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N-alpha-acetyltransferase 50 (hNaa50p) (EC 2.3.1.258) (N-acetyltransferase 13) (N-acetyltransferase 5) (hNAT5) (N-acetyltransferase san homolog) (hSAN) (N-epsilon-acetyltransferase 50) (EC 2.3.1.-) (NatE catalytic subunit)

 NAA50_HUMAN             Reviewed;         169 AA.
Q9GZZ1; D3DN74; Q68DQ1;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=N-alpha-acetyltransferase 50 {ECO:0000305};
Short=hNaa50p {ECO:0000303|PubMed:19744929, ECO:0000303|PubMed:22311970};
EC=2.3.1.258 {ECO:0000269|PubMed:19744929, ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970, ECO:0000269|PubMed:27484799};
AltName: Full=N-acetyltransferase 13;
AltName: Full=N-acetyltransferase 5 {ECO:0000303|PubMed:16507339};
Short=hNAT5 {ECO:0000303|PubMed:16507339};
AltName: Full=N-acetyltransferase san homolog {ECO:0000303|PubMed:16507339};
Short=hSAN {ECO:0000303|PubMed:16507339};
AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000305};
EC=2.3.1.- {ECO:0000269|PubMed:19744929};
AltName: Full=NatE catalytic subunit;
Name=NAA50 {ECO:0000312|HGNC:HGNC:29533};
Synonyms=MAK3 {ECO:0000303|Ref.18}, NAT13,
NAT5 {ECO:0000303|PubMed:16507339};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
INTERACTION WITH NAA15 AND NAA11, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16507339; DOI=10.1016/j.gene.2005.12.008;
Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E.,
Lillehaug J.R.;
"Cloning and characterization of hNAT5/hSAN: an evolutionarily
conserved component of the NatA protein N-alpha-acetyltransferase
complex.";
Gene 371:291-295(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-124.
PubMed=17502424; DOI=10.1083/jcb.200701043;
Hou F., Chu C.W., Kong X., Yokomori K., Zou H.;
"The acetyltransferase activity of San stabilizes the mitotic cohesin
at the centromeres in a shugoshin-independent manner.";
J. Cell Biol. 177:587-597(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
NOMENCLATURE.
PubMed=19660095; DOI=10.1186/1753-6561-3-S6-S2;
Polevoda B., Arnesen T., Sherman F.;
"A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
nomenclature, subunits and substrates.";
BMC Proc. 3:S2-S2(2009).
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
ACETYLATION AT LYS-34; LYS-37 AND LYS-140, AND MUTAGENESIS OF
34-LYS--LYS-37; ARG-84; TYR-124 AND LYS-140.
PubMed=19744929; DOI=10.1074/jbc.M109.001347;
Evjenth R., Hole K., Karlsen O.A., Ziegler M., Arnesen T.,
Lillehaug J.R.;
"Human Naa50p (Nat5/San) displays both protein N alpha- and N epsilon-
acetyltransferase activity.";
J. Biol. Chem. 284:31122-31129(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, ACETYLATION
[LARGE SCALE ANALYSIS] AT LYS-34 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22311970; DOI=10.1074/jbc.M111.326587;
Evjenth R.H., Brenner A.K., Thompson P.R., Arnesen T.,
Froeystein N.A., Lillehaug J.R.;
"Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN)
follows ordered sequential catalytic mechanism: combined kinetic and
NMR study.";
J. Biol. Chem. 287:10081-10088(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
SUBCELLULAR LOCATION.
PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M.,
Stoeve S.I., Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C.,
Ljostveit S., Ziegler M., Niere M., Gevaert K., Arnesen T.;
"An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
termini of transmembrane proteins and maintains Golgi integrity.";
Cell Rep. 10:1362-1374(2015).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-27 AND TYR-124.
PubMed=27422821; DOI=10.1074/jbc.M116.737585;
Rong Z., Ouyang Z., Magin R.S., Marmorstein R., Yu H.;
"Opposing functions of the N-terminal acetyltransferases Naa50 and
NatA in sister-chromatid cohesion.";
J. Biol. Chem. 291:19079-19091(2016).
[18] {ECO:0000244|PDB:2OB0, ECO:0000244|PDB:2PSW}
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COENZYME A.
