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D2HS90

- STPAP_AILME

UniProt

D2HS90 - STPAP_AILME

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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

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

Mg2+By similarity, Mn2+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
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

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. nuclear speck Source: UniProtKB
  2. nucleolus Source: UniProtKB
Complete GO annotation...

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.
InParanoidiD2HS90.

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

        10         20         30         40         50
MAAVDLDVQS LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRATR
60 70 80 90 100
KAQGLRSVFV SGFPRDVDSA QLTQYFQAFG PVASVVMDKD KGVFAIVEMG
110 120 130 140 150
DVGTREAVLS QPQHTLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLT
160 170 180 190 200
KALAEAPDVG AQMVKLVGLR ELSEAERQLR NLVVALMQEV FTEFFPGCVV
210 220 230 240 250
HPFGSSINSF DVHGCDLDLF LDLGDLEESQ PAPKAPESPS LDSALASPLD
260 270 280 290 300
PQALACTPAS PPDSQPPSPQ DSEALDFETP SSSLAPQTPD SALASETLAS
310 320 330 340 350
PQSLPPASPL QEDRGEGDLG KALELAEALS GEKTEGVAML ELVGSILRGC
360 370 380 390 400
VPGVYRVQTV PSARRPVVKF CHRPSGLHGD VSLSNRLALH NSRFLSLCSE
410 420 430 440 450
LDGRVRPLVY TLRCWAQGRG LSGSGPLLSN YALTLLVIYF LQTRDPPVLP
460 470 480 490 500
TVSQLTQKAG EGEQVEVDGW DCSFPRDASG LEPSTNKEPL SSLLAQFFSC
510 520 530 540 550
VSCWDLRGSL LSLREGQALP VAGDLPSNRW EGLRLGPMNL QDPFDLSHNV
560 570 580 590 600
AANVTSRVAG RLQNSCQAAA NYCRSLQYQR RSSRGRDWGL LPLLQPSSPS
610 620 630 640 650
SLLSATPIPL PPAPFTQLTA ALAQVLREAL GCHIEQGTKR LRSDRGGPEE
660 670 680 690 700
SPQGGTSKRL KLDGEEKSCE EGREEQQGYI RDHSEDGVEE MVVEVGEMVQ
710 720 730 740 750
DWVQSPGRPG EPPQMLREQL ATGEEGQSGH AALAEQGPKG PEAAREGSQG
760 770 780 790 800
ETGRGVSLSS VSWRCALWHR VWQGRRRARR RLQQQTKERG RGSAGTAEWL
810 820 830 840 850
AVEAQVTREL RGLSSAAQRP EAEPLLTFVA SASQVNQTLT VTPIQDSQGL
860
FPDLHHFLQV FLPQALRNL
Length:869
Mass (Da):94,063
Last modified:February 9, 2010 - v1
Checksum:i01BB7E4572A16511
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL193267 Genomic DNA. Translation: EFB28167.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
InParanoidi D2HS90.

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: November 26, 2014
This is version 29 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