PABP1_HUMAN
ID PABP1_HUMAN Reviewed; 636 AA.
AC P11940; Q15097; Q93004;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 254.
DE RecName: Full=Polyadenylate-binding protein 1 {ECO:0000305};
DE Short=PABP-1;
DE Short=Poly(A)-binding protein 1;
GN Name=PABPC1 {ECO:0000312|HGNC:HGNC:8554};
GN Synonyms=PAB1, PABP {ECO:0000303|PubMed:20102337}, PABP1, PABPC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2885805; DOI=10.1093/nar/15.12.4771;
RA Grange T., de Sa C.M., Oddos J., Pictet R.;
RT "Human mRNA polyadenylate binding protein: evolutionary conservation of a
RT nucleic acid binding motif.";
RL Nucleic Acids Res. 15:4771-4787(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RA Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O.;
RT "The human poly(A)-binding protein (PABP) gene: structural and functional
RT analysis.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-636 (ISOFORM 2).
RA Murphy E.P., McKenna N.J., Headon D.R.;
RT "Nucleotide sequence of a partial cDNA encoding a novel human
RT polyadenylate-binding protein.";
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 158-166; 189-196; 214-221;
RP 232-240; 291-309; 312-324; 357-370; 375-385; 482-506; 566-580 AND 605-620,
RP METHYLATION AT ARG-493, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166;
RP 187-208; 214-221; 232-240; 291-324; 334-348; 357-370; 375-385; 482-506;
RP 519-559; 566-620 AND 626-636, METHYLATION AT LYS-299 AND ARG-493, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=7908267; DOI=10.1006/excr.1994.1104;
RA Goerlach M., Burd C.G., Dreyfuss G.;
RT "The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding
RT specificity.";
RL Exp. Cell Res. 211:400-407(1994).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9582337; DOI=10.1074/jbc.273.21.13015;
RA Afonina E., Stauber R., Pavlakis G.N.;
RT "The human poly(A)-binding protein 1 shuttles between the nucleus and the
RT cytoplasm.";
RL J. Biol. Chem. 273:13015-13021(1998).
RN [10]
RP INTERACTION WITH PAIP1, AND DOMAIN.
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP
RT enhances translation.";
RL Nature 392:520-523(1998).
RN [11]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION IN A
RP COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
RX PubMed=11051545; DOI=10.1016/s0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction between
RT the poly(A) tail and a c-fos RNA coding determinant via a protein
RT complex.";
RL Cell 103:29-40(2000).
RN [12]
RP INTERACTION WITH PAIP2.
RX PubMed=11172725; DOI=10.1016/s1097-2765(01)00168-x;
RA Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
RA Burley S.K., Sonenberg N.;
RT "Translational repression by a novel partner of human poly(A) binding
RT protein, Paip2.";
RL Mol. Cell 7:205-216(2001).
RN [13]
RP INTERACTION WITH PAIP2.
RX PubMed=11438674; DOI=10.1128/mcb.21.15.5200-5213.2001;
RA Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V.,
RA Imataka H., O'Connor-McCourt M., Sonenberg N.;
RT "Dual interactions of the translational repressor Paip2 with poly(A)
RT binding protein.";
RL Mol. Cell. Biol. 21:5200-5213(2001).
RN [14]
RP METHYLATION AT ARG-455 AND ARG-460, AND MUTAGENESIS OF ARG-455 AND ARG-460.
RX PubMed=11850402; DOI=10.1093/embo-reports/kvf052;
RA Lee J., Bedford M.T.;
RT "PABP1 identified as an arginine methyltransferase substrate using high-
RT density protein arrays.";
RL EMBO Rep. 3:268-273(2002).
RN [15]
RP INTERACTION WITH PAIP1.
RX PubMed=11997512; DOI=10.1128/mcb.22.11.3769-3782.2002;
RA Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M.,
RA Sonenberg N.;
RT "Paip1 interacts with poly(A) binding protein through two independent
RT binding motifs.";
RL Mol. Cell. Biol. 22:3769-3782(2002).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [17]
RP PHOSPHORYLATION BY MAPKAPK2.
RX PubMed=12565831; DOI=10.1016/s0006-291x(03)00015-9;
RA Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.;
RT "Affinity purification of ARE-binding proteins identifies polyA-binding
RT protein 1 as a potential substrate in MK2-induced mRNA stabilization.";
RL Biochem. Biophys. Res. Commun. 301:665-670(2003).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [19]
RP INTERACTION WITH CSDE1.
RX PubMed=15314026; DOI=10.1101/gad.1219104;
RA Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S.,
RA Kahvejian A., Sonenberg N., Shyu A.-B.;
RT "UNR, a new partner of poly(A)-binding protein, plays a key role in
RT translationally coupled mRNA turnover mediated by the c-fos major coding-
RT region determinant.";
RL Genes Dev. 18:2010-2023(2004).
