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Protein

N-alpha-acetyltransferase 50

Gene

NAA50

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of a N-alpha-acetyltransferase complex containing NAA10 and NAA15, but NAA50 does not influence the acetyltransferase activity of NAA10: this multiprotein complex probably constitutes the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821).7 Publications

Catalytic activityi

Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA.4 Publications
Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA.4 Publications

Kineticsi

kcat is 7.2 min(-1) with M-L-G-P-E peptide. kcat is 7.2 min(-1) with M-L-D-P-E peptide. kcat is 10.9 min(-1) with M-I-G-P-E peptide. kcat is 6.8 min(-1) with M-L-A-L-I peptide. kcat is 2.3 min(-1) with M-L-G-T-G peptide. kcat is 5.6 min(-1) with M-L-G-T-E peptide.1 Publication
  1. KM=132.6 µM for M-A-A-A peptide1 Publication
  2. KM=126.1 µM for L-A-A-A peptide1 Publication
  3. KM=5 µM for Acetyl-CoA1 Publication
  4. KM=79 µM for M-L-G-P-E peptide1 Publication
  5. KM=91 µM for M-L-D-P-E peptide1 Publication
  6. KM=185 µM for M-I-G-P-E peptide1 Publication
  7. KM=190 µM for M-L-A-L-I peptide1 Publication
  8. KM=320 µM for M-L-G-T-G peptide1 Publication
  9. KM=416 µM for M-L-G-T-E peptide1 Publication
  10. KM=460 µM for M-L-R-P-E peptide1 Publication
  11. KM=478 µM for M-L-L-P-E peptide1 Publication
  12. KM=3734 µM for M-F-G-P-E peptide1 Publication

    pH dependencei

    Optimum pH is 7.5-8.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei31SubstrateCombined sources2 Publications1
    Active sitei731 Publication1
    Binding sitei75SubstrateCombined sources2 Publications1
    Active sitei1121 Publication1

    GO - Molecular functioni

    • H4 histone acetyltransferase activity Source: UniProtKB
    • peptide alpha-N-acetyltransferase activity Source: UniProtKB
    • peptidyl-lysine acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    • establishment of mitotic sister chromatid cohesion Source: UniProtKB
    • mitotic sister chromatid cohesion, centromeric Source: UniProtKB
    • N-terminal protein amino acid acetylation Source: UniProtKB

    Keywordsi

    Molecular functionAcyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.88. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-alpha-acetyltransferase 50Curated (EC:2.3.1.2584 Publications)
    Short name:
    hNaa50p2 Publications
    Alternative name(s):
    N-acetyltransferase 13
    N-acetyltransferase 51 Publication
    Short name:
    hNAT51 Publication
    N-acetyltransferase san homolog1 Publication
    Short name:
    hSAN1 Publication
    N-epsilon-acetyltransferase 50Curated (EC:2.3.1.-1 Publication)
    NatE catalytic subunit
    Gene namesi
    Name:NAA50Imported
    Synonyms:MAK31 Publication, NAT13, NAT51 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000121579.12.
    HGNCiHGNC:29533. NAA50.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi27F → A: Abolishes N-alpha-acetyltransferase activity. 2 Publications1
    Mutagenesisi28P → A: Strongly decreased N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi29V → A: Strongly decreased N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi31Y → A: Abolishes N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi34 – 37KFYK → AFYA: Decreased acetylation; when associated with A-140. 1 Publication4
    Mutagenesisi35F → A: Abolishes N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi73Y → A or F: Abolishes N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi84R → A: Strongly decreased N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi112H → A or F: Abolishes N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi124Y → F: Strongly decreased N-alpha-acetyltransferase activity. Impaired sister chromatid cohesion during mitosis. 3 Publications1
    Mutagenesisi139Y → A: Abolishes N-alpha-acetyltransferase activity. 1 Publication1
    Mutagenesisi140K → A: Decreased acetylation; when associated with 34-A-A-37. 1 Publication1
    Mutagenesisi142I → A: Decreased N-alpha-acetyltransferase activity. 1 Publication1

    Organism-specific databases

    DisGeNETi80218.
    OpenTargetsiENSG00000121579.
    PharmGKBiPA165697846.

    Polymorphism and mutation databases

    BioMutaiNAA50.
    DMDMi74733509.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002849021 – 169N-alpha-acetyltransferase 50Add BLAST169

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei12PhosphothreonineCombined sources1
    Modified residuei34N6-acetyllysine; by autocatalysisCombined sources1 Publication1
    Modified residuei37N6-acetyllysine; by autocatalysisCombined sources1 Publication1
    Modified residuei110PhosphotyrosineCombined sources1
    Modified residuei140N6-acetyllysine; by autocatalysis1 Publication1
    Isoform 2 (identifier: Q9GZZ1-2)
    Modified residuei34N6-acetyllysineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ9GZZ1.
    MaxQBiQ9GZZ1.
    PaxDbiQ9GZZ1.
    PeptideAtlasiQ9GZZ1.
    PRIDEiQ9GZZ1.

    PTM databases

    iPTMnetiQ9GZZ1.
    PhosphoSitePlusiQ9GZZ1.

    Expressioni

    Gene expression databases

    BgeeiENSG00000121579.
    CleanExiHS_NAT13.
    HS_NAT5.
    ExpressionAtlasiQ9GZZ1. baseline and differential.
    GenevisibleiQ9GZZ1. HS.

    Interactioni

    Subunit structurei

    Component of a complex composed of NAA50, NAA15 and NAA10 (PubMed:16507339). Interacts with NAA35 (By similarity).By similarity1 Publication

    Binary interactionsi

    Show more details

    Protein-protein interaction databases

    BioGridi123185. 40 interactors.
    IntActiQ9GZZ1. 10 interactors.
    STRINGi9606.ENSP00000240922.

    Structurei

    Secondary structure

    1169
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Turni13 – 15Combined sources3
    Helixi16 – 26Combined sources11
    Helixi33 – 39Combined sources7
    Helixi43 – 45Combined sources3
    Beta strandi46 – 51Combined sources6
    Beta strandi54 – 66Combined sources13
    Beta strandi69 – 79Combined sources11
    Helixi81 – 83Combined sources3
    Beta strandi85 – 87Combined sources3
    Helixi88 – 103Combined sources16
    Beta strandi107 – 114Combined sources8
    Helixi118 – 126Combined sources9
    Beta strandi130 – 135Combined sources6
    Beta strandi140 – 144Combined sources5
    Beta strandi147 – 153Combined sources7
    Helixi162 – 164Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2OB0X-ray1.80A/B/C2-169[»]
    2PSWX-ray2.10A/B/C2-169[»]
    3TFYX-ray2.75A/B/C1-169[»]
    4X5KX-ray2.49A1-169[»]
    ProteinModelPortaliQ9GZZ1.
    SMRiQ9GZZ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZZ1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini6 – 155N-acetyltransferasePROSITE-ProRule annotationAdd BLAST150

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni77 – 90Acetyl-CoA bindingCombined sources3 PublicationsAdd BLAST14
    Regioni117 – 126Coenzyme A bindingCombined sources3 Publications10
    Regioni138 – 141SubstrateCombined sources2 Publications4

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG3138. Eukaryota.
    COG0456. LUCA.
    GeneTreeiENSGT00390000009110.
    HOGENOMiHOG000238056.
    HOVERGENiHBG060820.
    InParanoidiQ9GZZ1.
    KOiK20793.
    OMAiIVETKEH.
    OrthoDBiEOG091G0PAG.
    PhylomeDBiQ9GZZ1.
    TreeFamiTF314841.

    Family and domain databases

    InterProiView protein in InterPro
    IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    PfamiView protein in Pfam
    PF00583. Acetyltransf_1. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiView protein in PROSITE
    PS51186. GNAT. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9GZZ1-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY
    60 70 80 90 100
    FNDIAVGAVC CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC
    110 120 130 140 150
    EKDGTFDNIY LHVQISNESA IDFYRKFGFE IIETKKNYYK RIEPADAHVL
    160
    QKNLKVPSGQ NADVQKTDN
    Length:169
    Mass (Da):19,398
    Last modified:March 1, 2001 - v1
    Checksum:i153A8021B74655CC
    GO
    Isoform 2 (identifier: Q9GZZ1-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-122: Missing.

    Note: No experimental confirmation available.Combined sources
    Show »
    Length:81
    Mass (Da):9,465
    Checksum:i72B366F6387B4FC5
    GO

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_02474735 – 122Missing in isoform 2. 1 PublicationAdd BLAST88

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK023090 mRNA. Translation: BAB14397.1.
    AK023256 mRNA. Translation: BAB14490.1.
    CR749314 mRNA. Translation: CAH18169.1.
    CH471052 Genomic DNA. Translation: EAW79629.1.
    CH471052 Genomic DNA. Translation: EAW79630.1.
    BC012731 mRNA. Translation: AAH12731.1.
    CCDSiCCDS2975.1. [Q9GZZ1-1]
    RefSeqiNP_079422.1. NM_025146.3. [Q9GZZ1-1]
    UniGeneiHs.372378.

    Genome annotation databases

    EnsembliENST00000240922; ENSP00000240922; ENSG00000121579. [Q9GZZ1-1]
    GeneIDi80218.
    KEGGihsa:80218.
    UCSCiuc003ean.3. human. [Q9GZZ1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiNAA50_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZZ1
    Secondary accession number(s): D3DN74, Q68DQ1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: March 1, 2001
    Last modified: October 25, 2017
    This is version 146 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families