ATAT_HUMAN
ID ATAT_HUMAN Reviewed; 421 AA.
AC Q5SQI0; A2AB28; Q3LIB0; Q5JP39; Q5JP40; Q5JP42; Q5SQI1; Q5SU03; Q86X42;
AC Q8NDK9; Q9BRS1; Q9H8X5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:24906155};
DE AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000255|HAMAP-Rule:MF_03130};
GN Name=ATAT1 {ECO:0000255|HAMAP-Rule:MF_03130};
GN Synonyms=C6orf134, MEC17 {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=Nbla00487;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE45758.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Neuroblastoma {ECO:0000312|EMBL:BAE45758.1};
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB14472.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3] {ECO:0000312|EMBL:AL732442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:EAX03306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH47303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH47303.1}, and
RC Lung {ECO:0000312|EMBL:AAH06105.1};
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-421 (ISOFORM 4).
RC TISSUE=Brain;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20829795; DOI=10.1038/nature09324;
RA Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
RA Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
RT "MEC-17 is an alpha-tubulin acetyltransferase.";
RL Nature 467:218-222(2010).
RN [8]
RP FUNCTION, INTERACTION WITH THE BBSOME COMPLEX, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ASP-157.
RX PubMed=21068373; DOI=10.1073/pnas.1013728107;
RA Shida T., Cueva J.G., Xu Z., Goodman M.B., Nachury M.V.;
RT "The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid
RT ciliogenesis and efficient mechanosensation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21517-21522(2010).
RN [9]
RP FUNCTION.
RX PubMed=23110214; DOI=10.1371/journal.pone.0048204;
RA Soppina V., Herbstman J.F., Skiniotis G., Verhey K.J.;
RT "Luminal localization of alpha-tubulin K40 acetylation by cryo-EM analysis
RT of fab-labeled microtubules.";
RL PLoS ONE 7:E48204-E48204(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION, INTERACTION WITH AP2A2, AND SUBCELLULAR LOCATION.
RX PubMed=24097348; DOI=10.1038/nature12571;
RA Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A., Franco M.,
RA Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C., Chavrier P.;
RT "alphaTAT1 catalyses microtubule acetylation at clathrin-coated pits.";
RL Nature 502:567-570(2013).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-323, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 1-196 IN COMPLEX WITH ACETYL-COA,
RP AND MUTAGENESIS OF GLN-58; SER-61; ILE-64 AND ARG-158.
RX PubMed=23071318; DOI=10.1073/pnas.1209343109;
RA Taschner M., Vetter M., Lorentzen E.;
RT "Atomic resolution structure of human alpha-tubulin acetyltransferase bound
RT to acetyl-CoA.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19649-19654(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 2-236 IN COMPLEX WITH ACETYL-COA,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP ILE-64; ARG-69; PHE-105; VAL-106; LEU-107; ASP-108; ASP-109; GLU-111;
RP GLU-115; GLU-117; CYS-120; ASP-157; ASN-182 AND PHE-183.
RX PubMed=23071314; DOI=10.1073/pnas.1209357109;
RA Friedmann D.R., Aguilar A., Fan J., Nachury M.V., Marmorstein R.;
RT "Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and
RT implications for tubulin-specific acetylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19655-19660(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-194 IN COMPLEX WITH ACETYL-COA,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-64; LYS-102 AND
RP ARG-158.
RX PubMed=24906155; DOI=10.1016/j.cell.2014.03.061;
RA Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L.,
RA Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.;
RT "Molecular basis for age-dependent microtubule acetylation by tubulin
RT acetyltransferase.";
RL Cell 157:1405-1415(2014).
CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC lumenal side of microtubules. Promotes microtubule destabilization and
CC accelerates microtubule dynamics; this activity may be independent of
CC acetylation activity. Acetylates alpha-tubulin with a slow enzymatic
CC rate, due to a catalytic site that is not optimized for acetyl
CC transfer. Enters the microtubule through each end and diffuses quickly
CC throughout the lumen of microtubules. Acetylates only long/old
CC microtubules because of its slow acetylation rate since it does not
CC have time to act on dynamically unstable microtubules before the enzyme
CC is released. Required for normal sperm flagellar function. Promotes
CC directional cell locomotion and chemotaxis, through AP2A2-dependent
CC acetylation of alpha-tubulin at clathrin-coated pits that are
CC concentrated at the leading edge of migrating cells. May facilitate
CC primary cilium assembly. {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:21068373,
CC ECO:0000269|PubMed:24097348, ECO:0000269|PubMed:24906155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-
CC acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA-
CC COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03130, ECO:0000269|PubMed:20829795,
CC ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:23110214,
CC ECO:0000269|PubMed:24906155};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 uM for free alpha-tubulin {ECO:0000269|PubMed:21068373,
CC ECO:0000269|PubMed:23071314};
CC KM=1.6 uM for polymerized tubulin (microtubules)
CC {ECO:0000269|PubMed:21068373, ECO:0000269|PubMed:23071314};
CC KM=2.2 uM for acetyl-CoA {ECO:0000269|PubMed:21068373,
CC ECO:0000269|PubMed:23071314};
CC Note=kcat is 2.2 h(-1) for the acetylation of polymerized tubulin
CC (microtubules), 0.35 h(-1) for the acetylation of free tubulin, and
CC 1.47 h(-1)with acetyl-CoA as substrate.;
CC -!- SUBUNIT: Component of the BBSome complex. Interacts with AP2 alpha-
CC adaptins, including AP2A2, but not with AP1 gamma-adaptin
CC (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin
CC acetylation, hence clathrin-coated pits are sites of microtubule
CC acetylation. {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:21068373, ECO:0000269|PubMed:23071314,
CC ECO:0000269|PubMed:23071318, ECO:0000269|PubMed:24097348}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:24097348}. Membrane, clathrin-coated pit
CC {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:24097348}. Cell
CC junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:24097348}. Cell projection, axon {ECO:0000255|HAMAP-
CC Rule:MF_03130}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03130}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-
CC Rule:MF_03130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000303|PubMed:14574404};
CC IsoId=Q5SQI0-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:14574404, ECO:0000303|PubMed:15489334};
CC IsoId=Q5SQI0-2; Sequence=VSP_052899, VSP_052900;
CC Name=3 {ECO:0000303|PubMed:14574404};
CC IsoId=Q5SQI0-3; Sequence=VSP_052901;
CC Name=4 {ECO:0000303|PubMed:12880961, ECO:0000303|PubMed:14574404};
CC IsoId=Q5SQI0-4; Sequence=VSP_052902, VSP_052904;
CC Name=5 {ECO:0000303|PubMed:14574404, ECO:0000303|PubMed:14702039};
CC IsoId=Q5SQI0-5; Sequence=VSP_052903;
CC Name=6 {ECO:0000303|PubMed:14574404};
CC IsoId=Q5SQI0-6; Sequence=VSP_052901, VSP_052902, VSP_052904;
CC Name=7 {ECO:0000303|PubMed:14574404, ECO:0000303|PubMed:15489334};
CC IsoId=Q5SQI0-7; Sequence=VSP_052901, VSP_052903;
CC -!- PTM: Autoacetylation strongly increases tubulin acetylation.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AB075512; BAE45758.1; -; mRNA.
DR EMBL; AK023220; BAB14472.1; -; mRNA.
DR EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03306.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03307.1; -; Genomic_DNA.
DR EMBL; BC006105; AAH06105.1; -; mRNA.
DR EMBL; BC047303; AAH47303.1; -; mRNA.
DR EMBL; AL833858; CAD38717.1; -; mRNA.
DR CCDS; CCDS4683.2; -. [Q5SQI0-4]
DR CCDS; CCDS54978.1; -. [Q5SQI0-2]
DR CCDS; CCDS59002.1; -. [Q5SQI0-6]
DR CCDS; CCDS83072.1; -. [Q5SQI0-5]
DR CCDS; CCDS83073.1; -. [Q5SQI0-7]
DR RefSeq; NP_001026892.1; NM_001031722.3. [Q5SQI0-2]
DR RefSeq; NP_001177653.1; NM_001190724.2.
DR RefSeq; NP_001241881.1; NM_001254952.2. [Q5SQI0-6]
DR RefSeq; NP_001305691.1; NM_001318762.1. [Q5SQI0-7]
DR RefSeq; NP_001305692.1; NM_001318763.1. [Q5SQI0-5]
DR RefSeq; NP_079185.2; NM_024909.3. [Q5SQI0-4]
DR PDB; 3VWD; X-ray; 1.25 A; A=1-194.
DR PDB; 3VWE; X-ray; 1.96 A; A=1-194.
DR PDB; 4B5O; X-ray; 1.05 A; A=1-196.
