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Protein

Poly(A) polymerase alpha

Gene

PAPOLA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions. Also active with manganese.1 Publication

Kineticsi

  1. KM=0.229 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091ATP
    Metal bindingi113 – 1131Magnesium 1; catalytic
    Metal bindingi113 – 1131Magnesium 2; catalytic
    Metal bindingi115 – 1151Magnesium 1; catalytic
    Metal bindingi115 – 1151Magnesium 2; catalytic
    Sitei153 – 1531Interaction with RNABy similarity
    Sitei158 – 1581Interaction with RNABy similarity
    Metal bindingi167 – 1671Magnesium 2; catalytic
    Binding sitei167 – 1671ATP
    Binding sitei228 – 2281ATP
    Binding sitei237 – 2371ATP
    Sitei328 – 3281Interaction with RNABy similarity
    Sitei399 – 3991Interaction with RNABy similarity
    Sitei524 – 5241Interaction with RNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi100 – 1023ATP
    Nucleotide bindingi113 – 1153ATP
    Nucleotide bindingi246 – 2472ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    • polynucleotide adenylyltransferase activity Source: UniProtKB
    • RNA binding Source: UniProtKB-KW

    GO - Biological processi

    • mRNA polyadenylation Source: UniProtKB
    • regulation of mRNA 3'-end processing Source: UniProtKB
    • RNA polyadenylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BRENDAi2.7.7.19. 908.
    ReactomeiREACT_311099. mRNA Splicing - Major Pathway.
    REACT_339317. mRNA 3'-end processing.
    REACT_342878. Processing of Intronless Pre-mRNAs.
    REACT_351678. Cleavage of Growing Transcript in the Termination Region.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) polymerase alpha (EC:2.7.7.19)
    Short name:
    PAP-alpha
    Alternative name(s):
    Polynucleotide adenylyltransferase alpha
    Gene namesi
    Name:PAPOLA
    Synonyms:PAP
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136 Componenti: Chromosome 21

    Subcellular locationi

    • Nucleus 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001F → D: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi113 – 1153DID → AIA: Abolishes most of the specific and non-specific polyadenylation activity.
    Mutagenesisi113 – 1131D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication
    Mutagenesisi115 – 1151D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication
    Mutagenesisi153 – 1531F → A: Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi156 – 1561V → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi162 – 1632DG → HA: Small decrease in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi167 – 1671D → A: Loss of enzyme activity. 2 Publications
    Mutagenesisi167 – 1671D → H: Abolishes most of the specific and non-specific polyadenylation activity. 2 Publications
    Mutagenesisi167 – 1671D → N: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 2 Publications
    Mutagenesisi186 – 1861D → H: Small decrease in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi194 – 1941D → H: No change in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi199 – 1991R → A: Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi202 – 2021N → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi203 – 2031G → H: Loss of enzyme activity. Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi208 – 2092DE → AA: Reduces by 60% non-specific and specific polyadenylation activity.
    Mutagenesisi208 – 2081D → A: Reduces by 60% non-specific rf and specific polyadenylation activity. 1 Publication
    Mutagenesisi208 – 2081D → H: Reduces by 20% non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi209 – 2091E → A: No change in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi228 – 2281K → A: Strongly decreased affinity for ATP. 1 Publication
    Mutagenesisi232 – 2321K → A: Decreased affinity for ATP. 1 Publication
    Mutagenesisi237 – 2371Y → A: Strongly decreased affinity for ATP. 1 Publication
    Mutagenesisi247 – 2471V → A or R: Strongly reduced affinity for RNA. 1 Publication
    Mutagenesisi291 – 2922EE → AA: Abolishes most of non-specific polyadenylation activity.
    Mutagenesisi291 – 2911E → A: Reduces by 60% non-specific polyadenylation activity. 1 Publication
    Mutagenesisi292 – 2921E → A: No change in non-specific polyadenylation activity. 1 Publication
    Mutagenesisi308 – 3081D → A: No change in non-specific and specific polyadenylation activity.
    Mutagenesisi317 – 3171T → G: Strongly decreased affinity for ATP.
    Mutagenesisi431 – 4322EE → AA: No change in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi455 – 4551D → A: Reduces by 30% non-specific polyadenylation activity. 1 Publication
    Mutagenesisi459 – 4591D → A: No change in non-specific polyadenylation activity. 1 Publication
    Mutagenesisi465 – 4651D → A: No change in non-specific and specific polyadenylation activity. 1 Publication
    Mutagenesisi635 – 6351K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-644; Q-730 and Q-734. 1 Publication
    Mutagenesisi635 – 6351K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-644; R-730 and R-734. 1 Publication
    Mutagenesisi644 – 6441K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-730 and Q-734. 1 Publication
    Mutagenesisi644 – 6441K → R: Large decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-730 and R-734. 1 Publication
    Mutagenesisi730 – 7301K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-734. 1 Publication
    Mutagenesisi730 – 7301K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-734. 1 Publication
    Mutagenesisi734 – 7341K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-730. 1 Publication
    Mutagenesisi734 – 7341K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-730. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Poly(A) polymerase alphaPRO_0000051611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241PhosphoserineBy similarity
    Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki445 – 445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki506 – 506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki507 – 507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei537 – 5371Phosphoserine; by MAPKBy similarity
    Modified residuei558 – 5581PhosphoserineBy similarity
    Modified residuei635 – 6351N6-acetyllysine1 Publication
    Modified residuei644 – 6441N6-acetyllysine1 Publication
    Modified residuei730 – 7301N6-acetyllysine; alternate1 Publication
    Cross-linki730 – 730Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei734 – 7341N6-acetyllysine; alternate1 Publication
    Cross-linki734 – 734Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity

    Post-translational modificationi

    Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity).By similarity
    Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity).By similarity
    Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP25500.

