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Protein

N-alpha-acetyltransferase 50

Gene

NAA50

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

Functioni

Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity.1 Publication

GO - Molecular functioni

  • H4 histone acetyltransferase activity Source: UniProtKB
  • peptide alpha-N-acetyltransferase activity Source: UniProtKB
  • peptidyl-lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB

GO - Biological processi

  • histone H4 acetylation Source: GOC
  • mitotic sister chromatid cohesion, centromeric Source: UniProtKB
  • N-terminal protein amino acid acetylation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.88. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 50 (EC:2.3.1.-)
Alternative name(s):
N-acetyltransferase 13
N-acetyltransferase 5
Short name:
hNAT5
N-acetyltransferase san homolog
Short name:
hSAN
NatE catalytic subunit
Gene namesi
Name:NAA50
Synonyms:MAK3, NAT13, NAT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:29533. NAA50.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165697846.

Polymorphism and mutation databases

BioMutaiNAA50.
DMDMi74733509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169N-alpha-acetyltransferase 50PRO_0000284902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphothreonineCombined sources
Modified residuei34 – 341N6-acetyllysineCombined sources
Modified residuei37 – 371N6-acetyllysineCombined sources
Modified residuei110 – 1101PhosphotyrosineCombined sources
Isoform 2 (identifier: Q9GZZ1-2)
Modified residuei34 – 341N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9GZZ1.
MaxQBiQ9GZZ1.
PaxDbiQ9GZZ1.
PRIDEiQ9GZZ1.

PTM databases

iPTMnetiQ9GZZ1.
PhosphoSiteiQ9GZZ1.

Expressioni

Gene expression databases

BgeeiQ9GZZ1.
CleanExiHS_NAT13.
HS_NAT5.
ExpressionAtlasiQ9GZZ1. baseline and differential.
GenevisibleiQ9GZZ1. HS.

Interactioni

Subunit structurei

Interacts with NAA35 (By similarity). Interacts with NAA15 and NAA11.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BHLHE40O145033EBI-1052523,EBI-711810
JMJD6Q6NYC13EBI-1052523,EBI-8464037
NAA10P412272EBI-1052523,EBI-747693
NAA15Q9BXJ92EBI-1052523,EBI-1042540

Protein-protein interaction databases

BioGridi123185. 31 interactions.
IntActiQ9GZZ1. 9 interactions.
STRINGi9606.ENSP00000240922.

Structurei

Secondary structure

1
169
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Turni13 – 153Combined sources
Helixi16 – 2611Combined sources
Helixi33 – 397Combined sources
Helixi43 – 453Combined sources
Beta strandi46 – 516Combined sources
Beta strandi54 – 6613Combined sources
Beta strandi69 – 7911Combined sources
Helixi81 – 833Combined sources
Beta strandi85 – 873Combined sources
Helixi88 – 10316Combined sources
Beta strandi107 – 1148Combined sources
Helixi118 – 1269Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi147 – 1537Combined sources
Helixi162 – 1643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OB0X-ray1.80A/B/C2-169[»]
2PSWX-ray2.10A/B/C2-169[»]
3TFYX-ray2.75A/B/C1-169[»]
4X5KX-ray2.49A1-169[»]
ProteinModelPortaliQ9GZZ1.
SMRiQ9GZZ1. Positions 4-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GZZ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 155150N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 9012Coenzyme A bindingAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3138. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00390000009110.
HOGENOMiHOG000238056.
HOVERGENiHBG060820.
InParanoidiQ9GZZ1.
OMAiSAIDFYQ.
OrthoDBiEOG7MWGZK.
PhylomeDBiQ9GZZ1.
TreeFamiTF314841.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9GZZ1-1) [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
MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY
60 70 80 90 100
FNDIAVGAVC CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC
110 120 130 140 150
EKDGTFDNIY LHVQISNESA IDFYRKFGFE IIETKKNYYK RIEPADAHVL
160
QKNLKVPSGQ NADVQKTDN
Length:169
Mass (Da):19,398
Last modified:March 1, 2001 - v1
Checksum:i153A8021B74655CC
GO
Isoform 2 (identifier: Q9GZZ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-122: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:81
Mass (Da):9,465
Checksum:i72B366F6387B4FC5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 12288Missing in isoform 2. 1 PublicationVSP_024747Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023090 mRNA. Translation: BAB14397.1.
AK023256 mRNA. Translation: BAB14490.1.
CR749314 mRNA. Translation: CAH18169.1.
CH471052 Genomic DNA. Translation: EAW79629.1.
CH471052 Genomic DNA. Translation: EAW79630.1.
BC012731 mRNA. Translation: AAH12731.1.
CCDSiCCDS2975.1. [Q9GZZ1-1]
RefSeqiNP_079422.1. NM_025146.3. [Q9GZZ1-1]
UniGeneiHs.372378.