DR PDB; 4B5P; X-ray; 1.60 A; A/B=1-196.
DR PDB; 4GS4; X-ray; 2.11 A; A=2-236.
DR PDB; 4IF5; X-ray; 1.70 A; A=1-193.
DR PDB; 4PK2; X-ray; 1.35 A; A=1-194.
DR PDB; 4PK3; X-ray; 1.35 A; A=1-194.
DR PDB; 4U9Y; X-ray; 2.20 A; A=1-194.
DR PDB; 4U9Z; X-ray; 1.80 A; A=1-194.
DR PDBsum; 3VWD; -.
DR PDBsum; 3VWE; -.
DR PDBsum; 4B5O; -.
DR PDBsum; 4B5P; -.
DR PDBsum; 4GS4; -.
DR PDBsum; 4IF5; -.
DR PDBsum; 4PK2; -.
DR PDBsum; 4PK3; -.
DR PDBsum; 4U9Y; -.
DR PDBsum; 4U9Z; -.
DR AlphaFoldDB; Q5SQI0; -.
DR SMR; Q5SQI0; -.
DR BioGRID; 123036; 18.
DR IntAct; Q5SQI0; 8.
DR STRING; 9606.ENSP00000327832; -.
DR iPTMnet; Q5SQI0; -.
DR PhosphoSitePlus; Q5SQI0; -.
DR BioMuta; ATAT1; -.
DR DMDM; 74743537; -.
DR EPD; Q5SQI0; -.
DR jPOST; Q5SQI0; -.
DR MassIVE; Q5SQI0; -.
DR PaxDb; Q5SQI0; -.
DR PeptideAtlas; Q5SQI0; -.
DR PRIDE; Q5SQI0; -.
DR ProteomicsDB; 63801; -. [Q5SQI0-1]
DR ProteomicsDB; 63802; -. [Q5SQI0-2]
DR ProteomicsDB; 63803; -. [Q5SQI0-3]
DR ProteomicsDB; 63804; -. [Q5SQI0-4]
DR ProteomicsDB; 63805; -. [Q5SQI0-5]
DR ProteomicsDB; 63806; -. [Q5SQI0-6]
DR ProteomicsDB; 63807; -. [Q5SQI0-7]
DR ABCD; Q5SQI0; 1 sequenced antibody.
DR Antibodypedia; 26411; 137 antibodies from 22 providers.
DR DNASU; 79969; -.
DR Ensembl; ENST00000318999.11; ENSP00000324222.7; ENSG00000137343.18. [Q5SQI0-7]
DR Ensembl; ENST00000319027.9; ENSP00000324459.5; ENSG00000137343.18. [Q5SQI0-6]
DR Ensembl; ENST00000329992.12; ENSP00000332374.8; ENSG00000137343.18. [Q5SQI0-4]
DR Ensembl; ENST00000330083.6; ENSP00000327832.5; ENSG00000137343.18. [Q5SQI0-2]
DR Ensembl; ENST00000376483.8; ENSP00000365666.4; ENSG00000137343.18. [Q5SQI0-5]
DR Ensembl; ENST00000376485.8; ENSP00000365668.4; ENSG00000137343.18. [Q5SQI0-1]
DR Ensembl; ENST00000383582.4; ENSP00000373076.4; ENSG00000206488.10. [Q5SQI0-2]
DR Ensembl; ENST00000383583.8; ENSP00000373077.4; ENSG00000206488.10. [Q5SQI0-4]
DR Ensembl; ENST00000383584.6; ENSP00000373078.2; ENSG00000206488.10. [Q5SQI0-7]
DR Ensembl; ENST00000383585.8; ENSP00000373079.4; ENSG00000206488.10. [Q5SQI0-1]
DR Ensembl; ENST00000400575.5; ENSP00000383419.1; ENSG00000206488.10. [Q5SQI0-5]
DR Ensembl; ENST00000400576.5; ENSP00000383420.1; ENSG00000206488.10. [Q5SQI0-6]
DR Ensembl; ENST00000411724.5; ENSP00000388617.1; ENSG00000234549.8. [Q5SQI0-5]
DR Ensembl; ENST00000416435.2; ENSP00000412993.2; ENSG00000235658.8. [Q5SQI0-2]
DR Ensembl; ENST00000416917.5; ENSP00000402998.1; ENSG00000234549.8. [Q5SQI0-7]
DR Ensembl; ENST00000417183.5; ENSP00000393868.1; ENSG00000231257.8. [Q5SQI0-7]
DR Ensembl; ENST00000418248.5; ENSP00000411362.1; ENSG00000231257.8. [Q5SQI0-5]
