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Recombinant Human Alpha-tubulin N-acetyltransferase 1 (ATAT1)

Recombinant Human Alpha-tubulin N-acetyltransferase 1 (ATAT1)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

ATAT1

Purity

>85% (SDS-PAGE)

Target Names

ATAT1

Uniprot NO.

Q5SQI0

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-421

Target Protein Sequence

MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG NQDSKQGEQE TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG GDILNARFIR NLQERRSTRP W
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

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Target Background

Function(From Uniprot)

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. 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.

Gene References into Functions

these results demonstrate alphaTAT1 enters the lumen of microtubules from open extremities and spreads K40 acetylation marks longitudinally along cellular microtubules; this mode of tip-directed microtubule acetylation may allow for selective acetylation of subsets of microtubules PMID:27752143
Depletion of the tubulin acetyltransferase TAT1 led to a significant increase in the frequency of microtubule breakage. PMID:28428427
cellular quiescence induces Mec17 to couple the production of acetylated microtubules and Myh10, whose accumulation overcomes the inhibitory role of Myh9 and initiates ciliogenesis PMID:25494100
These results suggest that alphaTAT1-mediated Wnt1 expression via microtubule acetylation is important for colon cancer progression. PMID:27836544
Studies indicate that alpha-tubulin acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). PMID:26227334
Results suggest that lithium chloride (LiCl) treatments activate alpha-tubulin N-acetyltransferase 1 (alphaTAT1) by the inhibition of glycogen synthase kinase 3 beta (GSK-3beta) and promote the alpha-tubulin acetylation, and then elongate the primary cilia. PMID:24760594
Data suggest that invariant residues Arg132 and Ser160 in catalytic domain of ATAT1 participate in stable interaction with CoA and acetyl-CoA; ATAT1 with mutation at either residue exhibits much faster intracellular degradation. PMID:25602620
Crystal structure of the catalytic core of human MEC-17 in complex with acetyl-CoA. MEC17 has large, conserved surface patch that is critical for enzymatic activity suggesting extensive interactions with alpha-tubulin. PMID:24846647
Mechanistic underpinnings for TAT activity and its preference for microtubules with slow turnover; cocrystal structures constrain TAT action to the microtubule lumen with Lys40 engaged in a suboptimal active site; despite the confined location of Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. PMID:24906155
microtubules contacting clathrin-coated pits become acetylated by alphaTAT1; in migrating cells, this mechanism ensures the acetylation of microtubules oriented towards the leading edge, thus promoting directional cell locomotion and chemotaxis PMID:24097348
cysteine residues play important catalytic roles through a ternary complex mechanism. alphaTAT1 mutations have analogous effects on tubulin acetylation in vitro and in cells PMID:23071314
analysis reveals a basic patch implicated in substrate binding and a conserved glutamine residue required for catalysis, demonstrating that the family of alpha-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases PMID:23071318

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Subcellular Location

Cytoplasm. Membrane, clathrin-coated pit. Cell junction, focal adhesion. Cell projection, axon. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle.

Protein Families

Acetyltransferase ATAT1 family

Database Links

HGNC: 21186

UNIGENE: Hs.654798

KEGG: hsa:79969

STRING: 9606.ENSP00000327832

OMIM: 615556

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