Reviewed, UniProtKB/Swiss-Prot P41227 (ARD1A_HUMAN)

Names and origin

Protein names

Recommended name:
    N-terminal acetyltransferase complex ARD1 subunit homolog A
    EC=2.3.1.88
    EC=2.3.1.-

Gene names

Name:	ARD1A
Synonyms:	ARD1, TE2

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	235 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In complex with NARG1, displays alpha (N-terminal) acetyltransferase activity. Without NARG1, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation.
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, and downregulates it when induced by hypoxia. Interacts with NARG1, NAT13 and with the ribosome.
Subcellular location	Cytoplasm. Nucleus. Note= According to Ref.4 it is cytoplasmic. According to Ref.2 it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes.
Tissue specificity	Ubiquitous.
Post-translational modification	Cleaved by caspases during apoptosis.
Sequence similarities	Belongs to the acetyltransferase family. ARD1 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA packaging Ref.1 Traceable author statement. Source: ProtInc N-terminal protein amino acid acetylation Ref.2 Inferred from direct assay. Source: UniProtKB internal protein amino acid acetylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.2 Inferred from direct assay. Source: UniProtKB nucleus Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	N-acetyltransferase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.2 Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 235	235	N-terminal acetyltransferase complex ARD1 subunit homolog A
Regions
	Domain	1 – 152	152	N-acetyltransferase
	Region	1 – 58	58	Interaction with NARG1
Amino acid modifications
	Modified residue	182	1	Phosphoserine
	Modified residue	186	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P41227-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 6393A907F5C2DDC4	FASTA	235	26,459
	10 20 30 40 50 60 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM 70 80 90 100 110 120 EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH 130 140 150 160 170 180 LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV 190 200 210 220 230 ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae." Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., Torri G., Toniolo D. Hum. Mol. Genet. 3:1061-1068(1994) [PubMed: 7981673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification and characterization of the human ARD1-NATH protein acetyltransferase complex." Arnesen T., Anderson D., Baldersheim C., Lanotte M., Varhaug J.E., Lillehaug J.R. Biochem. J. 386:433-443(2005) [PubMed: 15496142] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NARG1 AND RIBOSOMAL PROTEINS. Tissue: Thyroid carcinoma.
[3]	"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]. Tissue: Lung.
[4]	"Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation." Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H., Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W. Cell 111:709-720(2002) [PubMed: 12464182] [Abstract] Cited for: INTERACTION WITH HIF1A, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, MASS SPECTROMETRY. Tissue: Epithelium.
[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 NAT13.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, MASS SPECTROMETRY. Tissue: Epithelium.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X77588 mRNA. Translation: CAA54691.1. BC000308 mRNA. Translation: AAH00308.1. BC019312 mRNA. Translation: AAH19312.1.
PIR	I38333.
RefSeq	NP_003482.1.
UniGene	Hs.433291
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P41227.
PTM databases
PhosphoSite	P41227.
Genome annotation databases
Ensembl	ENSG00000102030. Homo sapiens. [Contig view]
GeneID	8260.
KEGG	hsa:8260.
NMPDR	fig|9606.3.peg.33620.
Organism-specific databases
H-InvDB	HIX0017143. HIX0031424.
HGNC	HGNC:18704. ARD1A.
HPA	CAB006269.
MIM	300013. gene.
PharmGKB	PA38648.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOVERGEN	P41227.
Gene expression databases
ArrayExpress	P41227.
CleanEx	HS_ARD1A.
GermOnline	ENSG00000102030. Homo sapiens.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProDom	P41227. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ARD1A_HUMAN

Accession

Primary (citable) accession number: P41227

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	July 22, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)