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 Q9JK23

Entry ID Method Resolution Chain Position Source
AF-Q9JK23-F1 Predicted AlphaFoldDB

15 variants for Q9JK23

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389428614 2 A>S No EVA
rs3389418494 3 A>T No EVA
rs3389376880 35 D>N No EVA
rs3389430431 41 Q>L No EVA
rs3406335828 48 V>A No EVA
rs3389396695 54 Q>* No EVA
rs3389434689 58 S>A No EVA
rs3406414866 61 A>G No EVA
rs3407265127 67 H>Q No EVA
rs3389418556 85 S>P No EVA
rs3389426586 120 V>I No EVA
rs3389425523 199 K>R No EVA
rs3389425492 203 C>W No EVA
rs3389420983 215 D>A No EVA
rs3389376898 284 Q>L No EVA

No associated diseases with Q9JK23

No regional properties for Q9JK23

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9JK23

Functions

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

6 GO annotations of cellular component

Name Definition
chaperone complex A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

2 GO annotations of molecular function

Name Definition
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
proteasome binding Binding to a proteasome, a large multisubunit protein complex that catalyzes protein degradation.

3 GO annotations of biological process

Name Definition
cerebellar granule cell precursor proliferation The multiplication or reproduction of neuroblasts that will give rise to granule cells. A granule cell is a glutamatergic interneuron found in the cerebellar cortex.
chaperone-mediated protein complex assembly The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
proteasome core complex assembly The aggregation, arrangement and bonding together of a mature, active 20S proteasome core particle complex that does not contain any regulatory particles.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q0P5F2 PSMG1 Proteasome assembly chaperone 1 Bos taurus (Bovine) PR
O95456 PSMG1 Proteasome assembly chaperone 1 Homo sapiens (Human) PR
10 20 30 40 50 60
MAATFFGEVV KAPCRAGTEE EEEEEEQSRR DTPEDREVRR QLARKREVRL LRRQTETSLE
70 80 90 100 110 120
AVLLETHPCS KFIIAVGSNA TAFLSAFVMN SGVWEEVGCA KLWNEWCRTT DTVRLSPTDV
130 140 150 160 170 180
FCVFYQLKSD PSVFLCQCSC YIAEDQQFQW LEKVFGFQPR KSMQVTVLTC RHITDYKTPE
190 200 210 220 230 240
STCSLSSPFL RALKTQTFKD ALCCPLLEQP NIVHDLSAAV LSYCQVWKIP AVLYLCYTDV
250 260 270 280
MKLDRVTVEA FKPLLSSRSL KCLVKNIPES TEILKKLMTT NEIQSNIYT