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

Type Name Position InterPro Accession
domain AAA+ ATPase domain 205 - 344 IPR003593
domain ATPase, AAA-type, core 209 - 341 IPR003959
conserved_site ATPase, AAA-type, conserved site 312 - 330 IPR003960
domain Proteasomal ATPase OB C-terminal domain 96 - 151 IPR032501

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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