LOCUS       NM_016100               1040 bp    mRNA    linear   PRI 02-APR-2024
DEFINITION  Homo sapiens N-alpha-acetyltransferase 20, NatB catalytic subunit
            (NAA20), transcript variant 1, mRNA.
ACCESSION   NM_016100
VERSION     NM_016100.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1040)
  AUTHORS   Santhosh Kumar,S., Naseri,N.N., Pather,S.R., Hallacli,E.,
            Ndayisaba,A., Buenaventura,C., Acosta,K., Roof,J., Fazelinia,H.,
            Spruce,L.A., Luk,K., Khurana,V., Rhoades,E. and Shalem,O.
  TITLE     Sequential CRISPR screening reveals partial NatB inhibition as a
            strategy to mitigate alpha-synuclein levels in human neurons
  JOURNAL   Sci Adv 10 (6), eadj4767 (2024)
   PUBMED   38335281
  REMARK    GeneRIF: Sequential CRISPR screening reveals partial NatB
            inhibition as a strategy to mitigate alpha-synuclein levels in
            human neurons.
REFERENCE   2  (bases 1 to 1040)
  AUTHORS   Qiao,L., Dong,C., Jia,W. and Ma,B.
  TITLE     NAA20 recruits Rin2 and promotes triple-negative breast cancer
            progression by regulating Rab5A-mediated activation of EGFR
            signaling
  JOURNAL   Cell Signal 112, 110922 (2023)
   PUBMED   37827343
  REMARK    GeneRIF: NAA20 recruits Rin2 and promotes triple-negative breast
            cancer progression by regulating Rab5A-mediated activation of EGFR
            signaling.
REFERENCE   3  (bases 1 to 1040)
  AUTHORS   Morrison,J., Altuwaijri,N.K., Bronstad,K., Aksnes,H., Alsaif,H.S.,
            Evans,A., Hashem,M., Wheeler,P.G., Webb,B.D., Alkuraya,F.S. and
            Arnesen,T.
  TITLE     Missense NAA20 variants impairing the NatB protein N-terminal
            acetyltransferase cause autosomal recessive developmental delay,
            intellectual disability, and microcephaly
  JOURNAL   Genet Med 23 (11), 2213-2218 (2021)
   PUBMED   34230638
  REMARK    GeneRIF: Missense NAA20 variants impairing the NatB protein
            N-terminal acetyltransferase cause autosomal recessive
            developmental delay, intellectual disability, and microcephaly.
REFERENCE   4  (bases 1 to 1040)
  AUTHORS   Lasa,M., Neri,L., Carte,B., Gazquez,C., Aragon,T. and Aldabe,R.
  TITLE     Maturation of NAA20 Aminoterminal End Is Essential to Assemble NatB
            N-Terminal Acetyltransferase Complex
  JOURNAL   J Mol Biol 432 (22), 5889-5901 (2020)
   PUBMED   32976911
  REMARK    GeneRIF: Maturation of NAA20 Aminoterminal End Is Essential to
            Assemble NatB N-Terminal Acetyltransferase Complex.
REFERENCE   5  (bases 1 to 1040)
  AUTHORS   Jung,T.Y., Ryu,J.E., Jang,M.M., Lee,S.Y., Jin,G.R., Kim,C.W.,
            Lee,C.Y., Kim,H., Kim,E., Park,S., Lee,S., Lee,C., Kim,W., Kim,T.,
            Lee,S.Y., Ju,B.G. and Kim,H.S.
  TITLE     Naa20, the catalytic subunit of NatB complex, contributes to
            hepatocellular carcinoma by regulating the LKB1-AMPK-mTOR axis
  JOURNAL   Exp Mol Med 52 (11), 1831-1844 (2020)
   PUBMED   33219302
  REMARK    GeneRIF: Naa20, the catalytic subunit of NatB complex, contributes
            to hepatocellular carcinoma by regulating the LKB1-AMPK-mTOR axis.
REFERENCE   6  (bases 1 to 1040)
  AUTHORS   Aksnes,H., Van Damme,P., Goris,M., Starheim,K.K., Marie,M.,
            Stove,S.I., Hoel,C., Kalvik,T.V., Hole,K., Glomnes,N., Furnes,C.,
            Ljostveit,S., Ziegler,M., Niere,M., Gevaert,K. and Arnesen,T.
  TITLE     An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic
            N termini of transmembrane proteins and maintains Golgi integrity
  JOURNAL   Cell Rep 10 (8), 1362-1374 (2015)
   PUBMED   25732826
REFERENCE   7  (bases 1 to 1040)
  AUTHORS   Van Damme,P., Lasa,M., Polevoda,B., Gazquez,C., Elosegui-Artola,A.,
            Kim,D.S., De Juan-Pardo,E., Demeyer,K., Hole,K., Larrea,E.,
            Timmerman,E., Prieto,J., Arnesen,T., Sherman,F., Gevaert,K. and
            Aldabe,R.
  TITLE     N-terminal acetylome analyses and functional insights of the
            N-terminal acetyltransferase NatB
  JOURNAL   Proc Natl Acad Sci U S A 109 (31), 12449-12454 (2012)
   PUBMED   22814378
  REMARK    GeneRIF: The human NatB complex composed of Naa20 (NAT3) and Naa25
            (MDM20) N-terminally acetylates Met-Glu-, Met-Asp-, Met-Asn- and
            Met-Gln- N-termini, and is important for the structure and function
            of actomyosin fibers and for proper cellular migration.
REFERENCE   8  (bases 1 to 1040)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   9  (bases 1 to 1040)
  AUTHORS   Starheim,K.K., Arnesen,T., Gromyko,D., Ryningen,A., Varhaug,J.E.
            and Lillehaug,J.R.
