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P04147

- PABP_YEAST

UniProt

P04147 - PABP_YEAST

Protein

Polyadenylate-binding protein, cytoplasmic and nuclear

Gene

PAB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.14 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) binding Source: SGD
    3. protein binding Source: IntAct
    4. ribonuclease inhibitor activity Source: SGD

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. mRNA transport Source: UniProtKB-KW
    3. negative regulation of catalytic activity Source: GOC
    4. regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
    5. regulation of translational initiation Source: SGD

    Keywords - Biological processi

    mRNA processing, mRNA transport, Translation regulation, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30326-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyadenylate-binding protein, cytoplasmic and nuclear
    Short name:
    PABP
    Short name:
    Poly(A)-binding protein
    Alternative name(s):
    ARS consensus-binding protein ACBP-67
    Polyadenylate tail-binding protein
    Gene namesi
    Name:PAB1
    Ordered Locus Names:YER165W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    SGDiS000000967. PAB1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm. Can be exported from the nucleus through at least 2 distinct pathways, the main being dependent on the exportin CRM1, and the second requiring MEX67 and ongoing mRNA export. Import is mediated by the importin SXM1.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic stress granule Source: SGD
    3. nucleus Source: SGD
    4. ribosome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121L → A: Impairs nuclear export; when associated with A-15. 1 Publication
    Mutagenesisi15 – 151L → A: Impairs nuclear export; when associated with A-12. 1 Publication
    Mutagenesisi79 – 791L → A in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with Q-166; Q-259 and Q-362. 1 Publication
    Mutagenesisi83 – 831Y → V in PAB1-16; reduces affinity for oligo(A) about 100-fold, impairs poly(A)-dependent translation, but still interacts with eIF4G; when associated with V-170. In PAB1-15; fails to bind RNA; when associated with V-170; V-263 and V-366. 2 Publications
    Mutagenesisi134 – 1363HPD → DKS in PAB1-134.
    Mutagenesisi148 – 1481V → A in PAB1-148; greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro; when associated with N-151. 1 Publication
    Mutagenesisi151 – 1511D → N in PAB1-148; greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro; when associated with A-148. 1 Publication
    Mutagenesisi157 – 1593IAT → VVC in PAB1-157; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro.
    Mutagenesisi166 – 1661K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-259 and Q-362. 1 Publication
    Mutagenesisi170 – 1701F → V in PAB1-6; selectively reduces poly(A) RNA binding. In PAB1-16; reduces affinity for oligo(A) about 100-fold, impairs poly(A)-dependent translation, but still interacts with eIF4G; when associated with V-83. In PAB1-15; fails to bind RNA; when associated with V-83; V-263 and V-366. 2 Publications
    Mutagenesisi175 – 1773EEG → TQE in PAB1-175; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro.
    Mutagenesisi180 – 1812KE → ER in PAB1-180; abolishes poly(A)-dependent translation and greatly reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G.
    Mutagenesisi184 – 1863DAL → EKM in PAB1-184; abolishes poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G.
    Mutagenesisi193 – 1975GQEIY → DRKVF in PAB1-193; moderately reduces stimulation of cap-dependent translation in vitro.
    Mutagenesisi199 – 2024APHL → GRFK in PAB1-199; moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro.
    Mutagenesisi259 – 2591K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-362. 1 Publication
    Mutagenesisi263 – 2631F → V in PAB1-7. In PAB1-15; fails to bind RNA; when associated with V-83; V-170 and V-366. 1 Publication
    Mutagenesisi362 – 3621K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-259. 1 Publication
    Mutagenesisi366 – 3661F → V in PAB1-8; selectively reduces poly(U) RNA binding. In PAB1-15; fails to bind RNA; when associated with V-83; V-170 and V-263. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 577576Polyadenylate-binding protein, cytoplasmic and nuclearPRO_0000081720Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei332 – 3321Phosphoserine1 Publication
    Modified residuei405 – 4051Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04147.
    PaxDbiP04147.
    PeptideAtlasiP04147.

    Expressioni

    Gene expression databases

    GenevestigatoriP04147.

