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Protein

N-alpha-acetyltransferase 20

Gene

Naa20

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

Functioni

Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 20 (EC:2.3.1.88)
Alternative name(s):
Methionine N-acetyltransferase
N-acetyltransferase 5
N-terminal acetyltransferase B complex catalytic subunit NAA20
N-terminal acetyltransferase B complex catalytic subunit NAT5
Short name:
NatB complex subunit NAT5
NatB catalytic subunit
Gene namesi
Name:Naa20
Synonyms:Nat5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915127. Naa20.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178N-alpha-acetyltransferase 20PRO_0000074535Add
BLAST

Proteomic databases

EPDiP61600.
MaxQBiP61600.
PRIDEiP61600.

PTM databases

iPTMnetiP61600.
PhosphoSiteiP61600.

Expressioni

Gene expression databases

BgeeiP61600.
ExpressionAtlasiP61600. baseline.
GenevisibleiP61600. MM.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25.By similarity

Protein-protein interaction databases

BioGridi212503. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP61600.
SMRiP61600. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000075046.
HOVERGENiHBG107217.
InParanoidiP61600.
KOiK17972.

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.

P61600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG
60 70 80 90 100
GELMGYIMGK AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS
110 120 130 140 150
ERKGGFFVDL FVRVSNQVAV NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY
160 170
DMRKALSRDT EKKSIIPLPH PVRPEDIE
Length:178
Mass (Da):20,368
Last modified:May 24, 2004 - v1
Checksum:iC5CCEA50CD60E097
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009229 mRNA. Translation: BAB26152.1.
BC009157 mRNA. Translation: AAH09157.1.
BC096451 mRNA. Translation: AAH96451.1.
BC116374 mRNA. Translation: AAI16375.1.
CCDSiCCDS50735.1.
RefSeqiNP_001135437.1. NM_001141965.1.
NP_080701.1. NM_026425.3.
UniGeneiMm.151168.
Mm.442235.

Genome annotation databases

EnsembliENSMUST00000110000; ENSMUSP00000105627; ENSMUSG00000002728.
GeneIDi67877.
KEGGimmu:67877.
UCSCiuc008mry.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009229 mRNA. Translation: BAB26152.1.
BC009157 mRNA. Translation: AAH09157.1.
BC096451 mRNA. Translation: AAH96451.1.
BC116374 mRNA. Translation: AAI16375.1.
CCDSiCCDS50735.1.
RefSeqiNP_001135437.1. NM_001141965.1.
NP_080701.1. NM_026425.3.
UniGeneiMm.151168.
Mm.442235.

3D structure databases

ProteinModelPortaliP61600.
SMRiP61600. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212503. 4 interactions.

PTM databases

iPTMnetiP61600.
PhosphoSiteiP61600.

Proteomic databases

EPDiP61600.
MaxQBiP61600.
PRIDEiP61600.

Protocols and materials databases

DNASUi67877.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110000; ENSMUSP00000105627; ENSMUSG00000002728.
GeneIDi67877.
KEGGimmu:67877.
UCSCiuc008mry.2. mouse.

Organism-specific databases

CTDi51126.
MGIiMGI:1915127. Naa20.

Phylogenomic databases

GeneTreeiENSGT00550000075046.
HOVERGENiHBG107217.
InParanoidiP61600.
KOiK17972.

Miscellaneous databases

ChiTaRSiNaa20. mouse.
PROiP61600.
SOURCEiSearch...

Gene expression databases

BgeeiP61600.
ExpressionAtlasiP61600. baseline.
GenevisibleiP61600. 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

  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: Tongue.
  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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNAA20_MOUSE
AccessioniPrimary (citable) accession number: P61600
Secondary accession number(s): Q14B28
, Q4VAC3, Q9D7H8, Q9H0Y4, Q9NQH6, Q9Y6D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 8, 2016
This is version 93 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.