    Expressioni

    Gene expression databases

    ExpressionAtlasiP25500. baseline.

    Interactioni

    Subunit structurei

    Monomer (PubMed:10944102, PubMed:15328606). Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (By similarity). Interacts with NUDT21; the interaction is diminished by acetylation (PubMed:17172643). Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (PubMed:17172643).By similarity3 Publications

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000005300.

    Structurei

    Secondary structure

    1
    739
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 233Combined sources
    Helixi33 – 4614Combined sources
    Helixi47 – 493Combined sources
    Helixi55 – 8228Combined sources
    Helixi87 – 904Combined sources
    Beta strandi96 – 1005Combined sources
    Helixi101 – 1055Combined sources
    Beta strandi114 – 1207Combined sources
    Helixi126 – 1294Combined sources
    Helixi132 – 1387Combined sources
    Beta strandi143 – 1497Combined sources
    Beta strandi152 – 1543Combined sources
    Beta strandi156 – 1616Combined sources
    Beta strandi164 – 1729Combined sources
    Beta strandi176 – 1783Combined sources
    Helixi187 – 1904Combined sources
    Helixi195 – 21117Combined sources
    Beta strandi213 – 2153Combined sources
    Helixi217 – 23317Combined sources
    Turni239 – 2424Combined sources
    Helixi246 – 25914Combined sources
    Helixi265 – 27713Combined sources
    Turni302 – 3043Combined sources
    Helixi306 – 3105Combined sources
    Beta strandi318 – 3214Combined sources
    Turni325 – 3284Combined sources
    Helixi331 – 35222Combined sources
    Helixi358 – 3614Combined sources
    Helixi367 – 3704Combined sources
    Beta strandi372 – 38312Combined sources
    Helixi384 – 39512Combined sources
    Helixi398 – 4069Combined sources
    Beta strandi411 – 4166Combined sources
    Beta strandi428 – 4303Combined sources
    Beta strandi433 – 44311Combined sources
    Helixi457 – 47317Combined sources
    Beta strandi482 – 4898Combined sources
    Helixi490 – 4934Combined sources
    Helixi494 – 4963Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F5AX-ray2.50A1-513[»]
    1Q78X-ray2.80A1-514[»]
    1Q79X-ray2.15A1-514[»]
    ProteinModelPortaliP25500.
    SMRiP25500. Positions 19-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25500.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni508 – 643136Ser/Thr-richAdd
    BLAST
    Regioni671 – 73969Required for interaction with NUDT21Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi490 – 50718Nuclear localization signal 1Add
    BLAST
    Motifi644 – 65916Nuclear localization signal 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the poly(A) polymerase family.Curated

    Phylogenomic databases

    eggNOGiCOG5186.
    GeneTreeiENSGT00390000017928.
    HOGENOMiHOG000204376.
    HOVERGENiHBG053502.
    InParanoidiP25500.
    KOiK14376.
    OMAiSPVTTQG.
    TreeFamiTF300842.

    Family and domain databases

    Gene3Di3.30.70.590. 1 hit.
    InterProiIPR002934. Nucleotidyltransferase.
    IPR011068. NuclTrfase_I_C.
    IPR007012. PolA_pol_cen_dom.
    IPR007010. PolA_pol_RNA-bd_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view]
    PANTHERiPTHR10682. PTHR10682. 1 hit.
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    PF04926. PAP_RNA-bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018425. PolyA_polymerase. 1 hit.
    SUPFAMiSSF55003. SSF55003. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Note: Additional isoforms seem to exist.

    Isoform Long (identifier: P25500-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG
    60 70 80 90 100
    VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF
    110 120 130 140 150
    GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE
    160 170 180 190 200
    EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS
    210 220 230 240 250
    LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA
    260 270 280 290 300
    MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
    310 320 330 340 350
    DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE
    360 370 380 390 400
    ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI
    410 420 430 440 450
    LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE
    460 470 480 490 500
    NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPSH
    510 520 530 540 550
    VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS AMKTSPLNSS
    560 570 580 590 600
    GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT
    610 620 630 640 650
    QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH
    660 670 680 690 700
    KEESPKKTKT EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT
    710 720 730
    ATSLLASQKT SSTDLSDIPA LPANPIPVIK NSIKLRLNR
    Length:739
    Mass (Da):82,441
    Last modified:January 23, 2007 - v3
    Checksum:i7C89C15E33232CFF
    GO
    Isoform Short (identifier: P25500-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         663-683: Missing.
         709-710: KT → II
         711-739: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:689
    Mass (Da):77,066
    Checksum:i20BECA9A51B9ED1A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801S → R in CAA45031 (PubMed:1896071).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei663 – 68321Missing in isoform Short. 1 PublicationVSP_004524Add
    BLAST
    Alternative sequencei709 – 7102KT → II in isoform Short. 1 PublicationVSP_004525
    Alternative sequencei711 – 73929Missing in isoform Short. 1 PublicationVSP_004526Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X61585 mRNA. Translation: CAA43782.1.
    X63436 mRNA. Translation: CAA45031.1.
    PIRiS17875.
    S17925.
    S18642.
    RefSeqiNP_788820.1. NM_176647.2. [P25500-1]
    UniGeneiBt.109586.

