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 Q9VRL3

Entry ID Method Resolution Chain Position Source
AF-Q9VRL3-F1 Predicted AlphaFoldDB

No variants for Q9VRL3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VRL3

No associated diseases with Q9VRL3

No regional properties for Q9VRL3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9VRL3

Functions

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

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
prefoldin complex A multisubunit chaperone that is capable of delivering unfolded proteins to cytosolic chaperonin, which it acts as a cofactor for. In humans, the complex is a heterohexamer of two PFD-alpha and four PFD-beta type subunits. In Saccharomyces cerevisiae, it also acts in the nucleus to regulate the rate of elongation by RNA polymerase II via a direct effect on histone dynamics.

1 GO annotations of molecular function

Name Definition
unfolded protein binding Binding to an unfolded protein.

1 GO annotations of biological process

Name Definition
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAKVASGTN KVFQNHDDVH ISFEDQQRIN RFAKHNARMD DFKAELETKR NELKSLEEAL
70 80 90 100 110 120
EEIELFDEDE DIPFLVGEVF LSHKLEKTQD MLKETKEQVL KEIAGVEAKA KVIKAEMDEL
130
KAHLYQRFGS NISLEAED