UniProt Accession

 THTPA_HUMAN; Q9BU02; D3DS50; G3V4J3 

Genbank Protein ID

 AF432862; AK057691; BX161435; BX378775; AL135999; CH471078; CH471078; BC002984 

Genbank Nucleotide ID

 AAM22403.1; BAB71546.1; CAD61907.1; EAW66140.1; EAW66141.1; AAH02984.1 

Protein Name

 Thiamine-triphosphatase 

Protein Synonyms/Alias

 ThTPase 

Gene Name

 THTPA 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
11	GLIEVERKFLPGPGT	ubiquitination	[1]
193	AQETAPAKLIVYLQR	acetylation	[2]
193	AQETAPAKLIVYLQR	ubiquitination	[1, 3, 4, 5, 6, 7]

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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] 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

 Hydrolase highly specific for thiamine triphosphate (ThTP). 

Sequence Annotation

 METAL 7 7 Magnesium (By similarity).
 METAL 9 9 Magnesium (By similarity).
 METAL 145 145 Magnesium (By similarity).
 METAL 157 157 Magnesium (By similarity).
 METAL 159 159 Magnesium (By similarity).
 BINDING 11 11 Substrate (By similarity).
 BINDING 55 55 Substrate (By similarity).
 BINDING 57 57 Substrate (By similarity).
 BINDING 65 65 Substrate (By similarity).
 BINDING 125 125 Substrate (By similarity).
 BINDING 193 193 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 230 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050333; F:thiamin-triphosphatase activity; IDA:UniProtKB.
 GO:0016311; P:dephosphorylation; IDA:UniProtKB.
 GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB.
 GO:0006772; P:thiamine metabolic process; TAS:UniProtKB. 

Interpro

 IPR023577; CYTH-like_domain.
 IPR012177; ThTPase. 

Pfam

 PF01928; CYTH 

SMART

  

PROSITE

  

PRINTS