Reviewed, UniProtKB/Swiss-Prot P07347 (ARD1_YEAST)

Names and origin

Protein names

Recommended name:
    N-terminal acetyltransferase A complex catalytic subunit ARD1
      Short name=NatA complex subunit ARD1
    EC=2.3.1.88
Alternative name(s):
    Arrest-defective protein 1

Gene names

Name:	ARD1
Ordered Locus Names:	YHR013C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. Ref.5
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate.
Subcellular location	Cytoplasm Ref.7.
Miscellaneous	Present with 3310 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the acetyltransferase family. ARD1 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid acetylation Ref.4 Inferred from direct assay. Source: SGD histone acetylation Inferred from mutant phenotype. Source: SGD
Cellular component	NatA complex Ref.6 Inferred from direct assay. Source: SGD
Molecular function	identical protein binding Ref.5 Inferred from physical interaction. Source: IntAct peptide alpha-N-acetyltransferase activity Ref.4 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-2796,EBI-2796
NAT1	P12945	2	EBI-2796,EBI-11868

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 238	238	N-terminal acetyltransferase A complex catalytic subunit ARD1		PRO_0000074529
Regions
	Domain	35 – 195	161	N-acetyltransferase
Experimental info
	Sequence conflict	37	1	I → T in AAA66323. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07347-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: AEB02BA5012D1137	FASTA	238	27,603
	10 20 30 40 50 60 MPINIRRATI NDIICMQNAN LHNLPENYMM KYYMYHILSW PEASFVATTT TLDCEDSDEQ 70 80 90 100 110 120 DENDKLELTL DGTNDGRTIK LDPTYLAPGE KLVGYVLVKM NDDPDQQNEP PNGHITSLSV 130 140 150 160 170 180 MRTYRRMGIA ENLMRQALFA LREVHQAEYV SLHVRQSNRA ALHLYRDTLA FEVLSIEKSY 190 200 210 220 230 YQDGEDAYAM KKVLKLEELQ ISNFTHRRLK ENEEKLEDDL ESDLLEDIIK QGVNDIIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways." Whiteway M., Szostak J.W. Cell 43:483-492(1985) [PubMed: 3907857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast." Mullen J.R., Kayne P.S., Moerschell R.P., Tsunasawa S., Gribskov M., Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R. EMBO J. 8:2067-2075(1989) [PubMed: 2551674] [Abstract] Cited for: CHARACTERIZATION.
[5]	"ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity." Park E.C., Szostak J.W. EMBO J. 11:2087-2093(1992) [PubMed: 1600941] [Abstract] Cited for: FUNCTION, INTERACTION WITH NAT1, SELF-ASSOCIATION.
[6]	"The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides." Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y., Ehrenhofer-Murray A., Rospert S. Mol. Cell. Biol. 23:7403-7414(2003) [PubMed: 14517307] [Abstract] Cited for: IDENTIFICATION IN THE NATA COMPLEX.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M11621 Genomic DNA. Translation: AAA66323.1. U10400 Genomic DNA. Translation: AAB68937.1. AY557822 Genomic DNA. Translation: AAS56148.1.
PIR	TWBYA1. S46783.
RefSeq	NP_011877.1.
3D structure databases
SMR	P07347. Positions 3-194.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6788N.
IntAct	P07347. 29 interactions.
STRING	P07347.
Proteomic databases
PeptideAtlas	P07347.
Genome annotation databases
Ensembl	YHR013C; YHR013C; YHR013C; Saccharomyces cerevisiae. [Genome view]
GeneID	856404.
KEGG	sce:YHR013C.
NMPDR	fig|4932.3.peg.3022.
Organism-specific databases
CYGD	YHR013c.
SGD	S000001055. ARD1.
Phylogenomic databases
eggNOG	fuNOG08135.
HOGENOM	HBG742014.
OMA	SWPEASF.
OrthoDB	EOG951G72.
PhylomeDB	P07347.
Enzyme and pathway databases
BRENDA	2.3.1.88. 250.
Gene expression databases
ArrayExpress	P07347.
Genevestigator	P07347.
GermOnline	YHR013C. Saccharomyces cerevisiae.
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]
ProtoNet	Search...
Other Resources
NextBio	981943.

Entry information

Entry name

ARD1_YEAST

Accession

Primary (citable) accession number: P07347

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1995
Last modified:	January 19, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)