  TITLE     Identification of the human N(alpha)-acetyltransferase complex B
            (hNatB): a complex important for cell-cycle progression
  JOURNAL   Biochem J 415 (2), 325-331 (2008)
   PUBMED   18570629
  REMARK    GeneRIF: Human N-acetyltransferase complexe NatB consists of human
            N-acetyltransferase 3 and human MDM20. hNAT3 knockdown results in
            an increase in G(0)/G(1)-phase cells.
            GeneRIF: hNat3 (NAT5) is the catalytic subunit and hMdm20 the
            auxiliary subunit of the human NatB N-terminal acetyltransferase
            complex. This ribosome associated complex acetylates nascent
            Met-Asp/Glu- polypeptides.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC008446.1, BU680824.1 and AL035454.18.
            
            On May 17, 2019 this sequence version replaced NM_016100.4.
            
            Summary: NAT5 is a component of N-acetyltransferase complex B
            (NatB). Human NatB performs cotranslational N(alpha)-terminal
            acetylation of methionine residues when they are followed by
            asparagine (Starheim et al., 2008 [PubMed 18570629]).[supplied by
            OMIM, Apr 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005181.1, SRR1163658.122270.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334982.9/ ENSP00000335636.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1007              BC008446.1         22-1028
            1008-1014           BU680824.1         17-23               c
            1015-1040           AL035454.18        14955-14980
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     gene            1..1040
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /note="N-alpha-acetyltransferase 20, NatB catalytic
                     subunit"
                     /db_xref="GeneID:51126"
                     /db_xref="HGNC:HGNC:15908"
                     /db_xref="MIM:610833"
     exon            1..88
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     CDS             36..572
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /EC_number="2.3.1.254"
                     /note="isoform a is encoded by transcript variant 1;
                     N-acetyltransferase 5, ARD1 subunit (arrest-defective 1,
                     S. cerevisiae, homolog); N-acetyltransferase 5
                     (GCN5-related, putative); N-acetyltransferase 5 (ARD1
                     homolog, S. cerevisiae); N-terminal acetyltransferase
                     complex ARD1 subunit; N-terminal acetyltransferase B
                     complex catalytic subunit NAT5; natB complex subunit NAT5;
                     N-terminal acetyltransferase B complex catalytic subunit
                     NAA20; N-acetyltransferase 3 homolog; natB catalytic
                     subunit; methionine N-acetyltransferase"
                     /codon_start=1
                     /product="N-alpha-acetyltransferase 20 isoform a"
                     /protein_id="NP_057184.1"
                     /db_xref="CCDS:CCDS13141.1"
                     /db_xref="GeneID:51126"
                     /db_xref="HGNC:HGNC:15908"
                     /db_xref="MIM:610833"
                     /translation="MTTLRAFTCDDLFRFNNINLDPLTETYGIPFYLQYLAHWPEYFI
                     VAEAPGGELMGYIMGKAEGSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISER
                     KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRKALSRDT
                     EKKSIIPLPHPVRPEDIE"
     exon            89..113
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     exon            114..204
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     exon            205..340
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     exon            341..486
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     exon            487..1040
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /inference="alignment:Splign:2.1.0"
     regulatory      975..980
                     /regulatory_class="polyA_signal_sequence"
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /note="hexamer: TATAAA"
     regulatory      993..998
                     /regulatory_class="polyA_signal_sequence"
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /note="hexamer: AATACA"
     polyA_site      1010
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
                     /note="major polyA site"
     polyA_site      1014
                     /gene="NAA20"
                     /gene_synonym="dJ1002M8.1; MRT73; NAT3; NAT3P; NAT5;
                     NAT5P"
ORIGIN      
        1 cttggcgaac ggtcttcgga agcggcggcg gcgcgatgac cacgctacgg gcctttacct
       61 gcgacgacct gttccgcttc aacaacatta acttggatcc acttacagaa acttatggga
      121 ttcctttcta cctacaatac ctcgcccact ggccagagta tttcattgtt gcagaggcac
      181 ctggtggaga attaatgggt tatattatgg gtaaagcaga aggctcagta gctagggaag
      241 aatggcacgg gcacgtcaca gctctgtctg ttgccccaga atttcgacgc cttggtttgg
      301 ctgctaaact tatggagtta ctagaggaga tttcagaaag aaagggtgga ttttttgtgg
      361 atctctttgt aagagtatct aaccaagttg cagttaacat gtacaagcag ttgggctaca
      421 gtgtatatag gacggtcata gagtactatt cggccagcaa cggggagcct gatgaggacg
      481 cttatgatat gaggaaagca ctttccaggg atactgagaa gaaatccatc ataccattac
      541 ctcatcctgt gaggcctgaa gacattgaat aaccctgggc agtggttctt aggcagatac
      601 tctagatgct ttatggacaa tattattttc attggatgat tctggagctc tattaggaga
      661 aaagtaatca ttttaggtct taaagacttc aagaaaatac aggttatcaa tttattttaa
      721 atctcattgt ttccagttag caatatcata cctattaaag ctgttcattg taacaaaatt
      781 caatcaaaaa ggcagctagg tcagaaggaa acataccact ctcatggttc atagtattca
      841 ctgtatgtat gctagggaaa agacttgctc cagtctcctc ctcagttctg tgcctgagaa
      901 ccactgctgc atatatttgt ttttaaattt tgtattgaac tgttaattga agctttaaaa
      961 gcatatatga aatgtataaa tctaagatgt ataatacatt attgactcta tgaatgtttt
     1021 ctgaagtttg ttagtcattt
//
