| Tag | Content |
|---|
| CPLM ID | CPLM-012957 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Speckle targeted PIP5K1A-regulated poly(A) polymerase |
Protein Synonyms/Alias | Star-PAP; RNA-binding motif protein 21; RNA-binding protein 21; U6 snRNA-specific terminal uridylyltransferase 1; U6-TUTase |
Gene Name | Tut1 |
Gene Synonyms/Alias | Rbm21 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 651 | RSEGARSKDSPLGGA | ubiquitination | [1] |
|
Reference | [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis. Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J. J Proteome Res. 2012 Sep 7;11(9):4722-32. [ PMID: 22871113] |
Functional Description | Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication- dependent histone mRNA degradation (By similarity). |
Sequence Annotation | DOMAIN 56 128 RRM.
DOMAIN 492 550 PAP-associated.
ZN_FING 16 40 C2H2-type.
METAL 216 216 Magnesium or manganese; catalytic (By
METAL 218 218 Magnesium or manganese; catalytic (By
MOD_RES 741 741 Phosphoserine (By similarity). |
Keyword | ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 866 AA |
Protein Sequence | MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV 60
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHT 120
LRVRPREQKE FQSPASKSPK GVDSNSHQLA QALAEAADVG AQMVKLVELR ELSEAERQLR 180
TLVVALMQEV FTEFFPGCVV HPFGSSVNSF DVHGCDLDLF LDLGDMEEPQ PDPQTPKLPE 240
ASSLDSTLAS SLDPQVLACT PASLDSLSPT SLQDSEALDF ETPSSLAPQT PDSALGSDTV 300
TSPQSLPPVS PLEEDRGEGK HRKELELAEA SKDEKEEATA VLELVGSILR GCVPGVYRVQ 360
TVPSARRPVV KFCHRPSGLH GDISLSNRLA LYNSRFLNLC SEMDSRVRPL VYTLRCWAQH 420
NGLSGGGPLL NNYALTLLVI YFLQTRDPPV LPTVAQLTQR SGEGEQVEVD GWDCSFPKDA 480
SRLEPSTNVE PLSSLLAQFF SCVSCWDLSG SLLSLREGQA LMVAGGLPSD LWEGLRLGPM 540
NLQDPFDLSH NVAANVTSRV AKRLQSSCGA AASYCRSLQY QQRSSRGRDW GLLPLLQPSS 600
PSSLLSAKLI PLPSAPFPQI ITALVSVLRE ALGCHIEQGT KRRRSEGARS KDSPLGGANK 660
RPRLSGQEKS CEEGKEEPQG CAGDHSENEV EEMVIELRET PQDWALLHCG PPGELPLMTA 720
KCLDKTAEQN PMEPEGAGEG SPGETEKEAS HPSSVSWRCA LWHQIWQGRR RARRRFQQQT 780
KEEGRGGPST GAEWLAVEAR VTQELKGPKS EQQRLQGEPL LTFVASASQA EQTLTVAPLQ 840
DPQGLFPGLH HFLQVFIPQA LKNLLK 866 |
Gene Ontology | GO:0016607; C:nuclear speck; ISS:UniProtKB. GO:0005730; C:nucleolus; ISS:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB. GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB. GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB. GO:0006379; P:mRNA cleavage; ISS:UniProtKB. GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB. GO:0016180; P:snRNA processing; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |