Prothymosin alpha (PTMA)
The protein contains 111 amino acids for an estimated molecular weight of 12203 Da.
Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. (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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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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Biological Process
Histone exchange
Negative regulation of apoptotic process
Transcription, DNA-templated
The reference OMIM entry for this protein is 188390
Prothymosin, alpha; ptma
Thymosin, alpha
CLONING
The thymus gland produces several hormones or hormone-like substances which are derived from a polypeptide precursor containing (in the rat) 113 amino acids and known as prothymosin-alpha. A peptide containing 28 amino acid residues, named thymosin-alpha-1, was originally isolated from calf thymosin fraction 5 and shown to restore various aspects of immune function in several in vitro and in vivo test systems. Thymosin-alpha-1 was subsequently isolated from a similar fraction from human thymosin and reported to have the same amino acid sequence as bovine thymosin-alpha-1. Haritos et al. (1984) isolated from fresh rat thymus a larger polypeptide named prothymosin-alpha, which contains the thymosin-alpha-1 sequence at its NH2 terminus. Prothymosin-alpha has also been isolated from human thymus. Goodall et al. (1986) constructed a cDNA library from human spleen mRNA and screened for clones containing cDNAs coding for prothymosin-alpha. Eschenfeldt and Berger (1986) identified cDNA clones for human prothymosin-alpha in cDNA libraries from staphylococcal endotoxin A-stimulated normal human lymphocytes. The encoded protein was found to be highly acidic (54 residues out of 111) and shared over 90% sequence homology with rat prothymosin-alpha. The peptide hormone thymosin-alpha-1 appeared at positions 2-29 of the prothymosin-alpha amino acid sequence. Manrow et al. (1992) concluded that of the 6 members of the prothymosin-alpha gene family that have been cloned and sequenced, only one is functional. Szabo et al. (1993) isolated a genomic clone encoding PTMA and subcloned and sequenced the 5-prime regulatory region.GENE FUNCTION
Jiang et al. (2003) identified a pathway that regulates mitochondria-initiated caspase activity. In this pathway, PHAP (600832) protein promoted caspase-9 (602234) activation after apoptosome formation, whereas PTMA negatively regulated caspase-9 activation by inhibiting apoptosome formation. A small molecular activator of caspase-3 (600636), PETCM, relieved PTMA inhibition and allowed apoptosome formation at a physiologic concentration of dATP. Elimination of PTMA expression by RNA interference sensitized cells to ultraviolet irradiation-induced apoptosis and negated the requirement of PETCM for caspase activation.MAPPING
Szabo et al. (1993) used a 5-prime flanking cloned probe to localize the prothymosin gene to human chromosome 2 by Southern analysis of somatic cell hybrids. ... 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 188390 was added.
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed