ID NAA30_HUMAN Reviewed; 362 AA. AC Q147X3; Q0IIN2; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 28-JAN-2026, entry version 144. DE RecName: Full=N-alpha-acetyltransferase 30; DE EC=2.3.1.256 {ECO:0000269|PubMed:19398576}; DE AltName: Full=N-acetyltransferase 12; DE AltName: Full=N-acetyltransferase MAK3 homolog; DE AltName: Full=NatC catalytic subunit; GN Name=NAA30; Synonyms=C14orf35, MAK3, NAT12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-55; THR-117; SER-152; RP SER-196 AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] RP NOMENCLATURE. RX PubMed=19660095; DOI=10.1186/1753-6561-3-s6-s2; RA Polevoda B., Arnesen T., Sherman F.; RT "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, RT subunits and substrates."; RL BMC Proc. 3:S2-S2(2009). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN NATC COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=19398576; DOI=10.1128/mcb.01909-08; RA Starheim K.K., Gromyko D., Evjenth R., Ryningen A., Varhaug J.E., RA Lillehaug J.R., Arnesen T.; RT "Knockdown of human N alpha-terminal acetyltransferase complex C leads to RT p53-dependent apoptosis and aberrant human Arl8b localization."; RL Mol. Cell. Biol. 29:3569-3581(2009). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-190 AND SER-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053; RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I., RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S., RA Ziegler M., Niere M., Gevaert K., Arnesen T.; RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N RT termini of transmembrane proteins and maintains Golgi integrity."; RL Cell Rep. 10:1362-1374(2015). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37891180; DOI=10.1038/s41467-023-42342-y; RA Varland S., Silva R.D., Kjosaas I., Faustino A., Bogaert A., Billmann M., RA Boukhatmi H., Kellen B., Costanzo M., Drazic A., Osberg C., Chan K., RA Zhang X., Tong A.H.Y., Andreazza S., Lee J.J., Nedyalkova L., Usaj M., RA Whitworth A.J., Andrews B.J., Moffat J., Myers C.L., Gevaert K., Boone C., RA Martinho R.G., Arnesen T.; RT "N-terminal acetylation shields proteins from degradation and promotes age- RT dependent motility and longevity."; RL Nat. Commun. 14:6774-6774(2023). CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C CC (NatC) complex (PubMed:19398576, PubMed:37891180). Catalyzes CC acetylation of the N-terminal methionine residues of peptides beginning CC with Met-Leu-Ala and Met-Leu-Gly (PubMed:19398576, PubMed:37891180). N- CC terminal acetylation protects proteins from ubiquitination and CC degradation by the N-end rule pathway (PubMed:37891180). Necessary for CC the lysosomal localization and function of ARL8B sugeesting that ARL8B CC is a NatC substrate (PubMed:19398576). {ECO:0000269|PubMed:19398576, CC ECO:0000269|PubMed:37891180}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-leucyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA + H(+); CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256; CC Evidence={ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-isoleucyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA + CC H(+); Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA- CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256; CC Evidence={ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-phenylalanyl-[protein] + acetyl-CoA = CC N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA CC + H(+); Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA- CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256; CC Evidence={ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-tryptophyl-[protein] + acetyl-CoA = CC N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA + CC H(+); Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA- CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256; CC Evidence={ECO:0000269|PubMed:19398576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-methionyl-L-tyrosyl-[protein] + acetyl-CoA = N- CC terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA + CC H(+); Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA- CC COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256; CC Evidence={ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}; CC -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC) CC complex, which is composed of NAA35, NAA38 and NAA30. CC {ECO:0000269|PubMed:19398576}. CC -!