Full text data of NAA50
NAA50
(MAK3, NAT13, NAT5)
[Confidence: low (only semi-automatic identification from reviews)]
N-alpha-acetyltransferase 50; 2.3.1.- (N-acetyltransferase 13; N-acetyltransferase 5; hNAT5; N-acetyltransferase san homolog; hSAN; NatE catalytic subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-alpha-acetyltransferase 50; 2.3.1.- (N-acetyltransferase 13; N-acetyltransferase 5; hNAT5; N-acetyltransferase san homolog; hSAN; NatE catalytic subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9GZZ1
ID NAA50_HUMAN Reviewed; 169 AA.
AC Q9GZZ1; D3DN74; Q68DQ1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=N-alpha-acetyltransferase 50;
DE EC=2.3.1.-;
DE AltName: Full=N-acetyltransferase 13;
DE AltName: Full=N-acetyltransferase 5;
DE Short=hNAT5;
DE AltName: Full=N-acetyltransferase san homolog;
DE Short=hSAN;
DE AltName: Full=NatE catalytic subunit;
GN Name=NAA50; Synonyms=MAK3, NAT13, NAT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP INTERACTION WITH NAA15 AND NAA11, MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=16507339; DOI=10.1016/j.gene.2005.12.008;
RA Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Cloning and characterization of hNAT5/hSAN: an evolutionarily
RT conserved component of the NatA protein N-alpha-acetyltransferase
RT complex.";
RL Gene 371:291-295(2006).
RN [7]
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 [8]
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:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RG Structural genomics consortium (SGC);
RT "Structure of human MAK3 homolog.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Probable catalytic component of the NAA11-NAA15 complex
CC which displays alpha (N-terminal) acetyltransferase activity.
CC -!- SUBUNIT: Interacts with NAA35 (By similarity). Interacts with
CC NAA15 and NAA11.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZZ1-2; Sequence=VSP_024747;
CC Note=No experimental confirmation available. Contains a
CC N6-acetyllysine at position 34;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT
CC subfamily.
CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK023090; BAB14397.1; -; mRNA.
DR EMBL; AK023256; BAB14490.1; -; mRNA.
DR EMBL; CR749314; CAH18169.1; -; mRNA.
DR EMBL; CH471052; EAW79629.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79630.1; -; Genomic_DNA.
DR EMBL; BC012731; AAH12731.1; -; mRNA.
DR RefSeq; NP_079422.1; NM_025146.2.
DR UniGene; Hs.372378; -.
DR PDB; 2OB0; X-ray; 1.80 A; A/B/C=2-169.
DR PDB; 2PSW; X-ray; 2.10 A; A/B/C=2-169.
DR PDB; 3TFY; X-ray; 2.75 A; A/B/C=1-169.
DR PDBsum; 2OB0; -.
DR PDBsum; 2PSW; -.
DR PDBsum; 3TFY; -.
DR ProteinModelPortal; Q9GZZ1; -.
DR SMR; Q9GZZ1; 4-169.
DR IntAct; Q9GZZ1; 3.
DR STRING; 9606.ENSP00000240922; -.
DR PhosphoSite; Q9GZZ1; -.
DR DMDM; 74733509; -.
DR PaxDb; Q9GZZ1; -.
DR PRIDE; Q9GZZ1; -.
DR DNASU; 80218; -.
DR Ensembl; ENST00000240922; ENSP00000240922; ENSG00000121579.
DR GeneID; 80218; -.
DR KEGG; hsa:80218; -.
DR UCSC; uc003ean.2; human.
DR CTD; 80218; -.
DR GeneCards; GC03M113437; -.
DR HGNC; HGNC:29533; NAA50.
DR MIM; 610834; gene.
DR neXtProt; NX_Q9GZZ1; -.
DR PharmGKB; PA165697846; -.
DR eggNOG; COG0456; -.
DR HOGENOM; HOG000238056; -.
DR HOVERGEN; HBG060820; -.
DR InParanoid; Q9GZZ1; -.
DR OMA; SAIDFYQ; -.
DR OrthoDB; EOG7MWGZK; -.
DR PhylomeDB; Q9GZZ1; -.
DR ChiTaRS; NAA50; human.
DR EvolutionaryTrace; Q9GZZ1; -.
DR GenomeRNAi; 80218; -.
DR NextBio; 70626; -.
DR PRO; PR:Q9GZZ1; -.
DR ArrayExpress; Q9GZZ1; -.
DR Bgee; Q9GZZ1; -.
DR CleanEx; HS_NAT13; -.
DR CleanEx; HS_NAT5; -.
DR Genevestigator; Q9GZZ1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; TAS:HGNC.