RN [20]
RP IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
RX PubMed=16356927; DOI=10.1093/nar/gki1014;
RA Patel G.P., Ma S., Bag J.;
RT "The autoregulatory translational control element of poly(A)-binding
RT protein mRNA forms a heteromeric ribonucleoprotein complex.";
RL Nucleic Acids Res. 33:7074-7089(2005).
RN [21]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH IGF2BP1, AND RNA-BINDING.
RX PubMed=17212783; DOI=10.1111/j.1742-4658.2006.05556.x;
RA Patel G.P., Bag J.;
RT "IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory
RT translational control element of PABP-mRNA through the KH III-IV domain.";
RL FEBS J. 273:5678-5690(2006).
RN [22]
RP INTERACTION WITH PAIP2B.
RX PubMed=16804161; DOI=10.1261/rna.106506;
RA Berlanga J.J., Baass A., Sonenberg N.;
RT "Regulation of poly(A) binding protein function in translation:
RT Characterization of the Paip2 homolog, Paip2B.";
RL RNA 12:1556-1568(2006).
RN [23]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [24]
RP INTERACTION WITH NFX1.
RX PubMed=17267499; DOI=10.1128/jvi.02007-06;
RA Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
RA Gafken P.R., Galloway D.A.;
RT "NFX1-123 and poly(A) binding proteins synergistically augment activation
RT of telomerase in human papillomavirus type 16 E6-expressing cells.";
RL J. Virol. 81:3786-3796(2007).
RN [25]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [26]
RP SUBCELLULAR LOCATION.
RX PubMed=18799579; DOI=10.1128/jvi.00872-08;
RA Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
RA Bolte S., Arold S.T., Poncet D.;
RT "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus
RT infection involves the interaction of NSP3 with eIF4G and RoXaN.";
RL J. Virol. 82:11283-11293(2008).
RN [27]
RP INTERACTION WITH DDX3X AND NXF1, AND SUBCELLULAR LOCATION.
RX PubMed=18596238; DOI=10.1091/mbc.e07-12-1264;
RA Lai M.C., Lee Y.H., Tarn W.Y.;
RT "The DEAD-box RNA helicase DDX3 associates with export messenger
RT ribonucleoproteins as well as tip-associated protein and participates in
RT translational control.";
RL Mol. Biol. Cell 19:3847-3858(2008).
RN [28]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH GSPT2.
RX PubMed=18447585; DOI=10.1371/journal.pbio.0060111;
RA Singh G., Rebbapragada I., Lykke-Andersen J.;
RT "A competition between stimulators and antagonists of Upf complex
RT recruitment governs human nonsense-mediated mRNA decay.";
RL PLoS Biol. 6:E111-E111(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [31]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [33]
RP REVIEW.
RX PubMed=20102337; DOI=10.1042/bj20091571;
RA Smith R.W., Gray N.K.;
RT "Poly(A)-binding protein (PABP): a common viral target.";
RL Biochem. J. 426:1-12(2010).
RN [34]
RP INTERACTION WITH LARP1.
RX PubMed=20430826; DOI=10.1093/nar/gkq294;
RA Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K., Tzolovsky G.,
RA Gabra H., Bushell M., Glover D.M., Willis A.E., Blagden S.P.;
RT "The RNA binding protein Larp1 regulates cell division, apoptosis and cell
RT migration.";
RL Nucleic Acids Res. 38:5542-5553(2010).
RN [35]
RP INTERACTION WITH HHV-5 PROTEIN UL69.
RX PubMed=20133758; DOI=10.1073/pnas.0914856107;
RA Aoyagi M., Gaspar M., Shenk T.E.;
RT "Human cytomegalovirus UL69 protein facilitates translation by associating
RT with the mRNA cap-binding complex and excluding 4EBP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010).
RN [36]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1 AND RACK1.
RX PubMed=20573744; DOI=10.1261/rna.2146910;
RA Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A.,
RA Fischer U.;
RT "A stimulatory role for the La-related protein 4B in translation.";
RL RNA 16:1488-1499(2010).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [39]
RP INTERACTION WITH SETX.
RX PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
RA Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
RT "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause
RT sites to promote Xrn2-dependent termination.";
RL Mol. Cell 42:794-805(2011).
RN [40]
RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=21883093; DOI=10.1042/bj20110739;
RA Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H.;
RT "Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1
RT in stress granule assembly and stress response.";
RL Biochem. J. 441:119-129(2012).
RN [41]
RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=22872150; DOI=10.1038/emboj.2012.220;
RA Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D.,
RA Ohlmann T.;
RT "DEAD-box protein DDX3 associates with eIF4F to promote translation of
RT selected mRNAs.";
RL EMBO J. 31:3745-3756(2012).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND THR-319, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [43]
RP INTERACTION WITH TRIM71.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [44]
RP INTERACTION WITH G3BP1 AND G3BP2.
