Q86UY6 · NAA40_HUMAN
- ProteinN-alpha-acetyltransferase 40
- GeneNAA40
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A (PubMed:21935442, PubMed:25619998).
In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (PubMed:21935442, PubMed:25619998).
Acts as a negative regulator of apoptosis (PubMed:26666750).
May play a role in hepatic lipid metabolism (By similarity).
In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (PubMed:21935442, PubMed:25619998).
Acts as a negative regulator of apoptosis (PubMed:26666750).
May play a role in hepatic lipid metabolism (By similarity).
Catalytic activity
- acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H+ + N-terminal N(alpha)-acetyl-L-seryl-[histone H4]
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 85 | substrate | ||||
Sequence: Y | ||||||
Binding site | 127-129 | substrate | ||||
Sequence: DVE | ||||||
Binding site | 138 | substrate | ||||
Sequence: Y | ||||||
Site | 139 | Essential for catalytic activity | ||||
Sequence: E | ||||||
Binding site | 140-142 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: VQL | ||||||
Binding site | 148-153 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RKGLGK | ||||||
Binding site | 174 | substrate | ||||
Sequence: T | ||||||
Binding site | 179 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 197 | substrate | ||||
Sequence: S | ||||||
Binding site | 211 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centriolar satellite | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | histone H2A acetyltransferase activity | |
Molecular Function | histone H4 acetyltransferase activity | |
Molecular Function | peptide-serine-alpha-N-acetyltransferase activity | |
Biological Process | lipid metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-alpha-acetyltransferase 40
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86UY6
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 85 | Strongly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 90 | Strongly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 100 | 5 times reduced N-alpha-acetyltransferase activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 127-129 | Strongly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: DVE → AVA | ||||||
Mutagenesis | 136 | Strongly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 136 | Slightly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 137 | Reduced N-alpha-acetyltransferase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 138 | Strongly reduced N-alpha-acetyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 139 | Abolished N-alpha-acetyltransferase activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 174 | Does not affect N-alpha-acetyltransferase activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 211 | Does not affect N-alpha-acetyltransferase activity. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 228 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000284897 | 2-237 | UniProt | N-alpha-acetyltransferase 40 | |||
Sequence: GRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRLGDPLEAFPVFKKYDRNGLNVSIECKRVSGLEPATVDWAFDLTKTNMQTMYEQSEWGWKDREKREEMTDDRAWYLIAWENSSVPVAFSHFRFDVECGDEVLYCYEVQLESKVRRKGLGKFLIQILQLMANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDDSSPSMSGCCGEDCSYEILSRRTKFGDSHHSHAGGHCGGCCH | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed; with the highest expression level in liver and the lowest expression in brain (at protein level).
Induction
Down-regulated in hepatocellular carcinoma tissues.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86UY6 | BTF3 P20290-2 | 3 | EBI-16356946, EBI-1054703 | |
BINARY | Q86UY6-1 | H4C9 P62805 | 3 | EBI-16140302, EBI-302023 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 63-216 | N-acetyltransferase | ||||
Sequence: SGLEPATVDWAFDLTKTNMQTMYEQSEWGWKDREKREEMTDDRAWYLIAWENSSVPVAFSHFRFDVECGDEVLYCYEVQLESKVRRKGLGKFLIQILQLMANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDDSSPSMSGCCGEDCSYEILSR |
Sequence similarities
Belongs to the acetyltransferase family. NAA40 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q86UY6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length237
- Mass (Da)27,194
- Last updated2003-06-01 v1
- ChecksumAED75B559073FCE1
Q86UY6-3
- Name2
- Differences from canonical
- 1-21: Missing
Q86UY6-4
- Name3
- Differences from canonical
- 1-51: MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRLGDPLEAFPVFKKYDRN → MPFVPKWTLPT
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK023910 EMBL· GenBank· DDBJ | BAB14720.1 EMBL· GenBank· DDBJ | mRNA | ||
AK299041 EMBL· GenBank· DDBJ | BAG61115.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300451 EMBL· GenBank· DDBJ | BAG62172.1 EMBL· GenBank· DDBJ | mRNA | ||
BX647309 EMBL· GenBank· DDBJ | CAI46006.1 EMBL· GenBank· DDBJ | Transcribed RNA | Sequence problems. | |
AP003780 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC041617 EMBL· GenBank· DDBJ | AAH41617.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052298 EMBL· GenBank· DDBJ | AAH52298.1 EMBL· GenBank· DDBJ | mRNA |