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P25500

- PAPOA_BOVIN

UniProt

P25500 - PAPOA_BOVIN

Protein

Poly(A) polymerase alpha

Gene

PAPOLA

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.1 Publication

    Catalytic activityi

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

    Cofactori

    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

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. manganese ion binding Source: UniProtKB
    4. polynucleotide adenylyltransferase activity Source: UniProtKB
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA polyadenylation Source: RefGenome
    2. mRNA splicing, via spliceosome Source: RefGenome
    3. RNA polyadenylation Source: UniProtKB
    4. termination of RNA polymerase II transcription Source: RefGenome

    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

    ReactomeiREACT_203211. mRNA 3'-end processing.
    REACT_205948. mRNA Splicing - Major Pathway.
    REACT_225642. Processing of Intronless Pre-mRNAs.

    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: Chromosome 21

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. nucleus Source: RefGenome

    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. 1 Publication
    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.
    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. 1 Publication
    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. 1 Publication
    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.
    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 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.

    Interactioni

    Subunit structurei

    Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1 By similarity. Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP.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 – 233
    Helixi33 – 4614
    Helixi47 – 493
    Helixi55 – 8228
    Helixi87 – 904
    Beta strandi96 – 1005
    Helixi101 – 1055
    Beta strandi114 – 1207
    Helixi126 – 1294
    Helixi132 – 1387
    Beta strandi143 – 1497
    Beta strandi152 – 1543
    Beta strandi156 – 1616
    Beta strandi164 – 1729
    Beta strandi176 – 1783
    Helixi187 – 1904
    Helixi195 – 21117
    Beta strandi213 – 2153
    Helixi217 – 23317
    Turni239 – 2424
    Helixi246 – 25914
    Helixi265 – 27713
    Turni302 – 3043
    Helixi306 – 3105
    Beta strandi318 – 3214
    Turni325 – 3284
    Helixi331 – 35222
    Helixi358 – 3614
    Helixi367 – 3704
    Beta strandi372 – 38312
    Helixi384 – 39512
    Helixi398 – 4069
    Beta strandi411 – 4166
    Beta strandi428 – 4303
    Beta strandi433 – 44311
    Helixi457 – 47317
    Beta strandi482 – 4898
    Helixi490 – 4934
    Helixi494 – 4963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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]
    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. Align

    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

    MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG    50
    VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF 100
    GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE 150
    EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS 200
    LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA 250
    MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW 300
    DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE 350
    ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI 400
    LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE 450
    NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPSH 500
    VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS AMKTSPLNSS 550
    GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT 600
    QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH 650
    KEESPKKTKT EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT 700
    ATSLLASQKT SSTDLSDIPA LPANPIPVIK NSIKLRLNR 739
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61585 mRNA. Translation: CAA43782.1 .
    X63436 mRNA. Translation: CAA45031.1 .
    PIRi S17875.
    S17925.
    S18642.
    RefSeqi NP_788820.1. NM_176647.2. [P25500-1 ]
    UniGenei Bt.109586.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F5A X-ray 2.50 A 1-513 [» ]
    1Q78 X-ray 2.80 A 1-514 [» ]
    1Q79 X-ray 2.15 A 1-514 [» ]
    ProteinModelPortali P25500.
    SMRi P25500. Positions 19-498.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000005300.

    Proteomic databases

    PRIDEi P25500.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000005300 ; ENSBTAP00000005300 ; ENSBTAG00000004054 . [P25500-1 ]
    GeneIDi 338051.
    KEGGi bta:338051.

    Organism-specific databases

    CTDi 10914.

    Phylogenomic databases

    eggNOGi COG5186.
    GeneTreei ENSGT00390000017928.
    HOGENOMi HOG000204376.
    HOVERGENi HBG053502.
    InParanoidi P25500.
    KOi K14376.
    OMAi SPVTTQG.
    TreeFami TF300842.

    Enzyme and pathway databases

    Reactomei REACT_203211. mRNA 3'-end processing.
    REACT_205948. mRNA Splicing - Major Pathway.
    REACT_225642. Processing of Intronless Pre-mRNAs.

    Miscellaneous databases

    EvolutionaryTracei P25500.
    NextBioi 20812502.

    Family and domain databases

    Gene3Di 3.30.70.590. 1 hit.
    InterProi IPR002934. Nucleotidyltransferase.
    IPR011068. NuclTrfase_I_C.
    IPR007012. PolA_pol_cen_dom.
    IPR007010. PolA_pol_RNA-bd_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view ]
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    PF04926. PAP_RNA-bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018425. PolyA_polymerase. 1 hit.
    SUPFAMi SSF55003. SSF55003. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 125 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