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Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1)

 PABP1_HUMAN             Reviewed;         636 AA.
P11940; Q15097; Q93004;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
23-MAY-2018, entry version 224.
RecName: Full=Polyadenylate-binding protein 1;
Short=PABP-1;
Short=Poly(A)-binding protein 1;
Name=PABPC1; Synonyms=PAB1, PABP1, PABPC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2885805; DOI=10.1093/nar/15.12.4771;
Grange T., de Sa C.M., Oddos J., Pictet R.;
"Human mRNA polyadenylate binding protein: evolutionary conservation
of a nucleic acid binding motif.";
Nucleic Acids Res. 15:4771-4787(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung;
Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O.;
"The human poly(A)-binding protein (PABP) gene: structural and
functional analysis.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-636 (ISOFORM 2).
Murphy E.P., McKenna N.J., Headon D.R.;
"Nucleotide sequence of a partial cDNA encoding a novel human
polyadenylate-binding protein.";
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 158-166; 189-196;
214-221; 232-240; 291-309; 312-324; 357-370; 375-385; 482-506; 566-580
AND 605-620, METHYLATION AT ARG-493, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153;
158-166; 187-208; 214-221; 232-240; 291-324; 334-348; 357-370;
375-385; 482-506; 519-559; 566-620 AND 626-636, METHYLATION AT LYS-299
AND ARG-493, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[8]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7908267; DOI=10.1006/excr.1994.1104;
Goerlach M., Burd C.G., Dreyfuss G.;
"The mRNA poly(A)-binding protein: localization, abundance, and RNA-
binding specificity.";
Exp. Cell Res. 211:400-407(1994).
[9]
SUBCELLULAR LOCATION.
PubMed=9582337; DOI=10.1074/jbc.273.21.13015;
Afonina E., Stauber R., Pavlakis G.N.;
"The human poly(A)-binding protein 1 shuttles between the nucleus and
the cytoplasm.";
J. Biol. Chem. 273:13015-13021(1998).
[10]
INTERACTION WITH PAIP1, AND DOMAIN.
PubMed=9548260; DOI=10.1038/33198;
Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
"Interaction of polyadenylate-binding protein with the eIF4G homologue
PAIP enhances translation.";
Nature 392:520-523(1998).
[11]
FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
IN A COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
Shyu A.-B.;
"A mechanism for translationally coupled mRNA turnover: interaction
between the poly(A) tail and a c-fos RNA coding determinant via a
protein complex.";
Cell 103:29-40(2000).
[12]
INTERACTION WITH PAIP2.
PubMed=11172725; DOI=10.1016/S1097-2765(01)00168-X;
Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
Burley S.K., Sonenberg N.;
"Translational repression by a novel partner of human poly(A) binding
protein, Paip2.";
Mol. Cell 7:205-216(2001).
[13]
INTERACTION WITH PAIP2.
PubMed=11438674; DOI=10.1128/MCB.21.15.5200-5213.2001;
Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V.,
Imataka H., O'Connor-McCourt M., Sonenberg N.;
"Dual interactions of the translational repressor Paip2 with poly(A)
binding protein.";
Mol. Cell. Biol. 21:5200-5213(2001).
[14]
METHYLATION AT ARG-455 AND ARG-460, AND MUTAGENESIS OF ARG-455 AND
ARG-460.
PubMed=11850402; DOI=10.1093/embo-reports/kvf052;
Lee J., Bedford M.T.;
"PABP1 identified as an arginine methyltransferase substrate using
high-density protein arrays.";
EMBO Rep. 3:268-273(2002).
[15]
INTERACTION WITH PAIP1.
PubMed=11997512; DOI=10.1128/MCB.22.11.3769-3782.2002;
Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A.,
O'Connor-McCourt M., Sonenberg N.;
"Paip1 interacts with poly(A) binding protein through two independent
binding motifs.";
Mol. Cell. Biol. 22:3769-3782(2002).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[17]
PHOSPHORYLATION BY MAPKAPK2.
PubMed=12565831; DOI=10.1016/S0006-291X(03)00015-9;
Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.;
"Affinity purification of ARE-binding proteins identifies polyA-
binding protein 1 as a potential substrate in MK2-induced mRNA
stabilization.";
Biochem. Biophys. Res. Commun. 301:665-670(2003).
[18]
INTERACTION WITH CSDE1.
PubMed=15314026; DOI=10.1101/gad.1219104;
Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W.,
Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.;
"UNR, a new partner of poly(A)-binding protein, plays a key role in
translationally coupled mRNA turnover mediated by the c-fos major
coding-region determinant.";
Genes Dev. 18:2010-2023(2004).
[19]
IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
PubMed=16356927; DOI=10.1093/nar/gki1014;
Patel G.P., Ma S., Bag J.;
"The autoregulatory translational control element of poly(A)-binding
protein mRNA forms a heteromeric ribonucleoprotein complex.";
Nucleic Acids Res. 33:7074-7089(2005).
[20]
FUNCTION, HOMODIMERIZATION, INTERACTION WITH IGF2BP1, AND RNA-BINDING.
