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Information on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase and Organism(s) Mus musculus and UniProt Accession Q8K341
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2.3.1.108 alpha-tubulin N-acetyltransferaseIUBMB Comments
The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of alpha-tubulin.
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Word Map
- 2.3.1.108
- trna
- histone
- chromatin
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anticodons
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wobble
- trnamet
- microtubule
- dysautonomia
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aminoacylated
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formylation
- cbp
- aminoacyl-trnas
- kluyveromyces
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zymocin
- methionyl-trna
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ikbkap
- trnaphe
- nua4
- rnapii
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six-subunit
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p-site
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non-histone
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complex-associated
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
elongator, lysine acetyltransferase, atat1, mec-17, tubulin acetyltransferase, alpha-tubulin acetyltransferase, atat-2, alpha-tubulin n-acetyltransferase 1, alpha-tubulin n-acetyltransferase, alpha-tubulin acetylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-CoA:alpha-tubulin-L-lysine Ne-acetyltransferase
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alpha-tubulin acetylase
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alpha-tubulin acetyltransferase
alpha-tubulin acetyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[alpha-tubulin]-L-lysine N6-acetyltransferase
The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of alpha-tubulin.
CAS REGISTRY NUMBER
COMMENTARY
99889-90-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [alpha-TAT1]-L-lysine
CoA + [alpha-TAT1]-N6-acetyl-L-lysine
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enzyme TAT1 acetylates itself in a regulatory mechanism that is required for effective modification of tubulin. Acetylation of multiple lysine residues on itself
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acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
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acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40
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additional information
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recombinant GST-MEC-17 directly acetylates purified tubulin from the MEC17-KO strain in vitro
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
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macrophages challenged by bacterial lipopolysaccharides undergo extensive microtubule acetylation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
acetylation of alpha-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on alpha-tubulin acetylation
strongest expression in nervous systems of embryonic and adult mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
physiological function
acetylation of alpha-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on alpha-tubulin acetylation. Acetylation of alpha-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 and HDAC6. Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells. Katanin, a microtubule-severing protein with enhanced activity on acetylated alpha-tubulin, is actively involved in adipogenesis
physiological function
alphaTAT1 promotes microtubule destabilization and accelerates microtubule dynamics. This effect persists in an alphaTAT1 mutant with no acetyltransferase activity, suggesting that interaction of alphaTAT1 with microtubules is the critical factor regulating microtubule stability
physiological function
mice with a targeted deletion of Atat1 display a loss of detectable K40 alpha-tubulin acetylation across multiple tissues and in cellular structures such as cilia and axons where acetylation is normally enriched. Mice are viable and develop normally, however, the absence of Atat1 impacts upon sperm motility and male mouse fertility, and increases microtubule stability
physiological function
exposure of primary mouse cortical neurons to soluble chondroitin sulfate proteoglycans and myelin-associated glycoprotein substrates causes an acute and RhoA-kinase-dependent reduction in alpha-tubulin acetylation and Atat1 protein levels, without changes to either axonal histone deacetylase-6 levels or histonedeacetylase-6 activity. The chondroitin sulfate proteoglycans and myelin-associated glycoprotein-induced reduction in Atat1 occurs primarily in the distal and middle regions of neurites and reconstitution of Atat1, either by Rho-associated kinase inhibition or lentiviral-mediated Atat1 overexpression, can restore neurite growth. Chondroitin sulfate proteoglycans and myelin-associated glycoprotein signaling decreases Atat1 levels posttranscriptionally via a Rho-associated kinase-dependent increase in Atat1 protein turnover
physiological function
protein p27Kip1 controls the transport of vesicles and organelles along the axon of mice cortical projection neurons in vitro. p27Kip1 stabilizes the alpha-tubulin acetyltransferase 1, thereby promoting the acetylation of microtubules. Cortical extracts isolated from P0 p27Kip1 KO mice show a reduced level of acetylated alpha-tubulin, and the protein level of Atat1 is reduced upon loss of p27Kip1
physiological function
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the K40 residue of alpha-tubulin is important in vertebrates, MEC-17 controls the levels of microtubule acetylation in mammalian cells
physiological function
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macrophages challenged by bacterial lipopolysaccharides undergo extensive microtubule acetylation. Suppression of lipopolysaccharide-induced microtubule acetylation by inactivating the tubulin acetyltransferase, MEC17, profoundly inhibits the induction of anti-inflammatory interlukin-10, a phenotype effectively reversed by an acetylation-mimicking alpha-tubulin mutant. Reversible microtubule acetylation is a kinase signaling modulator and a key component in the inflammatory response
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ATAT_MOUSE
421
0
47164
Swiss-Prot
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
enzyme catalyzes acetylation of multiple lysine residues on itself. Autoacetylation of alphaTAT1 increases its catalytic activity at microtubules
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged Mec-17 from Escherichia coli strain BL21 by glutathione affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akella, J.S.; Wloga, D.; Kim, J.; Starostina, N.G.; Lyons-Abbott, S.; Morrissette, N.S.; Dougan, S.T.; Kipreos, E.T.; Gaertig, J.
MEC-17 is an alpha-tubulin acetyltransferase
Nature
467
218-222
2010
Caenorhabditis elegans, Chlamydomonas reinhardtii, Danio rerio, Mus musculus, Tetrahymena thermophila
Yang, W.; Guo, X.; Thein, S.; Xu, F.; Sugii, S.; Baas, P.; Radda, G.; Han, W.
Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of alpha-tubulin
Biochem. J.
449
605-612
2013
Mus musculus (Q8K341)
Kalebic, N.; Martinez, C.; Perlas, E.; Hublitz, P.; Bilbao-Cortes, D.; Fiedorczuk, K.; Andolfo, A.; Heppenstall, P.A.
Tubulin acetyltransferase alphaTAT1 destabilizes microtubules independently of its acetylation activity
Mol. Cell. Biol.
33
1114-1123
2013
Mus musculus (Q8K341)
Kalebic, N.; Sorrentino, S.; Perlas, E.; Bolasco, G.; Martinez, C.; Heppenstall, P.
alphaTAT1 is the major alpha-tubulin acetyltransferase in mice
Nat. Commun.
4
1962
2013
Mus musculus (Q8K341), Mus musculus
Wang, B.; Rao, Y.H.; Inoue, M.; Hao, R.; Lai, C.H.; Chen, D.; McDonald, S.L.; Choi, M.C.; Wang, Q.; Shinohara, M.L.; Yao, T.P.
Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production
Nat. Commun.
5
3479
2014
Mus musculus
Morelli, G.; Even, A.; Gladwyn-Ng, I.; Le Bail, R.; Shilian, M.; Godin, J.D.; Peyre, E.; Hassan, B.A.; Besson, A.; Rigo, J.M.; Weil, M.; Brone, B.; Nguyen, L.
p27Kip1 modulates axonal transport by regulating alpha-tubulin acetyltransferase 1 stability
Cell Rep.
23
2429-2442
2018
Mus musculus (Q8K341)
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