Methionine adenosyltransferase
| methionine adenosyltransferase I, alpha | |
|---|---|
| Identifiers | |
| Symbol | MAT1A |
| Entrez | 4143 |
| HUGO | 6903 |
| OMIM | 250850 |
| RefSeq | NM_000429 |
| UniProt | Q00266 |
| Other data | |
| Locus | Chr. 10 q22 |
| methionine adenosyltransferase II, alpha | |
|---|---|
| Identifiers | |
| Symbol | MAT2A |
| Entrez | 4144 |
| HUGO | 6904 |
| OMIM | 601468 |
| RefSeq | NM_005911 |
| UniProt | P31153 |
| Other data | |
| Locus | Chr. 2 p11.2 |
| methionine adenosyltransferase II, beta | |
|---|---|
| Identifiers | |
| Symbol | MAT2B |
| Entrez | 27430 |
| HUGO | 6905 |
| OMIM | 605527 |
| RefSeq | NM_013283 |
| UniProt | Q9NZL9 |
| Other data | |
| Locus | Chr. 5 q34-q35 |
Methionine adenosyltransferase is an enzyme which catalyses the synthesis of S-adenosylmethionine (SAM) from methionine and ATP.
[edit] Conserved motifs in the 3'UTR of MAT2A mRNA
A computational comparative analysis of vertebrate genome sequences have identified a cluster of 6 conserved hairpin motifs in the 3'UTR of the MAT2A messenger RNA (mRNA) transcript.[1] The predicted hairpins (named A-F) have strong evolutionary conservation and 3 of the predicted RNA structures (hairpins A, C and D) have been confirmed by in-line probing analysis. No structural changes were observed for any of the hairpins in the presence of metabolites SAM, S-adenosylhomocysteine or L-Methioninine. They are proposed to be involved in transcript stability and their functionality is currently under investigation.[1]
[edit] References
- ^ a b Parker, B. J.; Moltke, I.; Roth, A.; Washietl, S.; Wen, J.; Kellis, M.; Breaker, R.; Pedersen, J. S. (2011). "New families of human regulatory RNA structures identified by comparative analysis of vertebrate genomes". Genome Research 21 (11): 1929–1943. doi:10.1101/gr.112516.110. PMC 3205577. PMID 21994249. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3205577.
[edit] External links
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