NAT5

Protein-coding gene in the species Homo sapiens
NAA20
Identifiers
AliasesNAA20, NAT3, NAT3P, NAT5, NAT5P, dJ1002M8.1, N(alpha)-acetyltransferase 20, NatB catalytic subunit, N-alpha-acetyltransferase 20, NatB catalytic subunit, MRT73
External IDsOMIM: 610833; MGI: 1915127; HomoloGene: 7165; GeneCards: NAA20; OMA:NAA20 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for NAA20
Genomic location for NAA20
Band20p11.23Start20,017,310 bp[1]
End20,033,655 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for NAA20
Genomic location for NAA20
Band2 G1|2 71.28 cMStart145,744,019 bp[2]
End145,758,345 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • tibialis anterior muscle

  • mucosa of pharynx

  • gingival epithelium

  • oral cavity

  • skin of arm

  • body of pancreas

  • right testis

  • deltoid muscle

  • left testis
Top expressed in
  • heart

  • quadriceps femoris muscle

  • epiblast

  • embryo

  • neural tube

  • right kidney

  • mesencephalon

  • ventricular zone

  • lip

  • thymus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • acyltransferase activity
  • peptide alpha-N-acetyltransferase activity
Cellular component
  • intracellular anatomical structure
  • NatB complex
  • cytosol
  • nucleus
  • cytoplasm
Biological process
  • N-terminal peptidyl-methionine acetylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51126

67877

Ensembl

ENSG00000173418

ENSMUSG00000002728

UniProt

P61599

P61600

RefSeq (mRNA)

NM_181528
NM_016100
NM_181527

NM_001141965
NM_026425

RefSeq (protein)

NP_057184
NP_852668
NP_852669

NP_001135437
NP_080701

Location (UCSC)Chr 20: 20.02 – 20.03 MbChr 2: 145.74 – 145.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

N-terminal acetyltransferase B complex catalytic subunit NAT5 is an enzyme that in humans is encoded by the NAT5 gene.[5][6]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000173418 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002728 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Sugiura N, Adams SM, Corriveau RA (Oct 2003). "An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development". J Biol Chem. 278 (41): 40113–20. doi:10.1074/jbc.M301218200. PMID 12888564.
  6. ^ "Entrez Gene: NAT5 N-acetyltransferase 5".

Further reading

  • Vitale N, Pacheco-Rodriguez G, Ferrans VJ, et al. (2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Polevoda B, Cardillo TS, Doyle TC, et al. (2003). "Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin". J. Biol. Chem. 278 (33): 30686–97. doi:10.1074/jbc.M304690200. PMID 12783868.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
  • Arnesen T, Anderson D, Torsvik J, et al. (2006). "Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex". Gene. 371 (2): 291–5. doi:10.1016/j.gene.2005.12.008. PMID 16507339.
  • Sánchez-Puig N, Fersht AR (2006). "Characterization of the native and fibrillar conformation of the human Nα-acetyltransferase ARD1". Protein Sci. 15 (8): 1968–76. doi:10.1110/ps.062264006. PMC 2242591. PMID 16823041.


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