L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASDHPPT)
The protein contains 309 amino acids for an estimated molecular weight of 35776 Da.
Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A, regardless of whether the CoA is presented in the free thiol form or as an acetyl thioester, to a serine residue of a broad range of acceptors including the acyl carrier domain of FASN. (updated: Feb. 10, 2021)
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.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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The reference OMIM entry for this protein is 607756
Alpha-aminoadipate semialdehyde dehydrogenase-phosphopantetheinyl transferase; aasdhppt
Aasdppt
Lys5, s. cerevisiae, homolog of
Cgi-80
Dkfzp566e2346
DESCRIPTION
In mammals, L-lysine is first catabolized to alpha-aminoadipate semialdehyde by the bifunctional enzyme alpha-aminoadipate semialdehyde synthase (AASS; 605113), followed by a conversion to alpha-aminoadipate (AAA) by alpha-aminoadipate semialdehyde dehydrogenase (AASDH). In S. cerevisiae, which synthesize rather than degrade lysine, the latter activity requires 2 distinct genes. LYS2 encodes the alpha-aminoadipate reductase activity, while LYS5 encodes a phosphopantetheinyl transferase activity that is required to activate LYS2 protein.CLONING
Praphanphoj et al. (2001) identified a full-length human cDNA homologous to the yeast LYS5 gene. The cDNA contains an open reading frame of 930 basepairs predicted to encode 309 amino acids, and the human protein is 26% identical to its yeast counterpart. Northern blot analysis detected a single transcript of approximately 3 kb in all tissues except testis, where there was an additional transcript of 1.5 kb. Expression is highest in brain followed by heart and skeletal muscle, and to a lesser extent in liver.MAPPING
By FISH, Praphanphoj et al. (2001) mapped the human AASDPPT gene to chromosome 11q22.GENE FUNCTION
Praphanphoj et al. (2001) used complementation studies in a yeast knockout of LYS5 to demonstrate that the human homolog encodes alpha-aminoadipate dehydrogenase-phosphopantetheinyl transferase activity. Kasahara and Kato (2003) fed mice a lysine-rich diet (containing 2,000-fold more free lysine than normal) and found that blood concentrations of lysine and 2-aminoadipic acid (AAA) were markedly increased. The level of U26, or mouse aminoadipic 6-semialdehyde dehydrogenase (AASDH), in the liver and heart of lysine-loaded mice was significantly higher than in control mice. Mouse AASS and Lys5 transcripts were also increased in the lysine-loaded mice. Kasahara and Kato (2003) concluded that U26, as well as AASS and LYS5, is involved in the lysine degradation pathway in mice. They found that pyrroloquinoline quinone (PQQ) is a crucial redox cofactor in this reaction and qualifies as a newcomer to the B group of vitamins. ... More on the omim web site
Feb. 16, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607756 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed