Naa10
entrez
56292
canonical
uniprot
Q9QY36
canonical
ensembl
ENSMUSG00000031388
resolver
ensp
ENSMUSP00000033763
resolver
ensp
ENSMUSP00000110029
resolver
ensp
ENSMUSP00000110031
resolver
enst
ENSMUST00000033763
resolver
enst
ENSMUST00000114387
resolver
enst
ENSMUST00000114389
resolver
genesymbol
Naa10
resolver
genesymbol_syn
Ard1
resolver
genesymbol_syn
Ard1a
resolver
genesymbol_syn
Te2
resolver
uniprot
B1AUY9
resolver
uniprot
F7CGX8
resolver
uniprot
Q3V4D5
resolver
uniprot
Q540H0
resolver
uniprot_entry
B1AUY9_MOUSE
resolver
uniprot_entry
F7CGX8_MOUSE
resolver
uniprot_entry
NAA10_MOUSE
resolver
uniprot_entry
Q3V4D5_MOUSE
resolver
uniprot_entry
Q540H0_MOUSE
resolver
amino_acid_sequence
MNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGKHMVLAALENKAENKGNVLLSSGEACREEKGLAAEDSGGDSKDLSEVSETTESTDVKDSSEASDSAS
uniprot
proteins
ec_number
2.3.1.255
uniprot
proteins
function
FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (PubMed:12888564). Acetylates amino termini that are devoid of initiator methionine (By similarity). The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development (By similarity). Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (By similarity). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (By similarity). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (By similarity). Acetylates HIST1H4A (By similarity). Acts as a negative regulator of sister chromatid cohesion during mitosis (By similarity). {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:12888564}.
uniprot
proteins
mass_dalton
26520
uniprot
proteins
post_translational_modification
PTM: Cleaved by caspases during apoptosis. {ECO:0000250|UniProtKB:P41227}.; PTM: Phosphorylation by IKBKB/IKKB at Ser-209 destabilises NAA10 and promotes its proteasome-mediated degradation.; PTM: Autoacetylated at Lys-136 which stimulates its catalytic activity. {ECO:0000250|UniProtKB:P41227}.
uniprot
proteins
protein_family
ARD1 subfamily
uniprot
proteins
protein_family
Acetyltransferase family
uniprot
proteins
pubmed
12464182
uniprot
proteins
pubmed
12888564
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
235
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12888564}. Nucleus {ECO:0000250|UniProtKB:P41227}. Note=Also present in the free cytosolic and cytoskeleton-bound polysomes. {ECO:0000250|UniProtKB:P41227}.
uniprot
proteins