Q147X3 (NAA30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-alpha-acetyltransferase 30
EC=2.3.1.88

Alternative name(s):
N-acetyltransferase 12
N-acetyltransferase MAK3 homolog
NatC catalytic subunit

Gene names

Name:	NAA30
Synonyms:	C14orf35, MAK3, NAT12

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	362 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B. Ref.6
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of NAA35, LSMD1 and NAA30.
Subcellular location	Cytoplasm Ref.6.
Sequence similarities	Belongs to the acetyltransferase family. MAK3 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	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide alpha-N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q147X3-1)

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: Q147X3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-79: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	N-alpha-acetyltransferase 30		PRO_0000320032
Regions
	Domain	214 – 362	149	N-acetyltransferase
	Compositional bias	5 – 30	26	Pro-rich
Amino acid modifications
	Modified residue	39	1	Phosphoserine Ref.4
	Modified residue	55	1	Phosphoserine Ref.4
	Modified residue	117	1	Phosphothreonine Ref.4
	Modified residue	152	1	Phosphoserine Ref.3 Ref.4
	Modified residue	190	1	Phosphoserine Ref.4
	Modified residue	196	1	Phosphoserine Ref.4
	Modified residue	199	1	Phosphoserine Ref.4
	Modified residue	233	1	N6-acetyllysine Ref.7
Natural variations
	Alternative sequence	43 – 79	37	Missing in isoform 2.		VSP_031581

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 6C9D69C980C090C0	FASTA	362	39,320
	10 20 30 40 50 60 MAEVPPGPSS LLPPPAPPAP AAVEPRCPFP AGAALACCSE DEEDDEEHEG GGSRSPAGGE 70 80 90 100 110 120 SATVAAKGHP CLRCPQPPQE QQQLNGLISP ELRHLRAAAS LKSKVLSVAE VAATTATPDG 130 140 150 160 170 180 GPRATATKGA GVHSGERPPH SLSSNARTAV PSPVEAAAAS DPAAARNGLA EGTEQEEEEE 190 200 210 220 230 240 DEQVRLLSSS LTADCSLRSP SGREVEPGED RTIRYVRYES ELQMPDIMRL ITKDLSEPYS 250 260 270 280 290 300 IYTYRYFIHN WPQLCFLAMV GEECVGAIVC KLDMHKKMFR RGYIAMLAVD SKYRRNGIGT 310 320 330 340 350 360 NLVKKAIYAM VEGDCDEVVL ETEITNKSAL KLYENLGFVR DKRLFRYYLN GVDALRLKLW LR
	Isoform 2 [UniParc]. Checksum: 9A1E7AF84F24143D	FASTA	325	35,580
	10 20 30 40 50 60 MAEVPPGPSS LLPPPAPPAP AAVEPRCPFP AGAALACCSE DEEQQQLNGL ISPELRHLRA 70 80 90 100 110 120 AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA 130 140 150 160 170 180 AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR 190 200 210 220 230 240 YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK 250 260 270 280 290 300 MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG 310 320 FVRDKRLFRY YLNGVDALRL KLWLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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] (ISOFORMS 1 AND 2).
[3]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"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 SER-39; SER-55; THR-117; SER-152; SER-190; SER-196 AND SER-199, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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.
[6]	"Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization." Starheim K.K., Gromyko D., Evjenth R., Ryningen A., Varhaug J.E., Lillehaug J.R., Arnesen T. Mol. Cell. Biol. 29:3569-3581(2009) [PubMed: 19398576] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN NATC COMPLEX, SUBCELLULAR LOCATION.
[7]	"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-233, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH471061 Genomic DNA. Translation: EAW80705.1. BC118589 mRNA. Translation: AAI18590.1. BC122557 mRNA. Translation: AAI22558.1.
IPI	IPI00219068. IPI00788069.
RefSeq	NP_001011713.2. NM_001011713.2.
UniGene	Hs.165465.
3D structure databases
ProteinModelPortal	Q147X3.
SMR	Q147X3. Positions 218-359.
ModBase	Search...
Protein-protein interaction databases
STRING	Q147X3.
PTM databases
PhosphoSite	Q147X3.
Polymorphism databases
DMDM	121948171.
Proteomic databases
PRIDE	Q147X3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298406; ENSP00000298406; ENSG00000139977.
GeneID	122830.
KEGG	hsa:122830.
UCSC	uc001xcx.2. human.
Organism-specific databases
CTD	122830.
GeneCards	GC14P057857.
H-InvDB	HIX0011696.
HGNC	HGNC:19844. NAA30.
neXtProt	NX_Q147X3.
PharmGKB	PA134931315.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15463.
GeneTree	ENSGT00390000005665.
HOGENOM	HBG282398.
HOVERGEN	HBG082671.
InParanoid	Q147X3.
OMA	AGVHSGE.
OrthoDB	EOG4KKZ4S.
PhylomeDB	Q147X3.
Gene expression databases
ArrayExpress	Q147X3.
Bgee	Q147X3.
CleanEx	HS_NAT12.
Genevestigator	Q147X3.
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.
KO	K00670.
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	81013.

Entry information

Entry name

NAA30_HUMAN

Accession

Primary (citable) accession number: Q147X3
Secondary accession number(s): Q0IIN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 52 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.