PABP_YEAST
ID PABP_YEAST Reviewed; 577 AA.
AC P04147; D3DM73;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
DE Short=PABP;
DE Short=Poly(A)-binding protein;
DE AltName: Full=ARS consensus-binding protein ACBP-67;
DE AltName: Full=Polyadenylate tail-binding protein;
GN Name=PAB1; OrderedLocusNames=YER165W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 9-29.
RX PubMed=3518950; DOI=10.1016/0092-8674(86)90557-x;
RA Sachs A.B., Bond M.W., Kornberg R.D.;
RT "A single gene from yeast for both nuclear and cytoplasmic polyadenylate-
RT binding proteins: domain structure and expression.";
RL Cell 45:827-835(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3537727; DOI=10.1128/mcb.6.8.2932-2943.1986;
RA Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., Dreyfuss G.;
RT "mRNA polyadenylate-binding protein: gene isolation and sequencing and
RT identification of a ribonucleoprotein consensus sequence.";
RL Mol. Cell. Biol. 6:2932-2943(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 8-17; 167-173 AND 242-248, AND CHARACTERIZATION.
RX PubMed=8127652; DOI=10.1093/nar/22.1.32;
RA Cockell M., Frutiger S., Hughes G.J., Gasser S.M.;
RT "The yeast protein encoded by PUB1 binds T-rich single stranded DNA.";
RL Nucleic Acids Res. 22:32-40(1994).
RN [7]
RP RNA-BINDING.
RX PubMed=3313012; DOI=10.1128/mcb.7.9.3268-3276.1987;
RA Sachs A.B., Davis R.W., Kornberg R.D.;
RT "A single domain of yeast poly(A)-binding protein is necessary and
RT sufficient for RNA binding and cell viability.";
RL Mol. Cell. Biol. 7:3268-3276(1987).
RN [8]
RP FUNCTION IN TRANSLATION INITIATION.
RX PubMed=2673535; DOI=10.1016/0092-8674(89)90938-0;
RA Sachs A.B., Davis R.W.;
RT "The poly(A) binding protein is required for poly(A) shortening and 60S
RT ribosomal subunit-dependent translation initiation.";
RL Cell 58:857-867(1989).
RN [9]
RP FUNCTION IN MRNA STABILIZATION.
RX PubMed=2565532; DOI=10.1128/mcb.9.2.659-670.1989;
RA Bernstein P., Peltz S.W., Ross J.;
RT "The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA
RT stability in vitro.";
RL Mol. Cell. Biol. 9:659-670(1989).
RN [10]
RP RNA-BINDING, AND DOMAINS.
RX PubMed=1675426; DOI=10.1128/mcb.11.7.3419-3424.1991;
RA Burd C.G., Matunis E.L., Dreyfuss G.;
RT "The multiple RNA-binding domains of the mRNA poly(A)-binding protein have
RT different RNA-binding activities.";
RL Mol. Cell. Biol. 11:3419-3424(1991).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=8413212; DOI=10.1128/mcb.13.10.6102-6113.1993;
RA Anderson J.T., Paddy M.R., Swanson M.S.;
RT "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein
RT in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:6102-6113(1993).
RN [12]
RP FUNCTION.
RX PubMed=7557393; DOI=10.1101/gad.9.19.2421;
RA Caponigro G., Parker R.;
RT "Multiple functions for the poly(A)-binding protein in mRNA decapping and
RT deadenylation in yeast.";
RL Genes Dev. 9:2421-2432(1995).
RN [13]
RP INTERACTION WITH TIF4632.
RX PubMed=9003792; DOI=10.1002/j.1460-2075.1996.tb01108.x;
RA Tarun S.Z. Jr., Sachs A.B.;
RT "Association of the yeast poly(A) tail binding protein with translation
RT initiation factor eIF-4G.";
RL EMBO J. 15:7168-7177(1996).
RN [14]
RP ACETYLATION AT ALA-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [15]
RP RNA-BINDING, AND MUTAGENESIS OF LEU-79; TYR-83; LYS-166; PHE-170; LYS-259;
RP PHE-263; LYS-362 AND PHE-366.
RX PubMed=9193001; DOI=10.1006/jmbi.1997.1013;
RA Deardorff J.A., Sachs A.B.;
RT "Differential effects of aromatic and charged residue substitutions in the
RT RNA binding domains of the yeast poly(A)-binding protein.";
RL J. Mol. Biol. 269:67-81(1997).
RN [16]
RP FUNCTION IN MRNA MATURATION, AND INTERACTION WITH RNA15.
RX PubMed=9199303; DOI=10.1128/mcb.17.7.3694;
RA Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.;
RT "Yeast Pab1 interacts with Rna15 and participates in the control of the
RT poly(A) tail length in vitro.";
RL Mol. Cell. Biol. 17:3694-3701(1997).
RN [17]
RP FUNCTION IN MRNA MATURATION.
RX PubMed=9223284; DOI=10.1073/pnas.94.15.7897;
RA Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W.;
RT "The major yeast poly(A)-binding protein is associated with cleavage factor
RT IA and functions in premessenger RNA 3'-end formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997).
RN [18]
RP INTERACTION WITH TIF4631 AND TIF4632.
RX PubMed=9256432; DOI=10.1073/pnas.94.17.9046;
RA Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.;
RT "Translation initiation factor eIF4G mediates in vitro poly(A) tail-
RT dependent translation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997).
RN [19]
RP FUNCTION IN MRNA STABILITY.
RX PubMed=9784497; DOI=10.1101/gad.12.20.3226;
RA Coller J.M., Gray N.K., Wickens M.P.;
RT "mRNA stabilization by poly(A) binding protein is independent of poly(A)
RT and requires translation.";
RL Genes Dev. 12:3226-3235(1998).
RN [20]
RP INTERACTION WITH TIF4631, AND ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP
RP STRUCTURE.
RX PubMed=9702200; DOI=10.1016/s1097-2765(00)80122-7;
RA Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.;
RT "Circularization of mRNA by eukaryotic translation initiation factors.";
RL Mol. Cell 2:135-140(1998).
RN [21]
RP INTERACTION WITH TIF4632, AND MUTAGENESIS OF TYR-83 AND PHE-170.
RX PubMed=9418852; DOI=10.1128/mcb.18.1.51;
RA Kessler S.H., Sachs A.B.;
RT "RNA recognition motif 2 of yeast Pab1p is required for its functional
RT interaction with eukaryotic translation initiation factor 4G.";
RL Mol. Cell. Biol. 18:51-57(1998).
RN [22]
RP INTERACTION WITH PBP1.
RX PubMed=9819425; DOI=10.1128/mcb.18.12.7383;
RA Mangus D.A., Amrani N., Jacobson A.;
RT "Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding
RT protein, regulates polyadenylation.";
RL Mol. Cell. Biol. 18:7383-7396(1998).
RN [23]
RP FUNCTION IN TRANSLATION STIMULATION, MUTAGENESIS OF 134-HIS--ASP-136;
RP VAL-148; ASP-151; 157-ILE--THR-159; 175-GLU--GLY-177; 180-LYS-GLU-181;
RP 184-ASP--LEU-186; 193-GLY--TYR-197 AND 199-ALA--LEU-202, AND INTERACTION
RP WITH TIF4631 AND TIF4632.
RX PubMed=10357826; DOI=10.1093/emboj/18.11.3153;
RA Otero L.J., Ashe M.P., Sachs A.B.;
RT "The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-
RT dependent and cap-dependent translation by distinct mechanisms.";
RL EMBO J. 18:3153-3163(1999).
RN [24]
RP INTERACTION WITH DCP1 AND TIF4631.
RX PubMed=10944120; DOI=10.1093/emboj/19.16.4372;
RA Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.;
RT "The eukaryotic mRNA decapping protein Dcp1 interacts physically and
RT functionally with the eIF4F translation initiation complex.";
RL EMBO J. 19:4372-4382(2000).
RN [25]
RP INTERACTION WITH SSA1.
RX PubMed=11279042; DOI=10.1074/jbc.m100266200;
RA Horton L.E., James P., Craig E.A., Hensold J.O.;
RT "The yeast hsp70 homologue Ssa is required for translation and interacts
RT with Sis1 and Pab1 on translating ribosomes.";
RL J. Biol. Chem. 276:14426-14433(2001).
RN [26]
RP FUNCTION IN MRNA DECAY, AND INTERACTION WITH PAT1.
RX PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1;
RA Tharun S., Parker R.;
RT "Targeting an mRNA for decapping: displacement of translation factors and
RT association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
RL Mol. Cell 8:1075-1083(2001).
RN [27]
RP FUNCTION IN REGULATION OF CCR4-NOT.
RX PubMed=11889048; DOI=10.1093/emboj/21.6.1427;
RA Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.;
RT "Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase
RT complex in Saccharomyces cerevisiae.";
RL EMBO J. 21:1427-1436(2002).
RN [28]
RP INTERACTION WITH SUP35.
RX PubMed=11971964; DOI=10.1128/mcb.22.10.3301-3315.2002;
RA Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G.,
RA Philippe M., Zhouravleva G.;
RT "Poly(A)-binding protein acts in translation termination via eukaryotic
RT release factor 3 interaction and does not influence [PSI(+)] propagation.";
RL Mol. Cell. Biol. 22:3301-3315(2002).
RN [29]
RP FUNCTION IN MRNA DECAY, AND INTERACTION WITH SUP35.
RX PubMed=12923185; DOI=10.1074/jbc.c300300200;
RA Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S.,
RA Katada T.;
RT "Translation termination factor eRF3 mediates mRNA decay through the
RT regulation of deadenylation.";
RL J. Biol. Chem. 278:38287-38291(2003).
RN [30]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [31]
RP INTERACTION WITH SUP35.
RX PubMed=15337765; DOI=10.1074/jbc.m405163200;
RA Kobayashi T., Funakoshi Y., Hoshino S., Katada T.;
RT "The GTP-binding release factor eRF3 as a key mediator coupling translation
RT termination to mRNA decay.";
RL J. Biol. Chem. 279:45693-45700(2004).
RN [32]
RP FUNCTION IN MRNA TRANSPORT, AND INTERACTION WITH ARF1.
RX PubMed=15356266; DOI=10.1091/mbc.e04-05-0411;
RA Trautwein M., Dengjel J., Schirle M., Spang A.;
RT "Arf1p provides an unexpected link between COPI vesicles and mRNA in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:5021-5037(2004).
RN [33]
RP FUNCTION IN PAN REGULATION, AND INTERACTION WITH PAN3 AND PBP1.
RX PubMed=15169912; DOI=10.1128/mcb.24.12.5521-5533.2004;
RA Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P., Jacobson A.;
RT "Positive and negative regulation of poly(A) nuclease.";
RL Mol. Cell. Biol. 24:5521-5533(2004).
RN [34]
RP INTERACTION WITH SUP35.
RX PubMed=15525991; DOI=10.1038/nature03060;
RA Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A.;
RT "A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated
RT mRNA decay.";
RL Nature 432:112-118(2004).
RN [35]
RP FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-12
RP AND LEU-15.
RX PubMed=15630021; DOI=10.1101/gad.1267005;
RA Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N.;
RT "Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex
RT recruited by Pab1, connect mRNA biogenesis to export.";
RL Genes Dev. 19:90-103(2005).
RN [36]
RP FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, AND INTERACTION WITH CRM1
RP AND SXM1.
RX PubMed=15769879; DOI=10.1261/rna.7291205;
RA Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K.;
RT "Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the
RT cytoplasm and functions in mRNA export.";
RL RNA 11:517-531(2005).
RN [37]
RP INTERACTION WITH TPA1.
RX PubMed=16809762; DOI=10.1128/mcb.02448-05;
RA Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.;
RT "Tpa1p is part of an mRNP complex that influences translation termination,
RT mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:5237-5248(2006).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [40]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [41]
RP METHYLATION AT ARG-107.
RX PubMed=23865587; DOI=10.1021/pr400556c;
RA Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL J. Proteome Res. 12:3884-3899(2013).
RN [42]
RP STRUCTURE BY NMR OF 489-577.
RX PubMed=11940585; DOI=10.1074/jbc.m201230200;
RA Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I.,
RA Sprules T., Gehring K.;
RT "Solution structure of the orphan PABC domain from Saccharomyces cerevisiae
RT poly(A)-binding protein.";
RL J. Biol. Chem. 277:22822-22828(2002).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important
CC mediator of the multiple roles of the poly(A) tail in mRNA biogenesis,
CC stability and translation. In the nucleus, interacts with the nuclear
CC cleavage factor IA (CFIA), which is required for both mRNA cleavage and
CC polyadenylation. Is also required for efficient mRNA export to the
CC cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to
CC affect poly(A) tail shortening, which may occur concomitantly with
CC either nucleocytoplasmic mRNA transport or translational initiation.
CC Regulates PAN activity via interaction with the stimulator PAN3 or the
CC inhibitor PBP1. In the cytoplasm, affects both translation and mRNA
CC decay. Stimulates translation by interaction with translation
CC initiation factor eIF4G, a subunit of the cap-binding complex eIF4F,
CC bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of
CC this circular mRNP structure appears to be critical for the synergistic
CC effects of the cap and the poly(A) tail in facilitating translation
CC initiation, recycling of ribosomes, and mRNA stability. Also regulates
CC translation termination by recruiting eukaryotic release factor 3
CC (eRF3). Interaction with eRF3 is also required for regulation of normal
CC mRNA decay through translation termination-coupled poly(A) shortening,
CC probably mediated by PAN. Loss of PAB1 from the mRNP after
CC deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic
CC mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with
CC COPI vesicles through its interaction with ARF1, and this is required
CC for correct localization of the asymmetrically distributed ASH1 mRNA.
CC {ECO:0000269|PubMed:10357826, ECO:0000269|PubMed:11741542,
CC ECO:0000269|PubMed:11889048, ECO:0000269|PubMed:12923185,
CC ECO:0000269|PubMed:15169912, ECO:0000269|PubMed:15356266,
CC ECO:0000269|PubMed:15630021, ECO:0000269|PubMed:15769879,
CC ECO:0000269|PubMed:2565532, ECO:0000269|PubMed:2673535,
CC ECO:0000269|PubMed:7557393, ECO:0000269|PubMed:9199303,
CC ECO:0000269|PubMed:9223284, ECO:0000269|PubMed:9784497}.
CC -!- SUBUNIT: Binds to poly(A) mRNA to form a periodic structure with a
CC packing density of one molecule per 25 adenylate residues. Interacts
CC with the nuclear export factor CRM1 and with the importin SXM1.
CC Interacts with RNA15, a component of the cleavage factor IA (CFIA)
CC complex. Interacts with translation initiation factor eIF4G (TIF4631 or
CC TIF4632) and release factor eRF3 (SUP35). Interacts with the PAB-
CC dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3.
CC Interacts with ARF1, DCP1, PBP1, the Hsp70 chaperone SSA1, and TPA1.
CC Interacts with PAT1 in an RNA-dependent manner.
CC {ECO:0000269|PubMed:10357826, ECO:0000269|PubMed:10944120,
CC ECO:0000269|PubMed:11279042, ECO:0000269|PubMed:11741542,
CC ECO:0000269|PubMed:11971964, ECO:0000269|PubMed:12923185,
CC ECO:0000269|PubMed:15169912, ECO:0000269|PubMed:15337765,
CC ECO:0000269|PubMed:15356266, ECO:0000269|PubMed:15525991,
CC ECO:0000269|PubMed:15769879, ECO:0000269|PubMed:16809762,
CC ECO:0000269|PubMed:9003792, ECO:0000269|PubMed:9199303,
CC ECO:0000269|PubMed:9256432, ECO:0000269|PubMed:9418852,
CC ECO:0000269|PubMed:9702200, ECO:0000269|PubMed:9819425}.
