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D2HS90 (STPAP_AILME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
ORF Names:PANDA_014931
OrganismAiluropoda melanoleuca (Giant panda) [Reference proteome]
Taxonomic identifier9646 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeAiluropoda

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 869869Speckle targeted PIP5K1A-regulated poly(A) polymerase
PRO_0000404589

Regions

Domain56 – 12873RRM
Domain490 – 54859PAP-associated
Zinc finger16 – 4025C2H2-type
Compositional bias229 – 30981Pro-rich

Sites

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

Sequences

Sequence LengthMass (Da)Tools
D2HS90 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 01BB7E4572A16511

FASTA86994,063
        10         20         30         40         50         60 
MAAVDLDVQS LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV 

        70         80         90        100        110        120 
SGFPRDVDSA QLTQYFQAFG PVASVVMDKD KGVFAIVEMG DVGTREAVLS QPQHTLGGHR 

       130        140        150        160        170        180 
LRVRPREQKE FQSPASKSPK GAAPDSHQLT KALAEAPDVG AQMVKLVGLR ELSEAERQLR 

       190        200        210        220        230        240 
NLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEESQ PAPKAPESPS 

       250        260        270        280        290        300 
LDSALASPLD PQALACTPAS PPDSQPPSPQ DSEALDFETP SSSLAPQTPD SALASETLAS 

       310        320        330        340        350        360 
PQSLPPASPL QEDRGEGDLG KALELAEALS GEKTEGVAML ELVGSILRGC VPGVYRVQTV 

       370        380        390        400        410        420 
PSARRPVVKF CHRPSGLHGD VSLSNRLALH NSRFLSLCSE LDGRVRPLVY TLRCWAQGRG 

       430        440        450        460        470        480 
LSGSGPLLSN YALTLLVIYF LQTRDPPVLP TVSQLTQKAG EGEQVEVDGW DCSFPRDASG 

       490        500        510        520        530        540 
LEPSTNKEPL SSLLAQFFSC VSCWDLRGSL LSLREGQALP VAGDLPSNRW EGLRLGPMNL 

       550        560        570        580        590        600 
QDPFDLSHNV AANVTSRVAG RLQNSCQAAA NYCRSLQYQR RSSRGRDWGL LPLLQPSSPS 

       610        620        630        640        650        660 
SLLSATPIPL PPAPFTQLTA ALAQVLREAL GCHIEQGTKR LRSDRGGPEE SPQGGTSKRL 

       670        680        690        700        710        720 
KLDGEEKSCE EGREEQQGYI RDHSEDGVEE MVVEVGEMVQ DWVQSPGRPG EPPQMLREQL 

       730        740        750        760        770        780 
ATGEEGQSGH AALAEQGPKG PEAAREGSQG ETGRGVSLSS VSWRCALWHR VWQGRRRARR 

       790        800        810        820        830        840 
RLQQQTKERG RGSAGTAEWL AVEAQVTREL RGLSSAAQRP EAEPLLTFVA SASQVNQTLT 

       850        860 
VTPIQDSQGL FPDLHHFLQV FLPQALRNL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GL193267 Genomic DNA. Translation: EFB28167.1.

3D structure databases

ProteinModelPortalD2HS90.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000115998.

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...

Entry information

Entry nameSTPAP_AILME
AccessionPrimary (citable) accession number: D2HS90
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 26 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