    Interactioni

    Subunit structurei

    Binds to poly(A) mRNA to form a periodic structure with a packing density of one molecule per 25 adenylate residues. Interacts with the nuclear export factor CRM1 and with the importin SXM1. Interacts with RNA15, a component of the cleavage factor IA (CFIA) complex. Interacts with translation initiation factor eIF4G (TIF4631 or TIF4632) and release factor eRF3 (SUP35). Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3. Interacts with ARF1, DCP1, PBP1, the Hsp70 chaperone SSA1, and TPA1. Interacts with PAT1 in an RNA-dependent manner.18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAN3P361025EBI-12823,EBI-12895
    TIF4631P3993516EBI-12823,EBI-9002
    TIF4632P399362EBI-12823,EBI-9006

    Protein-protein interaction databases

    BioGridi36918. 231 interactions.
    DIPiDIP-2275N.
    IntActiP04147. 172 interactions.
    MINTiMINT-693056.
    STRINGi4932.YER165W.

    Structurei

    Secondary structure

    1
    577
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi503 – 51715
    Helixi518 – 5203
    Helixi524 – 53411
    Helixi539 – 5468
    Helixi549 – 56820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IFWNMR-A491-577[»]
    ProteinModelPortaliP04147.
    SMRiP04147. Positions 38-414, 489-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04147.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 11679RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini126 – 20378RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini219 – 29678RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 39978RRM 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 56880PABCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 6153Required and sufficient for nuclear exportSequence AnalysisAdd
    BLAST
    Regioni281 – 31737Required and sufficient for nuclear importSequence AnalysisAdd
    BLAST
    Regioni473 – 577105Interaction with SUP35Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi12 – 176Nuclear export signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi422 – 43110Poly-Ala

    Domaini

    RNA recognition motifs (RRMs) 1 and 2 bind specifically to the poly(A) tail, whereas RRMs 3 and 4 bind non-specifically to polypyrimidine RNAs and may serve to bind to a different part of the messenger or to other RNAs. RRM 2 also mediates interaction with eIF-4G.1 Publication

    Sequence similaritiesi

    Contains 1 PABC domain.PROSITE-ProRule annotation
    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    GeneTreeiENSGT00630000089747.
    HOGENOMiHOG000217922.
    KOiK13126.
    OMAiAGRNGNF.
    OrthoDBiEOG706125.

    Family and domain databases

    Gene3Di1.10.1900.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR006515. PABP_1234.
    IPR002004. PABP_HYD.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00658. PABP. 1 hit.
    PF00076. RRM_1. 4 hits.
    [Graphical view]
    SMARTiSM00517. PolyA. 1 hit.
    SM00360. RRM. 4 hits.
    [Graphical view]
    SUPFAMiSSF63570. SSF63570. 1 hit.
    TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
    PROSITEiPS51309. PABC. 1 hit.
    PS50102. RRM. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04147-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADITDKTAE QLENLNIQDD QKQAATGSES QSVENSSASL YVGDLEPSVS    50
    EAHLYDIFSP IGSVSSIRVC RDAITKTSLG YAYVNFNDHE AGRKAIEQLN 100
    YTPIKGRLCR IMWSQRDPSL RKKGSGNIFI KNLHPDIDNK ALYDTFSVFG 150
    DILSSKIATD ENGKSKGFGF VHFEEEGAAK EAIDALNGML LNGQEIYVAP 200
    HLSRKERDSQ LEETKAHYTN LYVKNINSET TDEQFQELFA KFGPIVSASL 250
    EKDADGKLKG FGFVNYEKHE DAVKAVEALN DSELNGEKLY VGRAQKKNER 300
    MHVLKKQYEA YRLEKMAKYQ GVNLFVKNLD DSVDDEKLEE EFAPYGTITS 350
    AKVMRTENGK SKGFGFVCFS TPEEATKAIT EKNQQIVAGK PLYVAIAQRK 400
    DVRRSQLAQQ IQARNQMRYQ QATAAAAAAA AGMPGQFMPP MFYGVMPPRG 450
    VPFNGPNPQQ MNPMGGMPKN GMPPQFRNGP VYGVPPQGGF PRNANDNNQF 500
    YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ EVFPLLESDE 550
    LFEQHYKEAS AAYESFKKEQ EQQTEQA 577
    Length:577
    Mass (Da):64,344
    Last modified:January 23, 2007 - v4
    Checksum:i4F97E494753E17C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti426 – 4261A → R in AAA34838. (PubMed:3518950)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12780 Genomic DNA. Translation: AAA34838.1.
    M13371 Genomic DNA. Translation: AAA34787.1.
    D00023 Genomic DNA. Translation: BAA00017.1.
    U18922 Genomic DNA. Translation: AAB64692.1.
    AY692854 Genomic DNA. Translation: AAT92873.1.
    BK006939 Genomic DNA. Translation: DAA07827.1.
    PIRiA25221. DNBYPA.
    RefSeqiNP_011092.1. NM_001179055.1.

