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D2HS90

- STPAP_AILME

UniProt

D2HS90 - STPAP_AILME

Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

TUT1

Organism
Ailuropoda melanoleuca (Giant panda)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (09 Feb 2010)
      Previous versions | rss
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    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

    Magnesium or manganese.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi216 – 2161Magnesium or manganese; catalyticBy similarity
    Metal bindingi218 – 2181Magnesium or manganese; catalyticBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri16 – 4025C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. mRNA 3'-UTR binding Source: UniProtKB
    4. polynucleotide adenylyltransferase activity Source: UniProtKB
    5. RNA binding Source: UniProtKB
    6. RNA uridylyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. mRNA cleavage Source: UniProtKB
    2. mRNA polyadenylation Source: UniProtKB
    3. snRNA processing Source: UniProtKB

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-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
    ORF Names:PANDA_014931
    OrganismiAiluropoda melanoleuca (Giant panda)
    Taxonomic identifieri9646 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeAiluropoda
    ProteomesiUP000008912: Unplaced

    Subcellular locationi

    Nucleusnucleolus By similarity. Nucleus speckle By similarity

    GO - Cellular componenti

    1. mRNA cleavage and polyadenylation specificity factor complex Source: Ensembl
    2. nuclear speck Source: UniProtKB
    3. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 869869Speckle targeted PIP5K1A-regulated poly(A) polymerasePRO_0000404589Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    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

    Structurei

    3D structure databases

    ProteinModelPortaliD2HS90.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 12873RRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini490 – 54859PAP-associatedAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi229 – 30981Pro-richAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri16 – 4025C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    HOGENOMiHOG000115998.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR002058. PAP_assoc.
    IPR000504. RRM_dom.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PfamiPF03828. PAP_assoc. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    D2HS90-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVDLDVQS LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRATR    50
    KAQGLRSVFV SGFPRDVDSA QLTQYFQAFG PVASVVMDKD KGVFAIVEMG 100
    DVGTREAVLS QPQHTLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLT 150
    KALAEAPDVG AQMVKLVGLR ELSEAERQLR NLVVALMQEV FTEFFPGCVV 200
    HPFGSSINSF DVHGCDLDLF LDLGDLEESQ PAPKAPESPS LDSALASPLD 250
    PQALACTPAS PPDSQPPSPQ DSEALDFETP SSSLAPQTPD SALASETLAS 300
    PQSLPPASPL QEDRGEGDLG KALELAEALS GEKTEGVAML ELVGSILRGC 350
    VPGVYRVQTV PSARRPVVKF CHRPSGLHGD VSLSNRLALH NSRFLSLCSE 400
    LDGRVRPLVY TLRCWAQGRG LSGSGPLLSN YALTLLVIYF LQTRDPPVLP 450
    TVSQLTQKAG EGEQVEVDGW DCSFPRDASG LEPSTNKEPL SSLLAQFFSC 500
    VSCWDLRGSL LSLREGQALP VAGDLPSNRW EGLRLGPMNL QDPFDLSHNV 550
    AANVTSRVAG RLQNSCQAAA NYCRSLQYQR RSSRGRDWGL LPLLQPSSPS 600
    SLLSATPIPL PPAPFTQLTA ALAQVLREAL GCHIEQGTKR LRSDRGGPEE 650
    SPQGGTSKRL KLDGEEKSCE EGREEQQGYI RDHSEDGVEE MVVEVGEMVQ 700
    DWVQSPGRPG EPPQMLREQL ATGEEGQSGH AALAEQGPKG PEAAREGSQG 750
    ETGRGVSLSS VSWRCALWHR VWQGRRRARR RLQQQTKERG RGSAGTAEWL 800
    AVEAQVTREL RGLSSAAQRP EAEPLLTFVA SASQVNQTLT VTPIQDSQGL 850
    FPDLHHFLQV FLPQALRNL 869
    Length:869
    Mass (Da):94,063
    Last modified:February 9, 2010 - v1
    Checksum:i01BB7E4572A16511
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL193267 Genomic DNA. Translation: EFB28167.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL193267 Genomic DNA. Translation: EFB28167.1 .

    3D structure databases

    ProteinModelPortali D2HS90.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000115998.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR002058. PAP_assoc.
    IPR000504. RRM_dom.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    Pfami PF03828. PAP_assoc. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence and de novo assembly of the giant panda genome."
      Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.
      , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J.
      Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiSTPAP_AILME
    AccessioniPrimary (citable) accession number: D2HS90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [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

    External Data

    Dasty 3