NAA11_HUMAN
ID NAA11_HUMAN Reviewed; 229 AA.
AC Q9BSU3; Q66K19; Q6P479;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=N-alpha-acetyltransferase 11;
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P41227};
DE AltName: Full=N-terminal acetyltransferase complex ARD1 subunit homolog B;
DE Short=hARD2;
DE AltName: Full=NatA catalytic subunit Naa11;
GN Name=NAA11; Synonyms=ARD1B, ARD2;
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 MRNA].
RC TISSUE=Skin;
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 [2]
RP FUNCTION, INTERACTION WITH NAA15 AND HIF1A, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16638120; DOI=10.1186/1471-2091-7-13;
RA Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J.,
RA Kong X., Varhaug J.E., Lillehaug J.R.;
RT "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a
RT human protein N-alpha-acetyltransferase.";
RL BMC Biochem. 7:13-13(2006).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Displays alpha (N-terminal) acetyltransferase activity.
CC Proposed alternative catalytic subunit of the N-terminal
CC acetyltransferase A (NatA) complex. {ECO:0000269|PubMed:16638120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex
CC composed of NAA11 and NAA15 (Probable). Interacts with HIF1A.
CC {ECO:0000269|PubMed:16638120, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BSU3; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-2585120, EBI-11954993;
CC Q9BSU3; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-2585120, EBI-297683;
CC Q9BSU3; Q8WXS3-2: BAALC; NbExp=3; IntAct=EBI-2585120, EBI-13079214;
CC Q9BSU3; P30304: CDC25A; NbExp=3; IntAct=EBI-2585120, EBI-747671;
CC Q9BSU3; Q96FF9: CDCA5; NbExp=3; IntAct=EBI-2585120, EBI-718805;
CC Q9BSU3; Q8IUR6: CREBRF; NbExp=3; IntAct=EBI-2585120, EBI-1042699;
CC Q9BSU3; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-2585120, EBI-744366;
CC Q9BSU3; Q92845: KIFAP3; NbExp=3; IntAct=EBI-2585120, EBI-954040;
CC Q9BSU3; Q5VT66: MTARC1; NbExp=3; IntAct=EBI-2585120, EBI-11903927;
CC Q9BSU3; O60784-2: TOM1; NbExp=3; IntAct=EBI-2585120, EBI-12117154;
CC Q9BSU3; O43829: ZBTB14; NbExp=3; IntAct=EBI-2585120, EBI-10176632;
CC Q9BSU3; O95125: ZNF202; NbExp=3; IntAct=EBI-2585120, EBI-751960;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16638120}. Nucleus
CC {ECO:0000269|PubMed:16638120}.
CC -!- TISSUE SPECIFICITY: Present in several cell lines, with highest levels
CC in MCF-7 cells (at protein level). {ECO:0000269|PubMed:16638120}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04552.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH63623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH80651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC004552; AAH04552.2; ALT_INIT; mRNA.
DR EMBL; BC063623; AAH63623.1; ALT_INIT; mRNA.
DR EMBL; BC080651; AAH80651.1; ALT_INIT; mRNA.
DR CCDS; CCDS47084.1; -.
DR RefSeq; NP_116082.1; NM_032693.2.
DR RefSeq; XP_016864266.1; XM_017008777.1.
DR RefSeq; XP_016864267.1; XM_017008778.1.
DR RefSeq; XP_016864268.1; XM_017008779.1.
DR AlphaFoldDB; Q9BSU3; -.
DR SMR; Q9BSU3; -.
DR BioGRID; 124254; 166.
DR ComplexPortal; CPX-6273; NatA N-alpha-acetyltransferase complex, NAA11-NAA15 variant.
DR ComplexPortal; CPX-6274; NatA N-alpha-acetyltransferase complex, NAA11-NAA16 variant.
DR IntAct; Q9BSU3; 15.
DR STRING; 9606.ENSP00000286794; -.
DR iPTMnet; Q9BSU3; -.
DR PhosphoSitePlus; Q9BSU3; -.
DR BioMuta; NAA11; -.
DR DMDM; 158706520; -.
DR EPD; Q9BSU3; -.
DR jPOST; Q9BSU3; -.
DR MassIVE; Q9BSU3; -.
DR MaxQB; Q9BSU3; -.
DR PaxDb; Q9BSU3; -.
DR PeptideAtlas; Q9BSU3; -.
DR PRIDE; Q9BSU3; -.
DR ProteomicsDB; 78928; -.
DR Antibodypedia; 44611; 44 antibodies from 16 providers.
DR DNASU; 84779; -.
DR Ensembl; ENST00000286794.5; ENSP00000286794.4; ENSG00000156269.5.
DR GeneID; 84779; -.
DR KEGG; hsa:84779; -.
DR MANE-Select; ENST00000286794.5; ENSP00000286794.4; NM_032693.3; NP_116082.1.
DR UCSC; uc003hlt.5; human.
DR CTD; 84779; -.
DR DisGeNET; 84779; -.
DR GeneCards; NAA11; -.
DR HGNC; HGNC:28125; NAA11.
DR HPA; ENSG00000156269; Group enriched (brain, placenta, testis).
DR MIM; 619432; gene.
DR neXtProt; NX_Q9BSU3; -.
DR OpenTargets; ENSG00000156269; -.
DR PharmGKB; PA165664264; -.
DR VEuPathDB; HostDB:ENSG00000156269; -.
DR eggNOG; KOG3235; Eukaryota.
DR GeneTree; ENSGT00940000163834; -.
DR HOGENOM; CLU_013985_7_0_1; -.
DR InParanoid; Q9BSU3; -.
DR OMA; ETFGAHY; -.
DR OrthoDB; 1489230at2759; -.
DR PhylomeDB; Q9BSU3; -.
DR TreeFam; TF300078; -.
DR PathwayCommons; Q9BSU3; -.
DR SignaLink; Q9BSU3; -.
DR BioGRID-ORCS; 84779; 10 hits in 1079 CRISPR screens.
DR GenomeRNAi; 84779; -.
DR Pharos; Q9BSU3; Tbio.
DR PRO; PR:Q9BSU3; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BSU3; protein.
DR Bgee; ENSG00000156269; Expressed in secondary oocyte and 81 other tissues.
DR ExpressionAtlas; Q9BSU3; baseline and differential.
DR Genevisible; Q9BSU3; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031415; C:NatA complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..229
FT /note="N-alpha-acetyltransferase 11"
FT /id="PRO_0000305009"
FT DOMAIN 1..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..58
FT /note="Interaction with NAA15"
FT /evidence="ECO:0000250"
FT REGION 175..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 6
FT /note="A -> T (in dbSNP:rs3811765)"
FT /id="VAR_048164"
FT VARIANT 19
FT /note="L -> F (in dbSNP:rs17003712)"
FT /id="VAR_048165"
SQ SEQUENCE 229 AA; 25979 MW; F547D816A1E07ACE CRC64;
MNIRNAQPDD LMNMQHCNLL CLPENYQMKY YLYHGLSWPQ LSYIAEDEDG KIVGYVLAKM
EEEPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRPALH
LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LSQMADELRR QMDLKKGGYV VLGSRENQET
QGSTLSDSEE ACQQKNPATE ESGSDSKEPK ESVESTNVQD SSESSDSTS
