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Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

Tut1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Metal bindingi216Magnesium or manganese; catalyticBy similarity1
Metal bindingi218Magnesium or manganese; catalyticBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri16 – 40C2H2-typeAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, RNA-binding, Transferase
Biological processmRNA processing
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi1561043 Tut1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002541881 – 866Speckle targeted PIP5K1A-regulated poly(A) polymeraseAdd BLAST866

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei686PhosphoserineBy similarity1
Modified residuei741PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3MHT4
PRIDEiQ3MHT4

PTM databases

iPTMnetiQ3MHT4
PhosphoSitePlusiQ3MHT4

Expressioni

Gene expression databases

BgeeiENSRNOG00000020047
GenevisibleiQ3MHT4 RN

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 interactor
IntActiQ3MHT4, 1 interactor
STRINGi10116.ENSRNOP00000027187

Structurei

3D structure databases

ProteinModelPortaliQ3MHT4
SMRiQ3MHT4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 128RRMPROSITE-ProRule annotationAdd BLAST73
Domaini492 – 550PAP-associatedAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi229 – 311Pro-richAdd BLAST83

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri16 – 40C2H2-typeAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2277 Eukaryota
COG5260 LUCA
GeneTreeiENSGT00550000074490
HOVERGENiHBG079670
InParanoidiQ3MHT4
KOiK18709
OMAiFCHRPSG
OrthoDBiEOG091G091J
PhylomeDBiQ3MHT4
TreeFamiTF354308

Family and domain databases

CDDicd12279 RRM_TUT1, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR003604 Matrin/U1-like-C_Znf_C2H2
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR002058 PAP_assoc
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR034389 Star-PAP
IPR034388 Star-PAP_RRM
IPR036236 Znf_C2H2_sf
PANTHERiPTHR12271:SF11 PTHR12271:SF11, 1 hit
PfamiView protein in Pfam
PF03828 PAP_assoc, 1 hit
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SM00451 ZnF_U1, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
SSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

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 25, 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

Similar proteinsi

Entry informationi

Entry nameiSTPAP_RAT
AccessioniPrimary (citable) accession number: Q3MHT4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 25, 2005
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See 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

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