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 Q8UJC7

Entry ID Method Resolution Chain Position Source
AF-Q8UJC7-F1 Predicted AlphaFoldDB

No variants for Q8UJC7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8UJC7

No associated diseases with Q8UJC7

No regional properties for Q8UJC7

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8UJC7

Functions

Description
EC Number 2.7.4.27 Phosphotransferases with a phosphate group as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
ADP binding Binding to ADP, adenosine 5'-diphosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
phosphotransferase activity, phosphate group as acceptor Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to a phosphate group (acceptor).
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.

2 GO annotations of biological process

Name Definition
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
protein phosphorylation The process of introducing a phosphate group on to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MENKKSFFHL HLISDSTGET LMSAGRAVSA QFHTSMPVEH VYPMIRNQKQ LAQVIDLIDK
70 80 90 100 110 120
EPGIVLYTIV DQQLAEFLDL RCHAIGVPCV NVLEPIIGIF QTYLGAPSRR RVGAQHALNA
130 140 150 160 170 180
DYFARIEALN FAMDHDDGQM PETYDDADVV IIGISRTSKT PTSIYLANRG IKTANIPVVP
190 200 210 220 230 240
NVPLPESLYA ATRPLIVGLV ATSDRISQVR ENRDLGTTGG FDGGRYTDRA TIMEELKYAR
250 260 270
ALCARNNWPL IDVTRRSIEE TAAAILALRP RTR