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Protein

N-alpha-acetyltransferase 60

Gene

NAA60

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol (PubMed:25732826). 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:27550639, PubMed:27320834). 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).1 Publication4 Publications

Catalytic activityi

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.1 Publication
Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei34Required to recognizing and positioning the ethanethioate moiety ofacetyl-CoA to the right location to facilitate acetyl-transfer1 Publication1
Binding sitei38Sustrate1 PublicationImported1
Binding sitei81Sustrate1 PublicationImported1
Active sitei972 Publications1
Binding sitei99Sustrate1 PublicationImported1
Active sitei1382 Publications1
Binding sitei143Acetyl-CoA2 PublicationsImported1
Binding sitei165Sustrate1 PublicationImported1

GO - Molecular functioni

  • H4 histone acetyltransferase activity Source: UniProtKB
  • peptide alpha-N-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • N-terminal peptidyl-methionine acetylation Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywordsi

Molecular functionAcyltransferase, Chromatin regulator, Transferase
Biological processChromosome partition

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122390-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 601 PublicationImported (EC:2.3.1.881 Publication)
Short name:
hNaa602 Publications
Alternative name(s):
Histone acetyltransferase type B protein 41 Publication (EC:2.3.1.481 Publication)
Short name:
HAT41 Publication
N-acetyltransferase 15
N-alpha-acetyltransferase F
Short name:
NatF
Gene namesi
Name:NAA601 PublicationImported
Synonyms:HAT41 Publication, NAT15
ORF Names:UNQ2771/PRO7155
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25875. NAA60.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 192Cytoplasmic1 PublicationAdd BLAST192
Intramembranei193 – 236Helical1 PublicationAdd BLAST44
Topological domaini237 – 242Cytoplasmic1 Publication6

GO - Cellular componenti

  • Golgi membrane Source: UniProtKB

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19C → S: Does not affect localization to the Golgi apparatus; when associated with S-30; S-132; S-207 and S-222. 1 Publication1
Mutagenesisi30C → S: Does not affect localization to the Golgi apparatus; when associated with S-19; S-132; S-207 and S-222. 1 Publication1
Mutagenesisi34F → A: Abolished acetyltransferase activity. 1 Publication1
Mutagenesisi35P → A: Reduced acetyltransferase activity. 1 Publication1
Mutagenesisi36I → A: Reduced acetyltransferase activity. 1 Publication1
Mutagenesisi37E → A or F: Only slightly affects acetyltransferase activity. 1 Publication1
Mutagenesisi38Y → A: Strongly reduced acetyltransferase activity. 2 Publications1
Mutagenesisi79K → A: Slightly reduced acetyltransferase activity. 1 Publication1
Mutagenesisi79K → R or Q: Increased acetyltransferase activity. 1 Publication1
Mutagenesisi79K → R: Decreased acetyltransferase activity; when associated with R-105, R-109, R-121 and R-156. 1 Publication1
Mutagenesisi80E → A: Slightly increased acetyltransferase activity. 1 Publication1
Mutagenesisi81D → A: Slightly increased acetyltransferase activity. 2 Publications1
Mutagenesisi83D → A: Slightly increased acetyltransferase activity. 1 Publication1
Mutagenesisi84I → A: Slightly altered acetyltransferase activity. 1 Publication1
Mutagenesisi97Y → A or F: Abolished acetyltransferase activity. 2 Publications1
Mutagenesisi105K → R: Decreased acetyltransferase activity; when associated with R-79, R-109, R-121 and R-156. 1 Publication1
Mutagenesisi109K → R: Decreased acetyltransferase activity; when associated with R-79, R-105, R-121 and R-156. 1 Publication1
Mutagenesisi111G → A: Abolishes acetyltransferase activity. 1 Publication1
Mutagenesisi121K → R: Decreased acetyltransferase activity; when associated with R-79, R-105, R-109 and R-156. 1 Publication1
Mutagenesisi132C → S: Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-207 and S-222. 1 Publication1
Mutagenesisi138H → A or F: Abolished acetyltransferase activity. 2 Publications1
Mutagenesisi140L → A: Decreased acetyltransferase activity. 1 Publication1
Mutagenesisi143N → A: Strongly reduced acetyltransferase activity. 1 Publication1
Mutagenesisi156K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-121. 1 Publication1
Mutagenesisi164Y → A or F: Slightly altered acetyltransferase activity. 1 Publication1
Mutagenesisi165Y → A or F: Strongly reduced acetyltransferase activity. 2 Publications1
Mutagenesisi167I → A: Reduced acetyltransferase activity. 1 Publication1
Mutagenesisi207C → S: Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-222. 1 Publication1
Mutagenesisi220 – 221LL → AA: Does not affect localization to the Golgi apparatus. 1 Publication2
Mutagenesisi222C → S: Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-207. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000122390.
PharmGKBiPA164723438.

Polymorphism and mutation databases

BioMutaiNAA60.
DMDMi74733721.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003215661 – 242N-alpha-acetyltransferase 60Add BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei105N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei109N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei121N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei156N6-acetyllysine; by autocatalysis1 Publication1

Post-translational modificationi

Acetylated: autoacetylation is required for optimal acetyltransferase activity.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9H7X0.
MaxQBiQ9H7X0.
PaxDbiQ9H7X0.
PeptideAtlasiQ9H7X0.
PRIDEiQ9H7X0.

PTM databases

PhosphoSitePlusiQ9H7X0.

Expressioni

Inductioni

Isoform 2: Imprinted (PubMed:21593219). Promoter methylation of the paternal allele may restrict expression to the maternal allele in placenta and leukocytes (PubMed:21593219). Isoform 1: Biallelically expressed (PubMed:21593219).1 Publication

Gene expression databases

BgeeiENSG00000122390.
CleanExiHS_NAT15.
ExpressionAtlasiQ9H7X0. baseline and differential.
GenevisibleiQ9H7X0. HS.

Organism-specific databases

HPAiHPA040916.

Interactioni

Subunit structurei

Monomer and homodimer; monomer in presence of substrate and homodimer in its absence (PubMed:27320834).1 Publication

Protein-protein interaction databases

IntActiQ9H7X0. 1 interactor.
STRINGi9606.ENSP00000385903.

Structurei

Secondary structure

1242
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Beta strandi12 – 17Combined sources6
Helixi20 – 22Combined sources3
Helixi23 – 33Combined sources11
Helixi40 – 48Combined sources9
Beta strandi52 – 59Combined sources8
Beta strandi62 – 73Combined sources12
Helixi74 – 76Combined sources3
Helixi79 – 81Combined sources3
Turni82 – 87Combined sources6
Beta strandi94 – 103Combined sources10
Helixi105 – 107Combined sources3
Helixi112 – 128Combined sources17
Turni129 – 131Combined sources3
Beta strandi132 – 140Combined sources9
Helixi144 – 151Combined sources8
Turni152 – 154Combined sources3
Beta strandi156 – 167Combined sources12
Beta strandi170 – 180Combined sources11
Helixi190 – 201Combined sources12
Helixi206 – 208Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HGZX-ray1.38A4-242[»]
5HH0X-ray1.60A4-199[»]
5HH1X-ray1.80A4-199[»]
5ICVX-ray1.53A/B5-184[»]
5ICWX-ray1.95A/B/C/D3-184[»]
ProteinModelPortaliQ9H7X0.
SMRiQ9H7X0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 182N-acetyltransferasePROSITE-ProRule annotationAdd BLAST170

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni101 – 103Acetyl-CoA binding2 PublicationsImported3
Regioni109 – 114Acetyl-CoA binding2 PublicationsImported6
Regioni150 – 153Acetyl-CoA binding2 PublicationsImported4
Regioni162 – 173Required for homodimerization1 PublicationAdd BLAST12

