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Protein

Alpha-tubulin N-acetyltransferase 1

Gene

ATAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Required for normal sperm flagellar function. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly.UniRule annotation3 Publications

Catalytic activityi

Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine.UniRule annotation1 Publication

Kineticsi

kcat is 2.2 h(-1) for the acetylation of polymerized tubulin (microtubules), 0.35 h(-1) for the acetylation of free tubulin, and 1.47 h(-1)with acetyl-CoA as substrate.

  1. KM=2.0 µM for free alpha-tubulin2 Publications
  2. KM=1.6 µM for polymerized tubulin (microtubules)2 Publications
  3. KM=2.2 µM for acetyl-CoA2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei58 – 581Crucial for catalytic activity

    GO - Molecular functioni

    • coenzyme binding Source: MGI
    • tubulin N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_268265. Assembly of the primary cilium.

    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:ATAT1UniRule annotation
    Synonyms:C6orf134, MEC17UniRule annotation
    ORF Names:Nbla00487
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componentsi: Chromosome 6, Unplaced

    Organism-specific databases

    HGNCiHGNC:21186. ATAT1.

    Subcellular locationi

    GO - Cellular componenti

    • axon Source: UniProtKB-SubCell
    • coated pit Source: UniProtKB-SubCell
    • cytosol Source: Reactome
    • focal adhesion Source: UniProtKB-SubCell
    • microtubule bundle Source: Ensembl
    • mitotic spindle Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 581Q → A: Loss of acetyltransferase activity. 1 Publication
    Mutagenesisi61 – 611S → A: No effect on catalytic activity. 1 Publication
    Mutagenesisi64 – 641I → A: Strong reduction in acetyltransferase activity. 2 Publications
    Mutagenesisi69 – 691R → A: Strong reduction in acetyltransferase activity. 1 Publication
    Mutagenesisi105 – 1051F → A: Reduced activity. 1 Publication
    Mutagenesisi106 – 1061V → A: Reduced activity. 1 Publication
    Mutagenesisi107 – 1071L → A: Reduced activity. 1 Publication
    Mutagenesisi108 – 1081D → A: Reduced activity. 1 Publication
    Mutagenesisi109 – 1091D → A: Slight increase in activity. 1 Publication
    Mutagenesisi109 – 1091D → R: Marginal increase in activity. 1 Publication
    Mutagenesisi111 – 1111E → A: 2-fold increase in activity. 1 Publication
    Mutagenesisi111 – 1111E → R: No effect on catalytic activity. 1 Publication
    Mutagenesisi115 – 1151E → A: Reduced activity. 1 Publication
    Mutagenesisi117 – 1171E → A: Reduced activity. 1 Publication
    Mutagenesisi120 – 1201C → A or S: Strong reduction in microtubule acetylation. 1 Publication
    Mutagenesisi157 – 1571D → E or N: Strong reduction in microtubule acetylation. 2 Publications
    Mutagenesisi158 – 1581R → A: 20% of wild-type acetyltransferase activity. 1 Publication
    Mutagenesisi182 – 1821N → A: Strong reduction in activity. 1 Publication
    Mutagenesisi183 – 1831F → A: Strong reduction in activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134948212.

    Polymorphism and mutation databases

    BioMutaiATAT1.
    DMDMi74743537.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 421421Alpha-tubulin N-acetyltransferase 1PRO_0000348066Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-acetyllysine; by autocatalysisUniRule annotation
    Modified residuei146 – 1461N6-acetyllysine; by autocatalysisUniRule annotation
    Modified residuei233 – 2331N6-acetyllysine; by autocatalysisUniRule annotation
    Modified residuei244 – 2441N6-acetyllysine; by autocatalysisUniRule annotation

    Post-translational modificationi

    Autoacetylation strongly increases tubulin acetylation.UniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ5SQI0.
    PRIDEiQ5SQI0.

    PTM databases

    PhosphoSiteiQ5SQI0.

