NAA50
entrez
80218
canonical
uniprot
Q9GZZ1
canonical
ensembl
ENSG00000121579
resolver
ensp
ENSP00000240922
resolver
ensp
ENSP00000417837
resolver
enst
ENST00000493900
resolver
genesymbol
NAA50
resolver
genesymbol_syn
MAK3
resolver
genesymbol_syn
NAT13
resolver
genesymbol_syn
NAT5
resolver
hgnc
HGNC:29533
resolver
uniprot
D3DN74
resolver
uniprot
E7EQ69
resolver
uniprot
Q68DQ1
resolver
uniprot_entry
E7EQ69_HUMAN
resolver
uniprot_entry
NAA50_HUMAN
resolver
uniprot_sec
D3DN74
resolver
uniprot_sec
Q68DQ1
resolver
amino_acid_sequence
MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.258
uniprot
proteins
function
FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:21900231, PubMed:22311970, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (PubMed:16507339, PubMed:27484799, PubMed:29754825, PubMed:32042062). Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821). {ECO:0000269|PubMed:16507339, ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:19744929, ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970, ECO:0000269|PubMed:27422821, ECO:0000269|PubMed:27484799, ECO:0000269|PubMed:29754825, ECO:0000269|PubMed:32042062}.
uniprot
proteins
mass_dalton
19398
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="E->A: Restores the acetylation activity of the NatA complex."; /evidence="ECO:0000269|PubMed:32042062"; MUTAGEN 27; /note="F->A: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:27422821"; MUTAGEN 28; /note="P->A: Strongly decreased N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231"; MUTAGEN 29; /note="V->A: Strongly decreased N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231"; MUTAGEN 31; /note="Y->A: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231"; MUTAGEN 34..37; /note="KFYK->AFYA: Decreased acetylation; when associated with A-140."; /evidence="ECO:0000269|PubMed:19744929"; MUTAGEN 35; /note="F->A: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231"; MUTAGEN 53; /note="D->A: Restores the acetylation activity of the NatA complex."; /evidence="ECO:0000269|PubMed:32042062"; MUTAGEN 73; /note="Y->A,F: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:32042062"; MUTAGEN 75; /note="M->A: Reduces N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:32042062"; MUTAGEN 84; /note="R->A: Strongly decreased N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:19744929"; MUTAGEN 112; /note="H->A,F: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231"; MUTAGEN 124; /note="Y->F: Strongly decreased N-alpha-acetyltransferase activity. Impaired sister chromatid cohesion during mitosis."; /evidence="ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:19744929, ECO:0000269|PubMed:27422821"; MUTAGEN 138; /note="Y->A: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:32042062"; MUTAGEN 139; /note="Y->A: Abolishes N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:32042062"; MUTAGEN 140; /note="K->A: Decreased acetylation; when associated with 34-A-A-37."; /evidence="ECO:0000269|PubMed:19744929"; MUTAGEN 142; /note="I->A: Reduces N-alpha-acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:32042062
uniprot
proteins
protein_family
Acetyltransferase family
uniprot
proteins
protein_family
GNAT subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16507339
uniprot
proteins
pubmed
17502424
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19660095
uniprot
proteins
pubmed
19744929
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21900231
uniprot
proteins
pubmed
22311970
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25732826
uniprot
proteins
pubmed
27422821
uniprot
proteins
pubmed
27484799
uniprot
proteins
pubmed
29754825
uniprot
proteins
pubmed
32042062
uniprot
proteins
sequence_length
169
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16507339, ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:25732826, ECO:0000269|PubMed:27422821}. Nucleus {ECO:0000269|PubMed:25732826}. Note=Localizes to the cytoplasm in interphase cells (PubMed:17502424). {ECO:0000269|PubMed:17502424}.
uniprot
proteins