    Genome annotation databases

    EnsemblFungiiYER165W; YER165W; YER165W.
    GeneIDi856912.
    KEGGisce:YER165W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12780 Genomic DNA. Translation: AAA34838.1 .
    M13371 Genomic DNA. Translation: AAA34787.1 .
    D00023 Genomic DNA. Translation: BAA00017.1 .
    U18922 Genomic DNA. Translation: AAB64692.1 .
    AY692854 Genomic DNA. Translation: AAT92873.1 .
    BK006939 Genomic DNA. Translation: DAA07827.1 .
    PIRi A25221. DNBYPA.
    RefSeqi NP_011092.1. NM_001179055.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IFW NMR - A 491-577 [» ]
    ProteinModelPortali P04147.
    SMRi P04147. Positions 38-414, 489-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36918. 231 interactions.
    DIPi DIP-2275N.
    IntActi P04147. 172 interactions.
    MINTi MINT-693056.
    STRINGi 4932.YER165W.

    Proteomic databases

    MaxQBi P04147.
    PaxDbi P04147.
    PeptideAtlasi P04147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER165W ; YER165W ; YER165W .
    GeneIDi 856912.
    KEGGi sce:YER165W.

    Organism-specific databases

    SGDi S000000967. PAB1.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00630000089747.
    HOGENOMi HOG000217922.
    KOi K13126.
    OMAi AGRNGNF.
    OrthoDBi EOG706125.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30326-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04147.
    NextBioi 983356.
    PROi P04147.

    Gene expression databases

    Genevestigatori P04147.

