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NAA50_PONAB
ID   NAA50_PONAB             Reviewed;         169 AA.
AC   Q5RF28;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=N-alpha-acetyltransferase 50;
DE            EC=2.3.1.258 {ECO:0000250|UniProtKB:Q9GZZ1};
DE   AltName: Full=N-acetyltransferase NAT13;
DE   AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000250|UniProtKB:Q9GZZ1};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q9GZZ1};
DE   AltName: Full=NatE catalytic subunit;
GN   Name=NAA50; Synonyms=NAT13;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC       proteins that retain their initiating methionine (By similarity). Has a
CC       broad substrate specificity: able to acetylate the initiator methionine
CC       of most peptides, except for those with a proline in second position
CC       (By similarity). Also displays N-epsilon-acetyltransferase activity by
CC       mediating acetylation of the side chain of specific lysines on proteins
CC       (By similarity). Autoacetylates in vivo (By similarity). The relevance
CC       of N-epsilon-acetyltransferase activity is however unclear: able to
CC       acetylate H4 in vitro, but this result has not been confirmed in vivo
CC       (By similarity). Component of N-alpha-acetyltransferase complexes
CC       containing NAA10 and NAA15, which has N-alpha-acetyltransferase
CC       activity (By similarity). Does not influence the acetyltransferase
CC       activity of NAA10 (By similarity). However, it negatively regulates the
CC       N-alpha-acetyltransferase activity of the N-terminal acetyltransferase
CC       A complex (also called the NatA complex) (By similarity). The
CC       multiprotein complexes probably constitute the major contributor for N-
CC       terminal acetylation at the ribosome exit tunnel, with NAA10
CC       acetylating all amino termini that are devoid of methionine and NAA50
CC       acetylating other peptides (By similarity). Required for sister
CC       chromatid cohesion during mitosis by promoting binding of CDCA5/sororin
CC       to cohesin: may act by counteracting the function of NAA10 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9GZZ1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC         Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC         Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC         Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC         Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC         Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC         CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC         [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC         COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC         Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase E (NatE) complex
CC       at least composed of NAA10, NAA15 and NAA50 (By similarity). Interacts
CC       with NAA10 (By similarity). Interacts with NAA15 (By similarity).
CC       Predominantly interacts with NAA15 in the N-terminal acetyltransferase
CC       A complex (NatA complex); the interactions reduce the acetylation
CC       activity of the NatA complex (By similarity). Component of the N-
CC       terminal acetyltransferase E (NatE)/HYPK complex at least composed of
CC       NAA10, NAA15, NAA50 and HYPK (By similarity). Within the complex
CC       interacts with NAA15 (By similarity). Its capacity to interact with the
CC       NatA complex is reduced by HYPK (By similarity). Interacts with NAA35
CC       (By similarity). {ECO:0000250|UniProtKB:Q6PGB6,
CC       ECO:0000250|UniProtKB:Q9GZZ1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in
CC       interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR857333; CAH89629.1; -; mRNA.
DR   RefSeq; NP_001124730.1; NM_001131258.1.
DR   AlphaFoldDB; Q5RF28; -.
DR   BMRB; Q5RF28; -.
DR   SMR; Q5RF28; -.
DR   STRING; 9601.ENSPPYP00000015136; -.
DR   Ensembl; ENSPPYT00000015741; ENSPPYP00000015136; ENSPPYG00000013536.
DR   GeneID; 100171579; -.
DR   KEGG; pon:100171579; -.
DR   CTD; 80218; -.
DR   eggNOG; KOG3138; Eukaryota.
DR   GeneTree; ENSGT00390000009110; -.
DR   HOGENOM; CLU_013985_5_3_1; -.
DR   InParanoid; Q5RF28; -.
DR   OMA; IVETKEH; -.
DR   OrthoDB; 1536763at2759; -.
DR   TreeFam; TF314841; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISS:UniProtKB.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..169
FT                   /note="N-alpha-acetyltransferase 50"
FT                   /id="PRO_0000284904"
FT   DOMAIN          6..155
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          138..141
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         77..90
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         117..126
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   MOD_RES         37
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   MOD_RES         110
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   MOD_RES         140
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
SQ   SEQUENCE   169 AA;  19398 MW;  153A8021B74655CC CRC64;
     MKGSRIELGD VTPHNIKQLK RLNQVIFPVS YNDKFYKDVL EVGELAKLAY FNDIAVGAVC
     CRVDHSQNQK RLYIMTLGCL APYRRLGIGT KMLNHVLNIC EKDGTFDNIY LHVQISNESA
     IDFYRKFGFE IIETKKNYYK RIEPADAHVL QKNLKVPSGQ NADVQKTDN
 
 
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