Reviewed, UniProtKB/Swiss-Prot Q9QY36 (ARD1A_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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. Ref.1 Ref.2
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.
Subunit structure	Interacts with the ribosome By similarity. Interacts with HIF1A, NARG1 and NAT13.
Subcellular location	Cytoplasm. Ref.2
Tissue specificity	Ubiquitous. Ref.2
Developmental stage	Expressed throughout the developing brain from E11.5 through E17, continues to be expressed at P0, but then is down-regulated. Ref.2
Post-translational modification	Cleaved by caspases during apoptosis By similarity.
Sequence similarities	Belongs to the acetyltransferase family. ARD1 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.2 Inferred from direct assay. Source: MGI
Molecular function	peptide alpha-N-acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Ref.2 Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 235	235	N-terminal acetyltransferase complex ARD1 subunit homolog A		PRO_0000074533
Regions
	Domain	1 – 152	152	N-acetyltransferase
	Region	1 – 58	58	Interaction with NARG1 By similarity
Amino acid modifications
	Modified residue	205	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QY36-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AD2991C519277F29	FASTA	235	26,520
	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 HLELKEKGKH MVLAALENKA 190 200 210 220 230 ENKGNVLLSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HIF1A. Tissue: Embryo and T-cell.
[2]	"An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development." Sugiura N., Adams S.M., Corriveau R.A. J. Biol. Chem. 278:40113-40120(2003) [PubMed: 12888564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NARG1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Tissue: Brain.
[3]	"Comparative sequence analysis of the mouse L1cam locus and the corresponding region of human Xq28." Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK014469 mRNA. Translation: BAB29373.1. AF133093 Genomic DNA. No translation available.
IPI	IPI00465765.
RefSeq	NP_063923.1.
UniGene	Mm.305796
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QY36.
PTM databases
PhosphoSite	Q9QY36.
Proteomic databases
PRIDE	Q9QY36.
Genome annotation databases
Ensembl	ENSMUST00000033763; ENSMUSP00000033763; ENSMUSG00000031388; Mus musculus. [Genome view]
GeneID	56292.
KEGG	mmu:56292.
NMPDR	fig|10090.3.peg.21713.
UCSC	uc009tng.1. mouse.
Organism-specific databases
CTD	56292.
MGI	MGI:1915255. Ard1a.
Phylogenomic databases
HOVERGEN	Q9QY36.
OMA	KGHIVSV.
Enzyme and pathway databases
BRENDA	2.3.1.88. 244.
Gene expression databases
ArrayExpress	Q9QY36.
Bgee	Q9QY36.
Genevestigator	Q9QY36.
GermOnline	ENSMUSG00000031388. Mus musculus.
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	312200.
SOURCE	Search...

Entry information

Entry name

ARD1A_MOUSE

Accession

Primary (citable) accession number: Q9QY36

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)