Overview
| Uniprot ID | Q9GZZ1 |
| Protein Name | N-alpha-acetyltransferase 50 |
| Gene Name | NAA50 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 126 |
SAIDFYRKFGFEIIE |
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)
Protein Sequence
10
MKGSRIELGD
20
VTPHNIKQLK
30
RLNQVIFPVS
40
YNDKFYKDVL
50
EVGELAKLAY
60
FNDIAVGAVC
70
CRVDHSQNQK
80
RLYIMTLGCL
90
APYRRLGIGT
100
KMLNHVLNIC
110
EKDGTFDNIY
120
LHVQISNESA
130
IDFYRKFGFE
140
IIETKKNYYK
150
RIEPADAHVL
160
QKNLKVPSGQ
NADVQKTDN
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0031415 |
NatA complex |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0010485 |
histone H4 acetyltransferase activity |
| Molecular Function |
GO:0120518 |
protein N-terminal-methionine acetyltransferase activity |
| Molecular Function |
GO:0061733 |
protein-lysine-acetyltransferase activity |
| Molecular Function |
GO:0004596 |
protein-N-terminal amino-acid acetyltransferase activity |
| Biological Process |
GO:0034087 |
establishment of mitotic sister chromatid cohesion |
| Biological Process |
GO:0007064 |
mitotic sister chromatid cohesion |
| Biological Process |
GO:0071962 |
mitotic sister chromatid cohesion, centromeric |
| Biological Process |
GO:0006474 |
N-terminal protein amino acid acetylation |
| Biological Process |
GO:0043687 |
post-translational protein modification |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.