RX PubMed=23279204; DOI=10.1111/gtc.12023;
RA Matsuki H., Takahashi M., Higuchi M., Makokha G.N., Oie M., Fujii M.;
RT "Both G3BP1 and G3BP2 contribute to stress granule formation.";
RL Genes Cells 18:135-146(2013).
RN [45]
RP INTERACTION WITH URF1.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [46]
RP FUNCTION.
RX PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
RA Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J., Kim V.N.;
RT "Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
RL Cell 159:1365-1376(2014).
RN [47]
RP INTERACTION WITH LARP1.
RX PubMed=24532714; DOI=10.1101/gad.231407.113;
RA Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P.,
RA Roux P.P.;
RT "Proteomic analysis of cap-dependent translation identifies LARP1 as a key
RT regulator of 5'TOP mRNA translation.";
RL Genes Dev. 28:357-371(2014).
RN [48]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-385; ARG-419; ARG-432; ARG-436;
RP ARG-481; ARG-493; ARG-506 AND ARG-518, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [49]
RP INTERACTION WITH LARP1.
RX PubMed=25940091; DOI=10.1074/jbc.m114.621730;
RA Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y., Tahmasebi S.,
RA Healy D., Hoang H.D., Jensen J.M., Diao I.T., Lussier A., Dajadian C.,
RA Padmanabhan N., Wang W., Matta-Camacho E., Hearnden J., Smith E.M.,
RA Tsukumo Y., Yanagiya A., Morita M., Petroulakis E., Gonzalez J.L.,
RA Hernandez G., Alain T., Damgaard C.K.;
RT "La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP) mRNA
RT translation downstream of mTOR complex 1 (mTORC1).";
RL J. Biol. Chem. 290:15996-16020(2015).
RN [50]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [51]
RP INTERACTION WITH ENDOV, AND SUBCELLULAR LOCATION.
RX PubMed=27573237; DOI=10.1074/jbc.m116.730911;
RA Nawaz M.S., Vik E.S., Berges N., Fladeby C., Bjoeraas M., Dalhus B.,
RA Alseth I.;
RT "Regulation of Human Endonuclease V Activity and Relocalization to
RT Cytoplasmic Stress Granules.";
RL J. Biol. Chem. 291:21786-21801(2016).
RN [52]
RP INTERACTION WITH ZFC3H1.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
RN [53]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION (MICROBIAL INFECTION),
RP INTERACTION WITH SHFL, AND IDENTIFICATION IN A COMPLEX WITH SHFL AND LARP1.
RX PubMed=26735137; DOI=10.1371/journal.ppat.1005357;
RA Suzuki Y., Chin W.X., Han Q., Ichiyama K., Lee C.H., Eyo Z.W., Ebina H.,
RA Takahashi H., Takahashi C., Tan B.H., Hishiki T., Ohba K., Matsuyama T.,
RA Koyanagi Y., Tan Y.J., Sawasaki T., Chu J.J., Vasudevan S.G., Sano K.,
RA Yamamoto N.;
RT "Characterization of RyDEN (C19orf66) as an interferon-stimulated cellular
RT inhibitor against dengue virus replication.";
RL PLoS Pathog. 12:E1005357-E1005357(2016).
RN [54]
RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=28733330; DOI=10.1042/bcj20170354;
RA Copsey A.C., Cooper S., Parker R., Lineham E., Lapworth C., Jallad D.,
RA Sweet S., Morley S.J.;
RT "The helicase, DDX3X, interacts with poly(A)-binding protein 1 (PABP1) and
RT caprin-1 at the leading edge of migrating fibroblasts and is required for
RT efficient cell spreading.";
RL Biochem. J. 474:3109-3120(2017).
RN [55]
RP INTERACTION WITH TENT5C.
RX PubMed=28931820; DOI=10.1038/s41467-017-00578-5;
RA Mroczek S., Chlebowska J., Kulinski T.M., Gewartowska O., Gruchota J.,
RA Cysewski D., Liudkovska V., Borsuk E., Nowis D., Dziembowski A.;
RT "The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in
RT multiple myeloma.";
RL Nat. Commun. 8:619-619(2017).
RN [56]
RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
RX PubMed=29476152; DOI=10.1038/s41556-018-0045-z;
RA Huang H., Weng H., Sun W., Qin X., Shi H., Wu H., Zhao B.S., Mesquita A.,
RA Liu C., Yuan C.L., Hu Y.C., Huettelmaier S., Skibbe J.R., Su R., Deng X.,
RA Dong L., Sun M., Li C., Nachtergaele S., Wang Y., Hu C., Ferchen K.,
RA Greis K.D., Jiang X., Wei M., Qu L., Guan J.L., He C., Yang J., Chen J.;
RT "Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA
RT stability and translation.";
RL Nat. Cell Biol. 20:285-295(2018).
RN [57]
RP INTERACTION WITH HRSV M2-1 PROTEIN (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION.
