Atat1
entrez
73242
canonical
uniprot
Q8K341
canonical
ensembl
ENSMUSG00000024426
resolver
ensp
ENSMUSP00000053853
resolver
ensp
ENSMUSP00000056383
resolver
ensp
ENSMUSP00000076703
resolver
ensp
ENSMUSP00000115004
resolver
ensp
ENSMUSP00000122715
resolver
ensp
ENSMUSP00000296350
resolver
genesymbol
Atat1
resolver
genesymbol_syn
Mec17
resolver
uniprot
B8JJ75
resolver
uniprot
B8JJ77
resolver
uniprot
Q3UZR9
resolver
uniprot
Q8BM67
resolver
uniprot
Q8C1D1
resolver
uniprot
Q8K2M7
resolver
uniprot_entry
ATAT_MOUSE
resolver
uniprot_sec
B8JJ75
resolver
uniprot_sec
B8JJ77
resolver
uniprot_sec
Q3UZR9
resolver
uniprot_sec
Q8BM67
resolver
uniprot_sec
Q8C1D1
resolver
uniprot_sec
Q8K2M7
resolver
amino_acid_sequence
MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARPAGKGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPTSSLRATRHSRAAVADPIPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPDRGPLRPFVPEQELLRSLRLCPPHPTARLLLATDPGGSPAQRRRTRGTPWGLVAQSCHYSRHGGFNTSFLGTGNQERKQGEQEAEDRSASEDRVLLLDGSGEEPTQTGAPRAQAPPPQSWTVGGDIMNARVIRNLQERRSTRPW
uniprot
proteins
ec_number
2.3.1.108
uniprot
proteins
function
FUNCTION: 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. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:23275437, ECO:0000269|PubMed:23720746, ECO:0000269|PubMed:23748901, ECO:0000269|PubMed:24097348}.
uniprot
proteins
mass_dalton
47164
uniprot
proteins
mutagenesis
MUTAGEN 56; /note="K->R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-146; R-233 and R-244."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 134; /note="G->W: Loss of catalytic activity, but function in microtubule stability not affected; when associated with W-136 and P-139."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 136; /note="G->W: Loss of activity, but function in microtubule stability not affected; when associated with W-134 and P-139."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 139; /note="L->P: Loss of activity, but function in microtubule stability not affected; when associated with W-134 and W-136."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 146; /note="K->R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-233 and R-244."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 233; /note="K->R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-244."; /evidence="ECO:0000269|PubMed:23275437"; MUTAGEN 244; /note="K->R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-233."; /evidence="ECO:0000269|PubMed:23275437
uniprot
proteins
post_translational_modification
PTM: Autoacetylation strongly increases tubulin acetylation. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}.
uniprot
proteins
protein_family
Acetyltransferase ATAT1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20829795
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23275437
uniprot
proteins
pubmed
23720746
uniprot
proteins
pubmed
23748901
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24097348
uniprot
proteins
pubmed
24129315
uniprot
proteins
sequence_length
421
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Note=In primary root dorsal ganglion neurons, localizes with acetylated tubulin in axons. Recruited to the mitotic spindle during cell division. {ECO:0000269|PubMed:23275437}.
uniprot
proteins