ID   LSMD1_HUMAN             Reviewed;         125 AA.
AC   Q9BRA0; Q8N4M0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 153.
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).
CC   -!- FUNCTION: Auxillary component of the N-terminal acetyltransferase C
CC       (NatC) complex which catalyzes acetylation of N-terminal methionine
CC       residues. {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       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; 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_001320925.2. [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; 38.
DR   ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex.
DR   IntAct; Q9BRA0; 11.
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   EPD; Q9BRA0; -.
DR   jPOST; Q9BRA0; -.
DR   MassIVE; Q9BRA0; -.
DR   MaxQB; 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; 74 antibodies from 14 providers.
DR   DNASU; 84316; -.
DR   Ensembl; ENST00000333775.9; ENSP00000332103.5; ENSG00000183011.14. [Q9BRA0-2]
DR   Ensembl; ENST00000575771.6; ENSP00000460172.2; ENSG00000183011.14. [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   CTD; 84316; -.
DR   DisGeNET; 84316; -.
DR   GeneCards; NAA38; -.
DR   HGNC; HGNC:28212; NAA38.
DR   HPA; ENSG00000183011; Low tissue specificity.
DR   MIM; 617990; gene.
DR   neXtProt; NX_Q9BRA0; -.
DR   OpenTargets; ENSG00000183011; -.
DR   PharmGKB; PA142671503; -.
DR   VEuPathDB; HostDB:ENSG00000183011; -.
DR   eggNOG; KOG3168; Eukaryota.
DR   GeneTree; ENSGT00390000018418; -.
DR   InParanoid; Q9BRA0; -.
DR   OrthoDB; 298826at2759; -.
DR   PhylomeDB; Q9BRA0; -.
DR   TreeFam; TF323867; -.
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   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   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   PANTHER; PTHR10701:SF27; 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.
DR   Genevisible; Q9BRA0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Nucleus; Phosphoprotein; 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        26..41
FT                   /note="Basic and acidic residues"
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
//