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RNGTT is a non-receptor like tyrosine phosphatase. Mammalian capping enzymes are bifunctional proteins with both RNA 5 '- triphosphatase and guanylyltransferase activities. The N-terminal 237- aa triphosphatase domain contains (I/V)HCXXGXXR(S/T)G, a sequence corresponding to the conserved active-site motif in protein tyrosine phosphatases (PTPs). mRNA capping requires the sequential action of three enzymatic activities: RNA triphosphatase, guanylyl-transferase, and methyltransferase. The m7GpppN cap of eukaryotic mRNA is formed by a series of three enzymatic reactions in which the 5'-triphosphate end of nascent pre-mRNA is hydrolyzed to a 5'-diphosphate by RNA triphosphatase, then capped with GMP by GTP: RNA guanylyltransferase, and methylated by RNA (guanine-N7) methyltransferase. The human mRNA capping enzyme has two alternatively spliced isoforms of 597 and 541 aa that differ in their C-terminus.
Gene Name: | RNA guanylyltransferase and 5'-phosphatase |
Family/Subfamily: | Protein Phosphatase , Protein Phosphatase - Tyrosine non-receptor like other |
Synonyms: | RNGTT, CAP1A, HCAP, HCAP1, HCE, HCE1, MRNA-capping enzyme |
Target Sequences: | NM_003800 NP_003791.3 O60942 |
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