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 P40327

Entry ID Method Resolution Chain Position Source
3JCO EM 480 A I 1-437 PDB
3JCP EM 460 A I 1-437 PDB
4CR2 EM 770 A I 1-437 PDB
4CR3 EM 930 A I 1-437 PDB
4CR4 EM 880 A I 1-437 PDB
5A5B EM 950 A I 1-437 PDB
5MP9 EM 410 A I 1-437 PDB
5MPA EM 450 A I 1-437 PDB
5MPB EM 780 A I 1-437 PDB
5MPC EM 770 A I 1-437 PDB
5WVI EM 630 A I 1-437 PDB
5WVK EM 420 A I 1-437 PDB
6EF0 EM 443 A I 166-436 PDB
6EF1 EM 473 A I 167-437 PDB
6EF2 EM 427 A I 178-437 PDB
6EF3 EM 417 A I 1-437 PDB
6FVT EM 410 A I 53-437 PDB
6FVU EM 450 A I 54-437 PDB
6FVV EM 540 A I 53-437 PDB
6FVW EM 450 A I 53-437 PDB
6FVX EM 490 A I 53-437 PDB
6FVY EM 610 A I 53-437 PDB
6J2C EM 700 A I 1-437 PDB
6J2N EM 750 A I 1-437 PDB
6J2Q EM 380 A I 1-437 PDB
6J2X EM 380 A I 1-437 PDB
6J30 EM 450 A I 1-437 PDB
7QO4 EM 700 A I 1-437 PDB
7QO5 EM 600 A I 1-437 PDB
AF-P40327-F1 Predicted AlphaFoldDB

2 variants for P40327

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-439157 372 S>G No SGRP
s04-439158 372 S>N No SGRP

No associated diseases with P40327

5 regional properties for P40327

Type Name Position InterPro Accession
domain AAA+ ATPase domain 215 - 354 IPR003593
domain ATPase, AAA-type, core 219 - 351 IPR003959
conserved_site ATPase, AAA-type, conserved site 322 - 340 IPR003960
domain Proteasomal ATPase OB C-terminal domain 106 - 160 IPR032501
domain AAA ATPase, AAA+ lid domain 374 - 417 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
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.

3 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.

7 GO annotations of biological process

Name Definition
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.
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
positive regulation of protein catabolic process Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
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.
protein-containing complex localization A localization process that acts on a protein complex; the complex is transported to, or maintained in, a specific location.
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.

6 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
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
P46466 TBP2 26S proteasome regulatory subunit 4 homolog Oryza sativa subsp japonica (Rice) PR
Q9SL67 RPT2B 26S proteasome regulatory subunit 4 homolog B Arabidopsis thaliana (Mouse-ear cress) PR
Q9SZD4 RPT2A 26S proteasome regulatory subunit 4 homolog A Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGQGVSSGQD KKKKKGSNQK PKYEPPVQSK FGRKKRKGGP ATAEKLPNIY PSTRCKLKLL
70 80 90 100 110 120
RMERIKDHLL LEEEFVSNSE ILKPFEKKQE EEKKQLEEIR GNPLSIGTLE EIIDDDHAIV
130 140 150 160 170 180
TSPTMPDYYV SILSFVDKEL LEPGCSVLLH HKTMSIVGVL QDDADPMVSV MKMDKSPTES
190 200 210 220 230 240
YSDIGGLESQ IQEIKESVEL PLTHPELYEE MGIKPPKGVI LYGAPGTGKT LLAKAVANQT
250 260 270 280 290 300
SATFLRIVGS ELIQKYLGDG PRLCRQIFKV AGENAPSIVF IDEIDAIGTK RYDSNSGGER
310 320 330 340 350 360
EIQRTMLELL NQLDGFDDRG DVKVIMATNK IETLDPALIR PGRIDRKILF ENPDLSTKKK
370 380 390 400 410 420
ILGIHTSKMN LSEDVNLETL VTTKDDLSGA DIQAMCTEAG LLALRERRMQ VTAEDFKQAK
430
ERVMKNKVEE NLEGLYL