LSMD1_HUMAN
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 03-AUG-2022, entry version 144.
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 AlphaFoldDB; Q9BRA0; -.
DR SMR; Q9BRA0; -.
DR BioGRID; 124042; 37.
DR ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex.
DR IntAct; Q9BRA0; 11.
DR MINT; Q9BRA0; -.
DR STRING; 9606.ENSP00000332103; -.
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; Q9BRA0; -.
DR PeptideAtlas; Q9BRA0; -.
DR PRIDE; Q9BRA0; -.
DR ProteomicsDB; 78750; -. [Q9BRA0-1]
DR ProteomicsDB; 78751; -. [Q9BRA0-2]
DR TopDownProteomics; Q9BRA0-1; -. [Q9BRA0-1]
DR Antibodypedia; 58902; 63 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 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; 1549327at2759; -.
DR PhylomeDB; Q9BRA0; -.
DR TreeFam; TF323867; -.
DR BioCyc; MetaCyc:G66-33018-MON; -.
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; 405 hits in 1079 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 185 other tissues.
DR ExpressionAtlas; Q9BRA0; baseline and differential.
DR Genevisible; Q9BRA0; HS.
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:0017196; P:N-terminal peptidyl-methionine acetylation; IC:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR CDD; cd06168; LSMD1; 1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034110; LSMD1.
DR PANTHER; PTHR10701:SF17; PTHR10701:SF17; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW 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 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