RX PubMed=31649314; DOI=10.1038/s41598-019-51746-0;
RA Bouillier C., Cosentino G., Leger T., Rincheval V., Richard C.A.,
RA Desquesnes A., Sitterlin D., Blouquit-Laye S., Eleouet J.F., Gault E.,
RA Rameix-Welti M.A.;
RT "The Interactome analysis of the Respiratory Syncytial Virus protein M2-1
RT suggests a new role in viral mRNA metabolism post-transcription.";
RL Sci. Rep. 9:15258-15258(2019).
RN [58]
RP FUNCTION, AND INTERACTION WITH IGF2BP1.
RX PubMed=32245947; DOI=10.1038/s41467-020-15403-9;
RA Zhu S., Wang J.Z., Chen D., He Y.T., Meng N., Chen M., Lu R.X., Chen X.H.,
RA Zhang X.L., Yan G.R.;
RT "An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and
RT tumorigenesis.";
RL Nat. Commun. 11:1685-1685(2020).
RN [59]
RP INTERACTION WITH PAIP1.
RX PubMed=33876849; DOI=10.15252/embj.2019102277;
RA Lei J., Ma-Lauer Y., Han Y., Thoms M., Buschauer R., Jores J., Thiel V.,
RA Beckmann R., Deng W., Leonhardt H., Hilgenfeld R., von Brunn A.;
RT "The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with
RT human Paip1 to enhance viral RNA translation.";
RL EMBO J. 40:e102277-e102277(2021).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
RX PubMed=10499800; DOI=10.1016/s0092-8674(00)81517-2;
RA Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.;
RT "Recognition of polyadenylate RNA by the poly(A)-binding protein.";
RL Cell 98:835-845(1999).
RN [61]
RP STRUCTURE BY NMR OF 498-636, INTERACTION WITH GSPT1; PAIP1 AND PAIP2, AND
RP DOMAIN.
RX PubMed=11287632; DOI=10.1073/pnas.071024998;
RA Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.;
RT "Structure and function of the C-terminal PABC domain of human poly(A)-
RT binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001).
RN [62]
RP STRUCTURE BY NMR OF 541-623 IN COMPLEX WITH GSPT1.
RA Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I.,
RA Shimada I.;
RT "Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with
RT chemical exchange using two overlapping motifs.";
RL Submitted (MAY-2009) to the PDB data bank.
RN [63]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 544-626 IN COMPLEX WITH PAIP2, AND
RP DOMAIN.
RX PubMed=20096703; DOI=10.1016/j.jmb.2010.01.032;
RA Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.;
RT "Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-
RT binding protein.";
RL J. Mol. Biol. 397:397-407(2010).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 543-621 IN COMPLEX WITH LARP4B.
RA Grimm C., Pelz J.P.;
RT "LARP4B binds to the PABC1 MLLE domain via a variant PAM2 motif.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 544-626 IN COMPLEX WITH LARP4.
RX PubMed=21098120; DOI=10.1128/mcb.01162-10;
RA Yang R., Gaidamakov S.A., Xie J., Lee J., Martino L., Kozlov G.,
RA Crawford A.K., Russo A.N., Conte M.R., Gehring K., Maraia R.J.;
RT "La-related protein 4 binds poly(A), interacts with the poly(A)-binding
RT protein MLLE domain via a variant PAM2w motif, and can promote mRNA
RT stability.";
RL Mol. Cell. Biol. 31:542-556(2011).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA, including that of its own
CC transcript, and regulates processes of mRNA metabolism such as pre-mRNA
CC splicing and mRNA stability (PubMed:11051545, PubMed:17212783,
CC PubMed:25480299). Its function in translational initiation regulation
CC can either be enhanced by PAIP1 or repressed by PAIP2 (PubMed:11051545,
CC PubMed:20573744). Can probably bind to cytoplasmic RNA sequences other
CC than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing
CC mRNAs and contributes to MYC stability by binding to m6A-containing MYC
CC mRNAs (PubMed:32245947). Involved in translationally coupled mRNA
CC turnover (PubMed:11051545). Implicated with other RNA-binding proteins
CC in the cytoplasmic deadenylation/translational and decay interplay of
CC the FOS mRNA mediated by the major coding-region determinant of
CC instability (mCRD) domain (PubMed:11051545). Involved in regulation of
CC nonsense-mediated decay (NMD) of mRNAs containing premature stop
CC codons; for the recognition of premature termination codons (PTC) and
CC initiation of NMD a competitive interaction between UPF1 and PABPC1
CC with the ribosome-bound release factors is proposed (PubMed:18447585).
CC By binding to long poly(A) tails, may protect them from uridylation by
CC ZCCHC6/ZCCHC11 and hence contribute to mRNA stability
CC (PubMed:25480299). {ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:18447585,
CC ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:25480299,
CC ECO:0000269|PubMed:32245947}.
CC -!- FUNCTION: (Microbial infection) Positively regulates the replication of
CC dengue virus (DENV). {ECO:0000269|PubMed:26735137}.
CC -!- SUBUNIT: May form homodimers. Component of a multisubunit
CC autoregulatory ribonucleoprotein complex (ARC), at least composed of
CC IGF2BP1, PABPC1 and CSDE1 (PubMed:16356927). Directly interacts with
CC IGF2BP1; the interaction is enhanced by SEPIN14P20 peptide RBPR
CC (PubMed:32245947, PubMed:29476152). Part of a complex associated with
CC the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and
CC CSDE1/UNR (PubMed:11051545). Interacts with the PABPC1-interacting
CC motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2 (PubMed:9548260,
CC PubMed:11172725, PubMed:11438674, PubMed:11997512, PubMed:11287632,
CC PubMed:20096703, PubMed:33876849). Interacts with PAIP1 with a 1:1
CC stoichiometry and with PAIP2 with a 1:2 stoichiometry. The interaction
CC with CSDE1 is direct and RNA-independent. Found in a mRNP complex with
CC YBX2 (By similarity). Interacts with TENT2/GLD2 (By similarity).
CC Identified in the spliceosome C complex (PubMed:11991638). Identified
CC in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
CC IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1.
CC The interaction with DDX3X is direct and RNA-independent
CC (PubMed:18596238, PubMed:21883093, PubMed:22872150). This interaction
CC increases in stressed cells and decreases during cell recovery
CC (PubMed:21883093). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Interacts with NXF1/TAP
CC (PubMed:17267499, PubMed:18596238). Interacts with PIWIL1 (By
CC similarity). Interacts with AGO1, AGO2, GSPT1 and GSPT2
CC (PubMed:17932509, PubMed:18447585, Ref.62). Interacts with LARP4B
CC (Ref.64). Interacts (via the second and third RRM domains and the C-
CC terminus) with PAIP2B (via central acidic portion and C-terminus)
CC (PubMed:16804161, PubMed:11287632). Forms a complex with LARP1 and SHFL
CC (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:26735137).
CC Interacts with LARP4 (PubMed:21098120). Interacts with ZFC3H1 in a
CC RNase-sensitive manner (PubMed:27871484). Interacts with TRIM71 (via
CC NHL repeats) in an RNA-dependent manner (PubMed:23125361). Interacts
CC with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase
CC function (PubMed:28931820). Interacts with G3BP1 and G3BP2
CC (PubMed:23279204). Interacts with ENDOV; the interaction is RNA-
CC dependent and stimulates ENDOV activity (PubMed:27573237). Interacts
CC with UPF1; the interaction is RNA-dependent (PubMed:25220460).
CC Interacts with IGF2BP2 and IGF2BP3 (PubMed:29476152). May interact with
CC SETX (PubMed:21700224). {ECO:0000250|UniProtKB:P29341,
CC ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11172725,
CC ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:11438674,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:11997512,
CC ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:16356927,
CC ECO:0000269|PubMed:16804161, ECO:0000269|PubMed:17212783,
CC ECO:0000269|PubMed:17267499, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18447585,
CC ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:20096703, ECO:0000269|PubMed:20133758,
CC ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:20573744,
CC ECO:0000269|PubMed:21098120, ECO:0000269|PubMed:21700224,
CC ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150,
CC ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:23279204,
CC ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:26735137, ECO:0000269|PubMed:27573237,
CC ECO:0000269|PubMed:27871484, ECO:0000269|PubMed:28931820,
CC ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947,
CC ECO:0000269|PubMed:33876849, ECO:0000269|PubMed:9548260,
CC ECO:0000269|Ref.62}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with human
CC cytomegalovirus/HHV-5 protein UL69. {ECO:0000269|PubMed:20133758}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with human
CC respiratory syncytial virus (HRSV) M2-1 protein.
CC {ECO:0000269|PubMed:31649314}.