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IQK0. Eukaryota.
ENOG410Y94A. LUCA.
GeneTreeiENSGT00390000008314.
HOGENOMiHOG000280717.
HOVERGENiHBG061680.
InParanoidiQ9H7X0.
OMAiIYRQAHS.
OrthoDBiEOG091G0L3L.
PhylomeDBiQ9H7X0.
TreeFamiTF323980.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H7X0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK
60 70 80 90 100
KFFSLAATYR GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS
110 120 130 140 150
LGVVKEFRKH GIGSLLLESL KDHISTTAQD HCKAIYLHVL TTNNTAINFY
160 170 180 190 200
ENRDFKQHHY LPYYYSIRGV LKDGFTYVLY INGGHPPWTI LDYIQHLGSA
210 220 230 240
LASLSPCSIP HRVYRQAHSL LCSFLPWSGI SSKSGIEYSR TM
Length:242
Mass (Da):27,451
Last modified:March 1, 2001 - v1
Checksum:i11234F2C51DF55DE
GO
Isoform 2 (identifier: Q9H7X0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MTEVVPSSAL...KHLCGDWFPI → MFPRRRTERR...ASLSWEKSSR

Note: In placenta and leukocytes, expressed from the maternal allele, due to imprinting of the paternal allele.
Show »
Length:249
Mass (Da):28,375
Checksum:iE049FDCDA8FD6ECC
GO
Isoform 3 (identifier: Q9H7X0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Note: Produced by alternative splicing. No experimental confirmation available.
Show »
Length:177
Mass (Da):20,103
Checksum:i32C31E8C2E777D5D
GO
Isoform 4 (identifier: Q9H7X0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → ESTARPTACS...SVFCKELPAI

Note: Produced by alternative splicing. No experimental confirmation available.
Show »
Length:179
Mass (Da):19,493
Checksum:i806EE0412C45F54C
GO
Isoform 5 (identifier: Q9H7X0-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → EPHGLHPAPG...PPAEPAFLSI

Note: Produced by alternative splicing.Curated No experimental confirmation available.Curated
Show »
Length:190
Mass (Da):20,911
Checksum:iC82D743C3A3F0776
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87S → T in AAQ88907 (PubMed:12975309).Curated1
Sequence conflicti242M → I in CAG33605 (Ref. 3) Curated1
Isoform 5 (identifier: Q9H7X0-5)
Sequence conflicti180R → Q in BAG60760 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060995218H → Q. Corresponds to variant dbSNP:rs34464545Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0441221 – 65Missing in isoform 3. 1 PublicationAdd BLAST65
Alternative sequenceiVSP_0441231 – 36MTEVV…DWFPI → MFPRRRTERRLGDTGTRKKI AYRKAVPGGRKCGASLSWEK SSR in isoform 2. 1 PublicationAdd BLAST36
Alternative sequenceiVSP_044124113 – 242GSLLL…YSRTM → ESTARPTACSAASCHGRASL PRVASSTAGPCDVGWAAATR PHPSAARRARLPVHLTPSVF CKELPAI in isoform 4. 1 PublicationAdd BLAST130
Alternative sequenceiVSP_044125113 – 242GSLLL…YSRTM → EPHGLHPAPGLCTSQPEPLL HSAQSLPPGPQPALQLPAMV GHLFQEWHRVQPDHVMSAGQ PPPGPTLRPPAEPAFLSI in isoform 5. 1 PublicationAdd BLAST130

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358543 mRNA. Translation: AAQ88907.1.
AK024216 mRNA. Translation: BAB14853.1.
AK092005 mRNA. Translation: BAG52462.1.
AK297219 mRNA. Translation: BAG59702.1.
AK298566 mRNA. Translation: BAG60760.1.
AK302361 mRNA. Translation: BAG63686.1.
CR457324 mRNA. Translation: CAG33605.1.
AC004224 Genomic DNA. No translation available.
AC025283 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85358.1.
CH471112 Genomic DNA. Translation: EAW85359.1.
CH471112 Genomic DNA. Translation: EAW85360.1.
CH471112 Genomic DNA. Translation: EAW85361.1.
CH471112 Genomic DNA. Translation: EAW85362.1.
CH471112 Genomic DNA. Translation: EAW85363.1.
CH471112 Genomic DNA. Translation: EAW85364.1.
BC011267 mRNA. Translation: AAH11267.1.
CCDSiCCDS45396.1. [Q9H7X0-1]
CCDS81937.1. [Q9H7X0-2]
CCDS81938.1. [Q9H7X0-5]
CCDS81939.1. [Q9H7X0-4]
CCDS81941.1. [Q9H7X0-3]
RefSeqiNP_001077069.1. NM_001083600.2. [Q9H7X0-1]
NP_001077070.1. NM_001083601.2. [Q9H7X0-1]
NP_001304022.1. NM_001317093.1. [Q9H7X0-2]
NP_001304023.1. NM_001317094.1.
NP_001304024.1. NM_001317095.1. [Q9H7X0-3]
NP_001304025.1. NM_001317096.1. [Q9H7X0-5]
NP_001304026.1. NM_001317097.1. [Q9H7X0-4]
NP_001304027.1. NM_001317098.1. [Q9H7X0-4]
NP_079121.1. NM_024845.3. [Q9H7X0-1]
UniGeneiHs.513296.

Genome annotation databases

EnsembliENST00000360862; ENSP00000354108; ENSG00000122390. [Q9H7X0-3]
ENST00000407558; ENSP00000385903; ENSG00000122390. [Q9H7X0-1]
ENST00000414063; ENSP00000393224; ENSG00000122390. [Q9H7X0-1]
ENST00000421765; ENSP00000405873; ENSG00000122390. [Q9H7X0-5]
ENST00000424546; ENSP00000401237; ENSG00000122390. [Q9H7X0-2]
ENST00000570819; ENSP00000460763; ENSG00000122390. [Q9H7X0-4]
ENST00000572584; ENSP00000459057; ENSG00000122390. [Q9H7X0-1]
ENST00000572942; ENSP00000461730; ENSG00000122390. [Q9H7X0-4]
ENST00000573580; ENSP00000459055; ENSG00000122390. [Q9H7X0-3]
ENST00000575076; ENSP00000458667; ENSG00000122390. [Q9H7X0-1]
GeneIDi79903.
KEGGihsa:79903.
UCSCiuc002cvg.3. human. [Q9H7X0-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358543 mRNA. Translation: AAQ88907.1.
AK024216 mRNA. Translation: BAB14853.1.
AK092005 mRNA. Translation: BAG52462.1.
AK297219 mRNA. Translation: BAG59702.1.
AK298566 mRNA. Translation: BAG60760.1.
AK302361 mRNA. Translation: BAG63686.1.
CR457324 mRNA. Translation: CAG33605.1.
AC004224 Genomic DNA. No translation available.
AC025283 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85358.1.
CH471112 Genomic DNA. Translation: EAW85359.1.
CH471112 Genomic DNA. Translation: EAW85360.1.
CH471112 Genomic DNA. Translation: EAW85361.1.
CH471112 Genomic DNA. Translation: EAW85362.1.
CH471112 Genomic DNA. Translation: EAW85363.1.
CH471112 Genomic DNA. Translation: EAW85364.1.
BC011267 mRNA. Translation: AAH11267.1.
CCDSiCCDS45396.1. [Q9H7X0-1]
CCDS81937.1. [Q9H7X0-2]
CCDS81938.1. [Q9H7X0-5]
CCDS81939.1. [Q9H7X0-4]
CCDS81941.1. [Q9H7X0-3]
RefSeqiNP_001077069.1. NM_001083600.2. [Q9H7X0-1]
NP_001077070.1. NM_001083601.2. [Q9H7X0-1]
NP_001304022.1. NM_001317093.1. [Q9H7X0-2]
NP_001304023.1. NM_001317094.1.
NP_001304024.1. NM_001317095.1. [Q9H7X0-3]
NP_001304025.1. NM_001317096.1. [Q9H7X0-5]
NP_001304026.1. NM_001317097.1. [Q9H7X0-4]
NP_001304027.1. NM_001317098.1. [Q9H7X0-4]
NP_079121.1. NM_024845.3. [Q9H7X0-1]
UniGeneiHs.513296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HGZX-ray1.38A4-242[»]
5HH0X-ray1.60A4-199[»]
5HH1X-ray1.80A4-199[»]
5ICVX-ray1.53A/B5-184[»]
5ICWX-ray1.95A/B/C/D3-184[»]
ProteinModelPortaliQ9H7X0.
SMRiQ9H7X0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9H7X0. 1 interactor.
STRINGi9606.ENSP00000385903.

