Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P29468

- PAP_YEAST

UniProt

P29468 - PAP_YEAST

Protein

Poly(A) polymerase

Gene

PAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Polymerase component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.2 Publications

    Catalytic activityi

    ATP + RNA(n) = diphosphate + RNA(n+1).2 Publications

    Cofactori

    Binds 2 magnesium ions. Also active with manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi100 – 1001Magnesium 1; catalytic
    Metal bindingi100 – 1001Magnesium 2; catalytic
    Metal bindingi102 – 1021Magnesium 1; catalytic
    Metal bindingi102 – 1021Magnesium 2; catalytic
    Sitei140 – 1401Interaction with RNA
    Sitei145 – 1451Interaction with RNA
    Metal bindingi154 – 1541Magnesium 2; catalytic
    Binding sitei154 – 1541ATP1 Publication
    Binding sitei215 – 2151ATP1 Publication
    Binding sitei224 – 2241ATP1 Publication
    Sitei294 – 2941Interaction with RNA
    Sitei314 – 3141Interaction with RNA
    Sitei315 – 3151Interaction with RNA
    Sitei387 – 3871Interaction with RNA
    Sitei392 – 3921Interaction with RNA
    Sitei487 – 4871Interaction with RNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi87 – 893ATP1 Publication
    Nucleotide bindingi99 – 1024ATP1 Publication
    Nucleotide bindingi100 – 1023ATP1 Publication
    Nucleotide bindingi233 – 2342ATP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. mRNA polyadenylation Source: SGD
    2. RNA polyadenylation Source: UniProtKB
    3. snoRNA polyadenylation Source: SGD

    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

    BioCyciYEAST:G3O-31980-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) polymerase (EC:2.7.7.19)
    Short name:
    PAP
    Alternative name(s):
    Polynucleotide adenylyltransferase
    Gene namesi
    Name:PAP1
    Ordered Locus Names:YKR002W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKR002w.
    SGDiS000001710. PAP1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. mRNA cleavage and polyadenylation specificity factor complex Source: SGD
    2. nucleoplasm Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi154 – 1541D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi189 – 1891N → A: Slightly reduced rate of adenylyltransfer. 1 Publication
    Mutagenesisi215 – 2151K → A: Reduces rate of adenylyltransfer about four-fold. 1 Publication
    Mutagenesisi226 – 2261N → A: Reduces rate of adenylyltransfer by half. 1 Publication
    Mutagenesisi485 – 4851C → R: Abolishes interaction with FIP1; when associated with Y-489. 1 Publication
    Mutagenesisi489 – 4891V → Y: Abolishes interaction with FIP1; when associated with R-485. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 568568Poly(A) polymerasePRO_0000051621Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei452 – 4521Phosphoserine1 Publication
    Modified residuei550 – 5501Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29468.
    PaxDbiP29468.
    PeptideAtlasiP29468.

    Expressioni

    Gene expression databases

    GenevestigatoriP29468.

    Interactioni

    Subunit structurei

    Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with FIR1 and RRP6.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFT1Q066327EBI-12917,EBI-32872
    FIP1P4597611EBI-12917,EBI-6940
    NAB6Q037352EBI-12917,EBI-27955
    PTA1Q0132910EBI-12917,EBI-14145

    Protein-protein interaction databases

    BioGridi34134. 47 interactions.
    DIPiDIP-2297N.
    IntActiP29468. 28 interactions.
    MINTiMINT-375429.
    STRINGi4932.YKR002W.

    Structurei

    Secondary structure

    1
    568
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Beta strandi8 – 103
    Helixi20 – 3516
    Helixi42 – 6928
    Helixi74 – 796
    Beta strandi83 – 875
    Helixi88 – 925
    Beta strandi101 – 1077
    Helixi113 – 12513
    Beta strandi130 – 1367
    Beta strandi139 – 1413
    Beta strandi143 – 1486
    Beta strandi151 – 1599
    Beta strandi161 – 1633
    Helixi174 – 1774
    Helixi182 – 20019
    Helixi204 – 22017
    Helixi226 – 2283
    Helixi233 – 24614
    Helixi252 – 26514
    Beta strandi272 – 2754
    Beta strandi281 – 2833
    Turni289 – 2913
    Helixi293 – 2964
    Beta strandi305 – 3084
    Turni312 – 3154
    Helixi318 – 33922
    Helixi345 – 3484
    Helixi354 – 3574
    Beta strandi359 – 37012
    Helixi372 – 39423
    Beta strandi399 – 4046
    Beta strandi409 – 4146
    Beta strandi417 – 4193
    Helixi420 – 4278
    Helixi431 – 4344
    Helixi435 – 4384
    Turni444 – 4463
    Helixi451 – 4555
    Beta strandi458 – 47013
    Beta strandi475 – 4773
    Helixi482 – 49413
    Turni497 – 5004
    Beta strandi502 – 51312
    Helixi514 – 5163
    Helixi519 – 5213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FA0X-ray2.60A/B1-537[»]
    2HHPX-ray1.80A1-530[»]
    2O1PX-ray2.70A/B1-538[»]
    2Q66X-ray1.80A5-529[»]
    3C66X-ray2.60A/B1-526[»]
    ProteinModelPortaliP29468.
    SMRiP29468. Positions 3-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29468.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the poly(A) polymerase family.Curated

    Phylogenomic databases

    eggNOGiCOG5186.
    GeneTreeiENSGT00390000017928.
    HOGENOMiHOG000204376.
    KOiK14376.
    OMAiMSDGMAR.
    OrthoDBiEOG7M6DHG.

    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.

    Sequencei

    Sequence statusi: Complete.

    P29468-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQKVFGIT GPVSTVGATA AENKLNDSLI QELKKEGSFE TEQETANRVQ    50
    VLKILQELAQ RFVYEVSKKK NMSDGMARDA GGKIFTYGSY RLGVHGPGSD 100
    IDTLVVVPKH VTREDFFTVF DSLLRERKEL DEIAPVPDAF VPIIKIKFSG 150
    ISIDLICARL DQPQVPLSLT LSDKNLLRNL DEKDLRALNG TRVTDEILEL 200
    VPKPNVFRIA LRAIKLWAQR RAVYANIFGF PGGVAWAMLV ARICQLYPNA 250
    CSAVILNRFF IILSEWNWPQ PVILKPIEDG PLQVRVWNPK IYAQDRSHRM 300
    PVITPAYPSM CATHNITEST KKVILQEFVR GVQITNDIFS NKKSWANLFE 350
    KNDFFFRYKF YLEITAYTRG SDEQHLKWSG LVESKVRLLV MKLEVLAGIK 400
    IAHPFTKPFE SSYCCPTEDD YEMIQDKYGS HKTETALNAL KLVTDENKEE 450
    ESIKDAPKAY LSTMYIGLDF NIENKKEKVD IHIPCTEFVN LCRSFNEDYG 500
    DHKVFNLALR FVKGYDLPDE VFDENEKRPS KKSKRKNLDA RHETVKRSKS 550
    DAASGDNING TTAAVDVN 568
    Length:568
    Mass (Da):64,552
    Last modified:April 1, 1993 - v1
    Checksum:i759DE5210DC8D881
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60307 Genomic DNA. Translation: CAA42852.1.
    X65124 Genomic DNA. Translation: CAA46250.1.
    Z28227 Genomic DNA. Translation: CAA82072.1.
    BK006944 Genomic DNA. Translation: DAA09158.1.
    PIRiS19031.
    RefSeqiNP_012927.3. NM_001179792.3.

    Genome annotation databases

    EnsemblFungiiYKR002W; YKR002W; YKR002W.
    GeneIDi853871.
    KEGGisce:YKR002W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60307 Genomic DNA. Translation: CAA42852.1 .
    X65124 Genomic DNA. Translation: CAA46250.1 .
    Z28227 Genomic DNA. Translation: CAA82072.1 .
    BK006944 Genomic DNA. Translation: DAA09158.1 .
    PIRi S19031.
    RefSeqi NP_012927.3. NM_001179792.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FA0 X-ray 2.60 A/B 1-537 [» ]
    2HHP X-ray 1.80 A 1-530 [» ]
    2O1P X-ray 2.70 A/B 1-538 [» ]
    2Q66 X-ray 1.80 A 5-529 [» ]
    3C66 X-ray 2.60 A/B 1-526 [» ]
    ProteinModelPortali P29468.
    SMRi P29468. Positions 3-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34134. 47 interactions.
    DIPi DIP-2297N.
    IntActi P29468. 28 interactions.
    MINTi MINT-375429.
    STRINGi 4932.YKR002W.

    Proteomic databases

    MaxQBi P29468.
    PaxDbi P29468.
    PeptideAtlasi P29468.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKR002W ; YKR002W ; YKR002W .
    GeneIDi 853871.
    KEGGi sce:YKR002W.

    Organism-specific databases

    CYGDi YKR002w.
    SGDi S000001710. PAP1.

    Phylogenomic databases

    eggNOGi COG5186.
    GeneTreei ENSGT00390000017928.
    HOGENOMi HOG000204376.
    KOi K14376.
    OMAi MSDGMAR.
    OrthoDBi EOG7M6DHG.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31980-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P29468.
    NextBioi 975142.
    PROi P29468.

    Gene expression databases

    Genevestigatori P29468.

    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. "Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae."
      Lingner J., Kellermann J., Keller W.
      Nature 354:496-498(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 204510 / AB320.
    2. "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames."
      Duesterhoeft A., Philippsen P.
      Yeast 8:749-759(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts."
      del Olmo M., Mizrahi N., Gross S., Moore C.L.
      Mol. Gen. Genet. 255:209-218(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FIR1.
    6. "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p."
      Burkard K.T.D., Butler J.S.
      Mol. Cell. Biol. 20:604-616(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRP6.
    7. "Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends."
      Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J.
      J. Biol. Chem. 278:33000-33010(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP."
      Bard J., Zhelkovsky A.M., Helmling S., Earnest T.N., Moore C.L., Bohm A.
      Science 289:1346-1349(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537 IN COMPLEX WITH ATP ANALOG AND MANGANESE IONS.
    13. "X-ray crystallographic and steady state fluorescence characterization of the protein dynamics of yeast polyadenylate polymerase."
      Balbo P.B., Toth J., Bohm A.
      J. Mol. Biol. 366:1401-1415(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-530.
    14. "Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis."
      Balbo P.B., Bohm A.
      Structure 15:1117-1131(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-529 OF MUTANT ALA-154 IN COMPLEX WITH ATP; MAGNESIUM IONS AND OLIGONUCLEOTIDE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ASP-154; ASN-189; LYS-215 AND ASN-226.
    15. "Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein."
      Meinke G., Ezeokonkwo C., Balbo P., Stafford W., Moore C., Bohm A.
      Biochemistry 47:6859-6869(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537 IN COMPLEX WITH FIP1, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FIP1, MUTAGENESIS OF CYS-485 AND VAL-489.

    Entry informationi

    Entry nameiPAP_YEAST
    AccessioniPrimary (citable) accession number: P29468
    Secondary accession number(s): D6VXT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 17100 molecules/cell in log phase SD medium.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3