Methionine adenosyltransferase 2 subunit beta (MAT2B)
The protein contains 334 amino acids for an estimated molecular weight of 37552 Da.
Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine (PubMed:10644686, PubMed:23189196, PubMed:25075345). Can bind NADP (in vitro) (PubMed:23189196, PubMed:23425511). (updated: Oct. 25, 2017)
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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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:rs17849948 |
Biological Process
Methylation
One-carbon metabolic process
Regulation of catalytic activity
S-adenosylmethionine biosynthetic process
Small molecule metabolic process
Xenobiotic metabolic process
The reference OMIM entry for this protein is 605527
Methionine adenosyltransferase ii, beta; mat2b
DESCRIPTION
Methionine adenosyltransferase (MAT; EC 2.5.1.6) catalyzes the biosynthesis of S-adenosylmethionine (AdoMet) from methionine and ATP. MAT II is a broadly expressed MAT consisting of catalytic alpha and noncatalytic beta subunits encoded by MAT2A (601468) and MAT2B, respectively (summary by LeGros et al., 2000). For additional general information on MAT, see 601468.CLONING
LeGros et al. (2000) designed degenerate PCR primers to tryptic peptide sequence of MAT2B purified from human lymphocytes. They amplified a partial cDNA from Jurkat cells and extended the cDNA using 3-prime and 5-prime RACE. A full-length MAT2B cDNA amplified from normal human peripheral blood mononuclear cell RNA encodes a 334-amino acid protein with a molecular mass of 38 kD. LeGros et al. (2000) predicted 2 prominent hydrophobic segments from the sequence. MAT2B has sequence similarity with bacterial enzymes that catalyze the reduction of TDP-linked sugars; however, antibodies to MAT2B do not react with E. coli or yeast extracts. LeGros et al. (2000) expressed a recombinant histone-tagged MAT2B that had no MAT catalytic activity alone. However, the recombinant MAT2B associated spontaneously with the alpha subunit from human and E. coli, lowering the Km of MAT II for L-methionine, thus confirming a regulatory role for the beta subunit. ... More on the omim web site
Feb. 10, 2018: 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605527 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed