Q9H7X0 · NAA60_HUMAN
- ProteinN-alpha-acetyltransferase 60
- GeneNAA60
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids242 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met (PubMed:21750686, PubMed:25732826, PubMed:27320834, PubMed:27550639).
Required for normal chromosomal segregation during anaphase (PubMed:21750686).
May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences (PubMed:21981917).
Catalytic activity
- acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] = CoA + H+ + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane protein]
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 34 | Required to position thioacetyl group | ||||
Sequence: F | ||||||
Binding site | 38 | substrate | ||||
Sequence: Y | ||||||
Active site | 97 | |||||
Sequence: Y | ||||||
Binding site | 99 | substrate | ||||
Sequence: L | ||||||
Binding site | 101-103 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: LGV | ||||||
Binding site | 109-114 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: KHGIGS | ||||||
Active site | 138 | |||||
Sequence: H | ||||||
Binding site | 143 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 150-153 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: YENR | ||||||
Binding site | 165 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Molecular Function | histone acetyltransferase activity | |
Molecular Function | histone H4 acetyltransferase activity | |
Molecular Function | peptide alpha-N-acetyltransferase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | cell population proliferation | |
Biological Process | chromosome segregation | |
Biological Process | N-terminal peptidyl-methionine acetylation | |
Biological Process | N-terminal protein amino acid acetylation | |
Biological Process | nucleosome assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-alpha-acetyltransferase 60
- EC number
- Short nameshNaa60
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H7X0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-192 | Cytoplasmic | ||||
Sequence: MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILD | ||||||
Intramembrane | 193-236 | Helical | ||||
Sequence: YIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGI | ||||||
Topological domain | 237-242 | Cytoplasmic | ||||
Sequence: EYSRTM |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Basal ganglia calcification, idiopathic, 9, autosomal recessive (IBGC9)
- Note
- DescriptionA form of basal ganglia calcification, a genetically heterogeneous condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas.
- See alsoMIM:620786
Natural variants in IBGC9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089549 | 17 | L>R | in IBGC9; uncertain significance; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |
VAR_089550 | 44 | R>C | in IBGC9; uncertain significance; decreased activity of N-terminal protein amino acid acetylation; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |
VAR_089551 | 131 | H>Y | in IBGC9; uncertain significance; decreased activity of N-terminal protein amino acid acetylation; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |
VAR_089552 | 143 | N>T | in IBGC9; uncertain significance; may strongly decrease protein expression levels; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_089549 | 17 | in IBGC9; uncertain significance; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |||
Sequence: L → R | ||||||
Mutagenesis | 19 | Does not affect localization to the Golgi apparatus; when associated with S-30; S-132; S-207 and S-222. | ||||
Sequence: C → S | ||||||
Mutagenesis | 30 | Does not affect localization to the Golgi apparatus; when associated with S-19; S-132; S-207 and S-222. | ||||
Sequence: C → S | ||||||
Mutagenesis | 34 | Abolished acetyltransferase activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 35 | Reduced acetyltransferase activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 36 | Reduced acetyltransferase activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 37 | Only slightly affects acetyltransferase activity. | ||||
Sequence: E → A or F | ||||||
Mutagenesis | 38 | Strongly reduced acetyltransferase activity. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_089550 | 44 | in IBGC9; uncertain significance; decreased activity of N-terminal protein amino acid acetylation; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |||
Sequence: R → C | ||||||
Mutagenesis | 79 | Slightly reduced acetyltransferase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 79 | Increased acetyltransferase activity. | ||||
Sequence: K → R or Q | ||||||
Mutagenesis | 79 | Decreased acetyltransferase activity; when associated with R-105, R-109, R-121 and R-156. | ||||
Sequence: K → R | ||||||
Mutagenesis | 80 | Slightly increased acetyltransferase activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 81 | Slightly increased acetyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 83 | Slightly increased acetyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 84 | Slightly altered acetyltransferase activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 97 | Abolished acetyltransferase activity. | ||||
Sequence: Y → A or F | ||||||
Mutagenesis | 105 | Decreased acetyltransferase activity; when associated with R-79, R-109, R-121 and R-156. | ||||
Sequence: K → R | ||||||
Mutagenesis | 109 | Decreased acetyltransferase activity; when associated with R-79, R-105, R-121 and R-156. | ||||
Sequence: K → R | ||||||
Mutagenesis | 111 | Abolishes acetyltransferase activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 121 | Decreased acetyltransferase activity; when associated with R-79, R-105, R-109 and R-156. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_089551 | 131 | in IBGC9; uncertain significance; decreased activity of N-terminal protein amino acid acetylation; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |||
Sequence: H → Y | ||||||
Mutagenesis | 132 | Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-207 and S-222. | ||||
Sequence: C → S | ||||||
Mutagenesis | 138 | Abolished acetyltransferase activity. | ||||
Sequence: H → A or F | ||||||
Mutagenesis | 140 | Decreased acetyltransferase activity. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_089552 | 143 | in IBGC9; uncertain significance; may strongly decrease protein expression levels; when transfected RPE-1 cells, does not affect subcellular localization to the Golgi apparatus | |||
Sequence: N → T | ||||||
Mutagenesis | 143 | Strongly reduced acetyltransferase activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 156 | Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-121. | ||||
Sequence: K → R | ||||||
Mutagenesis | 164 | Slightly altered acetyltransferase activity. | ||||
Sequence: Y → A or F | ||||||
Mutagenesis | 165 | Strongly reduced acetyltransferase activity. | ||||
Sequence: Y → A or F | ||||||
Mutagenesis | 167 | Reduced acetyltransferase activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 207 | Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-222. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_060995 | 218 | in dbSNP:rs34464545 | |||
Sequence: H → Q | ||||||
Mutagenesis | 220-221 | Does not affect localization to the Golgi apparatus. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 222 | Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-207. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 285 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 chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000321566 | 1-242 | N-alpha-acetyltransferase 60 | |||
Sequence: MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM | ||||||
Modified residue | 79 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 105 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 109 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 121 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 156 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H7X0 | CASP6 P55212 | 3 | EBI-12260336, EBI-718729 | |
BINARY | Q9H7X0 | LAMP2 P13473-2 | 3 | EBI-12260336, EBI-21591415 | |
BINARY | Q9H7X0 | MEOX2 Q6FHY5 | 3 | EBI-12260336, EBI-16439278 | |
BINARY | Q9H7X0 | PRPF40A O75400-2 | 3 | EBI-12260336, EBI-5280197 | |
BINARY | Q9H7X0 | SH3GLB1 Q9Y371 | 3 | EBI-12260336, EBI-2623095 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-182 | N-acetyltransferase | ||||
Sequence: VSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYIN | ||||||
Region | 162-173 | Required for homodimerization | ||||
Sequence: PYYYSIRGVLKD |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative promoter usage & Alternative splicing.