CC -!- INTERACTION:
CC P11940; P05067: APP; NbExp=3; IntAct=EBI-81531, EBI-77613;
CC P11940; Q99700: ATXN2; NbExp=7; IntAct=EBI-81531, EBI-697691;
CC P11940; Q99700-5: ATXN2; NbExp=3; IntAct=EBI-81531, EBI-25891409;
CC P11940; O00571: DDX3X; NbExp=10; IntAct=EBI-81531, EBI-353779;
CC P11940; P06730: EIF4E; NbExp=5; IntAct=EBI-81531, EBI-73440;
CC P11940; Q04637: EIF4G1; NbExp=4; IntAct=EBI-81531, EBI-73711;
CC P11940; P15170-2: GSPT1; NbExp=2; IntAct=EBI-81531, EBI-9094806;
CC P11940; Q8IYD1: GSPT2; NbExp=8; IntAct=EBI-81531, EBI-3869637;
CC P11940; Q14103-4: HNRNPD; NbExp=2; IntAct=EBI-81531, EBI-432545;
CC P11940; P35568: IRS1; NbExp=2; IntAct=EBI-81531, EBI-517592;
CC P11940; Q09161: NCBP1; NbExp=9; IntAct=EBI-81531, EBI-464743;
CC P11940; Q86U42: PABPN1; NbExp=2; IntAct=EBI-81531, EBI-1226435;
CC P11940; Q9H074: PAIP1; NbExp=16; IntAct=EBI-81531, EBI-81519;
CC P11940; Q9BPZ3: PAIP2; NbExp=6; IntAct=EBI-81531, EBI-2957445;
CC P11940; Q58A45: PAN3; NbExp=4; IntAct=EBI-81531, EBI-2513054;
CC P11940; Q96Q15: SMG1; NbExp=2; IntAct=EBI-81531, EBI-1049832;
CC P11940; Q8NDV7: TNRC6A; NbExp=3; IntAct=EBI-81531, EBI-2269715;
CC P11940; Q9UPQ9: TNRC6B; NbExp=3; IntAct=EBI-81531, EBI-947158;
CC P11940; Q9HCJ0: TNRC6C; NbExp=22; IntAct=EBI-81531, EBI-6507625;
CC P11940; P50616: TOB1; NbExp=5; IntAct=EBI-81531, EBI-723281;
CC P11940; Q14106: TOB2; NbExp=6; IntAct=EBI-81531, EBI-2562000;
CC P11940; P14240: L; Xeno; NbExp=2; IntAct=EBI-81531, EBI-26968662;
CC P11940; Q9J0X9: UL54; Xeno; NbExp=3; IntAct=EBI-81531, EBI-7967856;
CC P11940-1; P10527: N; Xeno; NbExp=3; IntAct=EBI-352013, EBI-25649748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20573744,
CC ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:28733330,
CC ECO:0000269|PubMed:31649314, ECO:0000269|PubMed:7908267,
CC ECO:0000269|PubMed:9582337}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150,
CC ECO:0000269|PubMed:27573237}. Nucleus {ECO:0000269|PubMed:18799579,
CC ECO:0000269|PubMed:9582337}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:28733330}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs (PubMed:17289661). Shuttles
CC between the cytoplasm and the nucleus (PubMed:9582337). During stress
CC and in the absence of DDX3X, localizes to the nucleus
CC (PubMed:21883093). At the leading edge of migrating fibroblasts,
CC colocalizes with DDX3X (PubMed:28733330). Relocalizes to cytoplasmic
CC stress granules upon cellular stress where it colocalizes with ENDOV
CC (PubMed:27573237). In case of HRSV infection, localizes in cytoplasmic
CC inclusion bodies substructures called inclusion bodies associated
CC granules (IBAGs) (PubMed:31649314). {ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:28733330,
CC ECO:0000269|PubMed:31649314, ECO:0000269|PubMed:9582337}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11940-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11940-2; Sequence=VSP_009846;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last
CC 138 amino acids) regions interact with the PABPC1-interacting motif-1
CC (PAM1) and -2 (PAM2) of PAIP1, respectively.
CC {ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:11997512}.
CC -!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus (last
CC 138 amino acids) regions interact with the PABPC1-interacting motif-1
CC (PAM1) and -2 (PAM2) of PAIP2, respectively.
CC {ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:20096703}.
CC -!- PTM: Phosphorylated by MAPKAPK2. {ECO:0000269|PubMed:12565831}.
CC -!- PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to
CC asymmetric dimethylarginine. {ECO:0000269|PubMed:11850402,
CC ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
CC -!- MISCELLANEOUS: Many viruses shutoff host mRNA translational machinery
CC by inhibiting cellular PABPC1 activity using different mechanisms.
CC Picornaviruses, caliciviruses or lentiviruses encode proteases that
CC cleave PABPC1 at several defined sites in the proline-rich linker
CC region between RRMs and the C-terminal domain. Rotaviruses,
CC gammherpesviruses and bunyamwera virus relocalize PABPC1 from the
CC cytoplasm to the nucleus thus altering its function. Many of these
CC viruses translate their mRNA in a PABPC1-independent manner and are
CC unaffected by host PABPC1 inhibition.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was termed (Ref.5) polyadenylate binding protein II.
CC {ECO:0000305}.
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DR EMBL; Y00345; CAA68428.1; -; mRNA.
DR EMBL; U68104; AAD08718.1; -; Genomic_DNA.
DR EMBL; U68093; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68094; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68095; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68097; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68098; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68099; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68100; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68101; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68102; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; U68103; AAD08718.1; JOINED; Genomic_DNA.
DR EMBL; AP001205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015958; AAH15958.1; -; mRNA.
DR EMBL; BC023520; AAH23520.1; -; mRNA.
DR EMBL; Z48501; CAA88401.1; -; mRNA.
