UniProt Accession

 ATAT_HUMAN; Q5SQI0; A2AB28; Q3LIB0; Q5JP39; Q5JP40; Q5JP42; Q5SQI1; Q5SU03; Q86X42; Q8NDK9; Q9BRS1; Q9H8X5 

Genbank Protein ID

 AB075512; AK023220; AL845353; AL845353; AL662800; AL662800; AL662800; AL662800; AL662800; AL662800; AL732442; AL732442; AL732442; AL732442; AL732442; AL732442; AL845353; AL845353; AL845353; AL845353; BX119957; BX119957; BX119957; BX119957; BX119957; BX119957; BX908728; BX908728; BX908728; BX908728; BX908728; BX908728; CR753328; CR753328; CR753328; CR753328; CR753328; CR753328; CR759778; CR759778; CR759778; CR759778; CR759778; CR759778; CH471081; CH471081; BC006105; BC047303; AL833858 

Genbank Nucleotide ID

 BAE45758.1; BAB14472.1; CAI41872.2; CAI41875.2; CAI18164.1; CAI18165.1; CAI18166.2; CAI18167.2; CAI18168.2; CAM25498.1; CAI17752.1; CAI17753.1; CAI17754.2; CAI17755.1; CAM25005.1; CAM25006.1; CAI41870.1; CAI41871.1; CAI41873.2; CAI41874.2; CAM25912.1; CAM25913.1; CAM25914.1; CAM25915.1; CAM25916.1; CAM25917.1; CAQ07413.1; CAQ07414.1; CAQ07415.1; CAQ07416.1; CAQ07417.1; CAQ07418.1; CAP58454.1; CAP58455.1; CAP58456.1; CAP58457.1; CAP58458.1; CAP58459.1; CAQ09406.1; CAQ09407.1; CAQ09408.1; CAQ09409.1; CAQ09410.1; CAQ09411.1; EAX03306.1; EAX03307.1; AAH06105.1; AAH47303.1; CAD38717.1 

Protein Name

 Alpha-tubulin N-acetyltransferase 

Protein Synonyms/Alias

 Alpha-TAT; TAT; Acetyltransferase mec-17 homolog 

Gene Name

 ATAT1 

Gene Synonyms/Alias

 C6orf134; MEC17; Nbla00487 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
56	ELGKASAKAQNLSAP	ubiquitination	[1]
233	KRAEGDIKPYSSSDR	acetylation	[2, 3, 4]
380	SQDGSGEKPMHTAPP	acetylation	[4]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. 

Sequence Annotation

 REGION 124 137 Acetyl-CoA binding.
 REGION 160 169 Acetyl-CoA binding.  

Keyword

 3D-structure; Alternative splicing; Complete proteome; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 421 AA 

Protein Sequence

Gene Ontology

 GO:0019799; F:tubulin N-acetyltransferase activity; IMP:UniProtKB.
 GO:0071929; P:alpha-tubulin acetylation; IEA:InterPro.
 GO:0048666; P:neuron development; IEA:HAMAP.
 GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:HAMAP. 

Interpro

 IPR016181; Acyl_CoA_acyltransferase.
 IPR007965; Alpha-TAT. 

Pfam

 PF05301; Mec-17 

SMART

  

PROSITE

  

PRINTS