Q9H7X0-1
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
- Length242
- Mass (Da)27,451
- Last updated2001-03-01 v1
- Checksum11234F2C51DF55DE
Q9H7X0-2
- Name2
- NoteIn placenta and leukocytes, expressed from the maternal allele, due to imprinting of the paternal allele.
- Differences from canonical
- 1-36: MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPI → MFPRRRTERRLGDTGTRKKIAYRKAVPGGRKCGASLSWEKSSR
Q9H7X0-3
- Name3
- NoteProduced by alternative splicing.
- Differences from canonical
- 1-65: Missing
Q9H7X0-4
- Name4
- NoteProduced by alternative splicing.
- Differences from canonical
- 113-242: GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM → ESTARPTACSAASCHGRASLPRVASSTAGPCDVGWAAATRPHPSAARRARLPVHLTPSVFCKELPAI
Q9H7X0-5
- Name5
- NoteProduced by alternative splicing.
- Differences from canonical
- 113-242: GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM → EPHGLHPAPGLCTSQPEPLLHSAQSLPPGPQPALQLPAMVGHLFQEWHRVQPDHVMSAGQPPPGPTLRPPAEPAFLSI
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
I3L4T5 | I3L4T5_HUMAN | NAA60 | 80 | ||
I3L4Q3 | I3L4Q3_HUMAN | NAA60 | 87 | ||
I3L4Q5 | I3L4Q5_HUMAN | NAA60 | 93 | ||
I3L2K7 | I3L2K7_HUMAN | NAA60 | 141 | ||
I3L2M6 | I3L2M6_HUMAN | NAA60 | 121 | ||
I3L2B4 | I3L2B4_HUMAN | NAA60 | 120 | ||
I3L1X5 | I3L1X5_HUMAN | NAA60 | 77 | ||
I3L1T4 | I3L1T4_HUMAN | NAA60 | 129 | ||
I3L205 | I3L205_HUMAN | NAA60 | 106 | ||
I3L1B9 | I3L1B9_HUMAN | NAA60 | 41 | ||
I3L153 | I3L153_HUMAN | NAA60 | 134 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_044123 | 1-36 | in isoform 2 | |||
Sequence: MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPI → MFPRRRTERRLGDTGTRKKIAYRKAVPGGRKCGASLSWEKSSR | ||||||
Alternative sequence | VSP_044122 | 1-65 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 87 | in Ref. 1; AAQ88907 | ||||
Sequence: S → T | ||||||
Alternative sequence | VSP_044124 | 113-242 | in isoform 4 | |||
Sequence: GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM → ESTARPTACSAASCHGRASLPRVASSTAGPCDVGWAAATRPHPSAARRARLPVHLTPSVFCKELPAI | ||||||
Alternative sequence | VSP_044125 | 113-242 | in isoform 5 | |||
Sequence: GSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM → EPHGLHPAPGLCTSQPEPLLHSAQSLPPGPQPALQLPAMVGHLFQEWHRVQPDHVMSAGQPPPGPTLRPPAEPAFLSI | ||||||
Sequence conflict | 180 | In isoform Q9H7X0-5; in Ref. 2; BAG60760 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 242 | in Ref. 3; CAG33605 | ||||
Sequence: M → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY358543 EMBL· GenBank· DDBJ | AAQ88907.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024216 EMBL· GenBank· DDBJ | BAB14853.1 EMBL· GenBank· DDBJ | mRNA | ||
AK092005 EMBL· GenBank· DDBJ | BAG52462.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297219 EMBL· GenBank· DDBJ | BAG59702.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298566 EMBL· GenBank· DDBJ | BAG60760.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302361 EMBL· GenBank· DDBJ | BAG63686.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457324 EMBL· GenBank· DDBJ | CAG33605.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004224 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC025283 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471112 EMBL· GenBank· DDBJ | EAW85358.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85359.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85360.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85361.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85362.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85363.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85364.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011267 EMBL· GenBank· DDBJ | AAH11267.1 EMBL· GenBank· DDBJ | mRNA |