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Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

TUT1

Organism
Homo sapiens (Human)
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.3 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Enzyme regulationi

Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).1 Publication

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

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR binding Source: UniProtKB
  • polynucleotide adenylyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA uridylyltransferase activity Source: UniProtKB

GO - Biological processi

  • mRNA polyadenylation Source: UniProtKB
  • pre-mRNA cleavage required for polyadenylation Source: UniProtKB
  • snRNA processing Source: UniProtKB

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000149016.15
HGNCiHGNC:26184 TUT1
MIMi610641 gene
neXtProtiNX_Q9H6E5

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi216D → A: Abolishes adenylyltransferase activity; when associated with A-218. 1 Publication1
Mutagenesisi218D → A: Abolishes adenylyltransferase activity; when associated with A-216. 1 Publication1

Organism-specific databases

DisGeNETi64852
OpenTargetsiENSG00000149016
PharmGKBiPA162407405

Polymorphism and mutation databases

BioMutaiTUT1
DMDMi126302611

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002541861 – 874Speckle targeted PIP5K1A-regulated poly(A) polymeraseAdd BLAST874

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei750PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by CK1 in the proline-rich (Pro-rich) region.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H6E5
MaxQBiQ9H6E5
PaxDbiQ9H6E5
PeptideAtlasiQ9H6E5
PRIDEiQ9H6E5

PTM databases

iPTMnetiQ9H6E5
PhosphoSitePlusiQ9H6E5

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000149016
CleanExiHS_TUT1
ExpressionAtlasiQ9H6E5 baseline and differential
GenevisibleiQ9H6E5 HS

Organism-specific databases

HPAiHPA069055
HPA071838

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.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122325, 30 interactors
DIPiDIP-53651N
IntActiQ9H6E5, 17 interactors
MINTiQ9H6E5
STRINGi9606.ENSP00000308000

Structurei

Secondary structure

1874
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi57 – 61Combined sources5
Helixi69 – 76Combined sources8
Helixi77 – 79Combined sources3
Beta strandi82 – 87Combined sources6
Turni89 – 91Combined sources3
Beta strandi95 – 101Combined sources7
Helixi102 – 110Combined sources9
Beta strandi122 – 125Combined sources4
Helixi148 – 155Combined sources8
Beta strandi156 – 158Combined sources3
Helixi159 – 170Combined sources12
Helixi174 – 194Combined sources21
Beta strandi199 – 203Combined sources5
Helixi204 – 206Combined sources3
Beta strandi217 – 222Combined sources6
Helixi330 – 350Combined sources21
Beta strandi355 – 361Combined sources7
Beta strandi364 – 366Combined sources3
Beta strandi368 – 373Combined sources6
Turni374 – 377Combined sources4
Beta strandi378 – 385Combined sources8
Helixi388 – 402Combined sources15
Helixi406 – 419Combined sources14
Beta strandi423 – 429Combined sources7
Helixi431 – 443Combined sources13
Beta strandi444 – 447Combined sources4
Helixi453 – 459Combined sources7
Helixi479 – 481Combined sources3
Helixi491 – 504Combined sources14
Beta strandi510 – 513Combined sources4
Turni514 – 517Combined sources4
Beta strandi518 – 521Combined sources4
Beta strandi523 – 525Combined sources3
Helixi526 – 529Combined sources4
Beta strandi537 – 542Combined sources6
Turni551 – 554Combined sources4
Helixi557 – 574Combined sources18
Helixi577 – 580Combined sources4
Beta strandi584 – 586Combined sources3
Helixi591 – 595Combined sources5
Helixi600 – 606Combined sources7
Helixi616 – 628Combined sources13
Beta strandi629 – 631Combined sources3
Beta strandi634 – 636Combined sources3
Beta strandi764 – 770Combined sources7
Helixi778 – 791Combined sources14
Helixi805 – 812Combined sources8
Turni816 – 819Combined sources4
Beta strandi829 – 836Combined sources8
Beta strandi838 – 840Combined sources3
Beta strandi842 – 849Combined sources8
Beta strandi851 – 853Combined sources3
Helixi855 – 874Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5GNMR-A55-141[»]
5WU1X-ray2.80A/B141-874[»]
5WU2X-ray2.95A/B141-874[»]
5WU3X-ray2.70A/B141-874[»]
5WU4X-ray2.80A/B141-874[»]
5WU5X-ray3.40A/B/C/D141-874[»]
5WU6X-ray3.21A/B/C/D53-599[»]
ProteinModelPortaliQ9H6E5
SMRiQ9H6E5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H6E5

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 128RRMPROSITE-ProRule annotationAdd BLAST73
Domaini491 – 549PAP-associatedAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi229 – 310Pro-richAdd BLAST82

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
HOGENOMiHOG000115998
HOVERGENiHBG079670
InParanoidiQ9H6E5
KOiK18709
PhylomeDBiQ9H6E5

Family and domain databases

CDDicd12279 RRM_TUT1, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
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
SUPFAMiSSF54928 SSF54928, 1 hit
SSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

Sequencei

Sequence statusi: Complete.

Q9H6E5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR
60 70 80 90 100
KAQGLRSVFV SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG
110 120 130 140 150
DVGAREAVLS QSQHSLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLA
160 170 180 190 200
KALAEAADVG AQMIKLVGLR ELSEAERQLR SLVVALMQEV FTEFFPGCVV
210 220 230 240 250
HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS LDSALASPLD
260 270 280 290 300
PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA
310 320 330 340 350
SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG
360 370 380 390 400
CVPGVYRVQT VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS
410 420 430 440 450
ELDGRVRPLV YTLRCWAQGR GLSGSGPLLS NYALTLLVIY FLQTRDPPVL
460 470 480 490 500
PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS RLEPSINVEP LSSLLAQFFS
510 520 530 540 550
CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN LQDPFDLSHN
560 570 580 590 600
VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP
610 620 630 640 650
SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG
660 670 680 690 700
ESSQGGTSKR LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV
710 720 730 740 750
QDWAMQSPGQ PGDLPLTTGK HGAPGEEGQP SHAALAERGP KGHEAAQEWS
760 770 780 790 800
QGEAGKGASL PSSASWRCAL WHRVWQGRRR ARRRLQQQTK EGAGGGAGTR
810 820 830 840 850
AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD RMLTVTPLQD
860 870
PQGLFPDLHH FLQVFLPQAI RHLK
Length:874
Mass (Da):93,847
Last modified:February 20, 2007 - v2
Checksum:i85A4117A040FC90D
GO

Sequence cautioni

The sequence BAB15282 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66D → G in BAB15314 (PubMed:14702039).Curated1
Sequence conflicti809Q → R in BAF85299 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028833442L → F. Corresponds to variant dbSNP:rs3197865Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025920 mRNA Translation: BAB15282.1 Different initiation.
AK026000 mRNA Translation: BAB15314.1
AK292610 mRNA Translation: BAF85299.1
AP002990 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74029.1
BC005013 mRNA Translation: AAH05013.2
BC110910 mRNA Translation: AAI10911.1
BC128263 mRNA Translation: AAI28264.1
RefSeqiNP_073741.2, NM_022830.2
UniGeneiHs.728983

Genome annotation databases

EnsembliENST00000476907; ENSP00000419607; ENSG00000149016
GeneIDi64852
KEGGihsa:64852
UCSCiuc058cig.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSTPAP_HUMAN
AccessioniPrimary (citable) accession number: Q9H6E5
Secondary accession number(s): A1A527
, A8K995, Q2NL65, Q7L583, Q9H6H7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 20, 2007
Last modified: February 28, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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