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Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

TUT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
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

Enzyme and pathway databases

BioCyciZFISH:G66-32486-MONOMER.

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

HGNCiHGNC:26184. TUT1.

Subcellular locationi

GO - Cellular componenti

  • intercellular bridge Source: HPA
  • nuclear speck Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: HPA
Complete GO annotation...

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

HPAiHPA039253.

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122325. 27 interactors.
DIPiDIP-53651N.
IntActiQ9H6E5. 14 interactors.
MINTiMINT-7900460.
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 – 75Combined sources7
Helixi76 – 78Combined sources3
Beta strandi82 – 87Combined sources6
Beta strandi89 – 91Combined sources3
Beta strandi94 – 101Combined sources8
Helixi102 – 109Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5GNMR-A55-141[»]
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
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)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

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

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 rs3197865dbSNPEnsembl.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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5GNMR-A55-141[»]
ProteinModelPortaliQ9H6E5.
SMRiQ9H6E5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122325. 27 interactors.
DIPiDIP-53651N.
IntActiQ9H6E5. 14 interactors.
MINTiMINT-7900460.
STRINGi9606.ENSP00000308000.

PTM databases

iPTMnetiQ9H6E5.
PhosphoSitePlusiQ9H6E5.

Polymorphism and mutation databases

BioMutaiTUT1.
DMDMi126302611.

Proteomic databases

EPDiQ9H6E5.
MaxQBiQ9H6E5.
PaxDbiQ9H6E5.
PeptideAtlasiQ9H6E5.
PRIDEiQ9H6E5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi64852.
DisGeNETi64852.
GeneCardsiTUT1.
HGNCiHGNC:26184. TUT1.
HPAiHPA039253.
MIMi610641. gene.
neXtProtiNX_Q9H6E5.
OpenTargetsiENSG00000149016.
PharmGKBiPA162407405.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2277. Eukaryota.
COG5260. LUCA.
GeneTreeiENSGT00550000074490.
HOGENOMiHOG000115998.
HOVERGENiHBG079670.
InParanoidiQ9H6E5.
KOiK18709.
PhylomeDBiQ9H6E5.

Enzyme and pathway databases

BioCyciZFISH:G66-32486-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9H6E5.
GenomeRNAii64852.
PROiQ9H6E5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149016.
CleanExiHS_TUT1.
ExpressionAtlasiQ9H6E5. baseline and differential.
GenevisibleiQ9H6E5. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTPAP_HUMAN
AccessioniPrimary (citable) accession number: Q9H6E5
Secondary accession number(s): A1A527
, A8K995, Q2NL65, Q7L583, Q9H6H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 20, 2007
Last modified: November 2, 2016
This is version 124 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.