    Expressioni

    Gene expression databases

    BgeeiQ5SQI0.
    CleanExiHS_C6orf134.
    GenevisibleiQ5SQI0. HS.

    Organism-specific databases

    HPAiHPA046816.
    HPA050999.

    Interactioni

    Subunit structurei

    Component of the BBSome complex. Interacts with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-adaptin (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin acetylation, hence clathrin-coated pits are sites of microtubule acetylation.UniRule annotation4 Publications

    Protein-protein interaction databases

    BioGridi123036. 2 interactions.
    IntActiQ5SQI0. 1 interaction.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104Combined sources
    Beta strandi13 – 186Combined sources
    Helixi36 – 5722Combined sources
    Helixi67 – 726Combined sources
    Beta strandi76 – 816Combined sources
    Beta strandi93 – 1019Combined sources
    Beta strandi104 – 1074Combined sources
    Beta strandi109 – 1113Combined sources
    Beta strandi113 – 1164Combined sources
    Beta strandi119 – 1268Combined sources
    Helixi128 – 1303Combined sources
    Helixi135 – 14713Combined sources
    Helixi151 – 1533Combined sources
    Beta strandi155 – 1584Combined sources
    Helixi161 – 17111Combined sources
    Beta strandi182 – 1843Combined sources
    Turni187 – 1904Combined sources
    Helixi191 – 1944Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VWDX-ray1.25A1-194[»]
    3VWEX-ray1.96A1-194[»]
    4B5OX-ray1.05A1-196[»]
    4B5PX-ray1.60A/B1-196[»]
    4GS4X-ray2.11A2-236[»]
    4IF5X-ray1.70A1-193[»]
    4PK2X-ray1.35A1-194[»]
    4PK3X-ray1.35A1-194[»]
    ProteinModelPortaliQ5SQI0.
    SMRiQ5SQI0. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 190190N-acetyltransferase 1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 13714Acetyl-CoA bindingAdd
    BLAST
    Regioni160 – 16910Acetyl-CoA binding

    Sequence similaritiesi

    Belongs to the acetyltransferase ATAT1 family.UniRule annotation
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG249793.
    GeneTreeiENSGT00390000008276.
    HOVERGENiHBG055797.
    InParanoidiQ5SQI0.
    OMAiMHTAPPQ.
    OrthoDBiEOG76739W.
    PhylomeDBiQ5SQI0.
    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]
    PROSITEiPS51730. GNAT_ATAT. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 11 Publication (identifier: Q5SQI0-1) [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

            10         20         30         40         50
    MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL
    60 70 80 90 100
    GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG
    110 120 130 140 150
    YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE
    160 170 180 190 200
    PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS
    210 220 230 240 250
    LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP
    260 270 280 290 300
    WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP
    310 320 330 340 350
    HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG
    360 370 380 390 400
    NQDSKQGEQE TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG
    410 420
    GDILNARFIR NLQERRSTRP W
    Length:421
    Mass (Da):46,810
    Last modified:December 21, 2004 - v1
    Checksum:i6CC9B4B844930842
    GO
    Isoform 22 Publications (identifier: Q5SQI0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: Missing.
         13-36: ERITVLDQHLRPPARRPGTTTPAR → MWLTWPFCFLTITLREEGVCHLES

    Show »
    Length:409
    Mass (Da):45,574
    Checksum:iD2D140F7FADEDEEA
    GO
    Isoform 31 Publication (identifier: Q5SQI0-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         195-218: RPPAPSLRATRHSRAAAVDPTPAA → P

    Show »
    Length:398
    Mass (Da):44,458
    Checksum:i4E53964B391B8C4F
    GO
    Isoform 42 Publications (identifier: Q5SQI0-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         323-333: RGTPPGLVAQS → SSLPRSEESRY
         334-421: Missing.

    Show »
    Length:333
    Mass (Da):37,478
    Checksum:i9AF89C8C2FF122FC
    GO
    Isoform 52 Publications (identifier: Q5SQI0-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-421: Missing.

    Show »
    Length:323
    Mass (Da):36,342
    Checksum:iE3D8C0B120A640FB
    GO
    Isoform 61 Publication (identifier: Q5SQI0-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
         323-333: RGTPPGLVAQS → SSLPRSEESRY
         334-421: Missing.

    Show »
    Length:310
    Mass (Da):35,126
    Checksum:i1F8BD442CF9A9797
    GO
    Isoform 72 Publications (identifier: Q5SQI0-7) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
         324-421: Missing.

    Show »
    Length:300
    Mass (Da):33,990
    Checksum:i359BE466FD5562B1
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1212Missing in isoform 2. 2 PublicationsVSP_052899Add
    BLAST
    Alternative sequencei13 – 3624ERITV…TTPAR → MWLTWPFCFLTITLREEGVC HLES in isoform 2. 2 PublicationsVSP_052900Add
    BLAST
    Alternative sequencei195 – 21824RPPAP…PTPAA → P in isoform 3, isoform 6 and isoform 7. 2 PublicationsVSP_052901Add
    BLAST
    Alternative sequencei323 – 33311RGTPPGLVAQS → SSLPRSEESRY in isoform 4 and isoform 6. 3 PublicationsVSP_052902Add
    BLAST
    Alternative sequencei324 – 42198Missing in isoform 5 and isoform 7. 3 PublicationsVSP_052903Add
    BLAST
    Alternative sequencei334 – 42188Missing in isoform 4 and isoform 6. 3 PublicationsVSP_052904Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB075512 mRNA. Translation: BAE45758.1.
    AK023220 mRNA. Translation: BAB14472.1.
    AL845353 Genomic DNA. Translation: CAI41872.2.
    AL845353 Genomic DNA. Translation: CAI41875.2.
    AL662800 Genomic DNA. Translation: CAI18164.1.
    AL662800 Genomic DNA. Translation: CAI18165.1.
    AL662800 Genomic DNA. Translation: CAI18166.2.
    AL662800 Genomic DNA. Translation: CAI18167.2.
    AL662800 Genomic DNA. Translation: CAI18168.2.
    AL662800 Genomic DNA. Translation: CAM25498.1.
    AL732442 Genomic DNA. Translation: CAI17752.1.
    AL732442 Genomic DNA. Translation: CAI17753.1.
    AL732442 Genomic DNA. Translation: CAI17754.2.
    AL732442 Genomic DNA. Translation: CAI17755.1.
    AL732442 Genomic DNA. Translation: CAM25005.1.
