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

30 structures for Q01939

Entry ID Method Resolution Chain Position Source
3JCO EM 480 A J 1-405 PDB
3JCP EM 460 A J 1-405 PDB
4CR2 EM 770 A J 1-405 PDB
4CR3 EM 930 A J 1-405 PDB
4CR4 EM 880 A J 1-405 PDB
5A5B EM 950 A J 1-405 PDB
5MP9 EM 410 A J 1-405 PDB
5MPA EM 450 A J 1-405 PDB
5MPB EM 780 A J 1-405 PDB
5MPC EM 770 A J 1-405 PDB
5WVI EM 630 A J 1-405 PDB
5WVK EM 420 A J 1-405 PDB
6EF0 EM 443 A J 130-405 PDB
6EF1 EM 473 A J 133-405 PDB
6EF2 EM 427 A J 144-405 PDB
6EF3 EM 417 A J 1-405 PDB
6FVT EM 410 A J 1-405 PDB
6FVU EM 450 A J 1-405 PDB
6FVV EM 540 A J 1-405 PDB
6FVW EM 450 A J 3-405 PDB
6FVX EM 490 A J 1-405 PDB
6FVY EM 610 A J 1-405 PDB
6J2C EM 700 A J 1-405 PDB
6J2N EM 750 A J 1-405 PDB
6J2Q EM 380 A J 1-405 PDB
6J2X EM 380 A J 1-405 PDB
6J30 EM 450 A J 1-405 PDB
7QO4 EM 700 A J 1-405 PDB
7QO5 EM 600 A J 1-405 PDB
AF-Q01939-F1 Predicted AlphaFoldDB

3 variants for Q01939

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-411052 80 S>P No SGRP
s07-410965 109 A>T No SGRP
s07-410329 321 V>I No SGRP

No associated diseases with Q01939

5 regional properties for Q01939

Type Name Position InterPro Accession
domain AAA+ ATPase domain 181 - 320 IPR003593
domain ATPase, AAA-type, core 185 - 317 IPR003959
conserved_site ATPase, AAA-type, conserved site 288 - 306 IPR003960
domain Proteasomal ATPase OB C-terminal domain 72 - 127 IPR032501
domain AAA ATPase, AAA+ lid domain 341 - 383 IPR041569

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
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.
proteasome storage granule An aggregation of proteasome core protease (CP) and regulatory particle (RP) complexes that localizes in the cytoplasm as dot-like structures when cells are in a quiescent state.

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.
proteasome-activating activity Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
protein domain specific binding Binding to a specific domain of a protein.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.

9 GO annotations of biological process

Name Definition
chromatin remodeling A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication.
negative regulation of DNA-binding transcription factor activity Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
nonfunctional rRNA decay An rRNA catabolic process that results in the targeted detection and degradation of aberrant rRNAs contained within translationally defective ribosomes, thereby acting as a quality-control system.
nucleotide-excision repair A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
positive regulation of DNA-binding transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
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.
positive regulation of transcription elongation by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
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.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P33298 RPT3 26S proteasome regulatory subunit 6B homolog Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
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
P62194 PSMC5 26S proteasome regulatory subunit 8 Bos taurus (Bovine) PR
O18413 Rpt6 26S proteasome regulatory subunit 8 Drosophila melanogaster (Fruit fly) PR
P62195 PSMC5 26S proteasome regulatory subunit 8 Homo sapiens (Human) PR
P62196 Psmc5 26S proteasome regulatory subunit 8 Mus musculus (Mouse) PR
P62197 PSMC5 26S proteasome regulatory subunit 8 Sus scrofa (Pig) PR
P62198 Psmc5 26S proteasome regulatory subunit 8 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MTAAVTSSNI VLETHESGIK PYFEQKIQET ELKIRSKTEN VRRLEAQRNA LNDKVRFIKD
70 80 90 100 110 120
ELRLLQEPGS YVGEVIKIVS DKKVLVKVQP EGKYIVDVAK DINVKDLKAS QRVCLRSDSY
130 140 150 160 170 180
MLHKVLENKA DPLVSLMMVE KVPDSTYDMV GGLTKQIKEI KEVIELPVKH PELFESLGIA
190 200 210 220 230 240
QPKGVILYGP PGTGKTLLAR AVAHHTDCKF IRVSGAELVQ KYIGEGSRMV RELFVMAREH
250 260 270 280 290 300
APSIIFMDEI DSIGSTRVEG SGGGDSEVQR TMLELLNQLD GFETSKNIKI IMATNRLDIL
310 320 330 340 350 360
DPALLRPGRI DRKIEFPPPS VAARAEILRI HSRKMNLTRG INLRKVAEKM NGCSGADVKG
370 380 390 400
VCTEAGMYAL RERRIHVTQE DFELAVGKVM NKNQETAISV AKLFK