Full text data of NAA20
NAA20
(NAT5)
[Confidence: low (only semi-automatic identification from reviews)]
N-alpha-acetyltransferase 20; 2.3.1.88 (Methionine N-acetyltransferase; N-acetyltransferase 5; N-terminal acetyltransferase B complex catalytic subunit NAA20; N-terminal acetyltransferase B complex catalytic subunit NAT5; NatB complex subunit NAT5; NatB catalytic subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-alpha-acetyltransferase 20; 2.3.1.88 (Methionine N-acetyltransferase; N-acetyltransferase 5; N-terminal acetyltransferase B complex catalytic subunit NAA20; N-terminal acetyltransferase B complex catalytic subunit NAT5; NatB complex subunit NAT5; NatB catalytic subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61599
ID NAA20_HUMAN Reviewed; 178 AA.
AC P61599; A6NHA3; B2R4G4; Q5TFT7; Q9D7H8; Q9H0Y4; Q9NQH6; Q9Y6D2;
read moreDT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=N-alpha-acetyltransferase 20;
DE EC=2.3.1.88;
DE AltName: Full=Methionine N-acetyltransferase;
DE AltName: Full=N-acetyltransferase 5;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE Short=NatB complex subunit NAT5;
DE AltName: Full=NatB catalytic subunit;
GN Name=NAA20; Synonyms=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 [MRNA] (ISOFORM 1).
RA Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y.,
RA Yu M., Chen S., Mao M., Chen Z.;
RT "Human N-terminal acetyltransferase complex ard1 subunit homologue,
RT complete CDS.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Pancreas;
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 [7]
RP FUNCTION, INTERACTION WITH NAA25, AND SUBCELLULAR LOCATION.
RX PubMed=18570629; DOI=10.1042/BJ20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B
RT (hNatB): a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(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 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).
CC -!- FUNCTION: Catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides
CC beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins
CC with cell cycle functions are overrepresented in the pool of NatB
CC substrates. Required for maintaining the structure and function of
CC actomyosin fibers and for proper cellular migration.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + peptide = N(alpha)-acetylpeptide
CC + CoA.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC complex which is composed of NAA20 and NAA25.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61599-2; Sequence=VSP_045644;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1
CC subfamily.
CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BG548527; Type=Frameshift; Positions=111;
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DR EMBL; AF085355; AAD40190.1; -; mRNA.
DR EMBL; AL136641; CAB66576.1; -; mRNA.
DR EMBL; AK311819; BAG34761.1; -; mRNA.
DR EMBL; AL049538; CAI19341.1; -; Genomic_DNA.
DR EMBL; AL035454; CAI19341.1; JOINED; Genomic_DNA.
DR EMBL; AL035454; CAI42118.1; -; Genomic_DNA.
DR EMBL; AL049538; CAI42118.1; JOINED; Genomic_DNA.
DR EMBL; AL035454; CAX15127.1; -; Genomic_DNA.
DR EMBL; AL049538; CAX15127.1; JOINED; Genomic_DNA.
DR EMBL; AL049538; CAX15212.1; -; Genomic_DNA.
DR EMBL; AL035454; CAX15212.1; JOINED; Genomic_DNA.
DR EMBL; CH471133; EAX10214.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10215.1; -; Genomic_DNA.
DR EMBL; BC005181; AAH05181.1; -; mRNA.
DR EMBL; BC008446; AAH08446.1; -; mRNA.
DR EMBL; BG548527; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_057184.1; NM_016100.4.
DR RefSeq; NP_852669.1; NM_181528.3.
DR UniGene; Hs.368783; -.
DR UniGene; Hs.708298; -.
DR ProteinModelPortal; P61599; -.
DR SMR; P61599; 3-154.
DR IntAct; P61599; 1.
DR MINT; MINT-3022686; -.
DR STRING; 9606.ENSP00000335636; -.
DR PhosphoSite; P61599; -.
DR DMDM; 47606438; -.
DR PaxDb; P61599; -.
DR PRIDE; P61599; -.
DR DNASU; 51126; -.
DR Ensembl; ENST00000310450; ENSP00000311027; ENSG00000173418.
DR Ensembl; ENST00000334982; ENSP00000335636; ENSG00000173418.
DR GeneID; 51126; -.
DR KEGG; hsa:51126; -.
DR UCSC; uc002wrq.3; human.
DR CTD; 51126; -.
DR GeneCards; GC20P019997; -.
DR HGNC; HGNC:15908; NAA20.
DR MIM; 610833; gene.
DR neXtProt; NX_P61599; -.
DR PharmGKB; PA31449; -.
DR eggNOG; COG0456; -.
DR HOVERGEN; HBG107217; -.
DR InParanoid; P61599; -.
DR KO; K00670; -.
DR OMA; PWHAHIT; -.
DR OrthoDB; EOG7PP57X; -.
DR PhylomeDB; P61599; -.
DR ChiTaRS; NAA20; human.
DR GeneWiki; NAT5; -.
DR GenomeRNAi; 51126; -.
DR NextBio; 53927; -.
DR PRO; PR:P61599; -.
DR ArrayExpress; P61599; -.
DR Bgee; P61599; -.
DR CleanEx; HS_NAT5; -.
DR Genevestigator; P61599; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IEA:UniProtKB-EC.
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 Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1 178 N-alpha-acetyltransferase 20.
FT /FTId=PRO_0000074534.
FT DOMAIN 2 157 N-acetyltransferase.
FT VAR_SEQ 103 178 KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNG
FT EPDEDAYDMRKALSRDTEKKSIIPLPHPVRPEDIE -> YE
FT ESTFQGY (in isoform 2).
FT /FTId=VSP_045644.
FT CONFLICT 47 47 E -> V (in Ref. 2; CAB66576).
SQ SEQUENCE 178 AA; 20368 MW; C5CCEA50CD60E097 CRC64;
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE
//
ID NAA20_HUMAN Reviewed; 178 AA.
AC P61599; A6NHA3; B2R4G4; Q5TFT7; Q9D7H8; Q9H0Y4; Q9NQH6; Q9Y6D2;
read moreDT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=N-alpha-acetyltransferase 20;
DE EC=2.3.1.88;
DE AltName: Full=Methionine N-acetyltransferase;
DE AltName: Full=N-acetyltransferase 5;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE Short=NatB complex subunit NAT5;
DE AltName: Full=NatB catalytic subunit;
GN Name=NAA20; Synonyms=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 [MRNA] (ISOFORM 1).
RA Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y.,
RA Yu M., Chen S., Mao M., Chen Z.;
RT "Human N-terminal acetyltransferase complex ard1 subunit homologue,
RT complete CDS.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Pancreas;
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 [7]
RP FUNCTION, INTERACTION WITH NAA25, AND SUBCELLULAR LOCATION.
RX PubMed=18570629; DOI=10.1042/BJ20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B
RT (hNatB): a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(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 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).
CC -!- FUNCTION: Catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides
CC beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins
CC with cell cycle functions are overrepresented in the pool of NatB
CC substrates. Required for maintaining the structure and function of
CC actomyosin fibers and for proper cellular migration.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + peptide = N(alpha)-acetylpeptide
CC + CoA.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC complex which is composed of NAA20 and NAA25.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61599-2; Sequence=VSP_045644;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1
CC subfamily.
CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BG548527; Type=Frameshift; Positions=111;
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DR EMBL; AF085355; AAD40190.1; -; mRNA.
DR EMBL; AL136641; CAB66576.1; -; mRNA.
DR EMBL; AK311819; BAG34761.1; -; mRNA.
DR EMBL; AL049538; CAI19341.1; -; Genomic_DNA.
DR EMBL; AL035454; CAI19341.1; JOINED; Genomic_DNA.
DR EMBL; AL035454; CAI42118.1; -; Genomic_DNA.
DR EMBL; AL049538; CAI42118.1; JOINED; Genomic_DNA.
DR EMBL; AL035454; CAX15127.1; -; Genomic_DNA.
DR EMBL; AL049538; CAX15127.1; JOINED; Genomic_DNA.
DR EMBL; AL049538; CAX15212.1; -; Genomic_DNA.
DR EMBL; AL035454; CAX15212.1; JOINED; Genomic_DNA.
DR EMBL; CH471133; EAX10214.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10215.1; -; Genomic_DNA.
DR EMBL; BC005181; AAH05181.1; -; mRNA.
DR EMBL; BC008446; AAH08446.1; -; mRNA.
DR EMBL; BG548527; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_057184.1; NM_016100.4.
DR RefSeq; NP_852669.1; NM_181528.3.
DR UniGene; Hs.368783; -.
DR UniGene; Hs.708298; -.
DR ProteinModelPortal; P61599; -.
DR SMR; P61599; 3-154.
DR IntAct; P61599; 1.
DR MINT; MINT-3022686; -.
DR STRING; 9606.ENSP00000335636; -.
DR PhosphoSite; P61599; -.
DR DMDM; 47606438; -.
DR PaxDb; P61599; -.
DR PRIDE; P61599; -.
DR DNASU; 51126; -.
DR Ensembl; ENST00000310450; ENSP00000311027; ENSG00000173418.
DR Ensembl; ENST00000334982; ENSP00000335636; ENSG00000173418.
DR GeneID; 51126; -.
DR KEGG; hsa:51126; -.
DR UCSC; uc002wrq.3; human.
DR CTD; 51126; -.
DR GeneCards; GC20P019997; -.
DR HGNC; HGNC:15908; NAA20.
DR MIM; 610833; gene.
DR neXtProt; NX_P61599; -.
DR PharmGKB; PA31449; -.
DR eggNOG; COG0456; -.
DR HOVERGEN; HBG107217; -.
DR InParanoid; P61599; -.
DR KO; K00670; -.
DR OMA; PWHAHIT; -.
DR OrthoDB; EOG7PP57X; -.
DR PhylomeDB; P61599; -.
DR ChiTaRS; NAA20; human.
DR GeneWiki; NAT5; -.
DR GenomeRNAi; 51126; -.
DR NextBio; 53927; -.
DR PRO; PR:P61599; -.
DR ArrayExpress; P61599; -.
DR Bgee; P61599; -.
DR CleanEx; HS_NAT5; -.
DR Genevestigator; P61599; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IEA:UniProtKB-EC.
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 Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1 178 N-alpha-acetyltransferase 20.
FT /FTId=PRO_0000074534.
FT DOMAIN 2 157 N-acetyltransferase.
FT VAR_SEQ 103 178 KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNG
FT EPDEDAYDMRKALSRDTEKKSIIPLPHPVRPEDIE -> YE
FT ESTFQGY (in isoform 2).
FT /FTId=VSP_045644.
FT CONFLICT 47 47 E -> V (in Ref. 2; CAB66576).
SQ SEQUENCE 178 AA; 20368 MW; C5CCEA50CD60E097 CRC64;
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE
//
MIM
610833
*RECORD*
*FIELD* NO
610833
*FIELD* TI
*610833 N-ACETYLTRANSFERASE 5; NAT5
;;NAT3, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
DESCRIPTION
read more
NAT5 is a component of N-acetyltransferase complex B (NatB). Human NatB
performs cotranslational N(alpha)-terminal acetylation of methionine
residues when they are followed by asparagine (Starheim et al., 2008).
CLONING
By searching databases for sequences similar to yeast Nat3, Polevoda et
al. (2003) identified human NAT5, which encodes a deduced 178-amino acid
protein. Polevoda et al. (2003) identified NAT5 homologs in several
species, including nematode and plant.
By searching a database for sequences similar to yeast Nat3, followed by
PCR of a HeLa cell cDNA library, Starheim et al. (2008) cloned NAT5,
which they called NAT3. The deduced 178-amino acid protein has a
calculated molecular mass of 20.4 kD and contains a central
acetyltransferase domain. NAT3 shares 41.3% amino acid identity with its
yeast ortholog. Western blot analysis detected NAT3 in all human cell
lines examined. Immunofluorescence analysis of HeLa cells revealed
strong nuclear localization and weaker cytoplasmic localization of NAT3.
GENE FUNCTION
The yeast NatB complex is an N-terminal acetyltransferase that transfers
acetyl groups from acetyl-CoA to N-terminal alpha-amino groups. Polevoda
et al. (2003) showed that yeast Nat3, the homolog of NAT5, is a subunit
of the NatB acetyltransferase complex and was required for
acetyltransferase activity.
Using reciprocal immunoprecipitation analysis and Western blot analysis,
Starheim et al. (2008) showed that endogenous MDM20 (612755) and NAT3
interacted directly in HEK293 cells. The immunoprecipitated complex
showed NatB activity against the synthetic peptide MDEL, but not against
any other peptide examined. MDM20 and NAT3 also associated with isolated
HEK293 polysomes, as well as in the cytosolic fraction. Knockdown of
either protein via small interfering RNA disrupted cell cycle
progression. Knockdown of NAT3 led to reduced cell proliferation and
G0/G1 arrest, whereas knockdown of MDM20 decreased the number of cells
in the G0/G1 phase and resulted in some cell death. Starheim et al.
(2008) concluded that NAT3 is part of the NatB complex that acetylates
the N-terminal sequence met-asp-, and they suggested that NatB may have
an additional role in cell cycle progression.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAT5
gene to chromosome 20 (TMAP SHGC-35956).
*FIELD* RF
1. Polevoda, B.; Cardillo, T. S.; Doyle, T. C.; Bedi, G. S.; Sherman,
F.: Nat3p and Mdm20p are required for function of yeast NatB N-alpha-terminal
acetyltransferase and of actin and tropomyosin. J. Biol. Chem. 278:
30686-30697, 2003.
2. Starheim, K. K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug,
J. E.; Lillehaug, J. R.: Identification of the human N-alpha-acetyltransferase
complex B (hNatB): a complex important for cell-cycle progression. Biochem.
J. 415: 325-331, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/21/2009
*FIELD* CD
Patricia A. Hartz: 3/6/2007
*FIELD* ED
mgross: 04/23/2009
terry: 4/21/2009
wwang: 3/6/2007
*RECORD*
*FIELD* NO
610833
*FIELD* TI
*610833 N-ACETYLTRANSFERASE 5; NAT5
;;NAT3, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
DESCRIPTION
read more
NAT5 is a component of N-acetyltransferase complex B (NatB). Human NatB
performs cotranslational N(alpha)-terminal acetylation of methionine
residues when they are followed by asparagine (Starheim et al., 2008).
CLONING
By searching databases for sequences similar to yeast Nat3, Polevoda et
al. (2003) identified human NAT5, which encodes a deduced 178-amino acid
protein. Polevoda et al. (2003) identified NAT5 homologs in several
species, including nematode and plant.
By searching a database for sequences similar to yeast Nat3, followed by
PCR of a HeLa cell cDNA library, Starheim et al. (2008) cloned NAT5,
which they called NAT3. The deduced 178-amino acid protein has a
calculated molecular mass of 20.4 kD and contains a central
acetyltransferase domain. NAT3 shares 41.3% amino acid identity with its
yeast ortholog. Western blot analysis detected NAT3 in all human cell
lines examined. Immunofluorescence analysis of HeLa cells revealed
strong nuclear localization and weaker cytoplasmic localization of NAT3.
GENE FUNCTION
The yeast NatB complex is an N-terminal acetyltransferase that transfers
acetyl groups from acetyl-CoA to N-terminal alpha-amino groups. Polevoda
et al. (2003) showed that yeast Nat3, the homolog of NAT5, is a subunit
of the NatB acetyltransferase complex and was required for
acetyltransferase activity.
Using reciprocal immunoprecipitation analysis and Western blot analysis,
Starheim et al. (2008) showed that endogenous MDM20 (612755) and NAT3
interacted directly in HEK293 cells. The immunoprecipitated complex
showed NatB activity against the synthetic peptide MDEL, but not against
any other peptide examined. MDM20 and NAT3 also associated with isolated
HEK293 polysomes, as well as in the cytosolic fraction. Knockdown of
either protein via small interfering RNA disrupted cell cycle
progression. Knockdown of NAT3 led to reduced cell proliferation and
G0/G1 arrest, whereas knockdown of MDM20 decreased the number of cells
in the G0/G1 phase and resulted in some cell death. Starheim et al.
(2008) concluded that NAT3 is part of the NatB complex that acetylates
the N-terminal sequence met-asp-, and they suggested that NatB may have
an additional role in cell cycle progression.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAT5
gene to chromosome 20 (TMAP SHGC-35956).
*FIELD* RF
1. Polevoda, B.; Cardillo, T. S.; Doyle, T. C.; Bedi, G. S.; Sherman,
F.: Nat3p and Mdm20p are required for function of yeast NatB N-alpha-terminal
acetyltransferase and of actin and tropomyosin. J. Biol. Chem. 278:
30686-30697, 2003.
2. Starheim, K. K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug,
J. E.; Lillehaug, J. R.: Identification of the human N-alpha-acetyltransferase
complex B (hNatB): a complex important for cell-cycle progression. Biochem.
J. 415: 325-331, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/21/2009
*FIELD* CD
Patricia A. Hartz: 3/6/2007
*FIELD* ED
mgross: 04/23/2009
terry: 4/21/2009
wwang: 3/6/2007