    AL732442 Genomic DNA. Translation: CAM25006.1.
    AL845353 Genomic DNA. Translation: CAI41870.1.
    AL845353 Genomic DNA. Translation: CAI41871.1.
    AL845353 Genomic DNA. Translation: CAI41873.2.
    AL845353 Genomic DNA. Translation: CAI41874.2.
    BX119957 Genomic DNA. Translation: CAM25912.1.
    BX119957 Genomic DNA. Translation: CAM25913.1.
    BX119957 Genomic DNA. Translation: CAM25914.1.
    BX119957 Genomic DNA. Translation: CAM25915.1.
    BX119957 Genomic DNA. Translation: CAM25916.1.
    BX119957 Genomic DNA. Translation: CAM25917.1.
    BX908728 Genomic DNA. Translation: CAQ07413.1.
    BX908728 Genomic DNA. Translation: CAQ07414.1.
    BX908728 Genomic DNA. Translation: CAQ07415.1.
    BX908728 Genomic DNA. Translation: CAQ07416.1.
    BX908728 Genomic DNA. Translation: CAQ07417.1.
    BX908728 Genomic DNA. Translation: CAQ07418.1.
    CR753328 Genomic DNA. Translation: CAP58454.1.
    CR753328 Genomic DNA. Translation: CAP58455.1.
    CR753328 Genomic DNA. Translation: CAP58456.1.
    CR753328 Genomic DNA. Translation: CAP58457.1.
    CR753328 Genomic DNA. Translation: CAP58458.1.
    CR753328 Genomic DNA. Translation: CAP58459.1.
    CR759778 Genomic DNA. Translation: CAQ09406.1.
    CR759778 Genomic DNA. Translation: CAQ09407.1.
    CR759778 Genomic DNA. Translation: CAQ09408.1.
    CR759778 Genomic DNA. Translation: CAQ09409.1.
    CR759778 Genomic DNA. Translation: CAQ09410.1.
    CR759778 Genomic DNA. Translation: CAQ09411.1.
    CH471081 Genomic DNA. Translation: EAX03306.1.
    CH471081 Genomic DNA. Translation: EAX03307.1.
    BC006105 mRNA. Translation: AAH06105.1.
    BC047303 mRNA. Translation: AAH47303.1.
    AL833858 mRNA. Translation: CAD38717.1.
    CCDSiCCDS4683.2. [Q5SQI0-4]
    CCDS54978.1. [Q5SQI0-2]
    CCDS59002.1. [Q5SQI0-6]
    RefSeqiNP_001026892.1. NM_001031722.2. [Q5SQI0-2]
    NP_001241881.1. NM_001254952.1. [Q5SQI0-6]
    NP_079185.2. NM_024909.2. [Q5SQI0-4]
    XP_005249474.1. XM_005249417.1. [Q5SQI0-1]
    XP_005272955.1. XM_005272898.1. [Q5SQI0-1]
    XP_005275110.1. XM_005275053.1. [Q5SQI0-1]
    XP_005275245.1. XM_005275188.1. [Q5SQI0-1]
    XP_005275367.1. XM_005275310.1. [Q5SQI0-1]
    XP_005275540.1. XM_005275483.1. [Q5SQI0-1]
    XP_005275671.1. XM_005275614.1. [Q5SQI0-1]
    UniGeneiHs.654798.

    Genome annotation databases

    EnsembliENST00000318999; ENSP00000324222; ENSG00000137343. [Q5SQI0-7]
    ENST00000319027; ENSP00000324459; ENSG00000137343. [Q5SQI0-6]
    ENST00000329992; ENSP00000332374; ENSG00000137343. [Q5SQI0-4]
    ENST00000330083; ENSP00000327832; ENSG00000137343. [Q5SQI0-2]
    ENST00000376483; ENSP00000365666; ENSG00000137343. [Q5SQI0-5]
    ENST00000376485; ENSP00000365668; ENSG00000137343. [Q5SQI0-1]
    ENST00000383582; ENSP00000373076; ENSG00000206488. [Q5SQI0-2]
    ENST00000383583; ENSP00000373077; ENSG00000206488. [Q5SQI0-4]
    ENST00000383584; ENSP00000373078; ENSG00000206488. [Q5SQI0-7]
    ENST00000383585; ENSP00000373079; ENSG00000206488. [Q5SQI0-1]
    ENST00000400575; ENSP00000383419; ENSG00000206488. [Q5SQI0-5]
    ENST00000400576; ENSP00000383420; ENSG00000206488. [Q5SQI0-6]
    ENST00000411724; ENSP00000388617; ENSG00000234549. [Q5SQI0-5]
    ENST00000416435; ENSP00000412993; ENSG00000235658. [Q5SQI0-2]
    ENST00000416917; ENSP00000402998; ENSG00000234549. [Q5SQI0-7]
    ENST00000417183; ENSP00000393868; ENSG00000231257. [Q5SQI0-7]
    ENST00000418248; ENSP00000411362; ENSG00000231257. [Q5SQI0-5]
    ENST00000420586; ENSP00000411050; ENSG00000231257. [Q5SQI0-1]
    ENST00000423338; ENSP00000415000; ENSG00000223752. [Q5SQI0-7]
    ENST00000423654; ENSP00000403142; ENSG00000235658. [Q5SQI0-5]
    ENST00000424121; ENSP00000412198; ENSG00000223752. [Q5SQI0-6]
    ENST00000425448; ENSP00000391244; ENSG00000223752. [Q5SQI0-2]
    ENST00000428764; ENSP00000399509; ENSG00000235658. [Q5SQI0-4]
    ENST00000430611; ENSP00000409296; ENSG00000235658. [Q5SQI0-6]
    ENST00000432356; ENSP00000416994; ENSG00000234549. [Q5SQI0-1]
    ENST00000432643; ENSP00000416925; ENSG00000231257. [Q5SQI0-2]
    ENST00000442844; ENSP00000394914; ENSG00000235658. [Q5SQI0-1]
    ENST00000443114; ENSP00000405656; ENSG00000229061. [Q5SQI0-7]
    ENST00000443391; ENSP00000406071; ENSG00000229061. [Q5SQI0-6]
    ENST00000445486; ENSP00000398422; ENSG00000223752. [Q5SQI0-1]
    ENST00000445973; ENSP00000415408; ENSG00000231257. [Q5SQI0-6]
    ENST00000446100; ENSP00000393269; ENSG00000229061. [Q5SQI0-5]
    ENST00000448670; ENSP00000389129; ENSG00000229061. [Q5SQI0-2]
    ENST00000449905; ENSP00000399529; ENSG00000235658. [Q5SQI0-7]
    ENST00000450003; ENSP00000406421; ENSG00000223752. [Q5SQI0-4]
    ENST00000450220; ENSP00000405036; ENSG00000231257. [Q5SQI0-4]
    ENST00000454794; ENSP00000409067; ENSG00000229061. [Q5SQI0-1]
    ENST00000454987; ENSP00000410415; ENSG00000234549. [Q5SQI0-6]
    ENST00000456215; ENSP00000399452; ENSG00000234549. [Q5SQI0-4]
    ENST00000456704; ENSP00000394357; ENSG00000229061. [Q5SQI0-4]
    ENST00000457161; ENSP00000388171; ENSG00000223752. [Q5SQI0-5]
    ENST00000457334; ENSP00000398374; ENSG00000234549. [Q5SQI0-2]
    GeneIDi79969.
    KEGGihsa:79969.
    UCSCiuc003nqr.4. human. [Q5SQI0-4]
    uc003nqs.4. human. [Q5SQI0-6]
    uc003nqv.3. human. [Q5SQI0-2]
    uc003rdc.3. human. [Q5SQI0-1]
    uc003rdd.3. human. [Q5SQI0-7]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB075512 mRNA. Translation: BAE45758.1.
    AK023220 mRNA. Translation: BAB14472.1.
    AL845353 Genomic DNA. Translation: CAI41872.2.
    AL845353 Genomic DNA. Translation: CAI41875.2.
