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P04147

- PABP_YEAST

UniProt

P04147 - PABP_YEAST

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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

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. 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
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA transport, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30326-MONOMER.
ReactomeiREACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.

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
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi193 – 1975GQEIY → DRKVF in PAB1-193; moderately reduces stimulation of cap-dependent translation in vitro. 1 Publication
Mutagenesisi199 – 2024APHL → GRFK in PAB1-199; moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. 1 Publication
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 residuei107 – 1071Omega-N-methylarginine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei332 – 3321Phosphoserine1 Publication
Modified residuei405 – 4051Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Methylation, 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. 232 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 – 51715Combined sources
Helixi518 – 5203Combined sources
Helixi524 – 53411Combined sources
Helixi539 – 5468Combined sources
Helixi549 – 56820Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFWNMR-A491-577[»]
ProteinModelPortaliP04147.
SMRiP04147. Positions 38-453, 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.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
InParanoidiP04147.
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

        10         20         30         40         50
MADITDKTAE QLENLNIQDD QKQAATGSES QSVENSSASL YVGDLEPSVS
60 70 80 90 100
EAHLYDIFSP IGSVSSIRVC RDAITKTSLG YAYVNFNDHE AGRKAIEQLN
110 120 130 140 150
YTPIKGRLCR IMWSQRDPSL RKKGSGNIFI KNLHPDIDNK ALYDTFSVFG
160 170 180 190 200
DILSSKIATD ENGKSKGFGF VHFEEEGAAK EAIDALNGML LNGQEIYVAP
210 220 230 240 250
HLSRKERDSQ LEETKAHYTN LYVKNINSET TDEQFQELFA KFGPIVSASL
260 270 280 290 300
EKDADGKLKG FGFVNYEKHE DAVKAVEALN DSELNGEKLY VGRAQKKNER
310 320 330 340 350
MHVLKKQYEA YRLEKMAKYQ GVNLFVKNLD DSVDDEKLEE EFAPYGTITS
360 370 380 390 400
AKVMRTENGK SKGFGFVCFS TPEEATKAIT EKNQQIVAGK PLYVAIAQRK
410 420 430 440 450
DVRRSQLAQQ IQARNQMRYQ QATAAAAAAA AGMPGQFMPP MFYGVMPPRG
460 470 480 490 500
VPFNGPNPQQ MNPMGGMPKN GMPPQFRNGP VYGVPPQGGF PRNANDNNQF
510 520 530 540 550
YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ EVFPLLESDE
560 570
LFEQHYKEAS AAYESFKKEQ EQQTEQA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IFW NMR - A 491-577 [» ]
ProteinModelPortali P04147.
SMRi P04147. Positions 38-453, 489-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36918. 232 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 ENSGT00760000118913.
HOGENOMi HOG000217922.
InParanoidi P04147.
KOi K13126.
OMAi AGRNGNF.
OrthoDBi EOG706125.

Enzyme and pathway databases

BioCyci YEAST:G3O-30326-MONOMER.
Reactomei REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.

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

« Hide 'large scale' publications
  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. "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine."
    Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.
    J. Proteome Res. 12:3884-3899(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-107.
  42. "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: November 26, 2014
This is version 178 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