- INTERACTION: CC Q147X3; Q5VZE5: NAA35; NbExp=6; IntAct=EBI-9106461, EBI-9106478; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19398576, CC ECO:0000269|PubMed:25732826}. Nucleus {ECO:0000269|PubMed:25732826}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q147X3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q147X3-2; Sequence=VSP_031581; CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH471061; EAW80705.1; -; Genomic_DNA. DR EMBL; BC118589; AAI18590.1; -; mRNA. DR EMBL; BC122557; AAI22558.1; -; mRNA. DR CCDS; CCDS32088.1; -. [Q147X3-1] DR RefSeq; NP_001011713.2; NM_001011713.3. [Q147X3-1] DR PDB; 7MX2; EM; 3.64 A; A=211-362. DR PDB; 7RB3; EM; 3.10 A; A=211-362. DR PDBsum; 7MX2; -. DR PDBsum; 7RB3; -. DR AlphaFoldDB; Q147X3; -. DR EMDB; EMD-24070; -. DR EMDB; EMD-24393; -. DR SMR; Q147X3; -. DR BioGRID; 125797; 39. DR ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex. DR CORUM; Q147X3; -. DR FunCoup; Q147X3; 3582. DR IntAct; Q147X3; 31. DR STRING; 9606.ENSP00000452521; -. DR iPTMnet; Q147X3; -. DR PhosphoSitePlus; Q147X3; -. DR BioMuta; NAA30; -. DR DMDM; 121948171; -. DR jPOST; Q147X3; -. DR MassIVE; Q147X3; -. DR PaxDb; 9606-ENSP00000452521; -. DR PeptideAtlas; Q147X3; -. DR ProteomicsDB; 60184; -. [Q147X3-1] DR ProteomicsDB; 60185; -. [Q147X3-2] DR Pumba; Q147X3; -. DR Antibodypedia; 24132; 64 antibodies from 16 providers. DR DNASU; 122830; -. DR Ensembl; ENST00000556492.6; ENSP00000452521.1; ENSG00000139977.15. [Q147X3-1] DR GeneID; 122830; -. DR KEGG; hsa:122830; -. DR MANE-Select; ENST00000556492.6; ENSP00000452521.1; NM_001011713.3; NP_001011713.2. DR UCSC; uc001xcx.5; human. [Q147X3-1] DR AGR; HGNC:19844; -. DR ClinPGx; PA165479187; -. DR CTD; 122830; -. DR DisGeNET; 122830; -. DR GeneCards; NAA30; -. DR HGNC; HGNC:19844; NAA30. DR HPA; ENSG00000139977; Low tissue specificity. DR MIM; 617989; gene. DR OpenTargets; ENSG00000139977; -. DR VEuPathDB; HostDB:ENSG00000139977; -. DR eggNOG; KOG3139; Eukaryota. DR GeneTree; ENSGT00390000005665; -. DR HOGENOM; CLU_013985_0_0_1; -. DR InParanoid; Q147X3; -. DR OMA; VEPRCPF; -. DR OrthoDB; 249099at2759; -. DR PAN-GO; Q147X3; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q147X3; -. DR BioCyc; MetaCyc:ENSG00000139977-MONOMER; -. DR BRENDA; 2.3.1.256; 2681. DR PathwayCommons; Q147X3; -. DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network. DR SignaLink; Q147X3; -. DR SIGNOR; Q147X3; -. DR Agora; ENSG00000139977; -. DR BioGRID-ORCS; 122830; 246 hits in 1173 CRISPR screens. DR ChiTaRS; NAA30; human. DR GenomeRNAi; 122830; -. DR Pharos; Q147X3; Tbio. DR PRO; PR:Q147X3; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q147X3; protein. DR Bgee; ENSG00000139977; Expressed in secondary oocyte and 189 other cell types or tissues. DR ExpressionAtlas; Q147X3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031417; C:NatC complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0120518; F:protein N-terminal-methionine acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004596; F:protein-N-terminal amino-acid acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR CDD; cd04301; NAT_SF; 1. DR FunFam; 3.40.630.30:FF:000010; Putative N-alpha-acetyltransferase 30; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR044542; NAA30-like. DR PANTHER; PTHR45896; N-ALPHA-ACETYLTRANSFERASE 30; 1. DR PANTHER; PTHR45896:SF1; N-ALPHA-ACETYLTRANSFERASE 30; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing; KW Cytoplasm; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Transferase. FT CHAIN 1..362 FT /note="N-alpha-acetyltransferase 30" FT /id="PRO_0000320032" FT DOMAIN 214..362 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 38..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 113..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..48 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..165 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 173..182 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 117 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 233 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 43..79 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031581" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7RB3" FT HELIX 224..232 FT /evidence="ECO:0007829|PDB:7RB3" FT HELIX 241..250 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 256..260 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 263..273 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 281..289 FT /evidence="ECO:0007829|PDB:7RB3" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:7RB3" FT HELIX 298..312 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 316..323 FT /evidence="ECO:0007829|PDB:7RB3" FT HELIX 327..335 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 339..346 FT /evidence="ECO:0007829|PDB:7RB3" FT STRAND 354..360 FT /evidence="ECO:0007829|PDB:7RB3" SQ SEQUENCE 362 AA; 39320 MW; 6C9D69C980C090C0 CRC64; MAEVPPGPSS LLPPPAPPAP AAVEPRCPFP AGAALACCSE DEEDDEEHEG GGSRSPAGGE SATVAAKGHP CLRCPQPPQE QQQLNGLISP ELRHLRAAAS LKSKVLSVAE VAATTATPDG GPRATATKGA GVHSGERPPH SLSSNARTAV PSPVEAAAAS DPAAARNGLA EGTEQEEEEE DEQVRLLSSS LTADCSLRSP SGREVEPGED RTIRYVRYES ELQMPDIMRL ITKDLSEPYS IYTYRYFIHN WPQLCFLAMV GEECVGAIVC KLDMHKKMFR RGYIAMLAVD SKYRRNGIGT NLVKKAIYAM VEGDCDEVVL ETEITNKSAL KLYENLGFVR DKRLFRYYLN GVDALRLKLW LR //