ID   NAA38_HUMAN             Reviewed;         125 AA.
AC   Q9BRA0; Q8N4M0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   28-JAN-2026, entry version 161.
DE   RecName: Full=N-alpha-acetyltransferase 38, NatC auxiliary subunit;
DE   AltName: Full=LSM domain-containing protein 1;
DE   AltName: Full=Phosphonoformate immuno-associated protein 2;
GN   Name=NAA38; Synonyms=LSMD1, MAK31, PFAAP2;
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 [MRNA] (ISOFORM 1).
RA   Liu Y., Cheng J., Lu Y.;
RT   "Screening and cloning of a new immuno-associated gene regulated by
RT   phosphonoformate.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Pancreas, Prostate, and Uterus;
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-22; SER-25 AND SER-29, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [4]
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   [5]
RP   FUNCTION, IDENTIFICATION IN NATC COMPLEX, AND 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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
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   [8]
RP   FUNCTION.
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: Auxillary component of the N-terminal acetyltransferase C
CC       (NatC) complex which catalyzes acetylation of N-terminal methionine
CC       residues (PubMed:19398576, PubMed:37891180). N-terminal acetylation
CC       protects proteins from ubiquitination and degradation by the N-end rule
CC       pathway (PubMed:37891180). {ECO:0000269|PubMed:19398576,
CC       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       Q9BRA0; Q86V38: ATN1; NbExp=3; IntAct=EBI-9106509, EBI-11954292;
CC       Q9BRA0; Q92876: KLK6; NbExp=3; IntAct=EBI-9106509, EBI-2432309;
CC       Q9BRA0; Q92802: N4BP2L2; NbExp=3; IntAct=EBI-9106509, EBI-2514973;
CC       Q9BRA0; Q5VZE5: NAA35; NbExp=3; IntAct=EBI-9106509, EBI-9106478;
CC       Q9BRA0; O76083: PDE9A; NbExp=3; IntAct=EBI-9106509, EBI-742764;
CC       Q9BRA0; P86479: PRR20C; NbExp=3; IntAct=EBI-9106509, EBI-10172814;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19398576}. Nucleus
CC       {ECO:0000269|PubMed:19398576}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BRA0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BRA0-2; Sequence=VSP_027566;
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; AF530060; AAQ09944.1; -; mRNA.
DR   EMBL; BC006407; AAH06407.1; -; mRNA.
DR   EMBL; BC033861; AAH33861.1; -; mRNA.
DR   EMBL; BC051846; AAH51846.1; -; mRNA.
DR   EMBL; BC059944; AAH59944.1; -; mRNA.
DR   CCDS; CCDS11122.1; -. [Q9BRA0-2]
DR   CCDS; CCDS82060.1; -. [Q9BRA0-1]
DR   RefSeq; NP_001307854.1; NM_001320925.4. [Q9BRA0-1]
DR   RefSeq; NP_115732.2; NM_032356.5. [Q9BRA0-2]
DR   PDB; 7MX2; EM; 3.64 A; C=1-125.
DR   PDBsum; 7MX2; -.
DR   AlphaFoldDB; Q9BRA0; -.
DR   EMDB; EMD-24070; -.
DR   SMR; Q9BRA0; -.
DR   BioGRID; 124042; 40.
DR   ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex.
DR   CORUM; Q9BRA0; -.
DR   FunCoup; Q9BRA0; 1765.
DR   IntAct; Q9BRA0; 27.
DR   MINT; Q9BRA0; -.
DR   STRING; 9606.ENSP00000332103; -.
DR   GlyGen; Q9BRA0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BRA0; -.
DR   PhosphoSitePlus; Q9BRA0; -.
DR   BioMuta; NAA38; -.
DR   DMDM; 74732854; -.
DR   jPOST; Q9BRA0; -.
DR   MassIVE; Q9BRA0; -.
DR   PaxDb; 9606-ENSP00000332103; -.
DR   PeptideAtlas; Q9BRA0; -.
DR   ProteomicsDB; 78750; -. [Q9BRA0-1]
DR   ProteomicsDB; 78751; -. [Q9BRA0-2]
DR   Pumba; Q9BRA0; -.
