Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5SQI0

- ATAT_HUMAN

UniProt

Q5SQI0 - ATAT_HUMAN

Protein

Alpha-tubulin N-acetyltransferase 1

Gene

ATAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.3 PublicationsUniRule annotation

    Catalytic activityi

    Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine.1 PublicationUniRule annotation

    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

    1. tubulin N-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. alpha-tubulin acetylation Source: UniProtKB-HAMAP
    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:ATAT1UniRule annotation
    Synonyms:C6orf134, MEC17UniRule annotation
    ORF Names:Nbla00487
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21186. ATAT1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Membraneclathrin-coated pit 1 PublicationUniRule annotation. Cell junctionfocal adhesion 1 PublicationUniRule 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

    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.

    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.
    GenevestigatoriQ5SQI0.

    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.4 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi123036. 3 interactions.
    IntActiQ5SQI0. 1 interaction.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliQ5SQI0.
    SMRiQ5SQI0. Positions 1-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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

    Phylogenomic databases

    eggNOGiNOG249793.
    HOVERGENiHBG055797.
    InParanoidiQ5SQI0.
    OMAiMFNARFI.
    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]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    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

    MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL    50
    GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 100
    YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 150
    PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS 200
    LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP 250
    WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP 300
    HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG 350
    NQDSKQGEQE TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG 400
    GDILNARFIR NLQERRSTRP W 421
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi74743537.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4683.2. [Q5SQI0-4 ]
    CCDS54978.1. [Q5SQI0-2 ]
    CCDS59002.1. [Q5SQI0-6 ]
    RefSeqi NP_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 ]
    UniGenei Hs.654798.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VWD X-ray 1.25 A 1-194 [» ]
    3VWE X-ray 1.96 A 1-194 [» ]
    4B5O X-ray 1.05 A 1-196 [» ]
    4B5P X-ray 1.60 A/B 1-196 [» ]
    4GS4 X-ray 2.11 A 2-236 [» ]
    4IF5 X-ray 1.70 A 1-193 [» ]
    ProteinModelPortali Q5SQI0.
    SMRi Q5SQI0. Positions 1-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123036. 3 interactions.
    IntActi Q5SQI0. 1 interaction.

    PTM databases

    PhosphoSitei Q5SQI0.

    Polymorphism databases

    DMDMi 74743537.

    Proteomic databases

    PaxDbi Q5SQI0.
    PRIDEi Q5SQI0.

    Protocols and materials databases

    DNASUi 79969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318999 ; 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 ]
    GeneIDi 79969.
    KEGGi hsa:79969.
    UCSCi uc003nqr.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

    CTDi 79969.
    GeneCardsi GC06P030605.
    GC06Pj30584.
    GC06Pk30584.
    GC06Pl30639.
    GC06Pm30673.
    GC06Pn30584.
    GC06Po30586.
    H-InvDB HIX0166068.
    HIX0166337.
    HIX0166615.
    HIX0166865.
    HIX0167123.
    HIX0167356.
    HIX0184148.
    HGNCi HGNC:21186. ATAT1.
    HPAi HPA046816.
    HPA050999.
    MIMi 615556. gene.
    neXtProti NX_Q5SQI0.
    PharmGKBi PA134948212.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249793.
    HOVERGENi HBG055797.
    InParanoidi Q5SQI0.
    OMAi MFNARFI.
    OrthoDBi EOG76739W.
    PhylomeDBi Q5SQI0.
    TreeFami TF315643.

    Miscellaneous databases

    GenomeRNAii 79969.
    NextBioi 69981.
    PROi Q5SQI0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5SQI0.
    CleanExi HS_C6orf134.
    Genevestigatori Q5SQI0.

    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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 85 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