Q9GZZ1 (NAA50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NAA50
Synonyms:	MAK3, NAT13, NAT5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity. Ref.6
Subunit structure	Interacts with NAA35 By similarity. Interacts with NAA15 and NAA11. Ref.6
Subcellular location	Cytoplasm Ref.6.
Sequence similarities	Belongs to the acetyltransferase family. GNAT subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid acetylation Traceable author statement Ref.6. Source: HGNC
Cellular component	cytoplasm Inferred from direct assay Ref.6. Source: HGNC
Molecular function	N-acetyltransferase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.6. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9GZZ1-1)

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.

Isoform 2 (identifier: Q9GZZ1-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 169

169

N-alpha-acetyltransferase 50

PRO_0000284902

Regions

Domain

6 – 155

150

N-acetyltransferase

Region

79 – 90

12

Coenzyme A binding

Amino acid modifications

Modified residue

12

1

Phosphothreonine Ref.7

Modified residue

34

1

N6-acetyllysine Ref.9

Modified residue

37

1

N6-acetyllysine Ref.9

Modified residue

110

1

Phosphotyrosine Ref.5

Natural variations

Alternative sequence

35 – 122

88

Missing in isoform 2.

VSP_024747

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

169

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Turn

13 – 15

3

Helix

16 – 26

11

Helix

33 – 39

7

Helix

43 – 45

3

Beta strand

46 – 51

6

Beta strand

54 – 66

13

Beta strand

69 – 79

11

Helix

81 – 83

3

Helix

88 – 103

16

Beta strand

107 – 114

8

Helix

118 – 126

9

Beta strand

130 – 135

6

Beta strand

140 – 144

5

Beta strand

147 – 153

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 153A8021B74655CC	FASTA	169	19,398
	10 20 30 40 50 60 MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY FNDIAVGAVC 70 80 90 100 110 120 CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC EKDGTFDNIY LHVQISNESA 130 140 150 160 IDFYRKFGFE IIETKKNYYK RIEPADAHVL QKNLKVPSGQ NADVQKTDN
	Isoform 2 [UniParc]. Checksum: 72B366F6387B4FC5	FASTA	81	9,465
	10 20 30 40 50 60 MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYRKFG FEIIETKKNY YKRIEPADAH 70 80 VLQKNLKVPS GQNADVQKTD N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Small intestine.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, MASS SPECTROMETRY.
[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: 16507339] [Abstract] Cited for: INTERACTION WITH NAA15 AND NAA11, MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, MASS SPECTROMETRY. 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: 19660095] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018627.
IPI00470922.

RefSeq

NP_079422.1. NM_025146.2.

UniGene

Hs.372378.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OB0	X-ray	1.80	A/B/C	2-169	[»]
2PSW	X-ray	2.10	A/B/C	2-169	[»]
3TFY	X-ray	2.75	A/B/C	1-169	[»]

ProteinModelPortal

Q9GZZ1.

SMR

Q9GZZ1. Positions 4-169.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9GZZ1. 3 interactions.

STRING

Q9GZZ1.

PTM databases

PhosphoSite

Q9GZZ1.

Polymorphism databases

DMDM

74733509.

Proteomic databases

PRIDE

Q9GZZ1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000240922; ENSP00000240922; ENSG00000121579.

GeneID

80218.

KEGG

hsa:80218.

UCSC

uc003ean.1. human.

Organism-specific databases

CTD

80218.

GeneCards

GC03M113437.

H-InvDB

HIX0003559.

HGNC

HGNC:29533. NAA50.

MIM

610834. gene.

neXtProt

NX_Q9GZZ1.

PharmGKB

PA134960995.
PA165697846.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16073.

GeneTree

ENSGT00390000009110.

HOGENOM

HBG397974.

HOVERGEN

HBG060820.

InParanoid

Q9GZZ1.

OMA

LAYYNDI.

OrthoDB

EOG4H19WV.

PhylomeDB

Q9GZZ1.

Gene expression databases

ArrayExpress

Q9GZZ1.

Bgee

Q9GZZ1.

CleanEx

HS_NAT13.
HS_NAT5.

Genevestigator

Q9GZZ1.

Family and domain databases

InterPro

IPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

Pfam

PF00583. Acetyltransf_1. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

70626.

SOURCE

Search...

Entry information

Entry name

NAA50_HUMAN

Accession

Primary (citable) accession number: Q9GZZ1
Secondary accession number(s): D3DN74, Q68DQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.