NAA30_HUMAN
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 03-AUG-2022, entry version 128.
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).
CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C
CC (NatC) complex. Catalyzes acetylation of the N-terminal methionine
CC residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly.
CC Necessary for the lysosomal localization and function of ARL8B
CC sugeesting that ARL8B is a NatC substrate.
CC {ECO:0000269|PubMed:19398576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; 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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; 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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; 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=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC 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};
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=2; 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}.
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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_001011713.2. [Q147X3-1]
DR AlphaFoldDB; Q147X3; -.
DR SMR; Q147X3; -.
DR BioGRID; 125797; 32.
DR ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex.
DR IntAct; Q147X3; 4.
DR STRING; 9606.ENSP00000452521; -.
DR iPTMnet; Q147X3; -.
DR PhosphoSitePlus; Q147X3; -.
DR BioMuta; NAA30; -.
DR DMDM; 121948171; -.
DR EPD; Q147X3; -.
DR jPOST; Q147X3; -.
DR MassIVE; Q147X3; -.
DR MaxQB; Q147X3; -.
DR PaxDb; Q147X3; -.
DR PeptideAtlas; Q147X3; -.
DR PRIDE; Q147X3; -.
DR ProteomicsDB; 60184; -. [Q147X3-1]
DR ProteomicsDB; 60185; -. [Q147X3-2]
DR Antibodypedia; 24132; 71 antibodies from 17 providers.
DR DNASU; 122830; -.
DR Ensembl; ENST00000556492.6; ENSP00000452521.1; ENSG00000139977.14. [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 CTD; 122830; -.
DR DisGeNET; 122830; -.
DR GeneCards; NAA30; -.
DR HGNC; HGNC:19844; NAA30.
DR HPA; ENSG00000139977; Low tissue specificity.
DR MIM; 617989; gene.
DR neXtProt; NX_Q147X3; -.
DR OpenTargets; ENSG00000139977; -.
DR PharmGKB; PA165479187; -.
DR VEuPathDB; HostDB:ENSG00000139977; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00390000005665; -.
DR HOGENOM; CLU_013985_0_0_1; -.
DR InParanoid; Q147X3; -.
DR OMA; TDCQPEE; -.
DR PhylomeDB; Q147X3; -.
DR TreeFam; TF105925; -.
DR BioCyc; MetaCyc:ENSG00000139977-MON; -.
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 BioGRID-ORCS; 122830; 220 hits in 1095 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 188 other tissues.
DR ExpressionAtlas; Q147X3; baseline and differential.
DR Genevisible; Q147X3; HS.
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:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IDA:WormBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; 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..25
FT /note="Pro 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"
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