    Family and domain databases

    Gene3Di 1.10.1900.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR006515. PABP_1234.
    IPR002004. PABP_HYD.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00658. PABP. 1 hit.
    PF00076. RRM_1. 4 hits.
    [Graphical view ]
    SMARTi SM00517. PolyA. 1 hit.
    SM00360. RRM. 4 hits.
    [Graphical view ]
    SUPFAMi SSF63570. SSF63570. 1 hit.
    TIGRFAMsi TIGR01628. PABP-1234. 1 hit.
    PROSITEi PS51309. PABC. 1 hit.
    PS50102. RRM. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression."
      Sachs A.B., Bond M.W., Kornberg R.D.
      Cell 45:827-835(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 9-29.
    2. "mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence."
      Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., Dreyfuss G.
      Mol. Cell. Biol. 6:2932-2943(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "The yeast protein encoded by PUB1 binds T-rich single stranded DNA."
      Cockell M., Frutiger S., Hughes G.J., Gasser S.M.
      Nucleic Acids Res. 22:32-40(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-17; 167-173 AND 242-248, CHARACTERIZATION.
    7. "A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability."
      Sachs A.B., Davis R.W., Kornberg R.D.
      Mol. Cell. Biol. 7:3268-3276(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    8. "The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation."
      Sachs A.B., Davis R.W.
      Cell 58:857-867(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATION INITIATION.
    9. "The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro."
      Bernstein P., Peltz S.W., Ross J.
      Mol. Cell. Biol. 9:659-670(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA STABILIZATION.
    10. "The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities."
      Burd C.G., Matunis E.L., Dreyfuss G.
      Mol. Cell. Biol. 11:3419-3424(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, DOMAINS.
    11. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae."
      Anderson J.T., Paddy M.R., Swanson M.S.
      Mol. Cell. Biol. 13:6102-6113(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast."
      Caponigro G., Parker R.
      Genes Dev. 9:2421-2432(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G."
      Tarun S.Z. Jr., Sachs A.B.
      EMBO J. 15:7168-7177(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF4632.
    14. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2.
    15. "Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein."
      Deardorff J.A., Sachs A.B.
      J. Mol. Biol. 269:67-81(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, MUTAGENESIS OF LEU-79; TYR-83; LYS-166; PHE-170; LYS-259; PHE-263; LYS-362 AND PHE-366.
    16. "Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro."
      Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.
      Mol. Cell. Biol. 17:3694-3701(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA MATURATION, INTERACTION WITH RNA15.
    17. "The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation."
      Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W.
      Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA MATURATION.
    18. "Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation."
      Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.
      Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF4631 AND TIF4632.
    19. "mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation."
      Coller J.M., Gray N.K., Wickens M.P.
      Genes Dev. 12:3226-3235(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA STABILITY.
    20. "Circularization of mRNA by eukaryotic translation initiation factors."
      Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.
      Mol. Cell 2:135-140(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF4631, ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP STRUCTURE.
    21. "RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G."
      Kessler S.H., Sachs A.B.
      Mol. Cell. Biol. 18:51-57(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF4632, MUTAGENESIS OF TYR-83 AND PHE-170.
    22. "Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation."
      Mangus D.A., Amrani N., Jacobson A.
      Mol. Cell. Biol. 18:7383-7396(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PBP1.
    23. "The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms."
      Otero L.J., Ashe M.P., Sachs A.B.
      EMBO J. 18:3153-3163(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATION STIMULATION, MUTAGENESIS OF 134-HIS--ASP-136; VAL-148; ASP-151; 157-ILE--THR-159; 175-GLU--GLY-177; 180-LYS-GLU-181; 184-ASP--LEU-186; 193-GLY--TYR-197 AND 199-ALA--LEU-202, INTERACTION WITH TIF4631 AND TIF4632.
    24. "The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex."
      Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.
      EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCP1 AND TIF4631.
    25. "The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes."
      Horton L.E., James P., Craig E.A., Hensold J.O.
      J. Biol. Chem. 276:14426-14433(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSA1.
    26. "Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
      Tharun S., Parker R.
      Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAT1.
    27. "Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae."
      Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.
      EMBO J. 21:1427-1436(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CCR4-NOT.
    28. "Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation."
      Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G., Philippe M., Zhouravleva G.
      Mol. Cell. Biol. 22:3301-3315(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUP35.
    29. "Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation."
      Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S., Katada T.
      J. Biol. Chem. 278:38287-38291(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH SUP35.
    30. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    31. "The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay."
      Kobayashi T., Funakoshi Y., Hoshino S., Katada T.
      J. Biol. Chem. 279:45693-45700(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUP35.
    32. "Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae."
      Trautwein M., Dengjel J., Schirle M., Spang A.
      Mol. Biol. Cell 15:5021-5037(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA TRANSPORT, INTERACTION WITH ARF1.
    33. Cited for: FUNCTION IN PAN REGULATION, INTERACTION WITH PAN3 AND PBP1.
    34. "A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay."
      Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A.
      Nature 432:112-118(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUP35.
    35. "Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export."
      Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N.
      Genes Dev. 19:90-103(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-12 AND LEU-15.
    36. "Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export."
      Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K.
      RNA 11:517-531(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, INTERACTION WITH CRM1 AND SXM1.
    37. "Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae."
      Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.
      Mol. Cell. Biol. 26:5237-5248(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPA1.
    38. "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-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "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-332 AND SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Solution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein."
      Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I., Sprules T., Gehring K.
      J. Biol. Chem. 277:22822-22828(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 489-577.

    Entry informationi

    Entry nameiPABP_YEAST
    AccessioniPrimary (citable) accession number: P04147
    Secondary accession number(s): D3DM73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 176 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 198000 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3