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Protein

Alpha-tubulin N-acetyltransferase 1

Gene

Atat1

Organism
Rattus norvegicus (Rat)
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 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
Sitei58 – 581Crucial for catalytic activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-RNO-5617833. 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:Atat1
Synonyms:Mec17
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi1303066. 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

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Alpha-tubulin N-acetyltransferase 1PRO_0000348068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-acetyllysine; by autocatalysisUniRule annotationBy similarity
Modified residuei146 – 1461N6-acetyllysine; by autocatalysisUniRule annotationBy similarity
Modified residuei233 – 2331N6-acetyllysine; by autocatalysisUniRule annotationBy similarity
Modified residuei244 – 2441N6-acetyllysine; by autocatalysisUniRule annotationBy similarity
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineCombined sources

Post-translational modificationi

Autoacetylation strongly increases tubulin acetylation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6MG11.
PRIDEiQ6MG11.

PTM databases

iPTMnetiQ6MG11.
PhosphoSiteiQ6MG11.

Expressioni

Gene expression databases

ExpressionAtlasiQ6MG11. baseline and differential.
GenevisibleiQ6MG11. RN.

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 annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001065.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 13714Acetyl-CoA bindingUniRule annotationAdd
BLAST
Regioni160 – 16910Acetyl-CoA bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4601. Eukaryota.
ENOG4111Q8H. LUCA.
GeneTreeiENSGT00390000008276.
HOVERGENiHBG055797.
InParanoidiQ6MG11.
KOiK19573.
OMAiPMHTAPP.
OrthoDBiEOG76739W.
PhylomeDBiQ6MG11.
TreeFamiTF315643.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
HAMAPiMF_03130. mec17.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR007965. GNAT_ATAT.
[Graphical view]
PfamiPF05301. Acetyltransf_16. 1 hit.
[Graphical view]
PROSITEiPS51730. GNAT_ATAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6MG11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL
60 70 80 90 100
GKASAKAQHL PAPITSALRM QSNRHVIYVL KDTSARPAGK GAIIGFLKVG
110 120 130 140 150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE
160 170 180 190 200
PHQLAIDRPS PKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRSPTPS
210 220 230 240 250
LRATRHSRAA VVDPIPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP
260 270 280 290 300
WPLNRAPRRA TPPAHPPPRS SSLGNSPDRG PLRPFVPEQE LLRSLRLCPP
310 320 330 340 350
HPTARLLLAT DPGGSPAQRR RTRETPWGLV AQSCHYSRHG GFNTSFLGTG
360 370 380 390 400
NQERKQGEQE AEDRSASEDQ VLLQDGSGEE PTHTVAPRAQ APPAQSWMVG
410 420
GDILNARVIR NLQERRNTRP W
Length:421
Mass (Da):47,327
Last modified:July 5, 2004 - v1
Checksum:i8AE25A0BD01279AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX883048 Genomic DNA. Translation: CAE84036.1.
RefSeqiNP_997663.1. NM_212498.1.
UniGeneiRn.136935.

Genome annotation databases

EnsembliENSRNOT00000001065; ENSRNOP00000001065; ENSRNOG00000000809.
ENSRNOT00000080419; ENSRNOP00000074047; ENSRNOG00000000809.
GeneIDi361789.
KEGGirno:361789.
UCSCiRGD:1303066. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX883048 Genomic DNA. Translation: CAE84036.1.
RefSeqiNP_997663.1. NM_212498.1.
UniGeneiRn.136935.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001065.

PTM databases

iPTMnetiQ6MG11.
PhosphoSiteiQ6MG11.

Proteomic databases

PaxDbiQ6MG11.
PRIDEiQ6MG11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001065; ENSRNOP00000001065; ENSRNOG00000000809.
ENSRNOT00000080419; ENSRNOP00000074047; ENSRNOG00000000809.
GeneIDi361789.
KEGGirno:361789.
UCSCiRGD:1303066. rat.

Organism-specific databases

CTDi79969.
RGDi1303066. Atat1.

Phylogenomic databases

eggNOGiKOG4601. Eukaryota.
ENOG4111Q8H. LUCA.
GeneTreeiENSGT00390000008276.
HOVERGENiHBG055797.
InParanoidiQ6MG11.
KOiK19573.
OMAiPMHTAPP.
OrthoDBiEOG76739W.
PhylomeDBiQ6MG11.
TreeFamiTF315643.

Enzyme and pathway databases

ReactomeiR-RNO-5617833. Assembly of the primary cilium.

Miscellaneous databases

PROiQ6MG11.

Gene expression databases

ExpressionAtlasiQ6MG11. baseline and differential.
GenevisibleiQ6MG11. RN.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
HAMAPiMF_03130. mec17.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR007965. GNAT_ATAT.
[Graphical view]
PfamiPF05301. Acetyltransf_16. 1 hit.
[Graphical view]
PROSITEiPS51730. GNAT_ATAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
    Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
    Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-276 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATAT_RAT
AccessioniPrimary (citable) accession number: Q6MG11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 80 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.