DR Gene3D; 3.40.630.30; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1 169 N-alpha-acetyltransferase 50.
FT /FTId=PRO_0000284902.
FT DOMAIN 6 155 N-acetyltransferase.
FT REGION 79 90 Coenzyme A binding.
FT MOD_RES 12 12 Phosphothreonine.
FT MOD_RES 34 34 N6-acetyllysine.
FT MOD_RES 37 37 N6-acetyllysine.
FT MOD_RES 110 110 Phosphotyrosine.
FT VAR_SEQ 35 122 Missing (in isoform 2).
FT /FTId=VSP_024747.
FT STRAND 5 10
FT TURN 13 15
FT HELIX 16 26
FT HELIX 33 39
FT HELIX 43 45
FT STRAND 46 51
FT STRAND 54 66
FT STRAND 69 79
FT HELIX 81 83
FT STRAND 85 87
FT HELIX 88 103
FT STRAND 107 114
FT HELIX 118 126
FT STRAND 130 135
FT STRAND 140 144
FT STRAND 147 153
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
//
ID NAA50_HUMAN Reviewed; 169 AA.
AC Q9GZZ1; D3DN74; Q68DQ1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=N-alpha-acetyltransferase 50;
DE EC=2.3.1.-;
DE AltName: Full=N-acetyltransferase 13;
DE AltName: Full=N-acetyltransferase 5;
DE Short=hNAT5;
DE AltName: Full=N-acetyltransferase san homolog;
DE Short=hSAN;
DE AltName: Full=NatE catalytic subunit;
GN Name=NAA50; Synonyms=MAK3, NAT13, NAT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP INTERACTION WITH NAA15 AND NAA11, MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=16507339; DOI=10.1016/j.gene.2005.12.008;
RA Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Cloning and characterization of hNAT5/hSAN: an evolutionarily
RT conserved component of the NatA protein N-alpha-acetyltransferase
RT complex.";
RL Gene 371:291-295(2006).
RN [7]
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 [8]
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:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34 AND LYS-37, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RG Structural genomics consortium (SGC);
RT "Structure of human MAK3 homolog.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Probable catalytic component of the NAA11-NAA15 complex
CC which displays alpha (N-terminal) acetyltransferase activity.
CC -!- SUBUNIT: Interacts with NAA35 (By similarity). Interacts with
CC NAA15 and NAA11.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZZ1-2; Sequence=VSP_024747;
CC Note=No experimental confirmation available. Contains a
CC N6-acetyllysine at position 34;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT
CC subfamily.
CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK023090; BAB14397.1; -; mRNA.
DR EMBL; AK023256; BAB14490.1; -; mRNA.
DR EMBL; CR749314; CAH18169.1; -; mRNA.
DR EMBL; CH471052; EAW79629.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79630.1; -; Genomic_DNA.
DR EMBL; BC012731; AAH12731.1; -; mRNA.
DR RefSeq; NP_079422.1; NM_025146.2.
DR UniGene; Hs.372378; -.
DR PDB; 2OB0; X-ray; 1.80 A; A/B/C=2-169.
DR PDB; 2PSW; X-ray; 2.10 A; A/B/C=2-169.
DR PDB; 3TFY; X-ray; 2.75 A; A/B/C=1-169.
DR PDBsum; 2OB0; -.
DR PDBsum; 2PSW; -.
DR PDBsum; 3TFY; -.
DR ProteinModelPortal; Q9GZZ1; -.
DR SMR; Q9GZZ1; 4-169.
DR IntAct; Q9GZZ1; 3.
DR STRING; 9606.ENSP00000240922; -.
DR PhosphoSite; Q9GZZ1; -.
DR DMDM; 74733509; -.
DR PaxDb; Q9GZZ1; -.
DR PRIDE; Q9GZZ1; -.
DR DNASU; 80218; -.
DR Ensembl; ENST00000240922; ENSP00000240922; ENSG00000121579.
DR GeneID; 80218; -.
DR KEGG; hsa:80218; -.
DR UCSC; uc003ean.2; human.
DR CTD; 80218; -.
DR GeneCards; GC03M113437; -.
DR HGNC; HGNC:29533; NAA50.
DR MIM; 610834; gene.
DR neXtProt; NX_Q9GZZ1; -.
DR PharmGKB; PA165697846; -.
DR eggNOG; COG0456; -.
DR HOGENOM; HOG000238056; -.
DR HOVERGEN; HBG060820; -.
DR InParanoid; Q9GZZ1; -.
DR OMA; SAIDFYQ; -.
DR OrthoDB; EOG7MWGZK; -.
DR PhylomeDB; Q9GZZ1; -.
DR ChiTaRS; NAA50; human.
DR EvolutionaryTrace; Q9GZZ1; -.
DR GenomeRNAi; 80218; -.
DR NextBio; 70626; -.
DR PRO; PR:Q9GZZ1; -.
DR ArrayExpress; Q9GZZ1; -.
DR Bgee; Q9GZZ1; -.
DR CleanEx; HS_NAT13; -.
DR CleanEx; HS_NAT5; -.
DR Genevestigator; Q9GZZ1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; TAS:HGNC.
DR Gene3D; 3.40.630.30; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1 169 N-alpha-acetyltransferase 50.
FT /FTId=PRO_0000284902.
FT DOMAIN 6 155 N-acetyltransferase.
FT REGION 79 90 Coenzyme A binding.
FT MOD_RES 12 12 Phosphothreonine.
FT MOD_RES 34 34 N6-acetyllysine.
FT MOD_RES 37 37 N6-acetyllysine.
FT MOD_RES 110 110 Phosphotyrosine.
FT VAR_SEQ 35 122 Missing (in isoform 2).
FT /FTId=VSP_024747.
FT STRAND 5 10
FT TURN 13 15
FT HELIX 16 26
FT HELIX 33 39
FT HELIX 43 45
FT STRAND 46 51
FT STRAND 54 66
FT STRAND 69 79
FT HELIX 81 83
FT STRAND 85 87
FT HELIX 88 103
FT STRAND 107 114
FT HELIX 118 126
FT STRAND 130 135
FT STRAND 140 144
FT STRAND 147 153
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
//
MIM
610834
*RECORD*
*FIELD* NO
610834
*FIELD* TI
*610834 N-ACETYLTRANSFERASE 13; NAT13
;;NAT5, S. CEREVISIAE, HOMOLOG OF;;
SAN, DROSOPHILA, HOMOLOG OF
read more*FIELD* TX
CLONING
By searching for sequences similar to yeast Nat5, Arnesen et al. (2006)
identified human NAT13, which they called hNAT5. The deduced 169-amino
acid protein contains a motif essential for acetyl-CoA binding, and it
has a calculated molecular mass of 19.4 kD. NAT13 shares 25% identity
with yeast Nat5 and 70% identity with the Drosophila homolog, San.
RT-PCR detected NAT13 in all human cell lines examined. Epitope-tagged
NAT13 localized to the cytoplasm of transfected HeLa cells.
GENE FUNCTION
The N-alpha-acetyltransferase complex cotranslationally acetylates the N
termini of nascent polypeptides. In yeast, this complex contains Ard1
(300013), Nat1 (NARG1; 608000), and Nat5. By analyzing proteins
coimmunoprecipitated from human embryonic kidney cells, Arnesen et al.
(2006) found that NAT13, like yeast Nat5, associated with ARD1 and
NARG1.
MAPPING
By genomic sequence analysis, Arnesen et al. (2006) mapped the NAT13
gene to chromosome 3q13.2.
*FIELD* RF
1. 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.
*FIELD* CD
Patricia A. Hartz: 3/6/2007
*FIELD* ED
wwang: 03/06/2007
wwang: 3/6/2007
*RECORD*
*FIELD* NO
610834
*FIELD* TI
*610834 N-ACETYLTRANSFERASE 13; NAT13
;;NAT5, S. CEREVISIAE, HOMOLOG OF;;
SAN, DROSOPHILA, HOMOLOG OF
read more*FIELD* TX
CLONING
By searching for sequences similar to yeast Nat5, Arnesen et al. (2006)
identified human NAT13, which they called hNAT5. The deduced 169-amino
acid protein contains a motif essential for acetyl-CoA binding, and it
has a calculated molecular mass of 19.4 kD. NAT13 shares 25% identity
with yeast Nat5 and 70% identity with the Drosophila homolog, San.
RT-PCR detected NAT13 in all human cell lines examined. Epitope-tagged
NAT13 localized to the cytoplasm of transfected HeLa cells.
GENE FUNCTION
The N-alpha-acetyltransferase complex cotranslationally acetylates the N
termini of nascent polypeptides. In yeast, this complex contains Ard1
(300013), Nat1 (NARG1; 608000), and Nat5. By analyzing proteins
coimmunoprecipitated from human embryonic kidney cells, Arnesen et al.
(2006) found that NAT13, like yeast Nat5, associated with ARD1 and
NARG1.
MAPPING
By genomic sequence analysis, Arnesen et al. (2006) mapped the NAT13
gene to chromosome 3q13.2.
*FIELD* RF
1. 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.
*FIELD* CD
Patricia A. Hartz: 3/6/2007
*FIELD* ED
wwang: 03/06/2007
wwang: 3/6/2007