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Q9QY36 (NAA10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 10
EC=2.3.1.-
EC=2.3.1.88
Alternative name(s):
N-terminal acetyltransferase complex ARD1 subunit homolog A
NatA catalytic subunit
Gene names
Name:Naa10
Synonyms:Ard1, Ard1a, Te2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In complex with NAA15, displays alpha (N-terminal) acetyltransferase activity. Without NAA15, 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. Binds to MYLK. Associates with HYPK when in complex with NAA15 By similarity. Interacts with HIF1A, NAA15 and NAA50. Ref.1 Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235N-alpha-acetyltransferase 10
PRO_0000074533

Regions

Domain1 – 152152N-acetyltransferase
Region1 – 5858Interaction with NAA15 By similarity

Amino acid modifications

Modified residue2051Phosphoserine By similarity
Modified residue2131Phosphoserine By similarity
Modified residue2161Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QY36 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AD2991C519277F29

FASTA23526,520
        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

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NAA15, 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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK014469 mRNA. Translation: BAB29373.1.
AF133093 Genomic DNA. No translation available.
IPIIPI00465765.
RefSeqNP_063923.1. NM_019870.3.
UniGeneMm.246654.

3D structure databases

ProteinModelPortalQ9QY36.
SMRQ9QY36. Positions 3-149.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QY36. 7 interactions.
STRING10090.ENSMUSP00000033763.

PTM databases

PhosphoSiteQ9QY36.

Proteomic databases

PaxDbQ9QY36.
PRIDEQ9QY36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033763; ENSMUSP00000033763; ENSMUSG00000031388.
GeneID56292.
KEGGmmu:56292.
UCSCuc009tng.2. mouse.

Organism-specific databases

CTD8260.
MGIMGI:1915255. Naa10.

Phylogenomic databases

eggNOGCOG0456.
GeneTreeENSGT00550000074803.
HOGENOMHOG000078523.
HOVERGENHBG050561.
InParanoidQ9QY36.
KOK00670.
OrthoDBEOG4Z0B6F.

Gene expression databases

ArrayExpressQ9QY36.
BgeeQ9QY36.
GenevestigatorQ9QY36.
GermOnlineENSMUSG00000031388. Mus musculus.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312200.
SOURCESearch...

Entry information

Entry nameNAA10_MOUSE
AccessionPrimary (citable) accession number: Q9QY36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: May 1, 2000
Last modified: May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents