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Polyadenylate-binding protein, cytoplasmic and nuclear (PABP) (Poly(A)-binding protein) (ARS consensus-binding protein ACBP-67) (Polyadenylate tail-binding protein)

 PABP_YEAST              Reviewed;         577 AA.
P04147; D3DM73;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 205.
RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
Short=PABP;
Short=Poly(A)-binding protein;
AltName: Full=ARS consensus-binding protein ACBP-67;
AltName: Full=Polyadenylate tail-binding protein;
Name=PAB1; OrderedLocusNames=YER165W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 9-29.
PubMed=3518950; DOI=10.1016/0092-8674(86)90557-X;
Sachs A.B., Bond M.W., Kornberg R.D.;
"A single gene from yeast for both nuclear and cytoplasmic
polyadenylate-binding proteins: domain structure and expression.";
Cell 45:827-835(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=3537727; DOI=10.1128/MCB.6.8.2932;
Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., Dreyfuss G.;
"mRNA polyadenylate-binding protein: gene isolation and sequencing and
identification of a ribonucleoprotein consensus sequence.";
Mol. Cell. Biol. 6:2932-2943(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
PROTEIN SEQUENCE OF 8-17; 167-173 AND 242-248, AND CHARACTERIZATION.
PubMed=8127652; DOI=10.1093/nar/22.1.32;
Cockell M., Frutiger S., Hughes G.J., Gasser S.M.;
"The yeast protein encoded by PUB1 binds T-rich single stranded DNA.";
Nucleic Acids Res. 22:32-40(1994).
[7]
RNA-BINDING.
PubMed=3313012; DOI=10.1128/MCB.7.9.3268;
Sachs A.B., Davis R.W., Kornberg R.D.;
"A single domain of yeast poly(A)-binding protein is necessary and
sufficient for RNA binding and cell viability.";
Mol. Cell. Biol. 7:3268-3276(1987).
[8]
FUNCTION IN TRANSLATION INITIATION.
PubMed=2673535; DOI=10.1016/0092-8674(89)90938-0;
Sachs A.B., Davis R.W.;
"The poly(A) binding protein is required for poly(A) shortening and
60S ribosomal subunit-dependent translation initiation.";
Cell 58:857-867(1989).
[9]
FUNCTION IN MRNA STABILIZATION.
PubMed=2565532; DOI=10.1128/MCB.9.2.659;
Bernstein P., Peltz S.W., Ross J.;
"The poly(A)-poly(A)-binding protein complex is a major determinant of
mRNA stability in vitro.";
Mol. Cell. Biol. 9:659-670(1989).
[10]
RNA-BINDING, AND DOMAINS.
PubMed=1675426; DOI=10.1128/MCB.11.7.3419;
Burd C.G., Matunis E.L., Dreyfuss G.;
"The multiple RNA-binding domains of the mRNA poly(A)-binding protein
have different RNA-binding activities.";
Mol. Cell. Biol. 11:3419-3424(1991).
[11]
SUBCELLULAR LOCATION.
PubMed=8413212; DOI=10.1128/MCB.13.10.6102;
Anderson J.T., Paddy M.R., Swanson M.S.;
"PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding
protein in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 13:6102-6113(1993).
[12]
FUNCTION.
PubMed=7557393; DOI=10.1101/gad.9.19.2421;
Caponigro G., Parker R.;
"Multiple functions for the poly(A)-binding protein in mRNA decapping
and deadenylation in yeast.";
Genes Dev. 9:2421-2432(1995).
[13]
INTERACTION WITH TIF4632.
PubMed=9003792;
Tarun S.Z. Jr., Sachs A.B.;
"Association of the yeast poly(A) tail binding protein with
translation initiation factor eIF-4G.";
EMBO J. 15:7168-7177(1996).
[14]
ACETYLATION AT ALA-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
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.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[15]
RNA-BINDING, AND MUTAGENESIS OF LEU-79; TYR-83; LYS-166; PHE-170;
LYS-259; PHE-263; LYS-362 AND PHE-366.
PubMed=9193001; DOI=10.1006/jmbi.1997.1013;
Deardorff J.A., Sachs A.B.;
"Differential effects of aromatic and charged residue substitutions in
the RNA binding domains of the yeast poly(A)-binding protein.";
J. Mol. Biol. 269:67-81(1997).
[16]
FUNCTION IN MRNA MATURATION, AND INTERACTION WITH RNA15.
PubMed=9199303; DOI=10.1128/MCB.17.7.3694;
Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.;
"Yeast Pab1 interacts with Rna15 and participates in the control of
the poly(A) tail length in vitro.";
Mol. Cell. Biol. 17:3694-3701(1997).
[17]
FUNCTION IN MRNA MATURATION.
PubMed=9223284; DOI=10.1073/pnas.94.15.7897;
Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y.,
Keller W.;
"The major yeast poly(A)-binding protein is associated with cleavage
factor IA and functions in premessenger RNA 3'-end formation.";
Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997).
[18]
INTERACTION WITH TIF4631 AND TIF4632.
PubMed=9256432; DOI=10.1073/pnas.94.17.9046;
Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.;
"Translation initiation factor eIF4G mediates in vitro poly(A) tail-
dependent translation.";
Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997).
[19]
FUNCTION IN MRNA STABILITY.
PubMed=9784497; DOI=10.1101/gad.12.20.3226;
Coller J.M., Gray N.K., Wickens M.P.;
"mRNA stabilization by poly(A) binding protein is independent of
poly(A) and requires translation.";
Genes Dev. 12:3226-3235(1998).
[20]
INTERACTION WITH TIF4631, AND ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP
STRUCTURE.
PubMed=9702200; DOI=10.1016/S1097-2765(00)80122-7;
Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.;
"Circularization of mRNA by eukaryotic translation initiation
factors.";
Mol. Cell 2:135-140(1998).
[21]
INTERACTION WITH TIF4632, AND MUTAGENESIS OF TYR-83 AND PHE-170.
PubMed=9418852; DOI=10.1128/MCB.18.1.51;
Kessler S.H., Sachs A.B.;
"RNA recognition motif 2 of yeast Pab1p is required for its functional
interaction with eukaryotic translation initiation factor 4G.";
Mol. Cell. Biol. 18:51-57(1998).
[22]
INTERACTION WITH PBP1.
PubMed=9819425; DOI=10.1128/MCB.18.12.7383;
Mangus D.A., Amrani N., Jacobson A.;
"Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-
binding protein, regulates polyadenylation.";
Mol. Cell. Biol. 18:7383-7396(1998).
[23]
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, AND
INTERACTION WITH TIF4631 AND TIF4632.
PubMed=10357826; DOI=10.1093/emboj/18.11.3153;
Otero L.J., Ashe M.P., Sachs A.B.;
"The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-
dependent and cap-dependent translation by distinct mechanisms.";
EMBO J. 18:3153-3163(1999).
[24]
INTERACTION WITH DCP1 AND TIF4631.
PubMed=10944120; DOI=10.1093/emboj/19.16.4372;
Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.;
"The eukaryotic mRNA decapping protein Dcp1 interacts physically and
functionally with the eIF4F translation initiation complex.";
EMBO J. 19:4372-4382(2000).
[25]
INTERACTION WITH SSA1.
PubMed=11279042; DOI=10.1074/jbc.M100266200;
Horton L.E., James P., Craig E.A., Hensold J.O.;
"The yeast hsp70 homologue Ssa is required for translation and
interacts with Sis1 and Pab1 on translating ribosomes.";
J. Biol. Chem. 276:14426-14433(2001).
[26]
FUNCTION IN MRNA DECAY, AND INTERACTION WITH PAT1.
PubMed=11741542; DOI=10.1016/S1097-2765(01)00395-1;
Tharun S., Parker R.;
"Targeting an mRNA for decapping: displacement of translation factors
and association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
Mol. Cell 8:1075-1083(2001).
[27]
FUNCTION IN REGULATION OF CCR4-NOT.
PubMed=11889048; DOI=10.1093/emboj/21.6.1427;
Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.;
"Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase
complex in Saccharomyces cerevisiae.";
EMBO J. 21:1427-1436(2002).
[28]
INTERACTION WITH SUP35.
PubMed=11971964; DOI=10.1128/MCB.22.10.3301-3315.2002;
Cosson B., Couturier A., Chabelskaya S., Kiktev D.,
Inge-Vechtomov S.G., Philippe M., Zhouravleva G.;
"Poly(A)-binding protein acts in translation termination via
eukaryotic release factor 3 interaction and does not influence
[PSI(+)] propagation.";
Mol. Cell. Biol. 22:3301-3315(2002).
[29]
FUNCTION IN MRNA DECAY, AND INTERACTION WITH SUP35.
PubMed=12923185; DOI=10.1074/jbc.C300300200;
Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y.,
Hoshino S., Katada T.;
"Translation termination factor eRF3 mediates mRNA decay through the
regulation of deadenylation.";
J. Biol. Chem. 278:38287-38291(2003).
[30]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[31]
INTERACTION WITH SUP35.
PubMed=15337765; DOI=10.1074/jbc.M405163200;
Kobayashi T., Funakoshi Y., Hoshino S., Katada T.;
"The GTP-binding release factor eRF3 as a key mediator coupling
translation termination to mRNA decay.";
J. Biol. Chem. 279:45693-45700(2004).
[32]
FUNCTION IN MRNA TRANSPORT, AND INTERACTION WITH ARF1.
PubMed=15356266; DOI=10.1091/mbc.E04-05-0411;
Trautwein M., Dengjel J., Schirle M., Spang A.;
"Arf1p provides an unexpected link between COPI vesicles and mRNA in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 15:5021-5037(2004).
[33]
FUNCTION IN PAN REGULATION, AND INTERACTION WITH PAN3 AND PBP1.
PubMed=15169912; DOI=10.1128/MCB.24.12.5521-5533.2004;
Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P.,
Jacobson A.;
"Positive and negative regulation of poly(A) nuclease.";
Mol. Cell. Biol. 24:5521-5533(2004).
[34]
INTERACTION WITH SUP35.
PubMed=15525991; DOI=10.1038/nature03060;
Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S.,
Jacobson A.;
"A faux 3'-UTR promotes aberrant termination and triggers nonsense-
mediated mRNA decay.";
Nature 432:112-118(2004).
[35]
FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LEU-12 AND LEU-15.
PubMed=15630021; DOI=10.1101/gad.1267005;
Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N.;
"Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease
complex recruited by Pab1, connect mRNA biogenesis to export.";
Genes Dev. 19:90-103(2005).
[36]
FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, AND INTERACTION WITH
CRM1 AND SXM1.
PubMed=15769879; DOI=10.1261/rna.7291205;
Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K.;
"Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and
the cytoplasm and functions in mRNA export.";
RNA 11:517-531(2005).
[37]
INTERACTION WITH TPA1.
PubMed=16809762; DOI=10.1128/MCB.02448-05;
Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.;
"Tpa1p is part of an mRNP complex that influences translation
termination, mRNA deadenylation, and mRNA turnover in Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 26:5237-5248(2006).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-405, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[40]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-337, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[41]
METHYLATION AT ARG-107.
PubMed=23865587; DOI=10.1021/pr400556c;
Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
"Analysis of the proteome of Saccharomyces cerevisiae for
methylarginine.";
J. Proteome Res. 12:3884-3899(2013).
[42]
STRUCTURE BY NMR OF 489-577.
PubMed=11940585; DOI=10.1074/jbc.M201230200;
Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I.,
Sprules T., Gehring K.;
"Solution structure of the orphan PABC domain from Saccharomyces
cerevisiae poly(A)-binding protein.";
J. Biol. Chem. 277:22822-22828(2002).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10357826,
ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:11889048,
ECO:0000269|PubMed:12923185, ECO:0000269|PubMed:15169912,
ECO:0000269|PubMed:15356266, ECO:0000269|PubMed:15630021,
ECO:0000269|PubMed:15769879, ECO:0000269|PubMed:2565532,
ECO:0000269|PubMed:2673535, ECO:0000269|PubMed:7557393,
ECO:0000269|PubMed:9199303, ECO:0000269|PubMed:9223284,
ECO:0000269|PubMed:9784497}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10357826,
ECO:0000269|PubMed:10944120, ECO:0000269|PubMed:11279042,
ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:11971964,
ECO:0000269|PubMed:12923185, ECO:0000269|PubMed:15169912,
ECO:0000269|PubMed:15337765, ECO:0000269|PubMed:15356266,
ECO:0000269|PubMed:15525991, ECO:0000269|PubMed:15769879,
ECO:0000269|PubMed:16809762, ECO:0000269|PubMed:9003792,
ECO:0000269|PubMed:9199303, ECO:0000269|PubMed:9256432,
ECO:0000269|PubMed:9418852, ECO:0000269|PubMed:9702200,
ECO:0000269|PubMed:9819425}.
-!- INTERACTION:
P07260:CDC33; NbExp=2; IntAct=EBI-12823, EBI-150;
P20448:HCA4; NbExp=2; IntAct=EBI-12823, EBI-5612;
P36102:PAN3; NbExp=5; IntAct=EBI-12823, EBI-12895;
P39935:TIF4631; NbExp=19; IntAct=EBI-12823, EBI-9002;
P39936:TIF4632; NbExp=4; IntAct=EBI-12823, EBI-9006;
-!- SUBCELLULAR LOCATION: 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.
-!- DOMAIN: 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. {ECO:0000269|PubMed:1675426}.
-!- MISCELLANEOUS: Present with 198000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
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EMBL; M12780; AAA34838.1; -; Genomic_DNA.
EMBL; M13371; AAA34787.1; -; Genomic_DNA.
EMBL; D00023; BAA00017.1; -; Genomic_DNA.
EMBL; U18922; AAB64692.1; -; Genomic_DNA.
EMBL; AY692854; AAT92873.1; -; Genomic_DNA.
EMBL; BK006939; DAA07827.1; -; Genomic_DNA.
PIR; A25221; DNBYPA.
RefSeq; NP_011092.1; NM_001179055.1.
PDB; 1IFW; NMR; -; A=491-577.
PDBsum; 1IFW; -.
ProteinModelPortal; P04147; -.
SMR; P04147; -.
BioGrid; 36918; 624.
DIP; DIP-2275N; -.
IntAct; P04147; 187.
MINT; MINT-693056; -.
STRING; 4932.YER165W; -.
iPTMnet; P04147; -.
MaxQB; P04147; -.
PRIDE; P04147; -.
EnsemblFungi; YER165W; YER165W; YER165W.
GeneID; 856912; -.
KEGG; sce:YER165W; -.
EuPathDB; FungiDB:YER165W; -.
SGD; S000000967; PAB1.
GeneTree; ENSGT00760000118913; -.
HOGENOM; HOG000217922; -.
InParanoid; P04147; -.
KO; K13126; -.
OMA; RAAYYPA; -.
OrthoDB; EOG092C3SCB; -.
BioCyc; YEAST:G3O-30326-MONOMER; -.
Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SCE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-SCE-450520; HuR (ELAVL1) binds and stabilizes mRNA.
Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
EvolutionaryTrace; P04147; -.
PRO; PR:P04147; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005840; C:ribosome; IDA:SGD.
GO; GO:0008143; F:poly(A) binding; IDA:SGD.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:SGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD.
GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 4.
SUPFAM; SSF54928; SSF54928; 2.
SUPFAM; SSF63570; SSF63570; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Methylation;
mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Translation regulation;
Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298649}.
CHAIN 2 577 Polyadenylate-binding protein,
cytoplasmic and nuclear.
/FTId=PRO_0000081720.
DOMAIN 38 116 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 126 203 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 219 296 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 322 399 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 489 568 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
REGION 9 61 Required and sufficient for nuclear
export. {ECO:0000255}.
REGION 281 317 Required and sufficient for nuclear
import. {ECO:0000255}.
REGION 473 577 Interaction with SUP35.
MOTIF 12 17 Nuclear export signal. {ECO:0000255}.
COMPBIAS 422 431 Poly-Ala.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:9298649}.
MOD_RES 107 107 Omega-N-methylarginine.
{ECO:0000269|PubMed:23865587}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 337 337 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 12 12 L->A: Impairs nuclear export; when
associated with A-15.
{ECO:0000269|PubMed:15630021}.
MUTAGEN 15 15 L->A: Impairs nuclear export; when
associated with A-12.
{ECO:0000269|PubMed:15630021}.
MUTAGEN 79 79 L->A: In PAB1-14; fails to bind poly(U),
but not poly(A) RNA; when associated with
Q-166; Q-259 and Q-362.
{ECO:0000269|PubMed:9193001}.
MUTAGEN 83 83 Y->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. {ECO:0000269|PubMed:9193001,
ECO:0000269|PubMed:9418852}.
MUTAGEN 134 136 HPD->DKS: In PAB1-134.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 148 148 V->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.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 151 151 D->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.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 157 159 IAT->VVC: In PAB1-157; greatly reduces
poly(A)-dependent translation and
stimulation of cap-dependent translation
in vitro. {ECO:0000269|PubMed:10357826}.
MUTAGEN 166 166 K->Q: In PAB1-14; fails to bind poly(U),
but not poly(A) RNA; when associated with
A-79; Q-259 and Q-362.
{ECO:0000269|PubMed:9193001}.
MUTAGEN 170 170 F->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.
{ECO:0000269|PubMed:9193001,
ECO:0000269|PubMed:9418852}.
MUTAGEN 175 177 EEG->TQE: In PAB1-175; greatly reduces
poly(A)-dependent translation and
stimulation of cap-dependent translation
in vitro. {ECO:0000269|PubMed:10357826}.
MUTAGEN 180 181 KE->ER: In PAB1-180; abolishes poly(A)-
dependent translation and greatly reduces
stimulation of cap-dependent translation
in vitro. Impairs interaction with eIF4G.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 184 186 DAL->EKM: In PAB1-184; abolishes poly(A)-
dependent translation and moderately
reduces stimulation of cap-dependent
translation in vitro. Impairs interaction
with eIF4G.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 193 197 GQEIY->DRKVF: In PAB1-193; moderately
reduces stimulation of cap-dependent
translation in vitro.
{ECO:0000269|PubMed:10357826}.
MUTAGEN 199 202 APHL->GRFK: In PAB1-199; moderately
reduces poly(A)-dependent translation and
stimulation of cap-dependent translation
in vitro. {ECO:0000269|PubMed:10357826}.
MUTAGEN 259 259 K->Q: In PAB1-14; fails to bind poly(U),
but not poly(A) RNA; when associated with
A-79; Q-166 and Q-362.
{ECO:0000269|PubMed:9193001}.
MUTAGEN 263 263 F->V: In PAB1-7. In PAB1-15; fails to
bind RNA; when associated with V-83; V-
170 and V-366.
{ECO:0000269|PubMed:9193001}.
MUTAGEN 362 362 K->Q: In PAB1-14; fails to bind poly(U),
but not poly(A) RNA; when associated with
A-79; Q-166 and Q-259.
{ECO:0000269|PubMed:9193001}.
MUTAGEN 366 366 F->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.
{ECO:0000269|PubMed:9193001}.
CONFLICT 426 426 A -> R (in Ref. 1; AAA34838).
{ECO:0000305}.
HELIX 503 517 {ECO:0000244|PDB:1IFW}.
HELIX 518 520 {ECO:0000244|PDB:1IFW}.
HELIX 524 534 {ECO:0000244|PDB:1IFW}.
HELIX 539 546 {ECO:0000244|PDB:1IFW}.
HELIX 549 568 {ECO:0000244|PDB:1IFW}.
SEQUENCE 577 AA; 64344 MW; 4F97E494753E17C7 CRC64;
MADITDKTAE QLENLNIQDD QKQAATGSES QSVENSSASL YVGDLEPSVS EAHLYDIFSP
IGSVSSIRVC RDAITKTSLG YAYVNFNDHE AGRKAIEQLN YTPIKGRLCR IMWSQRDPSL
RKKGSGNIFI KNLHPDIDNK ALYDTFSVFG DILSSKIATD ENGKSKGFGF VHFEEEGAAK
EAIDALNGML LNGQEIYVAP HLSRKERDSQ LEETKAHYTN LYVKNINSET TDEQFQELFA
KFGPIVSASL EKDADGKLKG FGFVNYEKHE DAVKAVEALN DSELNGEKLY VGRAQKKNER
MHVLKKQYEA YRLEKMAKYQ GVNLFVKNLD DSVDDEKLEE EFAPYGTITS AKVMRTENGK
SKGFGFVCFS TPEEATKAIT EKNQQIVAGK PLYVAIAQRK DVRRSQLAQQ IQARNQMRYQ
QATAAAAAAA AGMPGQFMPP MFYGVMPPRG VPFNGPNPQQ MNPMGGMPKN GMPPQFRNGP
VYGVPPQGGF PRNANDNNQF YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ
EVFPLLESDE LFEQHYKEAS AAYESFKKEQ EQQTEQA


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