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Q6PH17

- ATAT_DANRE

UniProt

Q6PH17 - ATAT_DANRE

Protein

Alpha-tubulin N-acetyltransferase 1

Gene

atat1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May promote directional cell locomotion and chemotaxis By similarity. May be required for normal sperm flagellar function By similarity. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. Acetylates alpha-tubulin in neurons, but not in cilia.1 PublicationUniRule annotation

    Catalytic activityi

    Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei53 – 531Crucial for catalytic activity

    GO - Molecular functioni

    1. tubulin N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. alpha-tubulin acetylation Source: ZFIN
    2. neuron development Source: UniProtKB-HAMAP
    3. regulation of microtubule cytoskeleton organization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-tubulin N-acetyltransferase 1UniRule annotation (EC:2.3.1.108UniRule annotation)
    Short name:
    Alpha-TATUniRule annotation
    Short name:
    Alpha-TAT1UniRule annotation
    Short name:
    TATUniRule annotation
    Alternative name(s):
    Acetyltransferase mec-17 homologUniRule annotation
    Gene namesi
    Name:atat1
    Synonyms:mec17
    ORF Names:si:ch211-152p11.5, zgc:65893
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Chromosome 19

    Organism-specific databases

    ZFINiZDB-GENE-040426-2120. atat1.

    Subcellular locationi

    Cytoplasm UniRule annotation. Membraneclathrin-coated pit UniRule annotation. Cell junctionfocal adhesion UniRule annotation. Cell projectionaxon UniRule annotation. Cytoplasmcytoskeleton UniRule annotation. Cytoplasmcytoskeletonspindle UniRule annotation

    GO - Cellular componenti

    1. axon Source: UniProtKB-SubCell
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB-SubCell
    4. focal adhesion Source: UniProtKB-SubCell
    5. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Coated pit, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Morpholino knockdown of the protein causes developmental defects at 48 hours post-fertilization (hpf), including cilia curved body shape, short body axis, hydrocephalus, small head and small eyes. Morphants often do not respond, or have slow startle response, when probed with a needle, consistent with neuromuscular defects.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451L → A: Reduces activity to 30%. 1 Publication
    Mutagenesisi53 – 531Q → A: Reduces activity to 1.5%. 1 Publication
    Mutagenesisi117 – 1171D → A: Reduces activity to 3%. Causes the formation of a constitutive dimer in solution. 1 Publication
    Mutagenesisi126 – 1261R → E: Reduces activity to 19%. 1 Publication
    Mutagenesisi131 – 1311S → L: No effect. 1 Publication
    Mutagenesisi151 – 1511D → A: Reduces activity to 1%. 1 Publication
    Mutagenesisi154 – 1541S → A: Reduces activity to 8%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Alpha-tubulin N-acetyltransferase 1PRO_0000402067Add
    BLAST

    Expressioni

    Gene expression databases

    BgeeiQ6PH17.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000049367.

    Structurei

    Secondary structure

    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 44
    Helixi7 – 104
    Beta strandi13 – 208
    Helixi21 – 288
    Helixi35 – 5218
    Helixi62 – 676
    Beta strandi71 – 777
    Helixi80 – 834
    Beta strandi86 – 9510
    Beta strandi98 – 1014
    Beta strandi107 – 1104
    Beta strandi113 – 1208
    Helixi122 – 1243
    Helixi129 – 14113
    Helixi145 – 1473
    Beta strandi148 – 1525
    Helixi155 – 16511
    Beta strandi174 – 1796
    Helixi181 – 1833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4H6UX-ray2.45A/B1-188[»]
    4H6ZX-ray2.70A/B1-186[»]
    4HKFX-ray1.70A1-188[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni118 – 13114Acetyl-CoA bindingAdd
    BLAST
    Regioni154 – 16310Acetyl-CoA binding

    Sequence similaritiesi

    Belongs to the acetyltransferase ATAT1 family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG249793.
    GeneTreeiENSGT00390000008276.
    HOGENOMiHOG000257795.
    HOVERGENiHBG055797.
    InParanoidiQ6NZT0.
    OMAiKEENIHP.
    OrthoDBiEOG76739W.
    PhylomeDBiQ6PH17.
    TreeFamiTF315643.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    HAMAPiMF_03130. mec17.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR007965. Alpha-TAT.
    [Graphical view]
    PANTHERiPTHR12327. PTHR12327. 1 hit.
    PfamiPF05301. Mec-17. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PH17-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDFPYDLNAL FPERISVLDS NLSAGRKAHG RPDPLPQVTT VIDELGKASS    50
    KAQQLPAPIT SAAKLQANRH HLYLLKDGEQ NGGRGVIVGF LKVGYKKLFL 100
    LDQRGAHLET EPLCVLDFYV TETLQRHGYG SELFDFMLKH KQVEPAQMAY 150
    DRPSPKFLSF LEKRYDLRNS VPQVNNFVVF AGFFQSRSAV QLRKVPPRKP 200
    EGEIKPYSLM EREVVREEQR VLPWPFVRPG GPPHSPPLLP SSPQSRSLSV 250
    GSSPSRAPLR PAAATVLQQG QTPSSPLNDS CRAKRTSSLN RSRLSFH 297
    Length:297
    Mass (Da):33,202
    Last modified:July 5, 2004 - v1
    Checksum:i3F08861B19D635EB
    GO
    Isoform 2 (identifier: Q6PH17-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-297: AVQLRKVPPR...SLNRSRLSFH → GTPPSPLTDQ...LQGKTHQFSK