    AL662800 Genomic DNA. Translation: CAI18164.1.
    AL662800 Genomic DNA. Translation: CAI18165.1.
    AL662800 Genomic DNA. Translation: CAI18166.2.
    AL662800 Genomic DNA. Translation: CAI18167.2.
    AL662800 Genomic DNA. Translation: CAI18168.2.
    AL662800 Genomic DNA. Translation: CAM25498.1.
    AL732442 Genomic DNA. Translation: CAI17752.1.
    AL732442 Genomic DNA. Translation: CAI17753.1.
    AL732442 Genomic DNA. Translation: CAI17754.2.
    AL732442 Genomic DNA. Translation: CAI17755.1.
    AL732442 Genomic DNA. Translation: CAM25005.1.
    AL732442 Genomic DNA. Translation: CAM25006.1.
    AL845353 Genomic DNA. Translation: CAI41870.1.
    AL845353 Genomic DNA. Translation: CAI41871.1.
    AL845353 Genomic DNA. Translation: CAI41873.2.
    AL845353 Genomic DNA. Translation: CAI41874.2.
    BX119957 Genomic DNA. Translation: CAM25912.1.
    BX119957 Genomic DNA. Translation: CAM25913.1.
    BX119957 Genomic DNA. Translation: CAM25914.1.
    BX119957 Genomic DNA. Translation: CAM25915.1.
    BX119957 Genomic DNA. Translation: CAM25916.1.
    BX119957 Genomic DNA. Translation: CAM25917.1.
    BX908728 Genomic DNA. Translation: CAQ07413.1.
    BX908728 Genomic DNA. Translation: CAQ07414.1.
    BX908728 Genomic DNA. Translation: CAQ07415.1.
    BX908728 Genomic DNA. Translation: CAQ07416.1.
    BX908728 Genomic DNA. Translation: CAQ07417.1.
    BX908728 Genomic DNA. Translation: CAQ07418.1.
    CR753328 Genomic DNA. Translation: CAP58454.1.
    CR753328 Genomic DNA. Translation: CAP58455.1.
    CR753328 Genomic DNA. Translation: CAP58456.1.
    CR753328 Genomic DNA. Translation: CAP58457.1.
    CR753328 Genomic DNA. Translation: CAP58458.1.
    CR753328 Genomic DNA. Translation: CAP58459.1.
    CR759778 Genomic DNA. Translation: CAQ09406.1.
    CR759778 Genomic DNA. Translation: CAQ09407.1.
    CR759778 Genomic DNA. Translation: CAQ09408.1.
    CR759778 Genomic DNA. Translation: CAQ09409.1.
    CR759778 Genomic DNA. Translation: CAQ09410.1.
    CR759778 Genomic DNA. Translation: CAQ09411.1.
    CH471081 Genomic DNA. Translation: EAX03306.1.
    CH471081 Genomic DNA. Translation: EAX03307.1.
    BC006105 mRNA. Translation: AAH06105.1.
    BC047303 mRNA. Translation: AAH47303.1.
    AL833858 mRNA. Translation: CAD38717.1.
    CCDSiCCDS4683.2. [Q5SQI0-4]
    CCDS54978.1. [Q5SQI0-2]
    CCDS59002.1. [Q5SQI0-6]
    RefSeqiNP_001026892.1. NM_001031722.2. [Q5SQI0-2]
    NP_001241881.1. NM_001254952.1. [Q5SQI0-6]
    NP_079185.2. NM_024909.2. [Q5SQI0-4]
    XP_005249474.1. XM_005249417.1. [Q5SQI0-1]
    XP_005272955.1. XM_005272898.1. [Q5SQI0-1]
    XP_005275110.1. XM_005275053.1. [Q5SQI0-1]
    XP_005275245.1. XM_005275188.1. [Q5SQI0-1]
    XP_005275367.1. XM_005275310.1. [Q5SQI0-1]
    XP_005275540.1. XM_005275483.1. [Q5SQI0-1]
    XP_005275671.1. XM_005275614.1. [Q5SQI0-1]
    UniGeneiHs.654798.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VWDX-ray1.25A1-194[»]
    3VWEX-ray1.96A1-194[»]
    4B5OX-ray1.05A1-196[»]
    4B5PX-ray1.60A/B1-196[»]
    4GS4X-ray2.11A2-236[»]
    4IF5X-ray1.70A1-193[»]
    4PK2X-ray1.35A1-194[»]
    4PK3X-ray1.35A1-194[»]
    ProteinModelPortaliQ5SQI0.
    SMRiQ5SQI0. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi123036. 2 interactions.
    IntActiQ5SQI0. 1 interaction.