Structural genomics consortium (SGC);
"Structure of human MAK3 homolog.";
Submitted (JUN-2007) to the PDB data bank.
[19] {ECO:0000244|PDB:3TFY}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH COENZYME A AND
SUBSTRATE PEPTIDE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF PHE-27; PRO-28; VAL-29;
TYR-31; PHE-35; TYR-73; HIS-112; TYR-139 AND ILE-142.
PubMed=21900231; DOI=10.1074/jbc.M111.282863;
Liszczak G., Arnesen T., Marmorstein R.;
"Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase
complex reveals the molecular basis for substrate-specific
acetylation.";
J. Biol. Chem. 286:37002-37010(2011).
[20] {ECO:0000244|PDB:4X5K}
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH COENZYME A AND
SUBSTRATE PEPTIDE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND
CATALYTIC ACTIVITY.
PubMed=27484799; DOI=10.1074/jbc.M116.730432;
Reddi R., Saddanapu V., Chinthapalli D.K., Sankoju P., Sripadi P.,
Addlagatta A.;
"Human Naa50 protein displays broad substrate specificity for amino-
terminal acetylation: detailed structural and biochemical analysis
using tetrapeptide library.";
J. Biol. Chem. 291:20530-20538(2016).
-!- FUNCTION: 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). {ECO:0000269|PubMed:16507339,
ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27422821, ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
alanyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
seryl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
valyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
threonyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
lysyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
lysyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
leucyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
leucyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
phenylalanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-
methionyl-L-phenylalanyl-[protein] + CoA.
{ECO:0000269|PubMed:19744929, ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:22311970, ECO:0000269|PubMed:27484799}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-methionyl-L-
tyrosyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-
tyrosyl-[protein] + CoA. {ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:21900231, ECO:0000269|PubMed:22311970,
ECO:0000269|PubMed:27484799}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=132.6 uM for M-A-A-A peptide {ECO:0000269|PubMed:27484799};
KM=126.1 uM for L-A-A-A peptide {ECO:0000269|PubMed:27484799};
KM=5 uM for Acetyl-CoA {ECO:0000269|PubMed:22311970};
KM=79 uM for M-L-G-P-E peptide {ECO:0000269|PubMed:19744929};
KM=91 uM for M-L-D-P-E peptide {ECO:0000269|PubMed:19744929};
KM=185 uM for M-I-G-P-E peptide {ECO:0000269|PubMed:19744929};
KM=190 uM for M-L-A-L-I peptide {ECO:0000269|PubMed:19744929};
KM=320 uM for M-L-G-T-G peptide {ECO:0000269|PubMed:19744929};
KM=416 uM for M-L-G-T-E peptide {ECO:0000269|PubMed:19744929};
KM=460 uM for M-L-R-P-E peptide {ECO:0000269|PubMed:19744929};
KM=478 uM for M-L-L-P-E peptide {ECO:0000269|PubMed:19744929};
KM=3734 uM for M-F-G-P-E peptide {ECO:0000269|PubMed:19744929};
Note=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. {ECO:0000269|PubMed:19744929};
pH dependence:
Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:21900231};
-!- SUBUNIT: Component of a complex composed of NAA50, NAA15 and NAA10
(PubMed:16507339). Interacts with NAA35 (By similarity).
{ECO:0000250|UniProtKB:Q6PGB6, ECO:0000269|PubMed:16507339}.
-!- INTERACTION:
O14503:BHLHE40; NbExp=5; IntAct=EBI-1052523, EBI-711810;
Q6NYC1:JMJD6; NbExp=5; IntAct=EBI-1052523, EBI-8464037;
P41227:NAA10; NbExp=2; IntAct=EBI-1052523, EBI-747693;
Q9BXJ9:NAA15; NbExp=2; IntAct=EBI-1052523, EBI-1042540;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16507339,
ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:25732826,
ECO:0000269|PubMed:27422821}. Nucleus
{ECO:0000269|PubMed:25732826}. Note=Localizes to the cytoplasm in
interphase cells (PubMed:17502424). {ECO:0000269|PubMed:17502424}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9GZZ1-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZZ1-2; Sequence=VSP_024747;
Note=No experimental confirmation available. Contains a
N6-acetyllysine at position 34. {ECO:0000244|PubMed:19608861};
-!- SIMILARITY: Belongs to the acetyltransferase family. GNAT
subfamily. {ECO:0000305}.
