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Protein

N-alpha-acetyltransferase 11

Gene

Naa11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Displays alpha (N-terminal) acetyltransferase activity. Proposed alternative catalytic subunit of the N-terminal acetyltransferase A (NatA) complex (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 11 (EC:2.3.1.88)
Alternative name(s):
N-terminal acetyltransferase complex ARD1 subunit homolog B
NatA catalytic subunit Naa11
Gene namesi
Name:Naa11
Synonyms:Ard1b, Ard2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2141314. Naa11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218N-alpha-acetyltransferase 11PRO_0000305010Add
BLAST

Proteomic databases

EPDiQ3UX61.
MaxQBiQ3UX61.
PaxDbiQ3UX61.
PRIDEiQ3UX61.

PTM databases

iPTMnetiQ3UX61.
PhosphoSiteiQ3UX61.

Expressioni

Gene expression databases

BgeeiQ3UX61.
CleanExiMM_ARD1B.
ExpressionAtlasiQ3UX61. baseline and differential.
GenevisibleiQ3UX61. MM.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA11 and NAA15. Interacts with HIF1A (By similarity).By similarity

Protein-protein interaction databases

BioGridi220667. 25 interactions.
IntActiQ3UX61. 25 interactions.
STRINGi10090.ENSMUSP00000057336.

Structurei

3D structure databases

ProteinModelPortaliQ3UX61.
SMRiQ3UX61. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 152152N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5858Interaction with NAA15By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3235. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00550000074803.
HOGENOMiHOG000078523.
HOVERGENiHBG050561.
InParanoidiQ3UX61.
KOiK00670.
OMAiSWPEASF.
OrthoDBiEOG7T4MMM.
PhylomeDBiQ3UX61.
TreeFamiTF300078.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UX61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIRNARPDD LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDEDG
60 70 80 90 100
KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE
110 120 130 140 150
NFGAKYVSLH VRKSNRAALH LYSNTLNFQV SEVEPKYYAD GEDAYAMKRD
160 170 180 190 200
LSQMTDELRR QLVLKKNRYV VLGSEETQGG TLPDAGEACL PKNPTSKDSG
210
SSDSTDVQDS SEDLDSIS
Length:218
Mass (Da):24,671
Last modified:October 11, 2005 - v1
Checksum:i93DE5F40D09EED20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411G → V in BAE21577 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133248 mRNA. Translation: BAE21577.1.
AK135863 mRNA. Translation: BAE22702.1.
BC145776 mRNA. Translation: AAI45777.1.
CCDSiCCDS19453.1.
RefSeqiNP_001028363.1. NM_001033191.2.
UniGeneiMm.11746.

Genome annotation databases

EnsembliENSMUST00000060265; ENSMUSP00000057336; ENSMUSG00000046000.
GeneIDi97243.
KEGGimmu:97243.
UCSCiuc008yfw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133248 mRNA. Translation: BAE21577.1.
AK135863 mRNA. Translation: BAE22702.1.
BC145776 mRNA. Translation: AAI45777.1.
CCDSiCCDS19453.1.
RefSeqiNP_001028363.1. NM_001033191.2.
UniGeneiMm.11746.

3D structure databases

ProteinModelPortaliQ3UX61.
SMRiQ3UX61. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220667. 25 interactions.
IntActiQ3UX61. 25 interactions.
STRINGi10090.ENSMUSP00000057336.

PTM databases

iPTMnetiQ3UX61.
PhosphoSiteiQ3UX61.

Proteomic databases

EPDiQ3UX61.
MaxQBiQ3UX61.
PaxDbiQ3UX61.
PRIDEiQ3UX61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060265; ENSMUSP00000057336; ENSMUSG00000046000.
GeneIDi97243.
KEGGimmu:97243.
UCSCiuc008yfw.1. mouse.

Organism-specific databases

CTDi84779.
MGIiMGI:2141314. Naa11.

Phylogenomic databases

eggNOGiKOG3235. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00550000074803.
HOGENOMiHOG000078523.
HOVERGENiHBG050561.
InParanoidiQ3UX61.
KOiK00670.
OMAiSWPEASF.
OrthoDBiEOG7T4MMM.
PhylomeDBiQ3UX61.
TreeFamiTF300078.

Miscellaneous databases

PROiQ3UX61.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UX61.
CleanExiMM_ARD1B.
ExpressionAtlasiQ3UX61. baseline and differential.
GenevisibleiQ3UX61. MM.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Egg and Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase."
    Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J., Kong X., Varhaug J.E., Lillehaug J.R.
    BMC Biochem. 7:13-13(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiNAA11_MOUSE
AccessioniPrimary (citable) accession number: Q3UX61
Secondary accession number(s): Q3V0C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.