    Show »
    Length:305
    Mass (Da):33,198
    Checksum:iE6E63F28DE12E566
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei189 – 297109AVQLR…RLSFH → GTPPSPLTDQGMYGFFGPTE KSSPKKARGRDQTLFANGKR SGSGGAEGSPLAICSPRGSP PLSPSTSVISSIPFSQCGIL PQPGPASPRRGHGPPAGSDP LIPAQRQLQGKTHQFSK in isoform 2. 1 PublicationVSP_040229Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX511233 Genomic DNA. Translation: CAM56330.1.
    BC056749 mRNA. Translation: AAH56749.1.
    BC065981 mRNA. Translation: AAH65981.1.
    RefSeqiNP_998423.1. NM_213258.1. [Q6PH17-2]
    XP_005170079.1. XM_005170022.1. [Q6PH17-1]
    UniGeneiDr.6427.

    Genome annotation databases

    EnsembliENSDART00000049368; ENSDARP00000049367; ENSDARG00000004472. [Q6PH17-2]
    ENSDART00000103922; ENSDARP00000094698; ENSDARG00000004472. [Q6PH17-1]
    GeneIDi406389.
    KEGGidre:406389.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX511233 Genomic DNA. Translation: CAM56330.1 .
    BC056749 mRNA. Translation: AAH56749.1 .
    BC065981 mRNA. Translation: AAH65981.1 .
    RefSeqi NP_998423.1. NM_213258.1. [Q6PH17-2 ]
    XP_005170079.1. XM_005170022.1. [Q6PH17-1 ]
    UniGenei Dr.6427.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4H6U X-ray 2.45 A/B 1-188 [» ]
    4H6Z X-ray 2.70 A/B 1-186 [» ]
    4HKF X-ray 1.70 A 1-188 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000049367.

    Protocols and materials databases

    DNASUi 406389.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000049368 ; ENSDARP00000049367 ; ENSDARG00000004472 . [Q6PH17-2 ]
    ENSDART00000103922 ; ENSDARP00000094698 ; ENSDARG00000004472 . [Q6PH17-1 ]
    GeneIDi 406389.
    KEGGi dre:406389.

    Organism-specific databases

    CTDi 79969.
    ZFINi ZDB-GENE-040426-2120. atat1.

    Phylogenomic databases

    eggNOGi NOG249793.
    GeneTreei ENSGT00390000008276.
    HOGENOMi HOG000257795.
    HOVERGENi HBG055797.
    InParanoidi Q6NZT0.
    OMAi KEENIHP.
    OrthoDBi EOG76739W.
    PhylomeDBi Q6PH17.
    TreeFami TF315643.

    Miscellaneous databases

    NextBioi 20817998.

    Gene expression databases

    Bgeei Q6PH17.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    HAMAPi MF_03130. mec17.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR007965. Alpha-TAT.
    [Graphical view ]
    PANTHERi PTHR12327. PTHR12327. 1 hit.
    Pfami PF05301. Mec-17. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The zebrafish reference genome sequence and its relationship to the human genome."
      Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
      , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
      Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tuebingen.
    2. NIH - Zebrafish Gene Collection (ZGC) project
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Embryo.
    3. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    4. "Molecular basis of the acetyltransferase activity of MEC-17 towards alpha-tubulin."
      Li W., Zhong C., Li L., Sun B., Wang W., Xu S., Zhang T., Wang C., Bao L., Ding J.
      Cell Res. 22:1707-1711(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-188 IN COMPLEX WITH ACETYL-COA, MUTAGENESIS OF GLN-53.
    5. "Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus."
      Kormendi V., Szyk A., Piszczek G., Roll-Mecak A.
      J. Biol. Chem. 287:41569-41575(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-188 OF WILD-TYPE AND OF MUTANT ALA-117 IN COMPLEX WITH ACETYL-COA, SUBUNIT, MUTAGENESIS OF LEU-45; ASP-117; ARG-126; SER-131; ASP-151 AND SER-154.

    Entry informationi

    Entry nameiATAT_DANRE
    AccessioniPrimary (citable) accession number: Q6PH17
    Secondary accession number(s): Q6NZT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3