DR   TopDownProteomics; Q9BRA0-1; -. [Q9BRA0-1]
DR   Antibodypedia; 58902; 52 antibodies from 13 providers.
DR   DNASU; 84316; -.
DR   Ensembl; ENST00000333775.9; ENSP00000332103.5; ENSG00000183011.15. [Q9BRA0-2]
DR   Ensembl; ENST00000575771.6; ENSP00000460172.2; ENSG00000183011.15. [Q9BRA0-1]
DR   GeneID; 84316; -.
DR   KEGG; hsa:84316; -.
DR   MANE-Select; ENST00000575771.6; ENSP00000460172.2; NM_001320925.4; NP_001307854.1.
DR   UCSC; uc002giz.4; human. [Q9BRA0-1]
DR   AGR; HGNC:28212; -.
DR   ClinPGx; PA142671503; -.
DR   CTD; 84316; -.
DR   DisGeNET; 84316; -.
DR   GeneCards; NAA38; -.
DR   HGNC; HGNC:28212; NAA38.
DR   HPA; ENSG00000183011; Low tissue specificity.
DR   MIM; 617990; gene.
DR   OpenTargets; ENSG00000183011; -.
DR   VEuPathDB; HostDB:ENSG00000183011; -.
DR   eggNOG; KOG3168; Eukaryota.
DR   GeneTree; ENSGT00390000018418; -.
DR   InParanoid; Q9BRA0; -.
DR   OrthoDB; 368909at2759; -.
DR   PAN-GO; Q9BRA0; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9BRA0; -.
DR   BioCyc; MetaCyc:G66-33018-MONOMER; -.
DR   PathwayCommons; Q9BRA0; -.
DR   Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; Q9BRA0; -.
DR   SIGNOR; Q9BRA0; -.
DR   Agora; ENSG00000183011; -.
DR   BioGRID-ORCS; 84316; 427 hits in 1166 CRISPR screens.
DR   ChiTaRS; NAA38; human.
DR   GenomeRNAi; 84316; -.
DR   Pharos; Q9BRA0; Tdark.
DR   PRO; PR:Q9BRA0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9BRA0; protein.
DR   Bgee; ENSG00000183011; Expressed in prefrontal cortex and 187 other cell types or tissues.
DR   ExpressionAtlas; Q9BRA0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031417; C:NatC complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   CDD; cd06168; LSMD1; 1.
DR   FunFam; 2.30.30.100:FF:000028; N-alpha-acetyltransferase 38, NatC auxiliary subunit; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR034110; LSMD1_Sm.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   InterPro; IPR050914; snRNP_SmB/NAA38-like.
DR   PANTHER; PTHR10701:SF5; N-ALPHA-ACETYLTRANSFERASE 38, NATC AUXILIARY SUBUNIT; 1.
DR   PANTHER; PTHR10701; SMALL NUCLEAR RIBONUCLEOPROTEIN-ASSOCIATED PROTEIN B AND N; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Nucleus; Phosphoprotein; Proteomics identification; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..125
FT                   /note="N-alpha-acetyltransferase 38, NatC auxiliary
FT                   subunit"
FT                   /id="PRO_0000299155"
FT   DOMAIN          40..118
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..56
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..28
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..27
FT                   /note="MAGAGPTMLLREENGCCSRRQSSSSAG -> MAVAVGVRAAPVLGLARALVL
FT                   GLRGSQAARWRGWGTAAPGSLWALCECPAGCRELWFRGRAAWAARSERLLHPAQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027566"
FT   VARIANT         Q9BRA0-2:13
FT                   /note="L -> P (in dbSNP:rs8522)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082914"
SQ   SEQUENCE   125 AA;  13514 MW;  DF6048668C06EFB5 CRC64;
     MAGAGPTMLL REENGCCSRR QSSSSAGDSD GEREDSAAER ARQQLEALLN KTMRIRMTDG
     RTLVGCFLCT DRDCNVILGS AQEFLKPSDS FSAGEPRVLG LAMVPGHHIV SIEVQRESLT
     GPPYL
//