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 27-MAR-2024, entry version 248. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-4728; -. DR SMR; P04147; -. DR BioGRID; 36918; 731. DR DIP; DIP-2275N; -. DR IntAct; P04147; 217. DR MINT; P04147; -. DR STRING; 4932.YER165W; -. DR iPTMnet; P04147; -. DR MaxQB; P04147; -. DR PaxDb; 4932-YER165W; -. DR PeptideAtlas; P04147; -. DR EnsemblFungi; YER165W_mRNA; YER165W; YER165W. DR GeneID; 856912; -. DR KEGG; sce:YER165W; -. DR AGR; SGD:S000000967; -. 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; DHMNGKE; -. DR OrthoDB; 21912at2759; -. DR BioCyc; YEAST:G3O-30326-MONOMER; -. DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-SCE-72649; Translation initiation complex formation. 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 BioGRID-ORCS; 856912; 6 hits in 10 CRISPR screens. 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:0043232; C:intracellular non-membrane-bounded organelle; IDA:DisProt. 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:0140693; F:molecular condensate scaffold activity; IDA:DisProt. 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:0008428; F:ribonuclease inhibitor activity; IDA:SGD. 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; cd12378; RRM1_I_PABPs; 1. DR CDD; cd12379; RRM2_I_PABPs; 1. DR CDD; cd12380; RRM3_I_PABPs; 1. DR CDD; cd12381; RRM4_I_PABPs; 1. DR DisProt; DP01538; -. DR Gene3D; 3.30.70.330; -; 4. DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1. 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; IPR034364; PABP_RRM1. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR045305; RRM2_I_PABPs. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR003954; RRM_dom_euk. DR NCBIfam; TIGR01628; PABP-1234; 1. DR PANTHER; PTHR24012:SF491; POLYADENYLATE-BINDING PROTEIN; 1. DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1. 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; SSF63570; PABC (PABP) domain; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. 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; FT V-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 FT cap-dependent translation in vitro; when associated with FT N-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 FT cap-dependent translation in vitro; when associated with FT A-148." FT /evidence="ECO:0000269|PubMed:10357826" FT MUTAGEN 157..159 FT /note="IAT->VVC: In PAB1-157; greatly reduces FT poly(A)-dependent translation and stimulation of FT cap-dependent 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 FT PAB1-15; fails to bind RNA; when associated with V-83; FT V-263 and 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 FT poly(A)-dependent translation and stimulation of FT cap-dependent 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 FT cap-dependent translation in vitro. Impairs interaction FT with 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 FT cap-dependent translation in vitro. Impairs interaction FT with 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 FT poly(A)-dependent translation and stimulation of FT cap-dependent 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 //