CC -!- INTERACTION:
CC P04147; P53849: GIS2; NbExp=2; IntAct=EBI-12823, EBI-29244;
CC P04147; P36102: PAN3; NbExp=5; IntAct=EBI-12823, EBI-12895;
CC P04147; P39935: TIF4631; NbExp=16; IntAct=EBI-12823, EBI-9002;
CC P04147; P39936: TIF4632; NbExp=2; IntAct=EBI-12823, EBI-9006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm.
CC Can be exported from the nucleus through at least 2 distinct pathways,
CC the main being dependent on the exportin CRM1, and the second requiring
CC MEX67 and ongoing mRNA export. Import is mediated by the importin SXM1.
CC -!- DOMAIN: RNA recognition motifs (RRMs) 1 and 2 bind specifically to the
CC poly(A) tail, whereas RRMs 3 and 4 bind non-specifically to
CC polypyrimidine RNAs and may serve to bind to a different part of the
CC messenger or to other RNAs. RRM 2 also mediates interaction with eIF-
CC 4G. {ECO:0000269|PubMed:1675426}.
CC -!- MISCELLANEOUS: Present with 198000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; M12780; AAA34838.1; -; Genomic_DNA.
DR EMBL; M13371; AAA34787.1; -; Genomic_DNA.
DR EMBL; D00023; BAA00017.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64692.1; -; Genomic_DNA.
DR EMBL; AY692854; AAT92873.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07827.1; -; Genomic_DNA.
DR PIR; A25221; DNBYPA.
DR RefSeq; NP_011092.1; NM_001179055.1.
DR PDB; 1IFW; NMR; -; A=491-577.
DR PDB; 6R5K; EM; 4.80 A; D/F/H=1-577.
DR PDBsum; 1IFW; -.
DR PDBsum; 6R5K; -.
DR AlphaFoldDB; P04147; -.
DR BMRB; P04147; -.
DR SMR; P04147; -.
DR BioGRID; 36918; 684.
DR DIP; DIP-2275N; -.
DR IntAct; P04147; 217.
DR MINT; P04147; -.
DR STRING; 4932.YER165W; -.
DR iPTMnet; P04147; -.
DR MaxQB; P04147; -.
DR PaxDb; P04147; -.
DR PRIDE; P04147; -.
DR EnsemblFungi; YER165W_mRNA; YER165W; YER165W.
DR GeneID; 856912; -.
DR KEGG; sce:YER165W; -.
DR SGD; S000000967; PAB1.
DR VEuPathDB; FungiDB:YER165W; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000169027; -.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; P04147; -.
DR OMA; HNESLKA; -.
DR BioCyc; YEAST:G3O-30326-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P04147; -.
DR PRO; PR:P04147; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P04147; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IDA:SGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0008143; F:poly(A) binding; IDA:SGD.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:SGD.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR DisProt; DP01538; -.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Translation regulation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..577
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000081720"
FT DOMAIN 38..116
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 126..203
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 219..296
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 322..399
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 489..568
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..61
FT /note="Required and sufficient for nuclear export"
FT /evidence="ECO:0000255"
FT REGION 281..317
FT /note="Required and sufficient for nuclear import"
FT /evidence="ECO:0000255"
FT REGION 473..577
FT /note="Interaction with SUP35"
FT MOTIF 12..17
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 9..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:23865587"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 12
FT /note="L->A: Impairs nuclear export; when associated with
FT A-15."
FT /evidence="ECO:0000269|PubMed:15630021"
FT MUTAGEN 15
FT /note="L->A: Impairs nuclear export; when associated with
FT A-12."
FT /evidence="ECO:0000269|PubMed:15630021"
FT MUTAGEN 79
FT /note="L->A: In PAB1-14; fails to bind poly(U), but not
FT poly(A) RNA; when associated with Q-166; Q-259 and Q-362."
FT /evidence="ECO:0000269|PubMed:9193001"
FT MUTAGEN 83
FT /note="Y->V: In PAB1-16; reduces affinity for oligo(A)
FT about 100-fold, impairs poly(A)-dependent translation, but
FT still interacts with eIF4G; when associated with V-170. In
FT PAB1-15; fails to bind RNA; when associated with V-170; V-
FT 263 and V-366."
