Thiamine-triphosphatase (THTPA)
The protein contains 230 amino acids for an estimated molecular weight of 25566 Da.
Hydrolase highly specific for thiamine triphosphate (ThTP). (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs34015250 |
The reference OMIM entry for this protein is 611612
Thiamine triphosphatase; thtpa
Thtpase
DESCRIPTION
Thiamine triphosphatase (THTPA) catalyzes the hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), which is the major cellular form of thiamine (vitamin B1) (Lakaye et al., 2002).CLONING
By database analysis using peptide sequence from purified bovine soluble thiamine triphosphate as probe, followed by RT-PCR of human brain poly(A+) RNA, Lakaye et al. (2002) cloned THTPA. The deduced 230-amino acid protein has a predicted molecular mass of 25.55 kD and contains a high percentage of negatively-charged residues (17.4% glutamic acid and aspartic acid). THTPA shares 80% and 70% sequence identity with the bovine and macaque Thtpa enzymes, respectively. All 3 enzyme homologs contain several potential phosphorylation sites. Dot-blot hybridization of multiple human tissues detected widespread THTPA expression, but only at low levels. The highest hybridization signals were observed in uterus, testis, and prostate, followed by bladder, kidney, lung, and thyroid gland. Lower signals were detected in various brain regions with no detectable signal in cerebellum. Expression was particularly low in the digestive system, fetal tissues, and transformed cell lines.GENE FUNCTION
Lakaye et al. (2002) determined that both recombinant THTPA and native THTPA enzyme purified from human cerebellar cortex catalyzed the highly specific hydrolysis of thiamine triphosphate to thiamine diphosphate. THTPA displayed an optimal pH of 8.5, similar to that observed in the bovine enzyme, although the human enzyme had a broader pH spectrum. Lakaye et al. (2002) noted that human THTPA displayed remarkable insensitivity to chemical denaturation and proteolysis.MAPPING
By genomic sequence analysis, Lakaye et al. (2002) mapped the THTPA gene to chromosome 14. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 611612 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed