LOCUS       NP_001399996             421 aa            linear   PRI 23-JUL-2024
DEFINITION  alpha-tubulin N-acetyltransferase 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001399996
VERSION     NP_001399996.1
DBSOURCE    REFSEQ: accession NM_001413067.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Choi,J.H., Jeong,J., Kim,J., You,E., Keum,S., Song,S., Hwang,Y.E.,
            Ji,M., Park,K.S. and Rhee,S.
  TITLE     Genetic disruption of ATAT1 causes RhoA downregulation through
            abnormal truncation of C/EBPbeta
  JOURNAL   BMB Rep 57 (6), 293-298 (2024)
   PUBMED   38835115
  REMARK    GeneRIF: Genetic disruption of ATAT1 causes RhoA downregulation
            through abnormal truncation of C/EBPbeta.
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Iuzzolino,A., Pellegrini,F.R., Rotili,D., Degrassi,F. and
            Trisciuoglio,D.
  TITLE     The alpha-tubulin acetyltransferase ATAT1: structure, cellular
            functions, and its emerging role in human diseases
  JOURNAL   Cell Mol Life Sci 81 (1), 193 (2024)
   PUBMED   38652325
  REMARK    GeneRIF: The alpha-tubulin acetyltransferase ATAT1: structure,
            cellular functions, and its emerging role in human diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Yoshimoto,S., Morita,H., Okamura,K., Hiraki,A. and Hashimoto,S.
  TITLE     alphaTAT1-induced tubulin acetylation promotes ameloblastoma
            migration and invasion
  JOURNAL   Lab Invest 102 (1), 80-89 (2022)
   PUBMED   34508164
  REMARK    GeneRIF: alphaTAT1-induced tubulin acetylation promotes
            ameloblastoma migration and invasion.
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Ko,P., Choi,J.H., Song,S., Keum,S., Jeong,J., Hwang,Y.E., Kim,J.W.
            and Rhee,S.
  TITLE     Microtubule Acetylation Controls MDA-MB-231 Breast Cancer Cell
            Invasion through the Modulation of Endoplasmic Reticulum Stress
  JOURNAL   Int J Mol Sci 22 (11), 6018 (2021)
   PUBMED   34199510
  REMARK    GeneRIF: Microtubule Acetylation Controls MDA-MB-231 Breast Cancer
            Cell Invasion through the Modulation of Endoplasmic Reticulum
            Stress.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Taschner,M., Vetter,M. and Lorentzen,E.
  TITLE     Atomic resolution structure of human alpha-tubulin
            acetyltransferase bound to acetyl-CoA
  JOURNAL   Proc Natl Acad Sci U S A 109 (48), 19649-19654 (2012)
   PUBMED   23071318
  REMARK    GeneRIF: analysis reveals a basic patch implicated in substrate
            binding and a conserved glutamine residue required for catalysis,
            demonstrating that the family of alpha-tubulin acetyltransferases
            uses a reaction mechanism different from other lysine
            acetyltransferases
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Friedmann,D.R., Aguilar,A., Fan,J., Nachury,M.V. and Marmorstein,R.
  TITLE     Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and
            implications for tubulin-specific acetylation
  JOURNAL   Proc Natl Acad Sci U S A 109 (48), 19655-19660 (2012)
   PUBMED   23071314
  REMARK    GeneRIF: cysteine residues play important catalytic roles through a
            ternary complex mechanism. alphaTAT1 mutations have analogous
            effects on tubulin acetylation in vitro and in cells
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Castro-Castro,A., Janke,C., Montagnac,G., Paul-Gilloteaux,P. and
            Chavrier,P.
  TITLE     ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a
            balance of acetylation of alpha-tubulin and cortactin and regulate
            MT1-MMP trafficking and breast tumor cell invasion
  JOURNAL   Eur J Cell Biol 91 (11-12), 950-960 (2012)
   PUBMED   22902175
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Shida,T., Cueva,J.G., Xu,Z., Goodman,M.B. and Nachury,M.V.
  TITLE     The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes
            rapid ciliogenesis and efficient mechanosensation
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21517-21522 (2010)
   PUBMED   21068373
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Akella,J.S., Wloga,D., Kim,J., Starostina,N.G., Lyons-Abbott,S.,
            Morrissette,N.S., Dougan,S.T., Kipreos,E.T. and Gaertig,J.
  TITLE     MEC-17 is an alpha-tubulin acetyltransferase
  JOURNAL   Nature 467 (7312), 218-222 (2010)
   PUBMED   20829795
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662800.4.
            
            Summary: This gene encodes a protein that localizes to
            clathrin-coated pits, where it acetylates alpha tubulin on lysine
            40. This process may be important in microtubule growth, for
            instance during chemotaxis and the formation of cilium. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.376731.1,
                                           SRR18074967.3672947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376485.9/ ENSP00000365668.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..421
                     /product="alpha-tubulin N-acetyltransferase 1 isoform 7"
                     /EC_number="2.3.1.108"
                     /note="alpha-tubulin N-acetyltransferase 1;
                     acetyltransferase mec-17 homolog"
                     /calculated_mol_wt=46679
     Region          10..190
                     /region_name="Acetyltransf_16"
                     /note="GNAT acetyltransferase, Mec-17; pfam05301"
                     /db_xref="CDD:461616"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q8K341,
                     ECO:0000255|HAMAP-Rule:MF_03130; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            58
                     /site_type="other"
                     /note="Crucial for catalytic activity.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03130,
                     ECO:0000269|PubMed:23071318; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q8K341,
                     ECO:0000255|HAMAP-Rule:MF_03130; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Region          <195..324
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          196..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q8K341,
                     ECO:0000255|HAMAP-Rule:MF_03130; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q8K341,
                     ECO:0000255|HAMAP-Rule:MF_03130; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Region          252..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6MG11; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            305
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K341; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Region          306..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     Site            323
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5SQI0.1)"
     CDS             1..421
                     /gene="ATAT1"
                     /gene_synonym="alpha-TAT; alpha-TAT1; C6orf134; MEC17;
                     Nbla00487; TAT"
                     /coded_by="NM_001413067.1:13..1278"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:79969"
                     /db_xref="HGNC:HGNC:21186"
                     /db_xref="MIM:615556"
ORIGIN      
        1 mefpfdvdal fperitvldq hlrpparrpg tttparvdlq qqimtiidel gkasakaqnl
       61 sapitsasrm qsnrhvvyil kdssarpagk gaiigfikvg ykklfvlddr eahneveplc
      121 ildfyihesv qrhghgrelf qymlqkerve phqlaidrps qkllkflnkh ynlettvpqv
      181 nnfvifegff ahqhrppaps lratrhsraa avdptpaapa rklppkraeg dikpysssdr
      241 eflkvavepp wplnraprra tppahppprs sslgnsperg plrpfvpeqe llrslrlcpp
      301 hptarlllaa dpggspaqrr rtrgtppglv aqsccysrhg gvnssspntg nqdskqgeqe
      361 tknrsaseeq alsqdgsgek pmhtappqap appaqswtvg gdilnarfir nlqerrstrp
      421 w
//