FT /evidence="ECO:0000269|PubMed:9193001,
FT ECO:0000269|PubMed:9418852"
FT MUTAGEN 134..136
FT /note="HPD->DKS: In PAB1-134."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 148
FT /note="V->A: In PAB1-148; greatly reduces poly(A)-dependent
FT translation and moderately reduces stimulation of cap-
FT dependent translation in vitro; when associated with N-
FT 151."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 151
FT /note="D->N: In PAB1-148; greatly reduces poly(A)-dependent
FT translation and moderately reduces stimulation of cap-
FT dependent translation in vitro; when associated with A-
FT 148."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 157..159
FT /note="IAT->VVC: In PAB1-157; greatly reduces poly(A)-
FT dependent translation and stimulation of cap-dependent
FT translation in vitro."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 166
FT /note="K->Q: In PAB1-14; fails to bind poly(U), but not
FT poly(A) RNA; when associated with A-79; Q-259 and Q-362."
FT /evidence="ECO:0000269|PubMed:9193001"
FT MUTAGEN 170
FT /note="F->V: In PAB1-6; selectively reduces poly(A) RNA
FT binding. In PAB1-16; reduces affinity for oligo(A) about
FT 100-fold, impairs poly(A)-dependent translation, but still
FT interacts with eIF4G; when associated with V-83. In PAB1-
FT 15; fails to bind RNA; when associated with V-83; V-263 and
FT V-366."
FT /evidence="ECO:0000269|PubMed:9193001,
FT ECO:0000269|PubMed:9418852"
FT MUTAGEN 175..177
FT /note="EEG->TQE: In PAB1-175; greatly reduces poly(A)-
FT dependent translation and stimulation of cap-dependent
FT translation in vitro."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 180..181
FT /note="KE->ER: In PAB1-180; abolishes poly(A)-dependent
FT translation and greatly reduces stimulation of cap-
FT dependent translation in vitro. Impairs interaction with
FT eIF4G."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 184..186
FT /note="DAL->EKM: In PAB1-184; abolishes poly(A)-dependent
FT translation and moderately reduces stimulation of cap-
FT dependent translation in vitro. Impairs interaction with
FT eIF4G."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 193..197
FT /note="GQEIY->DRKVF: In PAB1-193; moderately reduces
FT stimulation of cap-dependent translation in vitro."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 199..202
FT /note="APHL->GRFK: In PAB1-199; moderately reduces poly(A)-
FT dependent translation and stimulation of cap-dependent
FT translation in vitro."
FT /evidence="ECO:0000269|PubMed:10357826"
FT MUTAGEN 259
FT /note="K->Q: In PAB1-14; fails to bind poly(U), but not
FT poly(A) RNA; when associated with A-79; Q-166 and Q-362."
FT /evidence="ECO:0000269|PubMed:9193001"
FT MUTAGEN 263
FT /note="F->V: In PAB1-7. In PAB1-15; fails to bind RNA; when
FT associated with V-83; V-170 and V-366."
FT /evidence="ECO:0000269|PubMed:9193001"
FT MUTAGEN 362
FT /note="K->Q: In PAB1-14; fails to bind poly(U), but not
FT poly(A) RNA; when associated with A-79; Q-166 and Q-259."
FT /evidence="ECO:0000269|PubMed:9193001"
FT MUTAGEN 366
FT /note="F->V: In PAB1-8; selectively reduces poly(U) RNA
FT binding. In PAB1-15; fails to bind RNA; when associated
FT with V-83; V-170 and V-263."
FT /evidence="ECO:0000269|PubMed:9193001"
FT CONFLICT 426
FT /note="A -> R (in Ref. 1; AAA34838)"
FT /evidence="ECO:0000305"
FT HELIX 503..517
FT /evidence="ECO:0007829|PDB:1IFW"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:1IFW"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:1IFW"
FT HELIX 539..546
FT /evidence="ECO:0007829|PDB:1IFW"
FT HELIX 549..568
FT /evidence="ECO:0007829|PDB:1IFW"
SQ 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