DR CCDS; CCDS6289.1; -. [P11940-1]
DR PIR; A93668; DNHUPA.
DR PIR; S52491; S52491.
DR RefSeq; NP_002559.2; NM_002568.3. [P11940-1]
DR RefSeq; XP_005250918.1; XM_005250861.2. [P11940-1]
DR PDB; 1CVJ; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-190.
DR PDB; 1G9L; NMR; -; A=498-636.
DR PDB; 1JGN; NMR; -; A=544-636.
DR PDB; 1JH4; NMR; -; A=544-636.
DR PDB; 2K8G; NMR; -; A=90-182.
DR PDB; 2RQG; NMR; -; B=541-623.
DR PDB; 2RQH; NMR; -; B=541-623.
DR PDB; 2X04; X-ray; 1.49 A; A/B=545-619.
DR PDB; 3KTP; X-ray; 1.50 A; A=544-626.
DR PDB; 3KTR; X-ray; 1.70 A; A=544-626.
DR PDB; 3KUI; X-ray; 2.30 A; A=544-626.
DR PDB; 3KUJ; X-ray; 1.40 A; A=544-626.
DR PDB; 3KUR; X-ray; 2.50 A; A/B/C/D/E/F/G/H=544-617.
DR PDB; 3KUS; X-ray; 1.40 A; A/B=544-626.
DR PDB; 3KUT; X-ray; 1.50 A; A/B=544-626.
DR PDB; 3PKN; X-ray; 1.80 A; A=544-626.
DR PDB; 3PTH; X-ray; 1.70 A; A=543-621.
DR PDB; 4F02; X-ray; 2.00 A; A/D=1-190.
DR PDB; 4F25; X-ray; 1.90 A; A=99-199.
DR PDB; 4F26; X-ray; 2.00 A; A=99-199.
DR PDB; 5DX1; X-ray; 1.93 A; F/G/H/I=449-466.
DR PDB; 5DX8; X-ray; 1.94 A; E/F/G/H=449-466.
DR PDB; 5DXA; X-ray; 2.07 A; F/G/I=449-466.
DR PDB; 5LGP; X-ray; 2.04 A; E/F/G/H=447-458.
DR PDB; 5LGQ; X-ray; 2.11 A; E/F/G/H=456-466.
DR PDB; 5LGR; X-ray; 2.00 A; E/F/G/H=447-458.
DR PDB; 5LGS; X-ray; 2.10 A; E/F/G/H=456-464.
DR PDB; 7BN3; X-ray; 1.93 A; A/B/C=544-626.
DR PDBsum; 1CVJ; -.
DR PDBsum; 1G9L; -.
DR PDBsum; 1JGN; -.
DR PDBsum; 1JH4; -.
DR PDBsum; 2K8G; -.
DR PDBsum; 2RQG; -.
DR PDBsum; 2RQH; -.
DR PDBsum; 2X04; -.
DR PDBsum; 3KTP; -.
DR PDBsum; 3KTR; -.
DR PDBsum; 3KUI; -.
DR PDBsum; 3KUJ; -.
DR PDBsum; 3KUR; -.
DR PDBsum; 3KUS; -.
DR PDBsum; 3KUT; -.
DR PDBsum; 3PKN; -.
DR PDBsum; 3PTH; -.
DR PDBsum; 4F02; -.
DR PDBsum; 4F25; -.
DR PDBsum; 4F26; -.
DR PDBsum; 5DX1; -.
DR PDBsum; 5DX8; -.
DR PDBsum; 5DXA; -.
DR PDBsum; 5LGP; -.
DR PDBsum; 5LGQ; -.
DR PDBsum; 5LGR; -.
DR PDBsum; 5LGS; -.
DR PDBsum; 7BN3; -.
DR AlphaFoldDB; P11940; -.
DR BMRB; P11940; -.
DR SMR; P11940; -.
DR BioGRID; 117939; 492.
DR ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
DR CORUM; P11940; -.
DR DIP; DIP-31613N; -.
DR ELM; P11940; -.
DR IntAct; P11940; 194.
DR MINT; P11940; -.
DR STRING; 9606.ENSP00000313007; -.
DR BindingDB; P11940; -.
DR ChEMBL; CHEMBL1293286; -.
DR MoonDB; P11940; Predicted.
DR GlyGen; P11940; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11940; -.
DR MetOSite; P11940; -.
DR PhosphoSitePlus; P11940; -.
DR SwissPalm; P11940; -.
DR BioMuta; PABPC1; -.
DR DMDM; 3183544; -.
DR EPD; P11940; -.
DR jPOST; P11940; -.
DR MassIVE; P11940; -.
DR MaxQB; P11940; -.
DR PaxDb; P11940; -.
DR PeptideAtlas; P11940; -.
DR PRIDE; P11940; -.