Genome annotation databases

EnsembliENST00000240922; ENSP00000240922; ENSG00000121579. [Q9GZZ1-1]
GeneIDi80218.
KEGGihsa:80218.
UCSCiuc003ean.3. human. [Q9GZZ1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023090 mRNA. Translation: BAB14397.1.
AK023256 mRNA. Translation: BAB14490.1.
CR749314 mRNA. Translation: CAH18169.1.
CH471052 Genomic DNA. Translation: EAW79629.1.
CH471052 Genomic DNA. Translation: EAW79630.1.
BC012731 mRNA. Translation: AAH12731.1.
CCDSiCCDS2975.1. [Q9GZZ1-1]
RefSeqiNP_079422.1. NM_025146.3. [Q9GZZ1-1]
UniGeneiHs.372378.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OB0X-ray1.80A/B/C2-169[»]
2PSWX-ray2.10A/B/C2-169[»]
3TFYX-ray2.75A/B/C1-169[»]
4X5KX-ray2.49A1-169[»]
ProteinModelPortaliQ9GZZ1.
SMRiQ9GZZ1. Positions 4-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123185. 31 interactions.
IntActiQ9GZZ1. 9 interactions.
STRINGi9606.ENSP00000240922.

PTM databases

iPTMnetiQ9GZZ1.
PhosphoSiteiQ9GZZ1.

Polymorphism and mutation databases

BioMutaiNAA50.
DMDMi74733509.

Proteomic databases

EPDiQ9GZZ1.
MaxQBiQ9GZZ1.
PaxDbiQ9GZZ1.
PRIDEiQ9GZZ1.

Protocols and materials databases

DNASUi80218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000240922; ENSP00000240922; ENSG00000121579. [Q9GZZ1-1]
GeneIDi80218.
KEGGihsa:80218.
UCSCiuc003ean.3. human. [Q9GZZ1-1]

Organism-specific databases

CTDi80218.
GeneCardsiNAA50.
HGNCiHGNC:29533. NAA50.
MIMi610834. gene.
neXtProtiNX_Q9GZZ1.
PharmGKBiPA165697846.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3138. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00390000009110.
HOGENOMiHOG000238056.
HOVERGENiHBG060820.
InParanoidiQ9GZZ1.
OMAiSAIDFYQ.
OrthoDBiEOG7MWGZK.
PhylomeDBiQ9GZZ1.
TreeFamiTF314841.

Enzyme and pathway databases

BRENDAi2.3.1.88. 2681.

Miscellaneous databases

ChiTaRSiNAA50. human.
EvolutionaryTraceiQ9GZZ1.
GenomeRNAii80218.
PROiQ9GZZ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZZ1.
CleanExiHS_NAT13.
HS_NAT5.
ExpressionAtlasiQ9GZZ1. baseline and differential.
GenevisibleiQ9GZZ1. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex."
    Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., Lillehaug J.R.
    Gene 371:291-295(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAA15 AND NAA11, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates."
    Polevoda B., Arnesen T., Sherman F.
    BMC Proc. 3:S2-S2(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structure of human MAK3 homolog."
    Structural genomics consortium (SGC)
    Submitted (JUN-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COENZYME A.

Entry informationi

Entry nameiNAA50_HUMAN
AccessioniPrimary (citable) accession number: Q9GZZ1
Secondary accession number(s): D3DN74, Q68DQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.