PTM databases

PhosphoSitePlusiQ9H7X0.

Polymorphism and mutation databases

BioMutaiNAA60.
DMDMi74733721.

Proteomic databases

EPDiQ9H7X0.
MaxQBiQ9H7X0.
PaxDbiQ9H7X0.
PeptideAtlasiQ9H7X0.
PRIDEiQ9H7X0.

Protocols and materials databases

DNASUi79903.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360862; ENSP00000354108; ENSG00000122390. [Q9H7X0-3]
ENST00000407558; ENSP00000385903; ENSG00000122390. [Q9H7X0-1]
ENST00000414063; ENSP00000393224; ENSG00000122390. [Q9H7X0-1]
ENST00000421765; ENSP00000405873; ENSG00000122390. [Q9H7X0-5]
ENST00000424546; ENSP00000401237; ENSG00000122390. [Q9H7X0-2]
ENST00000570819; ENSP00000460763; ENSG00000122390. [Q9H7X0-4]
ENST00000572584; ENSP00000459057; ENSG00000122390. [Q9H7X0-1]
ENST00000572942; ENSP00000461730; ENSG00000122390. [Q9H7X0-4]
ENST00000573580; ENSP00000459055; ENSG00000122390. [Q9H7X0-3]
ENST00000575076; ENSP00000458667; ENSG00000122390. [Q9H7X0-1]
GeneIDi79903.
KEGGihsa:79903.
UCSCiuc002cvg.3. human. [Q9H7X0-1]

Organism-specific databases

CTDi79903.
GeneCardsiNAA60.
H-InvDBHIX0012768.
HIX0173265.
HGNCiHGNC:25875. NAA60.
HPAiHPA040916.
MIMi614246. gene.
neXtProtiNX_Q9H7X0.
OpenTargetsiENSG00000122390.
PharmGKBiPA164723438.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQK0. Eukaryota.
ENOG410Y94A. LUCA.
GeneTreeiENSGT00390000008314.
HOGENOMiHOG000280717.
HOVERGENiHBG061680.
InParanoidiQ9H7X0.
OMAiIYRQAHS.
OrthoDBiEOG091G0L3L.
PhylomeDBiQ9H7X0.
TreeFamiTF323980.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122390-MONOMER.

Miscellaneous databases

ChiTaRSiNAA60. human.
GenomeRNAii79903.
PROiQ9H7X0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122390.
CleanExiHS_NAT15.
ExpressionAtlasiQ9H7X0. baseline and differential.
GenevisibleiQ9H7X0. HS.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNAA60_HUMAN
AccessioniPrimary (citable) accession number: Q9H7X0
Secondary accession number(s): B3KRQ0
, B4DLZ0, B4DPZ8, B4DYC4, D3DUC2, E7EQ65, Q6IA31, Q6UX26
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2001
Last modified: January 18, 2017
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

According to a report, displays histone acetyltransferase activity while localized in the Golgi apparatus (PubMed:21981917). May mediates acetylation of free histone H4 and promote nucleosome assembly (PubMed:21981917). Such results are however unclear in vivo and recent reports strongly suggest that it acts as a N-alpha-acetyltransferase that specifically targets N-terminal residues of transmembrane proteins (PubMed:21750686, PubMed:25732826).3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.