Search by BoMiProt ID - Bomi9424


Primary Information

BoMiProt ID Bomi9424
Protein Name Speckle targeted PIP5K1A-regulated poly(A) polymerase/RNA-binding motif protein 21/U6 snRNA-specific terminal uridylyltransferase 1
Organism Bos taurus
Uniprot IdQ1JPD6
Milk FractionWhey,MFGM
Ref Sequence Id NP_001073791.1
Aminoacid Length 871
Molecular Weight 93811
Fasta Sequence https://www.uniprot.org/uniprot/Q1JPD6.fasta
Gene Name TUT1/RBM21
Gene Id 616339
Protein Existence Status reviewed

Secondary Information

Protein Function Take part in RNA uridylylation .RNA uridylylation plays a pivotal role in the biogenesis and metabolism of functional RNAs, and regulates cellular gene expression.Does polyadenylation of a select set of mRNAs, such as HMOX1.TUT1 catalyzes oligo-uridylylation of U6 small nuclear (sn) RNA, which catalyzes mRNA splicing which is important for furthur U6 snRNA maturation,U4/U6-di-snRNP formation, and U6 snRNA recycling during mRNA splicing.
Biochemical Properties Exhibit template-independent uridylylation activity at 3'-end of specific RNAs.It is a multi-domain protein composed of an N-terminal ZF, N-terminal RRM, a catalytic motif in the middle, and an uncharacterized C-terminal domain.The catalytic motif is composed of nucleotidyltransferase domain and PAP-associated domain.The palm domain of human TUT1 consists of five-stranded β-sheets and two α-helices, and three catalytic carboxylates (Asp216, Asp218, and Asp381).The structure of TUT1 palm domain shares homology with those of DNA polymerase β family proteins.The finger domain has a helical structure with ten α-helices and three α-sheets, and is homologous to the central domain of PAPα.The incoming nucleotide is located in the cleft between the palm and fingers.
PTMs Phosphorylation,Deubiquitination
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q1JPD6|STPAP_BOVIN Speckle targeted PIP5K1A-regulated poly(A) polymerase OS=Bos taurus OX=9913 GN=TUT1 PE=2 SV=1 MAAVDSDIEPLPRGGFRCCLCHITTANQPSLDAHLGGRKHRHLVELRATRKAQGLRSVFV SGFPRDVDSTQLSEYFQAFGPVASVVMDKDKGVFAIVEMGDLGAREAVLSQPQHSLGGRR LRVRPREQIEFQSPASRSPKRVAPDSHQLIKALAEAPDVEAQMVKLVGLRELSEAERQLR SLVVALMQEVFAEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLDEPQPAPKAPESPS LDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFEAPSSSLAPRTPDSALASETLA SPRSLPPASPLQEDQGDGDQGKAVELAEALKGEKAEGGAMLELVGSILRGCVPGVYRVQT VPSARCPVVKFCHRPSGLHGDISLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGR GLSGSGPLLNNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEQVEVDGWDCSFPRDASRL EPSTNKEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALSVAGGLPSNLSEGLRLGPMNLQ DPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSS ILSATPIPLPPASFTQLTAVLAQVLREALGCHIEQGTKRLRSEGGGPGEPPQGGTSKRAK LDGQKKSCEEGPEEQQGCAGEHGEDGVEEMVIEVGESVQDWVMRSPGQLGELPLMTGKHL ATREEGQSGTAALAKQGPRGPEAACEGS*748QAEAEKRVSLTVSWRCALWHRVWQGRRRARRR LQQQIKEGGGSGAGSGAEWLATEAQVTRELRGLSSTEQRPEAEPLLTFVASTSQADQSLT VTPLQDSQGLFPDLHHFLQVFLPQALRNLLK
Predicted Disorder Regions 131-143, 233-321, 648-702, 722-752, 787-794, 814-817
DisProt Annotation n
TM Helix Prediction No TM helices
Significance of PTMs ubiquitin specific peptidase 15 (USP15), deubiquitinates terminal uridylyl transferase 1 (TUT1) at K63,which is imp for global RNA metabolism. deubiquitination promotes TUT1 redistribution to the nucleoplasm in a cell-specific manner.TUT1 deubiquitination increases an enzymatic activity of itself.Deubiquitinated TUT1 modifies U6 snRNA in the nucleoplasm and then stabilizes it. Phosphorylation is important for TUT1 activation.
Bibliography 1.Kim J, Nakamura J, Hamada C, Taketomi T, Yano S, Okajima T, Kashiwabara SI, Baba T, Sato B, Chiba T, Tsuruta F. USP15 Deubiquitinates TUT1 Associated with RNA Metabolism and Maintains Cerebellar Homeostasis. Mol Cell Biol. 2020 Oct 13;40(21):e00098-20. doi: 10.1128/MCB.00098-20. PMID: 32839293; PMCID: PMC7556847. 2.Yashiro Y, Tomita K. Function and Regulation of Human Terminal Uridylyltransferases. Front Genet. 2018 Nov 12;9:538. doi: 10.3389/fgene.2018.00538. PMID: 30483311; PMCID: PMC6240794.