    PTM databases

    PhosphoSiteiQ5SQI0.

    Polymorphism and mutation databases

    BioMutaiATAT1.
    DMDMi74743537.

    Proteomic databases

    PaxDbiQ5SQI0.
    PRIDEiQ5SQI0.

    Protocols and materials databases

    DNASUi79969.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000318999; ENSP00000324222; ENSG00000137343. [Q5SQI0-7]
    ENST00000319027; ENSP00000324459; ENSG00000137343. [Q5SQI0-6]
    ENST00000329992; ENSP00000332374; ENSG00000137343. [Q5SQI0-4]
    ENST00000330083; ENSP00000327832; ENSG00000137343. [Q5SQI0-2]
    ENST00000376483; ENSP00000365666; ENSG00000137343. [Q5SQI0-5]
    ENST00000376485; ENSP00000365668; ENSG00000137343. [Q5SQI0-1]
    ENST00000383582; ENSP00000373076; ENSG00000206488. [Q5SQI0-2]
    ENST00000383583; ENSP00000373077; ENSG00000206488. [Q5SQI0-4]
    ENST00000383584; ENSP00000373078; ENSG00000206488. [Q5SQI0-7]
    ENST00000383585; ENSP00000373079; ENSG00000206488. [Q5SQI0-1]
    ENST00000400575; ENSP00000383419; ENSG00000206488. [Q5SQI0-5]
    ENST00000400576; ENSP00000383420; ENSG00000206488. [Q5SQI0-6]
    ENST00000411724; ENSP00000388617; ENSG00000234549. [Q5SQI0-5]
    ENST00000416435; ENSP00000412993; ENSG00000235658. [Q5SQI0-2]
    ENST00000416917; ENSP00000402998; ENSG00000234549. [Q5SQI0-7]
    ENST00000417183; ENSP00000393868; ENSG00000231257. [Q5SQI0-7]
    ENST00000418248; ENSP00000411362; ENSG00000231257. [Q5SQI0-5]
    ENST00000420586; ENSP00000411050; ENSG00000231257. [Q5SQI0-1]
    ENST00000423338; ENSP00000415000; ENSG00000223752. [Q5SQI0-7]
    ENST00000423654; ENSP00000403142; ENSG00000235658. [Q5SQI0-5]
    ENST00000424121; ENSP00000412198; ENSG00000223752. [Q5SQI0-6]
    ENST00000425448; ENSP00000391244; ENSG00000223752. [Q5SQI0-2]
    ENST00000428764; ENSP00000399509; ENSG00000235658. [Q5SQI0-4]
    ENST00000430611; ENSP00000409296; ENSG00000235658. [Q5SQI0-6]
    ENST00000432356; ENSP00000416994; ENSG00000234549. [Q5SQI0-1]
    ENST00000432643; ENSP00000416925; ENSG00000231257. [Q5SQI0-2]
    ENST00000442844; ENSP00000394914; ENSG00000235658. [Q5SQI0-1]
    ENST00000443114; ENSP00000405656; ENSG00000229061. [Q5SQI0-7]
    ENST00000443391; ENSP00000406071; ENSG00000229061. [Q5SQI0-6]
    ENST00000445486; ENSP00000398422; ENSG00000223752. [Q5SQI0-1]
    ENST00000445973; ENSP00000415408; ENSG00000231257. [Q5SQI0-6]
    ENST00000446100; ENSP00000393269; ENSG00000229061. [Q5SQI0-5]
    ENST00000448670; ENSP00000389129; ENSG00000229061. [Q5SQI0-2]
    ENST00000449905; ENSP00000399529; ENSG00000235658. [Q5SQI0-7]
    ENST00000450003; ENSP00000406421; ENSG00000223752. [Q5SQI0-4]
    ENST00000450220; ENSP00000405036; ENSG00000231257. [Q5SQI0-4]
    ENST00000454794; ENSP00000409067; ENSG00000229061. [Q5SQI0-1]
    ENST00000454987; ENSP00000410415; ENSG00000234549. [Q5SQI0-6]
    ENST00000456215; ENSP00000399452; ENSG00000234549. [Q5SQI0-4]
    ENST00000456704; ENSP00000394357; ENSG00000229061. [Q5SQI0-4]
    ENST00000457161; ENSP00000388171; ENSG00000223752. [Q5SQI0-5]
    ENST00000457334; ENSP00000398374; ENSG00000234549. [Q5SQI0-2]
    GeneIDi79969.
    KEGGihsa:79969.
    UCSCiuc003nqr.4. human. [Q5SQI0-4]
    uc003nqs.4. human. [Q5SQI0-6]
    uc003nqv.3. human. [Q5SQI0-2]
    uc003rdc.3. human. [Q5SQI0-1]
    uc003rdd.3. human. [Q5SQI0-7]