DR ProteomicsDB; 52814; -. [P11940-1]
DR ProteomicsDB; 52815; -. [P11940-2]
DR Antibodypedia; 3159; 247 antibodies from 31 providers.
DR DNASU; 26986; -.
DR Ensembl; ENST00000318607.10; ENSP00000313007.5; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000520142.2; ENSP00000430012.2; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000520804.2; ENSP00000428749.2; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000521865.6; ENSP00000429119.2; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000522658.6; ENSP00000428840.2; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000522720.2; ENSP00000429790.2; ENSG00000070756.17. [P11940-1]
DR Ensembl; ENST00000523555.6; ENSP00000429892.2; ENSG00000070756.17. [P11940-1]
DR GeneID; 26986; -.
DR KEGG; hsa:26986; -.
DR MANE-Select; ENST00000318607.10; ENSP00000313007.5; NM_002568.4; NP_002559.2.
DR UCSC; uc003yjs.2; human. [P11940-1]
DR CTD; 26986; -.
DR DisGeNET; 26986; -.
DR GeneCards; PABPC1; -.
DR HGNC; HGNC:8554; PABPC1.
DR HPA; ENSG00000070756; Low tissue specificity.
DR MIM; 604679; gene.
DR neXtProt; NX_P11940; -.
DR OpenTargets; ENSG00000070756; -.
DR PharmGKB; PA32880; -.
DR VEuPathDB; HostDB:ENSG00000070756; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000153773; -.
DR InParanoid; P11940; -.
DR OMA; SHAEQKD; -.
DR PhylomeDB; P11940; -.
DR TreeFam; TF300458; -.
DR PathwayCommons; P11940; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P11940; -.
DR SIGNOR; P11940; -.
DR BioGRID-ORCS; 26986; 607 hits in 1030 CRISPR screens.
DR ChiTaRS; PABPC1; human.
DR EvolutionaryTrace; P11940; -.
DR GeneWiki; PABPC1; -.
DR GenomeRNAi; 26986; -.
DR Pharos; P11940; Tbio.
DR PRO; PR:P11940; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P11940; protein.
DR Bgee; ENSG00000070756; Expressed in parotid gland and 202 other tissues.
DR ExpressionAtlas; P11940; baseline and differential.
DR Genevisible; P11940; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; IDA:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:CAFA.
DR GO; GO:0008494; F:translation activator activity; TAS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; TAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR IDEAL; IID00193; -.
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; 3.
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; Alternative splicing; Cell projection;
KW Cytoplasm; Direct protein sequencing; Host-virus interaction; Methylation;
KW mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..636
FT /note="Polyadenylate-binding protein 1"
FT /id="PRO_0000081698"
FT DOMAIN 11..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 99..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..268
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..370
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 542..619
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 166..289
FT /note="CSDE1-binding"
FT REGION 541..636
FT /note="(Microbial infection) Binding to HRSV M2-1 protein"
FT /evidence="ECO:0000269|PubMed:31649314"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 299
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 436
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 455
FT /note="Omega-N-methylated arginine; by CARM1; partial"
FT /evidence="ECO:0000305|PubMed:11850402"
FT MOD_RES 460
FT /note="Omega-N-methylated arginine; by CARM1; partial"
FT /evidence="ECO:0000305|PubMed:11850402"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P29341"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 493
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 493
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT MOD_RES 493
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 506
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 518
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 447..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_009846"
FT MUTAGEN 455
FT /note="R->A: Greatly reduces methylation by CARM1 (in
FT vitro); when associated with A-460."
FT /evidence="ECO:0000269|PubMed:11850402"
FT MUTAGEN 460
FT /note="R->A: Greatly reduces methylation by CARM1 (in
FT vitro); when associated with A-455."
FT /evidence="ECO:0000269|PubMed:11850402"
FT CONFLICT 211..213
FT /note="Missing (in Ref. 1; CAA68428)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="M -> I (in Ref. 5; CAA88401)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="I -> V (in Ref. 1; CAA68428)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4F02"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:4F02"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4F02"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:4F02"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4F02"
FT STRAND 51..61
FT /evidence="ECO:0007829|PDB:4F02"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4F02"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4F02"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:4F02"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4F25"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4F25"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4F25"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4F25"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4F25"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4F25"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2K8G"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4F25"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:4F02"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:3KUJ"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:3KUJ"
FT HELIX 558..573
FT /evidence="ECO:0007829|PDB:3KUJ"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:3KUJ"
FT HELIX 578..585
FT /evidence="ECO:0007829|PDB:3KUJ"
FT HELIX 590..598
FT /evidence="ECO:0007829|PDB:3KUJ"
FT HELIX 600..619
FT /evidence="ECO:0007829|PDB:3KUJ"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:1JGN"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:1G9L"
SQ SEQUENCE 636 AA; 70671 MW; 2EB1B02A346132EE CRC64;
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE
AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA
AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ
RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ
GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
