CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007472
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-alpha-acetyltransferase 10 
Protein Synonyms/Alias
 N-terminal acetyltransferase complex ARD1 subunit homolog A; NatA catalytic subunit 
Gene Name
 NAA10 
Gene Synonyms/Alias
 ARD1; ARD1A; TE2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78HITSLAVKRSHRRLGubiquitination[1, 2, 3, 4, 5]
89RRLGLAQKLMDQASRubiquitination[1, 2, 3, 4, 5, 6, 7]
105MIENFNAKYVSLHVRubiquitination[1, 5]
136QISEVEPKYYADGEDacetylation[8]
148GEDAYAMKRDLTQMAubiquitination[1, 2, 3, 4, 5, 6]
179VLGAIENKVESKGNSacetylation[9]
179VLGAIENKVESKGNSubiquitination[2, 3, 10, 11]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 In complex with NAA15, displays alpha (N-terminal) acetyltransferase activity. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. 
Sequence Annotation
 DOMAIN 1 152 N-acetyltransferase.
 REGION 1 58 Interaction with NAA15.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 182 182 Phosphoserine.
 MOD_RES 186 186 Phosphoserine.
 MOD_RES 205 205 Phosphoserine.
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 216 216 Phosphoserine.  
Keyword
 Acetylation; Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm; Disease mutation; Nucleus; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 235 AA 
Protein Sequence
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM 60
EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH 120
LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV 180
ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS 235 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0008080; F:N-acetyltransferase activity; TAS:ProtInc.
 GO:0004596; F:peptide alpha-N-acetyltransferase activity; IEA:EC.
 GO:0006323; P:DNA packaging; TAS:ProtInc.
 GO:0006475; P:internal protein amino acid acetylation; TAS:ProtInc.
 GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR000182; GNAT_dom. 
Pfam
 PF00583; Acetyltransf_1 
SMART
  
PROSITE
 PS51186; GNAT 
PRINTS