    Organism-specific databases

    CTDi79969.
    GeneCardsiGC06P030610.
    GC06Pj30584.
    GC06Pk30584.
    GC06Pl30639.
    GC06Pm30673.
    GC06Pn30584.
    GC06Po30586.
    H-InvDBHIX0166068.
    HIX0166337.
    HIX0166615.
    HIX0166865.
    HIX0167123.
    HIX0167356.
    HIX0184148.
    HGNCiHGNC:21186. ATAT1.
    HPAiHPA046816.
    HPA050999.
    MIMi615556. gene.
    neXtProtiNX_Q5SQI0.
    PharmGKBiPA134948212.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG249793.
    GeneTreeiENSGT00390000008276.
    HOVERGENiHBG055797.
    InParanoidiQ5SQI0.
    OMAiMHTAPPQ.
    OrthoDBiEOG76739W.
    PhylomeDBiQ5SQI0.
    TreeFamiTF315643.

    Enzyme and pathway databases

    ReactomeiREACT_268265. Assembly of the primary cilium.

    Miscellaneous databases

    GenomeRNAii79969.
    NextBioi69981.
    PROiQ5SQI0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ5SQI0.
    CleanExiHS_C6orf134.
    GenevisibleiQ5SQI0. HS.

    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]
    PROSITEiPS51730. GNAT_ATAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
      Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
      Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: NeuroblastomaImported.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
      Tissue: BrainImported and LungImported.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-421 (ISOFORM 4).
      Tissue: Brain.
    7. Cited for: FUNCTION, CATALYTIC ACTIVITY.
    8. "The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation."
      Shida T., Cueva J.G., Xu Z., Goodman M.B., Nachury M.V.
      Proc. Natl. Acad. Sci. U.S.A. 107:21517-21522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE BBSOME COMPLEX, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-157.
    9. Cited for: FUNCTION, INTERACTION WITH AP2A2, SUBCELLULAR LOCATION.
    10. "Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA."
      Taschner M., Vetter M., Lorentzen E.
      Proc. Natl. Acad. Sci. U.S.A. 109:19649-19654(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 1-196 IN COMPLEX WITH ACETYL-COA, MUTAGENESIS OF GLN-58; SER-61; ILE-64 AND ARG-158.
    11. "Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and implications for tubulin-specific acetylation."
      Friedmann D.R., Aguilar A., Fan J., Nachury M.V., Marmorstein R.
      Proc. Natl. Acad. Sci. U.S.A. 109:19655-19660(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 2-236 IN COMPLEX WITH ACETYL-COA, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ILE-64; ARG-69; PHE-105; VAL-106; LEU-107; ASP-108; ASP-109; GLU-111; GLU-115; GLU-117; CYS-120; ASP-157; ASN-182 AND PHE-183.

    Entry informationi

    Entry nameiATAT_HUMAN
    AccessioniPrimary (citable) accession number: Q5SQI0
    Secondary accession number(s): A2AB28
    , Q3LIB0, Q5JP39, Q5JP40, Q5JP42, Q5SQI1, Q5SU03, Q86X42, Q8NDK9, Q9BRS1, Q9H8X5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: December 21, 2004
    Last modified: June 24, 2015
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.