Primary Information |
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BoMiProt ID | Bomi9424 |
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Protein Name | Speckle targeted PIP5K1A-regulated poly(A) polymerase/RNA-binding motif protein 21/U6 snRNA-specific terminal uridylyltransferase 1 |
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Organism | Bos taurus |
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Uniprot ID | Q1JPD6 |
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Milk Fraction | Whey,MFGM |
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Ref Sequence ID | NP_001073791.1 |
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Aminoacid Length | 871 |
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Molecular Weight | 93811 |
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FASTA Sequence |
Download |
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Gene Name | TUT1/RBM21 |
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Gene ID | 616339 |
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Protein Existence Status | reviewed |
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Secondary Information |
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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. |
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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. |
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PTMs | Phosphorylation,Deubiquitination |
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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 |
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Predicted Disorder Regions | 131-143, 233-321, 648-702, 722-752, 787-794, 814-817 |
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DisProt Annotation | n |
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TM Helix Prediction | No TM helices |
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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. |
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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. |