    Genome annotation databases

    EnsembliENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054. [P25500-1]
    GeneIDi338051.
    KEGGibta:338051.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X61585 mRNA. Translation: CAA43782.1.
    X63436 mRNA. Translation: CAA45031.1.
    PIRiS17875.
    S17925.
    S18642.
    RefSeqiNP_788820.1. NM_176647.2. [P25500-1]
    UniGeneiBt.109586.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F5AX-ray2.50A1-513[»]
    1Q78X-ray2.80A1-514[»]
    1Q79X-ray2.15A1-514[»]
    ProteinModelPortaliP25500.
    SMRiP25500. Positions 19-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000005300.

    Proteomic databases

    PRIDEiP25500.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054. [P25500-1]
    GeneIDi338051.
    KEGGibta:338051.

    Organism-specific databases

    CTDi10914.

    Phylogenomic databases

    eggNOGiCOG5186.
    GeneTreeiENSGT00390000017928.
    HOGENOMiHOG000204376.
    HOVERGENiHBG053502.
    InParanoidiP25500.
    KOiK14376.
    OMAiSPVTTQG.
    TreeFamiTF300842.

    Enzyme and pathway databases

    BRENDAi2.7.7.19. 908.
    ReactomeiREACT_311099. mRNA Splicing - Major Pathway.
    REACT_339317. mRNA 3'-end processing.
    REACT_342878. Processing of Intronless Pre-mRNAs.
    REACT_351678. Cleavage of Growing Transcript in the Termination Region.

    Miscellaneous databases

    EvolutionaryTraceiP25500.
    NextBioi20812502.

    Gene expression databases

    ExpressionAtlasiP25500. baseline.

    Family and domain databases

    Gene3Di3.30.70.590. 1 hit.
    InterProiIPR002934. Nucleotidyltransferase.
    IPR011068. NuclTrfase_I_C.
    IPR007012. PolA_pol_cen_dom.
    IPR007010. PolA_pol_RNA-bd_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view]
    PANTHERiPTHR10682. PTHR10682. 1 hit.
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    PF04926. PAP_RNA-bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018425. PolyA_polymerase. 1 hit.
    SUPFAMiSSF55003. SSF55003. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase."
      Wahle E., Martin G., Schiltz E., Keller W.
      EMBO J. 10:4251-4257(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 1-21; 207-255 AND 386-397.
      Tissue: Thymus.
    2. Wahle E.
      Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Primary structure and expression of bovine poly(A) polymerase."
      Raabe T., Bollum F.J., Manley J.L.
      Nature 353:229-234(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 97-103 AND 445-468.
      Tissue: Heart muscle.
    4. "Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases."
      Martin G., Keller W.
      EMBO J. 15:2593-2603(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS, MUTAGENESIS OF ASP-113; ASP-115; 162-ASP-GLY-163; ASP-167; ASP-186; ASP-194; ASP-208; GLU-209; GLU-291; GLU-292; 431-GLU-GLU-432; ASP-455; ASP-459 AND ASP-465.
    5. "Inhibition of poly(A) polymerase requires p34cdc2/cyclin B phosphorylation of multiple consensus and non-consensus sites."
      Colgan D.F., Murthy K.G., Zhao W., Prives C., Manley J.L.
      EMBO J. 17:1053-1062(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, FUNCTION.
    6. "Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing."
      Shimazu T., Horinouchi S., Yoshida M.
      J. Biol. Chem. 282:4470-4478(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-635; LYS-644; LYS-730 AND LYS-734, INTERACTION WITH NUDT21 AND KPBN1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-635; LYS-644; LYS-730 AND LYS-734.
    7. "Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP."
      Martin G., Keller W., Doublie S.
      EMBO J. 19:4193-4203(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-513 IN COMPLEX WITH ATP ANALOG AND MANGANESE IONS.
    8. "Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase."
      Martin G., Moglich A., Keller W., Doublie S.
      J. Mol. Biol. 341:911-925(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-513 IN COMPLEX WITH MAGNESIUM IONS; MANGANESE IONS AND ATP ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF PHE-100; PHE-153; VAL-156; ASP-167; ARG-199; ASN-202; GLY-203; LYS-228; LYS-232; TYR-237 AND VAL-247.

    Entry informationi

    Entry nameiPAPOA_BOVIN
    AccessioniPrimary (citable) accession number: P25500
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.