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EMBL; AK023090; BAB14397.1; -; mRNA.
EMBL; AK023256; BAB14490.1; -; mRNA.
EMBL; CR749314; CAH18169.1; -; mRNA.
EMBL; CH471052; EAW79629.1; -; Genomic_DNA.
EMBL; CH471052; EAW79630.1; -; Genomic_DNA.
EMBL; BC012731; AAH12731.1; -; mRNA.
CCDS; CCDS2975.1; -. [Q9GZZ1-1]
RefSeq; NP_079422.1; NM_025146.3. [Q9GZZ1-1]
UniGene; Hs.372378; -.
PDB; 2OB0; X-ray; 1.80 A; A/B/C=2-169.
PDB; 2PSW; X-ray; 2.10 A; A/B/C=2-169.
PDB; 3TFY; X-ray; 2.75 A; A/B/C=1-169.
PDB; 4X5K; X-ray; 2.49 A; A=1-169.
PDBsum; 2OB0; -.
PDBsum; 2PSW; -.
PDBsum; 3TFY; -.
PDBsum; 4X5K; -.
ProteinModelPortal; Q9GZZ1; -.
SMR; Q9GZZ1; -.
BioGrid; 123185; 40.
IntAct; Q9GZZ1; 10.
STRING; 9606.ENSP00000240922; -.
iPTMnet; Q9GZZ1; -.
PhosphoSitePlus; Q9GZZ1; -.
BioMuta; NAA50; -.
DMDM; 74733509; -.
EPD; Q9GZZ1; -.
MaxQB; Q9GZZ1; -.
PaxDb; Q9GZZ1; -.
PeptideAtlas; Q9GZZ1; -.
PRIDE; Q9GZZ1; -.
DNASU; 80218; -.
Ensembl; ENST00000240922; ENSP00000240922; ENSG00000121579. [Q9GZZ1-1]
GeneID; 80218; -.
KEGG; hsa:80218; -.
UCSC; uc003ean.3; human. [Q9GZZ1-1]
CTD; 80218; -.
DisGeNET; 80218; -.
EuPathDB; HostDB:ENSG00000121579.12; -.
GeneCards; NAA50; -.
HGNC; HGNC:29533; NAA50.
MIM; 610834; gene.
neXtProt; NX_Q9GZZ1; -.
OpenTargets; ENSG00000121579; -.
PharmGKB; PA165697846; -.
eggNOG; KOG3138; Eukaryota.
eggNOG; COG0456; LUCA.
GeneTree; ENSGT00390000009110; -.
HOGENOM; HOG000238056; -.
HOVERGEN; HBG060820; -.
InParanoid; Q9GZZ1; -.
KO; K20793; -.
OMA; IVETKEH; -.
OrthoDB; EOG091G0PAG; -.
PhylomeDB; Q9GZZ1; -.
TreeFam; TF314841; -.
BRENDA; 2.3.1.88; 2681.
ChiTaRS; NAA50; human.
EvolutionaryTrace; Q9GZZ1; -.
GenomeRNAi; 80218; -.
PRO; PR:Q9GZZ1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000121579; -.
CleanEx; HS_NAT13; -.
CleanEx; HS_NAT5; -.
ExpressionAtlas; Q9GZZ1; baseline and differential.
Genevisible; Q9GZZ1; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; IDA:UniProtKB.
GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:UniProtKB.
GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; IDA:UniProtKB.
GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 169 N-alpha-acetyltransferase 50.
/FTId=PRO_0000284902.
DOMAIN 6 155 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 77 90 Acetyl-CoA binding.
{ECO:0000244|PDB:2PSW,
ECO:0000244|PDB:3TFY,
ECO:0000244|PDB:4X5K,
ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27484799,
ECO:0000269|Ref.18}.
REGION 117 126 Coenzyme A binding.
{ECO:0000244|PDB:2PSW,
ECO:0000244|PDB:3TFY,
ECO:0000244|PDB:4X5K,
ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27484799,
ECO:0000269|Ref.18}.
REGION 138 141 Substrate. {ECO:0000244|PDB:3TFY,
ECO:0000244|PDB:4X5K,
ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27484799}.
