PIMT Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation. Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family. Ubiquitously expressed. High expression in heart, skeletal muscle, kidney, liver and placenta. Note: This description may include information from UniProtKB.
Protein type: EC 2.1.1.-; Methyltransferase; Nuclear receptor co-regulator; RNA processing
Chromosomal Location of human Ortholog: 8q12.1
Cellular Component:  Cajal body; cytoplasm; cytosol; nucleolus; nucleoplasm; nucleus; small nuclear ribonucleoprotein complex
Molecular Function:  protein binding; RNA methyltransferase activity; RNA trimethylguanosine synthase activity
Biological Process:  7-methylguanosine cap hypermethylation; 7-methylguanosine RNA capping; ribonucleoprotein complex biogenesis; spliceosomal snRNP assembly
Reference #:  Q96RS0 (UniProtKB)
Alt. Names/Synonyms: Cap-specific guanine-N2 methyltransferase; CLL-associated antigen KW-2; DKFZp762A163; FLJ22995; HCA137; Hepatocellular carcinoma-associated antigen 137; NCOA6IP; nuclear receptor coactivator 6 interacting protein; Nuclear receptor coactivator 6-interacting protein; PIMT; PIPMT; PRIP-interacting protein PIPMT; PRIP-interacting protein with methyltransferase domain; PRIP-interacting protein with methyltransferase motif; SEREX-defined; TGS1; Trimethylguanosine synthase; trimethylguanosine synthase 1; trimethylguanosine synthase homolog (S. cerevisiae)
Gene Symbols: TGS1
Molecular weight: 96,620 Da
Basal Isoelectric point: 4.84  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

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