RBM21 Highly specific terminal uridylyltransferase that exclusively accepts U6 snRNA as substrate. U6 snRNA is unique in that nucleotides are both added to and removed from its 3'-end. U6-TUTase is responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Does not play a role in replication-dependent histone mRNA degradation. Note: This description may include information from UniProtKB.
Protein type: EC; EC; Nucleolus; Transferase
Chromosomal Location of Human Ortholog: 11q12.3
Cellular Component:  cytosol; nuclear speck; nucleolus; nucleus
Molecular Function:  ATP binding; enzyme binding; metal ion binding; mRNA 3'-UTR binding; polynucleotide adenylyltransferase activity; protein binding; RNA binding; RNA uridylyltransferase activity
Biological Process:  mRNA polyadenylation; pre-mRNA cleavage required for polyadenylation; snRNA processing
Reference #:  Q9H6E5 (UniProtKB)
Alt. Names/Synonyms: FLJ21850; FLJ22267; FLJ22347; MGC131987; MGC149809; nuclear speckle targeted phosphatidylinositol 4-phosphate 5-kinase type I-alpha regulated-poly(A) polymerase; nuclear speckle-targeted PIPK1A-regulated-poly(A) polymerase; PAP-associated domain-containing 2; PAPD2; poly(A) polymerase associated domain containing 2; RBM21; RNA binding motif protein 21; RNA-binding motif protein 21; RNA-binding protein 21; Speckle targeted PIP5K1A-regulated poly(A) polymerase; STARPAP; terminal uridylyl transferase 1, U6 snRNA-specific; TUT1; TUTase; U6 snRNA-specific terminal uridylyltransferase 1; U6-TUTase
Gene Symbols: TUT1
Molecular weight: 93,847 Da
Basal Isoelectric point: 5.8  Predict pI for various phosphorylation states
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Protein Structure Not Found.

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