ACT_SITE 73 73 {ECO:0000269|PubMed:21900231}.
ACT_SITE 112 112 {ECO:0000269|PubMed:21900231}.
BINDING 31 31 Substrate. {ECO:0000244|PDB:3TFY,
ECO:0000244|PDB:4X5K,
ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27484799}.
BINDING 75 75 Substrate. {ECO:0000244|PDB:3TFY,
ECO:0000244|PDB:4X5K,
ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27484799}.
MOD_RES 12 12 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 34 34 N6-acetyllysine; by autocatalysis.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:19744929}.
MOD_RES 37 37 N6-acetyllysine; by autocatalysis.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:19744929}.
MOD_RES 110 110 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 140 140 N6-acetyllysine; by autocatalysis.
{ECO:0000269|PubMed:19744929}.
VAR_SEQ 35 122 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_024747.
MUTAGEN 27 27 F->A: Abolishes N-alpha-acetyltransferase
activity. {ECO:0000269|PubMed:21900231,
ECO:0000269|PubMed:27422821}.
MUTAGEN 28 28 P->A: Strongly decreased N-alpha-
acetyltransferase activity.
{ECO:0000269|PubMed:21900231}.
MUTAGEN 29 29 V->A: Strongly decreased N-alpha-
acetyltransferase activity.
{ECO:0000269|PubMed:21900231}.
MUTAGEN 31 31 Y->A: Abolishes N-alpha-acetyltransferase
activity. {ECO:0000269|PubMed:21900231}.
MUTAGEN 34 37 KFYK->AFYA: Decreased acetylation; when
associated with A-140.
{ECO:0000269|PubMed:19744929}.
MUTAGEN 35 35 F->A: Abolishes N-alpha-acetyltransferase
activity. {ECO:0000269|PubMed:21900231}.
MUTAGEN 73 73 Y->A,F: Abolishes N-alpha-
acetyltransferase activity.
{ECO:0000269|PubMed:21900231}.
MUTAGEN 84 84 R->A: Strongly decreased N-alpha-
acetyltransferase activity.
{ECO:0000269|PubMed:19744929}.
MUTAGEN 112 112 H->A,F: Abolishes N-alpha-
acetyltransferase activity.
{ECO:0000269|PubMed:21900231}.
MUTAGEN 124 124 Y->F: Strongly decreased N-alpha-
acetyltransferase activity. Impaired
sister chromatid cohesion during mitosis.
{ECO:0000269|PubMed:17502424,
ECO:0000269|PubMed:19744929,
ECO:0000269|PubMed:27422821}.
MUTAGEN 139 139 Y->A: Abolishes N-alpha-acetyltransferase
activity. {ECO:0000269|PubMed:21900231}.
MUTAGEN 140 140 K->A: Decreased acetylation; when
associated with 34-A-A-37.
{ECO:0000269|PubMed:19744929}.
MUTAGEN 142 142 I->A: Decreased N-alpha-acetyltransferase
activity. {ECO:0000269|PubMed:21900231}.
STRAND 5 10 {ECO:0000244|PDB:2OB0}.
TURN 13 15 {ECO:0000244|PDB:2OB0}.
HELIX 16 26 {ECO:0000244|PDB:2OB0}.
HELIX 33 39 {ECO:0000244|PDB:2OB0}.
HELIX 43 45 {ECO:0000244|PDB:2OB0}.
STRAND 46 51 {ECO:0000244|PDB:2OB0}.
STRAND 54 66 {ECO:0000244|PDB:2OB0}.
STRAND 69 79 {ECO:0000244|PDB:2OB0}.
HELIX 81 83 {ECO:0000244|PDB:2OB0}.
STRAND 85 87 {ECO:0000244|PDB:4X5K}.
HELIX 88 103 {ECO:0000244|PDB:2OB0}.
STRAND 107 114 {ECO:0000244|PDB:2OB0}.
HELIX 118 126 {ECO:0000244|PDB:2OB0}.
STRAND 130 135 {ECO:0000244|PDB:2OB0}.
STRAND 140 144 {ECO:0000244|PDB:2OB0}.
STRAND 147 153 {ECO:0000244|PDB:2OB0}.
HELIX 162 164 {ECO:0000244|PDB:2OB0}.
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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