P33298
Gene name |
RPT3 (YNT1, YTA2, YDR394W, D9509.14) |
Protein name |
26S proteasome regulatory subunit 6B homolog |
Names |
Protein YNT1, Tat-binding homolog 2 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YDR394W |
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
32 structures for P33298
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2DZN | X-ray | 220 A | B/D/F | 348-428 | PDB |
| 2DZO | X-ray | 300 A | B/D | 348-428 | PDB |
| 3JCO | EM | 480 A | K | 1-428 | PDB |
| 3JCP | EM | 460 A | K | 1-428 | PDB |
| 4CR2 | EM | 770 A | K | 1-428 | PDB |
| 4CR3 | EM | 930 A | K | 1-428 | PDB |
| 4CR4 | EM | 880 A | K | 1-428 | PDB |
| 5A5B | EM | 950 A | K | 1-428 | PDB |
| 5MP9 | EM | 410 A | K | 1-428 | PDB |
| 5MPA | EM | 450 A | K | 1-428 | PDB |
| 5MPB | EM | 780 A | K | 1-428 | PDB |
| 5MPC | EM | 770 A | K | 1-428 | PDB |
| 5WVI | EM | 630 A | K | 1-428 | PDB |
| 5WVK | EM | 420 A | K | 1-428 | PDB |
| 6EF0 | EM | 443 A | K | 157-428 | PDB |
| 6EF1 | EM | 473 A | K | 153-428 | PDB |
| 6EF2 | EM | 427 A | K | 170-428 | PDB |
| 6EF3 | EM | 417 A | K | 1-428 | PDB |
| 6FVT | EM | 410 A | K | 35-428 | PDB |
| 6FVU | EM | 450 A | K | 35-428 | PDB |
| 6FVV | EM | 540 A | K | 35-428 | PDB |
| 6FVW | EM | 450 A | K | 45-428 | PDB |
| 6FVX | EM | 490 A | K | 35-428 | PDB |
| 6FVY | EM | 610 A | K | 35-428 | PDB |
| 6J2C | EM | 700 A | K | 1-428 | PDB |
| 6J2N | EM | 750 A | K | 1-428 | PDB |
| 6J2Q | EM | 380 A | K | 1-428 | PDB |
| 6J2X | EM | 380 A | K | 1-428 | PDB |
| 6J30 | EM | 450 A | K | 1-428 | PDB |
| 7QO4 | EM | 700 A | K | 1-428 | PDB |
| 7QO5 | EM | 600 A | K | 1-428 | PDB |
| AF-P33298-F1 | Predicted | AlphaFoldDB |
1 variants for P33298
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s04-1262691 | 340 | F>S | No | SGRP |
No associated diseases with P33298
4 regional properties for P33298
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
| 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. |
4 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. |
| identical protein binding | Binding to an identical protein or proteins. |
| proteasome-activating activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of RNA polymerase II transcription preinitiation complex assembly | Any process that activates or increases the frequency, rate or extent of RNA polymerase II transcriptional preinitiation complex assembly. |
| proteasome regulatory particle assembly | The aggregation, arrangement and bonding together of a mature, active proteasome regulatory particle complex. |
| 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. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P40327 | RPT2 | 26S proteasome regulatory subunit 4 homolog | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P33299 | RPT1 | 26S proteasome regulatory subunit 7 homolog | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q01939 | RPT6 | 26S proteasome regulatory subunit 8 homolog | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P43686 | PSMC4 | 26S proteasome regulatory subunit 6B | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEELGIVTPV | EKAVEEKPAV | KSYASLLAQL | NGTVNNNSAL | SNVNSDIYFK | LKKLEKEYEL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTLQEDYIKD | EQRHLKRELK | RAQEEVKRIQ | SVPLVIGQFL | EPIDQNTGIV | SSTTGMSYVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RILSTLDREL | LKPSMSVALH | RHSNALVDIL | PPDSDSSISV | MGENEKPDVT | YADVGGLDMQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KQEIREAVEL | PLVQADLYEQ | IGIDPPRGVL | LYGPPGTGKT | MLVKAVANST | KAAFIRVNGS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EFVHKYLGEG | PRMVRDVFRL | ARENAPSIIF | IDEVDSIATK | RFDAQTGSDR | EVQRILIELL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQMDGFDQST | NVKVIMATNR | ADTLDPALLR | PGRLDRKIEF | PSLRDRRERR | LIFGTIASKM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SLAPEADLDS | LIIRNDSLSG | AVIAAIMQEA | GLRAVRKNRY | VILQSDLEEA | YATQVKTDNT |
| VDKFDFYK |