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Q9H6E5

- STPAP_HUMAN

UniProt

Q9H6E5 - STPAP_HUMAN

Protein

Speckle targeted PIP5K1A-regulated poly(A) polymerase

Gene

TUT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      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.3 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Enzyme regulationi

    Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).1 Publication

    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. enzyme binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. mRNA 3'-UTR binding Source: UniProtKB
    5. polynucleotide adenylyltransferase activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. RNA binding Source: UniProtKB
    8. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:26184. TUT1.

    Subcellular locationi

    GO - Cellular componenti

    1. intercellular bridge Source: HPA
    2. nuclear speck Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi216 – 2161D → A: Abolishes adenylyltransferase activity; when associated with A-218. 1 Publication
    Mutagenesisi218 – 2181D → A: Abolishes adenylyltransferase activity; when associated with A-216. 1 Publication

    Organism-specific databases

    PharmGKBiPA162407405.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 874874Speckle targeted PIP5K1A-regulated poly(A) polymerasePRO_0000254186Add
    BLAST

    Post-translational modificationi

    Phosphorylated by CK1 in the proline-rich (Pro-rich) region.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H6E5.
    PaxDbiQ9H6E5.
    PRIDEiQ9H6E5.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9H6E5.
    BgeeiQ9H6E5.
    CleanExiHS_TUT1.
    GenevestigatoriQ9H6E5.

    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

    Protein-protein interaction databases

    BioGridi122325. 14 interactions.
    DIPiDIP-53651N.
    IntActiQ9H6E5. 12 interactions.
    MINTiMINT-7900460.
    STRINGi9606.ENSP00000278279.

    Structurei

    Secondary structure

    1
    874
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi57 – 615
    Helixi69 – 757
    Helixi76 – 783
    Beta strandi82 – 876
    Beta strandi89 – 913
    Beta strandi94 – 1018
    Helixi102 – 1098

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E5GNMR-A55-141[»]
    ProteinModelPortaliQ9H6E5.
    SMRiQ9H6E5. Positions 23-141, 148-226, 333-610.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H6E5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 12873RRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 54959PAP-associatedAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi229 – 31082Pro-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

    eggNOGiCOG5260.
    HOGENOMiHOG000115998.
    HOVERGENiHBG079670.
    InParanoidiQ9H6E5.
    OrthoDBiEOG7353WD.
    PhylomeDBiQ9H6E5.

    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.

    Q9H6E5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR    50
    KAQGLRSVFV SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG 100
    DVGAREAVLS QSQHSLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLA 150
    KALAEAADVG AQMIKLVGLR ELSEAERQLR SLVVALMQEV FTEFFPGCVV 200
    HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS LDSALASPLD 250
    PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA 300
    SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG 350
    CVPGVYRVQT VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS 400
    ELDGRVRPLV YTLRCWAQGR GLSGSGPLLS NYALTLLVIY FLQTRDPPVL 450
    PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS RLEPSINVEP LSSLLAQFFS 500
    CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN LQDPFDLSHN 550
    VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP 600
    SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG 650
    ESSQGGTSKR LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV 700
    QDWAMQSPGQ PGDLPLTTGK HGAPGEEGQP SHAALAERGP KGHEAAQEWS 750
    QGEAGKGASL PSSASWRCAL WHRVWQGRRR ARRRLQQQTK EGAGGGAGTR 800
    AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD RMLTVTPLQD 850
    PQGLFPDLHH FLQVFLPQAI RHLK 874
    Length:874
    Mass (Da):93,847
    Last modified:February 20, 2007 - v2
    Checksum:i85A4117A040FC90D
    GO

    Sequence cautioni

    The sequence BAB15282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661D → G in BAB15314. (PubMed:14702039)Curated
    Sequence conflicti809 – 8091Q → R in BAF85299. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti442 – 4421L → F.
    Corresponds to variant rs3197865 [ dbSNP | Ensembl ].
    VAR_028833

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi126302611.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_073741.2. NM_022830.2.
    UniGenei Hs.728983.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E5G NMR - A 55-141 [» ]
    ProteinModelPortali Q9H6E5.
    SMRi Q9H6E5. Positions 23-141, 148-226, 333-610.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122325. 14 interactions.
    DIPi DIP-53651N.
    IntActi Q9H6E5. 12 interactions.
    MINTi MINT-7900460.
    STRINGi 9606.ENSP00000278279.

    Polymorphism databases

    DMDMi 126302611.

    Proteomic databases

    MaxQBi Q9H6E5.
    PaxDbi Q9H6E5.
    PRIDEi Q9H6E5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000476907 ; ENSP00000419607 ; ENSG00000149016 .
    GeneIDi 64852.
    KEGGi hsa:64852.

    Organism-specific databases

    CTDi 64852.
    GeneCardsi GC11M062342.
    HGNCi HGNC:26184. TUT1.
    HPAi HPA039253.
    MIMi 610641. gene.
    neXtProti NX_Q9H6E5.
    PharmGKBi PA162407405.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5260.
    HOGENOMi HOG000115998.
    HOVERGENi HBG079670.
    InParanoidi Q9H6E5.
    OrthoDBi EOG7353WD.
    PhylomeDBi Q9H6E5.

    Miscellaneous databases

    EvolutionaryTracei Q9H6E5.
    GenomeRNAii 64852.
    NextBioi 66977.
    PROi Q9H6E5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H6E5.
    Bgeei Q9H6E5.
    CleanExi HS_TUT1.
    Genevestigatori Q9H6E5.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon and Eye.
    5. "Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
      Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
      RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, SUBCELLULAR LOCATION.
    6. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
    7. "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
      Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
      Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
    8. "CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
      Gonzales M.L., Mellman D.L., Anderson R.A.
      J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CK1.
    9. "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
      Laishram R.S., Anderson R.A.
      EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ADENYLYLTRANSFERASE, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
    10. "Solution structure of RNA binding domain in RNA binding motif protein 21."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 54-141.

    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: October 1, 2014
    This is version 103 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

    External Data

    Dasty 3