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RNGTT / HCAP

RNA guanylyltransferase and 5'-phosphatase

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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If you do not find the reagent or information you require, please contact Customer.Support@LSBio.com to inquire about additional products in development.

PLEASE NOTE

For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).