NAT8
entrez
9027
canonical
uniprot
Q9UHE5
canonical
ensembl
ENSG00000144035
resolver
ensembl
ENSG00000291479
resolver
ensp
ENSP00000272425
resolver
ensp
ENSP00000516938
resolver
ensp
ENSP00000522444
resolver
ensp
ENSP00000522445
resolver
ensp
ENSP00000522446
resolver
ensp
ENSP00000522447
resolver
enst
ENST00000272425
resolver
enst
ENST00000707634
resolver
enst
ENST00000852385
resolver
enst
ENST00000852386
resolver
enst
ENST00000852387
resolver
enst
ENST00000852388
resolver
genesymbol
NAT8
resolver
genesymbol_syn
CML1
resolver
genesymbol_syn
GLA
resolver
genesymbol_syn
TSC501
resolver
hgnc
HGNC:18069
resolver
uniprot
O75839
resolver
uniprot
Q6LEU4
resolver
uniprot
Q96QI8
resolver
uniprot
Q9UQ17
resolver
uniprot_entry
NAT8_HUMAN
resolver
uniprot_sec
O75839
resolver
uniprot_sec
Q6LEU4
resolver
uniprot_sec
Q96QI8
resolver
uniprot_sec
Q9UQ17
resolver
amino_acid_sequence
MAPCHIRKYQESDRQWVVGLLSRGMAEHAPATFRQLLKLPRTLILLLGGPLALLLVSGSWLLALVFSISLFPALWFLAKKPWTEYVDMTLCTDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTGQSFFCVWARLVALHTVHFIYHLPSSKVGSL
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.80
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). May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (PubMed:19011241). N(6)-lysine acetylation in the ER maintains protein homeostasis and regulates reticulophagy (By similarity). Alternatively, acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids (PubMed:20392701). This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. {ECO:0000250|UniProtKB:Q9JIY7, ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:20392701, ECO:0000269|PubMed:22267734, ECO:0000269|PubMed:24556617, ECO:0000269|PubMed:31945187}.
uniprot
proteins
mass_dalton
25619
uniprot
proteins
mutagenesis
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 149; /note="R->K: Loss of the cysteine S-conjugate N-acetyltransferase activity. No effect on protein expression."; /evidence="ECO:0000269|PubMed:20392701"; 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
pathway_participation
PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000269|PubMed:20392701}.
uniprot
proteins
protein_family
NAT8 family
uniprot
proteins
pubmed
11397015
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19011241
uniprot
proteins
pubmed
20392701
uniprot
proteins
pubmed
22267734
uniprot
proteins
pubmed
24556617
uniprot
proteins
pubmed
31945187
uniprot
proteins
pubmed
9852678
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:20392701}; Single-pass type II membrane protein {ECO:0000305|PubMed:19011241}.
uniprot
proteins
transmembrane_region
TRANSMEM 43..63; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins