NAT9_MOUSE
ID NAT9_MOUSE Reviewed; 241 AA.
AC Q3UG98; Q8C1G5; Q9D151;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha/beta-tubulin-N-acetyltransferase 9 {ECO:0000250|UniProtKB:Q9BTE0};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9BTE0};
GN Name=Nat9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 215-241, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: N-acetyltransferase that mediates the acetylation of the N-
CC terminal residues of alpha- and beta-tubulin.
CC {ECO:0000250|UniProtKB:Q9BTE0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-[tubulin] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-methionyl-[tubulin];
CC Xref=Rhea:RHEA:69607, Rhea:RHEA-COMP:17729, Rhea:RHEA-COMP:17730,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64731, ChEBI:CHEBI:133414;
CC Evidence={ECO:0000250|UniProtKB:Q9BTE0};
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25613.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003948; BAB23087.1; -; mRNA.
DR EMBL; AK020083; BAC25613.1; ALT_FRAME; mRNA.
DR EMBL; AK082469; BAC38501.1; -; mRNA.
DR EMBL; AK148048; BAE28311.1; -; mRNA.
DR EMBL; AL606487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011315; AAH11315.1; -; mRNA.
DR CCDS; CCDS25622.1; -.
DR RefSeq; NP_079676.1; NM_025400.3.
DR RefSeq; XP_006533984.1; XM_006533921.3.
DR RefSeq; XP_006533985.1; XM_006533922.2.
DR AlphaFoldDB; Q3UG98; -.
DR SMR; Q3UG98; -.
DR BioGRID; 211273; 3.
DR MINT; Q3UG98; -.
DR STRING; 10090.ENSMUSP00000099329; -.
DR iPTMnet; Q3UG98; -.
DR PhosphoSitePlus; Q3UG98; -.
DR EPD; Q3UG98; -.
DR MaxQB; Q3UG98; -.
DR PaxDb; Q3UG98; -.
DR PeptideAtlas; Q3UG98; -.
DR PRIDE; Q3UG98; -.
DR ProteomicsDB; 252778; -.
DR Antibodypedia; 19466; 68 antibodies from 19 providers.
DR DNASU; 66176; -.
DR Ensembl; ENSMUST00000103038; ENSMUSP00000099327; ENSMUSG00000015542.
DR Ensembl; ENSMUST00000103039; ENSMUSP00000099328; ENSMUSG00000015542.
DR Ensembl; ENSMUST00000103040; ENSMUSP00000099329; ENSMUSG00000015542.
DR Ensembl; ENSMUST00000103041; ENSMUSP00000099330; ENSMUSG00000015542.
DR GeneID; 66176; -.
DR KEGG; mmu:66176; -.
DR UCSC; uc007mgr.1; mouse.
DR CTD; 26151; -.
DR MGI; MGI:1913426; Nat9.
DR VEuPathDB; HostDB:ENSMUSG00000015542; -.
DR eggNOG; KOG4135; Eukaryota.
DR GeneTree; ENSGT00390000012745; -.
DR HOGENOM; CLU_073102_1_1_1; -.
DR InParanoid; Q3UG98; -.
DR OMA; EARHVPK; -.
DR OrthoDB; 1507385at2759; -.
DR PhylomeDB; Q3UG98; -.
DR TreeFam; TF315021; -.
DR BioGRID-ORCS; 66176; 4 hits in 76 CRISPR screens.
DR PRO; PR:Q3UG98; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UG98; protein.
DR Bgee; ENSMUSG00000015542; Expressed in spermatocyte and 244 other tissues.
DR Genevisible; Q3UG98; MM.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006473; P:protein acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039135; NAT9-like.
DR PANTHER; PTHR13256; PTHR13256; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Reference proteome;
KW Transferase.
FT CHAIN 1..241
FT /note="Alpha/beta-tubulin-N-acetyltransferase 9"
FT /id="PRO_0000286875"
FT DOMAIN 34..181
FT /note="N-acetyltransferase"
FT CONFLICT 15
FT /note="V -> A (in Ref. 1; BAE28311)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="E -> K (in Ref. 1; BAC25613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27663 MW; BC3E0C2C20E5554E CRC64;
MKLNQNTMLV GKKVVLVPYT SEHVPRYHEW MKSEELRHLT ASEQLTLQQE YEMQCSWCED
EDKCTFIVLD AEKWQAQPRP PEESCMVGDV NLFLTDLEDP TLGEIEVMIA EPSYRRQGLG
TEASLLIMSY GVTKLGLTKF EAKIGQENEP SIRMFQKLHF KQVAMSNVFQ EVTLRLAVSE
PERKWILEQT SHMEERPYRT RKAEPVTATL SEQKSWNCPL PRPDGCMGDT SAVSSVCARL
S
