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Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

Tut1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

UTP + RNA(n) = diphosphate + RNA(n+1).
ATP + RNA(n) = diphosphate + RNA(n+1).

Cofactori

Mg2+By similarity, Mn2+By similarity

Enzyme regulationi

Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi216 – 2161Magnesium or manganese; catalyticBy similarity
Metal bindingi218 – 2181Magnesium or manganese; catalyticBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 4025C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. mRNA 3'-UTR binding Source: UniProtKB
  4. polynucleotide adenylyltransferase activity Source: UniProtKB
  5. RNA binding Source: UniProtKB
  6. RNA uridylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. mRNA cleavage Source: UniProtKB
  2. mRNA polyadenylation Source: UniProtKB
  3. snRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Speckle targeted PIP5K1A-regulated poly(A) polymerase (EC:2.7.7.19)
Short name:
Star-PAP
Alternative name(s):
RNA-binding motif protein 21
Short name:
RNA-binding protein 21
U6 snRNA-specific terminal uridylyltransferase 1 (EC:2.7.7.52)
Short name:
U6-TUTase
Gene namesi
Name:Tut1
Synonyms:Rbm21
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1561043. Tut1.

Subcellular locationi

Nucleusnucleolus By similarity. Nucleus speckle By similarity

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866Speckle targeted PIP5K1A-regulated poly(A) polymerasePRO_0000254188Add
BLAST

Post-translational modificationi

Phosphorylated by CK1 in the proline-rich (Pro-rich) region.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3MHT4.
PRIDEiQ3MHT4.

PTM databases

PhosphoSiteiQ3MHT4.

Expressioni

Gene expression databases

GenevestigatoriQ3MHT4.

Interactioni

Subunit structurei

Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction is direct. Interacts with PIP5K1A; interaction (By similarity).By similarity

Protein-protein interaction databases

BioGridi270623. 1 interaction.
IntActiQ3MHT4. 1 interaction.
STRINGi10116.ENSRNOP00000027187.

Structurei

3D structure databases

ProteinModelPortaliQ3MHT4.
SMRiQ3MHT4. Positions 55-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 12873RRMPROSITE-ProRule annotationAdd
BLAST
Domaini492 – 55059PAP-associatedAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi229 – 31183Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated
Contains 1 C2H2-type zinc finger.Curated
Contains 1 PAP-associated domain.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 4025C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
HOVERGENiHBG079670.
InParanoidiQ3MHT4.
KOiK18709.
OMAiREALGCH.
OrthoDBiEOG7353WD.
PhylomeDBiQ3MHT4.
TreeFamiTF354308.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3MHT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR
60 70 80 90 100
KAQGLRSVFV SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG
110 120 130 140 150
DISAREAVLS QPKHSLGGHT LRVRPREQKE FQSPASKSPK GVDSNSHQLA
160 170 180 190 200
QALAEAADVG AQMVKLVELR ELSEAERQLR TLVVALMQEV FTEFFPGCVV
210 220 230 240 250
HPFGSSVNSF DVHGCDLDLF LDLGDMEEPQ PDPQTPKLPE ASSLDSTLAS
260 270 280 290 300
SLDPQVLACT PASLDSLSPT SLQDSEALDF ETPSSLAPQT PDSALGSDTV
310 320 330 340 350
TSPQSLPPVS PLEEDRGEGK HRKELELAEA SKDEKEEATA VLELVGSILR
360 370 380 390 400
GCVPGVYRVQ TVPSARRPVV KFCHRPSGLH GDISLSNRLA LYNSRFLNLC
410 420 430 440 450
SEMDSRVRPL VYTLRCWAQH NGLSGGGPLL NNYALTLLVI YFLQTRDPPV
460 470 480 490 500
LPTVAQLTQR SGEGEQVEVD GWDCSFPKDA SRLEPSTNVE PLSSLLAQFF
510 520 530 540 550
SCVSCWDLSG SLLSLREGQA LMVAGGLPSD LWEGLRLGPM NLQDPFDLSH
560 570 580 590 600
NVAANVTSRV AKRLQSSCGA AASYCRSLQY QQRSSRGRDW GLLPLLQPSS
610 620 630 640 650
PSSLLSAKLI PLPSAPFPQI ITALVSVLRE ALGCHIEQGT KRRRSEGARS
660 670 680 690 700
KDSPLGGANK RPRLSGQEKS CEEGKEEPQG CAGDHSENEV EEMVIELRET
710 720 730 740 750
PQDWALLHCG PPGELPLMTA KCLDKTAEQN PMEPEGAGEG SPGETEKEAS
760 770 780 790 800
HPSSVSWRCA LWHQIWQGRR RARRRFQQQT KEEGRGGPST GAEWLAVEAR
810 820 830 840 850
VTQELKGPKS EQQRLQGEPL LTFVASASQA EQTLTVAPLQ DPQGLFPGLH
860
HFLQVFIPQA LKNLLK
Length:866
Mass (Da):94,378
Last modified:October 24, 2005 - v1
Checksum:iE85DE9E051D30412
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104695 mRNA. Translation: AAI04696.1.
RefSeqiNP_001029073.1. NM_001033901.1.
UniGeneiRn.129389.

Genome annotation databases

EnsembliENSRNOT00000027187; ENSRNOP00000027187; ENSRNOG00000020047.
GeneIDi499314.
KEGGirno:499314.
UCSCiRGD:1561043. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104695 mRNA. Translation: AAI04696.1.
RefSeqiNP_001029073.1. NM_001033901.1.
UniGeneiRn.129389.

3D structure databases

ProteinModelPortaliQ3MHT4.
SMRiQ3MHT4. Positions 55-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi270623. 1 interaction.
IntActiQ3MHT4. 1 interaction.
STRINGi10116.ENSRNOP00000027187.

PTM databases

PhosphoSiteiQ3MHT4.

Proteomic databases

PaxDbiQ3MHT4.
PRIDEiQ3MHT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027187; ENSRNOP00000027187; ENSRNOG00000020047.
GeneIDi499314.
KEGGirno:499314.
UCSCiRGD:1561043. rat.

Organism-specific databases

CTDi64852.
RGDi1561043. Tut1.

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
HOVERGENiHBG079670.
InParanoidiQ3MHT4.
KOiK18709.
OMAiREALGCH.
OrthoDBiEOG7353WD.
PhylomeDBiQ3MHT4.
TreeFamiTF354308.

Miscellaneous databases

NextBioi702524.
PROiQ3MHT4.

Gene expression databases

GenevestigatoriQ3MHT4.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiSTPAP_RAT
AccessioniPrimary (citable) accession number: Q3MHT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 30, 2006
Last sequence update: October 24, 2005
Last modified: February 3, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.