No | EVA | |
| rs3388752354 | 302 | L>F | No | EVA | |
| rs3388745934 | 348 | L>F | No | EVA | |
| rs3388741427 | 368 | I>N | No | EVA | |
| rs3388728299 | 375 | R>H | No | EVA | |
| rs3388735716 | 380 | S>N | No | EVA | |
| rs3388749538 | 398 | R>* | No | EVA | |
| rs3388731334 | 414 | N>Y | No | EVA | |
| rs3388749507 | 416 | V>A | No | EVA | |
| rs3388749542 | 423 | F>L | No | EVA |
No associated diseases with P46471
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasmic ribonucleoprotein granule | A ribonucleoprotein granule located in the cytoplasm. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| P-body | A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. |
| proteasome accessory complex | A protein complex, that caps one or both ends of the proteasome core complex and regulates entry into, or exit from, the proteasome core complex. |
| proteasome complex | A large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. In eukaryotes, this complex consists of the barrel shaped proteasome core complex and one or two associated proteins or complexes that act in regulating entry into or exit from the core. |
| proteasome regulatory particle, base subcomplex | The subcomplex of the proteasome regulatory particle that directly associates with the proteasome core complex. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| general transcription initiation factor binding | Binding to a general transcription initiation factor, a protein that contributes to transcription start site selection and transcription initiation. |
| proteasome-activating activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome. |
| TBP-class protein binding | Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P33299 | RPT1 | 26S proteasome regulatory subunit 7 homolog | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q5E9F9 | PSMC2 | 26S proteasome regulatory subunit 7 | Bos taurus (Bovine) | PR |
| P35998 | PSMC2 | 26S proteasome regulatory subunit 7 | Homo sapiens (Human) | PR |
| P62196 | Psmc5 | 26S proteasome regulatory subunit 8 | Mus musculus (Mouse) | PR |
| O88685 | Psmc3 | 26S proteasome regulatory subunit 6A | Mus musculus (Mouse) | PR |
| Q63347 | Psmc2 | 26S proteasome regulatory subunit 7 | Rattus norvegicus (Rat) | PR |
| Q0WQM8 | At1g53790 | F-box protein At1g53790 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPDYLGADQR | KTKEEEKDDK | PIRALDEGDI | ALLKTYGQST | YSRQIKQVED | DIQQLLKKIN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELTGIKESDT | GLAPPALWDL | AADKQTLQSE | QPLQVARCTK | IINADSEDPK | YIINVKQFAK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FVVDLSDQVA | PTDIEEGMRV | GVDRNKYQIH | IPLPPKIDPT | VTMMQVEEKP | DVTYSDVGGC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEQIEKLREV | VETPLLHPER | FVNLGIEPPK | GVLLFGPPGT | GKTLCARAVA | NRTDACFIRV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGSELVQKYV | GEGARMVREL | FEMARTKKAC | LIFFDEIDAI | GGARFDDGAG | GDNEVQRTML |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELINQLDGFD | PRGNIKVLMA | TNRPDTLDPA | LMRPGRLDRK | IEFSLPDLEG | RTHIFKIHAR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SMSVERDIRF | ELLARLCPNS | TGAEIRSVCT | EAGMFAIRAR | RKIATEKDFL | EAVNKVIKSY |
| 430 | |||||
| AKFSATPRYM | TYN |