Q9UHF3
uniprot
Q9UHF3
canonical
activity_regulation
ACTIVITY REGULATION: Allosterically regulated by acetylation at residue Lys-99. {ECO:0000269|PubMed:31945187}.
uniprot
proteins
amino_acid_sequence
MAPYHIRKYQESDRKSVVGLLSGGMAEHAPATFRRLLKLPRTLILLLGGALALLLVSGSWILALVFSLSLLPALWFLAKKPWTRYVDIALRTDMSDITKSYLSECGSCFWVAESEEKVVGTVGALPVDDPTLREKRLQLFHLSVDNEHRGQGIAKALVRTVLQFARDQGYSEVVLDTSNIQLSAMGLYQSLGFKKTGQSFFHVWARLVDLHTVHFIYHLPSAQAGRL
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
function
FUNCTION: Endoplasmic reticulum (ER)-membrane-bound lysine N-acetyltransferase catalyzing the N6-acetylation of lysine residues in the lumen of the ER in various proteins, including PROM1 and BACE1, using acetyl-CoA as acetyl donor (PubMed:19011241, PubMed:22267734, PubMed:24556617, PubMed:31945187). Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1 (PubMed:24556617). Acetylates and stabilizes BACE1 immature protein, leading to increased steady-state levels in neurons. By acting on BACE1 expression, may regulate amyloid beta-peptide formation (PubMed:19011241, PubMed:22267734). N(6)-lysine acetylation in ER maintains protein homeostasis and regulates reticulophagy (By similarity). {ECO:0000250|UniProtKB:E0CYC6, ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:22267734, ECO:0000269|PubMed:24556617, ECO:0000269|PubMed:31945187}.
uniprot
proteins
mass_dalton
25366
uniprot
proteins
mutagenesis
MUTAGEN 99; /note="K->E,R: Diminishes protein-lysine N6-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:31945187"; MUTAGEN 149; /note="R->A: Exhibits reduced protein-lysine N6-acetyltransferase activity; when associated with A-183 and A-190."; /evidence="ECO:0000269|PubMed:31945187"; MUTAGEN 183; /note="S->A: Exhibits reduced protein-lysine N6-acetyltransferase activity; when associated with A-149 and A-190."; /evidence="ECO:0000269|PubMed:31945187"; MUTAGEN 190; /note="S->A: Exhibits reduced protein-lysine N6-acetyltransferase activity; when associated with A-149 and A-183."; /evidence="ECO:0000269|PubMed:31945187
uniprot
proteins
post_translational_modification
PTM: Acetylation on Lys-99 modulates enzymatic activity. {ECO:0000269|PubMed:31945187}.
uniprot
proteins
protein_family
NAT8 family
uniprot
proteins
pubmed
11397015
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16395595
uniprot
proteins
pubmed
19011241
uniprot
proteins
pubmed
22267734
uniprot
proteins
pubmed
24556617
uniprot
proteins
pubmed
31945187
uniprot
proteins
sequence_length
227
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:24556617}; Single-pass type II membrane protein {ECO:0000305|PubMed:19011241}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19011241}; Single-pass type II membrane protein {ECO:0000305|PubMed:19011241}. Note=Enriched in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:24556617}.
uniprot
proteins
transmembrane_region
TRANSMEM 43..63; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000305|PubMed:19011241
uniprot
proteins