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Q1JPD6 (STPAP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Speckle targeted PIP5K1A-regulated poly(A) polymerase

Short name=Star-PAP
EC=2.7.7.19
Alternative name(s):
RNA-binding motif protein 21
Short name=RNA-binding protein 21
U6 snRNA-specific terminal uridylyltransferase 1
Short name=U6-TUTase
EC=2.7.7.52
Gene names
Name:TUT1
Synonyms:RBM21
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length871 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

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

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

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

Subunit structure

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.

Subcellular location

Nucleusnucleolus By similarity. Nucleus speckle By similarity.

Post-translational modification

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

Sequence similarities

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

Contains 1 C2H2-type zinc finger.

Contains 1 PAP-associated domain.

Contains 1 RRM (RNA recognition motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 871871Speckle targeted PIP5K1A-regulated poly(A) polymerase
PRO_0000254185

Regions

Domain56 – 12873RRM
Domain489 – 54759PAP-associated
Zinc finger16 – 4025C2H2-type
Compositional bias229 – 31082Pro-rich

Sites

Metal binding2161Magnesium or manganese; catalytic By similarity
Metal binding2181Magnesium or manganese; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1JPD6 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: E681018AFBA18459

FASTA87193,811
        10         20         30         40         50         60 
MAAVDSDIEP LPRGGFRCCL CHITTANQPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV 

        70         80         90        100        110        120 
SGFPRDVDST QLSEYFQAFG PVASVVMDKD KGVFAIVEMG DLGAREAVLS QPQHSLGGRR 

       130        140        150        160        170        180 
LRVRPREQIE FQSPASRSPK RVAPDSHQLI KALAEAPDVE AQMVKLVGLR ELSEAERQLR 

       190        200        210        220        230        240 
SLVVALMQEV FAEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLDEPQ PAPKAPESPS 

       250        260        270        280        290        300 
LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFEA PSSSLAPRTP DSALASETLA 

       310        320        330        340        350        360 
SPRSLPPASP LQEDQGDGDQ GKAVELAEAL KGEKAEGGAM LELVGSILRG CVPGVYRVQT 

       370        380        390        400        410        420 
VPSARCPVVK FCHRPSGLHG DISLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR 

       430        440        450        460        470        480 
GLSGSGPLLN NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEQVEVDGWD CSFPRDASRL 

       490        500        510        520        530        540 
EPSTNKEPLS SLLAQFFSCV SCWDLRGSLL SLREGQALSV AGGLPSNLSE GLRLGPMNLQ 

       550        560        570        580        590        600 
DPFDLSHNVA ANVTSRVAGR LQNCCRAAAN YCRSLQYQRR SSRGRDWGLL PLLQPSSPSS 

       610        620        630        640        650        660 
ILSATPIPLP PASFTQLTAV LAQVLREALG CHIEQGTKRL RSEGGGPGEP PQGGTSKRAK 

       670        680        690        700        710        720 
LDGQKKSCEE GPEEQQGCAG EHGEDGVEEM VIEVGESVQD WVMRSPGQLG ELPLMTGKHL 

       730        740        750        760        770        780 
ATREEGQSGT AALAKQGPRG PEAACEGSQA EAEKRVSLTV SWRCALWHRV WQGRRRARRR 

       790        800        810        820        830        840 
LQQQIKEGGG SGAGSGAEWL ATEAQVTREL RGLSSTEQRP EAEPLLTFVA STSQADQSLT 

       850        860        870 
VTPLQDSQGL FPDLHHFLQV FLPQALRNLL K 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT025417 mRNA. Translation: ABF57373.1.
RefSeqNP_001073791.1. NM_001080322.1.
UniGeneBt.21690.

3D structure databases

ProteinModelPortalQ1JPD6.
SMRQ1JPD6. Positions 55-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000015724.

Proteomic databases

PRIDEQ1JPD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID616339.
KEGGbta:616339.

Organism-specific databases

CTD64852.

Phylogenomic databases

eggNOGCOG5260.
HOVERGENHBG079670.
InParanoidQ1JPD6.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR002058. PAP_assoc.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20900088.

Entry information

Entry nameSTPAP_BOVIN
AccessionPrimary (citable) accession number: Q1JPD6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families