DR Ensembl; ENST00000420586.6; ENSP00000411050.2; ENSG00000231257.8. [Q5SQI0-1]
DR Ensembl; ENST00000423338.5; ENSP00000415000.1; ENSG00000223752.8. [Q5SQI0-7]
DR Ensembl; ENST00000423654.5; ENSP00000403142.1; ENSG00000235658.8. [Q5SQI0-5]
DR Ensembl; ENST00000424121.5; ENSP00000412198.1; ENSG00000223752.8. [Q5SQI0-6]
DR Ensembl; ENST00000425448.2; ENSP00000391244.2; ENSG00000223752.8. [Q5SQI0-2]
DR Ensembl; ENST00000428764.6; ENSP00000399509.2; ENSG00000235658.8. [Q5SQI0-4]
DR Ensembl; ENST00000430611.5; ENSP00000409296.1; ENSG00000235658.8. [Q5SQI0-6]
DR Ensembl; ENST00000432356.6; ENSP00000416994.2; ENSG00000234549.8. [Q5SQI0-1]
DR Ensembl; ENST00000432643.6; ENSP00000416925.2; ENSG00000231257.8. [Q5SQI0-2]
DR Ensembl; ENST00000442844.6; ENSP00000394914.2; ENSG00000235658.8. [Q5SQI0-1]
DR Ensembl; ENST00000443114.5; ENSP00000405656.1; ENSG00000229061.8. [Q5SQI0-7]
DR Ensembl; ENST00000443391.5; ENSP00000406071.1; ENSG00000229061.8. [Q5SQI0-6]
DR Ensembl; ENST00000445486.6; ENSP00000398422.2; ENSG00000223752.8. [Q5SQI0-1]
DR Ensembl; ENST00000445973.5; ENSP00000415408.1; ENSG00000231257.8. [Q5SQI0-6]
DR Ensembl; ENST00000446100.5; ENSP00000393269.1; ENSG00000229061.8. [Q5SQI0-5]
DR Ensembl; ENST00000448670.2; ENSP00000389129.2; ENSG00000229061.8. [Q5SQI0-2]
DR Ensembl; ENST00000449905.5; ENSP00000399529.1; ENSG00000235658.8. [Q5SQI0-7]
DR Ensembl; ENST00000450003.6; ENSP00000406421.2; ENSG00000223752.8. [Q5SQI0-4]
DR Ensembl; ENST00000450220.2; ENSP00000405036.2; ENSG00000231257.8. [Q5SQI0-4]
DR Ensembl; ENST00000454794.6; ENSP00000409067.2; ENSG00000229061.8. [Q5SQI0-1]
DR Ensembl; ENST00000454987.5; ENSP00000410415.1; ENSG00000234549.8. [Q5SQI0-6]
DR Ensembl; ENST00000456215.6; ENSP00000399452.2; ENSG00000234549.8. [Q5SQI0-4]
DR Ensembl; ENST00000456704.6; ENSP00000394357.2; ENSG00000229061.8. [Q5SQI0-4]
DR Ensembl; ENST00000457161.5; ENSP00000388171.1; ENSG00000223752.8. [Q5SQI0-5]
DR Ensembl; ENST00000457334.2; ENSP00000398374.2; ENSG00000234549.8. [Q5SQI0-2]
DR GeneID; 79969; -.
DR KEGG; hsa:79969; -.
DR MANE-Select; ENST00000330083.6; ENSP00000327832.5; NM_001031722.4; NP_001026892.1. [Q5SQI0-2]
DR UCSC; uc003nqr.5; human. [Q5SQI0-1]
DR CTD; 79969; -.
DR DisGeNET; 79969; -.
DR GeneCards; ATAT1; -.
DR HGNC; HGNC:21186; ATAT1.
DR HPA; ENSG00000137343; Low tissue specificity.
DR MIM; 615556; gene.
DR neXtProt; NX_Q5SQI0; -.
DR OpenTargets; ENSG00000137343; -.
DR PharmGKB; PA134948212; -.
DR VEuPathDB; HostDB:ENSG00000137343; -.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_025013_0_0_1; -.
DR InParanoid; Q5SQI0; -.
DR OMA; SRQRCGQ; -.
DR PhylomeDB; Q5SQI0; -.
DR TreeFam; TF315643; -.
DR BioCyc; MetaCyc:ENSG00000137343-MON; -.
DR BRENDA; 2.3.1.108; 2681.
DR PathwayCommons; Q5SQI0; -.
DR Reactome; R-HSA-5617833; Cilium Assembly.
DR SignaLink; Q5SQI0; -.
DR BioGRID-ORCS; 79969; 23 hits in 1083 CRISPR screens.
DR ChiTaRS; ATAT1; human.
DR GenomeRNAi; 79969; -.
DR Pharos; Q5SQI0; Tbio.
DR PRO; PR:Q5SQI0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5SQI0; protein.
DR Bgee; ENSG00000137343; Expressed in cortical plate and 93 other tissues.
DR ExpressionAtlas; Q5SQI0; baseline and differential.
DR Genevisible; Q5SQI0; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0097427; C:microtubule bundle; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IDA:WormBase.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; TAS:Reactome.
DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule.
DR GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR DisProt; DP02419; -.
DR HAMAP; MF_03130; mec17; 1.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Cell junction; Cell projection; Coated pit; Cytoplasm; Cytoskeleton;
KW Membrane; Methylation; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000348066"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 196..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:23071318,
FT ECO:0000269|PubMed:24906155"
FT BINDING 160..169
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:23071318,
FT ECO:0000269|PubMed:24906155"
FT SITE 58
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23071318"
FT MOD_RES 56
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 146
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 233
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 244
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG11"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K341"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14574404,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052899"
FT VAR_SEQ 13..36
FT /note="ERITVLDQHLRPPARRPGTTTPAR -> MWLTWPFCFLTITLREEGVCHLES
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14574404,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052900"
FT VAR_SEQ 195..218
FT /note="RPPAPSLRATRHSRAAAVDPTPAA -> P (in isoform 3, isoform
FT 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14574404,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052901"
FT VAR_SEQ 323..333
FT /note="RGTPPGLVAQS -> SSLPRSEESRY (in isoform 4 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:12880961,
FT ECO:0000303|PubMed:14574404, ECO:0000303|PubMed:17974005"
FT /id="VSP_052902"
FT VAR_SEQ 324..421
FT /note="Missing (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14574404,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_052903"
FT VAR_SEQ 334..421
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12880961,
FT ECO:0000303|PubMed:14574404, ECO:0000303|PubMed:17974005"
FT /id="VSP_052904"
FT MUTAGEN 58
FT /note="Q->A: Loss of acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23071318"
FT MUTAGEN 61
FT /note="S->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:23071318"
FT MUTAGEN 64
FT /note="I->A: Strong reduction in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23071314,
FT ECO:0000269|PubMed:23071318, ECO:0000269|PubMed:24906155"
FT MUTAGEN 69
FT /note="R->A: Strong reduction in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 102
FT /note="K->A: Strong reduction in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24906155"
FT MUTAGEN 105
FT /note="F->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 106
FT /note="V->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 107
FT /note="L->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 108
FT /note="D->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 109
FT /note="D->A: Slight increase in activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 109
FT /note="D->R: Marginal increase in activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 111
FT /note="E->A: 2-fold increase in activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 111
FT /note="E->R: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 115
FT /note="E->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 117
FT /note="E->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 120
FT /note="C->A,S: Strong reduction in microtubule
FT acetylation."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 157
FT /note="D->E,N: Strong reduction in microtubule
FT acetylation."
FT /evidence="ECO:0000269|PubMed:21068373,
FT ECO:0000269|PubMed:23071314"
FT MUTAGEN 158
FT /note="R->A: 20% of wild-type acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23071318,
FT ECO:0000269|PubMed:24906155"
FT MUTAGEN 182
FT /note="N->A: Strong reduction in activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT MUTAGEN 183
FT /note="F->A: Strong reduction in activity."
FT /evidence="ECO:0000269|PubMed:23071314"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 36..57
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4B5P"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4B5O"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:4B5O"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4B5O"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:3VWD"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:3VWD"
SQ SEQUENCE 421 AA; 46810 MW; 6CC9B4B844930842 CRC64;
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL GKASAKAQNL
SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHRPPAPS LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR
EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP
HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG NQDSKQGEQE
TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG GDILNARFIR NLQERRSTRP
W