PubMed=17212783; DOI=10.1111/j.1742-4658.2006.05556.x;
Patel G.P., Bag J.;
"IMP1 interacts with poly(A)-binding protein (PABP) and the
autoregulatory translational control element of PABP-mRNA through the
KH III-IV domain.";
FEBS J. 273:5678-5690(2006).
[21]
INTERACTION WITH PAIP2B.
PubMed=16804161; DOI=10.1261/rna.106506;
Berlanga J.J., Baass A., Sonenberg N.;
"Regulation of poly(A) binding protein function in translation:
Characterization of the Paip2 homolog, Paip2B.";
RNA 12:1556-1568(2006).
[22]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[23]
INTERACTION WITH NFX1.
PubMed=17267499; DOI=10.1128/JVI.02007-06;
Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
Gafken P.R., Galloway D.A.;
"NFX1-123 and poly(A) binding proteins synergistically augment
activation of telomerase in human papillomavirus type 16 E6-expressing
cells.";
J. Virol. 81:3786-3796(2007).
[24]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[25]
SUBCELLULAR LOCATION.
PubMed=18799579; DOI=10.1128/JVI.00872-08;
Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
Bolte S., Arold S.T., Poncet D.;
"Nuclear localization of cytoplasmic poly(A)-binding protein upon
rotavirus infection involves the interaction of NSP3 with eIF4G and
RoXaN.";
J. Virol. 82:11283-11293(2008).
[26]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH GSPT2.
PubMed=18447585; DOI=10.1371/journal.pbio.0060111;
Singh G., Rebbapragada I., Lykke-Andersen J.;
"A competition between stimulators and antagonists of Upf complex
recruitment governs human nonsense-mediated mRNA decay.";
PLoS Biol. 6:E111-E111(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19029303; DOI=10.1261/rna.1175909;
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RNPs.";
RNA 15:104-115(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
REVIEW.
PubMed=20102337; DOI=10.1042/BJ20091571;
Smith R.W., Gray N.K.;
"Poly(A)-binding protein (PABP): a common viral target.";
Biochem. J. 426:1-12(2010).
[32]
INTERACTION WITH LARP1.
PubMed=20430826; DOI=10.1093/nar/gkq294;
Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K.,
Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E.,
Blagden S.P.;
"The RNA binding protein Larp1 regulates cell division, apoptosis and
cell migration.";
Nucleic Acids Res. 38:5542-5553(2010).
[33]
INTERACTION WITH HHV-5 PROTEIN UL69.
PubMed=20133758; DOI=10.1073/pnas.0914856107;
Aoyagi M., Gaspar M., Shenk T.E.;
"Human cytomegalovirus UL69 protein facilitates translation by
associating with the mRNA cap-binding complex and excluding 4EBP1.";
Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1 AND RACK1.
PubMed=20573744; DOI=10.1261/rna.2146910;
Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A.,
Fischer U.;
"A stimulatory role for the La-related protein 4B in translation.";
RNA 16:1488-1499(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
INTERACTION WITH SETX.
PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
"Human senataxin resolves RNA/DNA hybrids formed at transcriptional
pause sites to promote Xrn2-dependent termination.";
Mol. Cell 42:794-805(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND THR-319, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
INTERACTION WITH TRIM71.
PubMed=23125361; DOI=10.1093/nar/gks1032;
Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
"The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
function.";
Nucleic Acids Res. 41:518-532(2013).
[40]
FUNCTION.
PubMed=25480299; DOI=10.1016/j.cell.2014.10.055;
Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J.,
Kim V.N.;
"Uridylation by TUT4 and TUT7 marks mRNA for degradation.";
Cell 159:1365-1376(2014).
[41]
INTERACTION WITH LARP1.
PubMed=24532714; DOI=10.1101/gad.231407.113;
Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G.,
Gygi S.P., Roux P.P.;
"Proteomic analysis of cap-dependent translation identifies LARP1 as a
key regulator of 5'TOP mRNA translation.";
Genes Dev. 28:357-371(2014).
[42]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-385; ARG-419; ARG-432;
ARG-436; ARG-481; ARG-493; ARG-506 AND ARG-518, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[43]
INTERACTION WITH LARP1.
PubMed=25940091; DOI=10.1074/jbc.M114.621730;
Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y.,
Tahmasebi S., Healy D., Hoang H.D., Jensen J.M., Diao I.T.,
Lussier A., Dajadian C., Padmanabhan N., Wang W., Matta-Camacho E.,
Hearnden J., Smith E.M., Tsukumo Y., Yanagiya A., Morita M.,
Petroulakis E., Gonzalez J.L., Hernandez G., Alain T., Damgaard C.K.;
"La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP)
mRNA translation downstream of mTOR complex 1 (mTORC1).";
J. Biol. Chem. 290:15996-16020(2015).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[45]
INTERACTION WITH ZFC3H1.
PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
Jensen T.H.;
"Identification of a nuclear exosome decay pathway for processed
transcripts.";
Mol. Cell 64:520-533(2016).
[46]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH RYDEN,
AND IDENTIFICATION IN A COMPLEX WITH RYDEN AND LARP1.
PubMed=26735137; DOI=10.1371/journal.ppat.1005357;
Suzuki Y., Chin W.X., Han Q., Ichiyama K., Lee C.H., Eyo Z.W.,
Ebina H., Takahashi H., Takahashi C., Tan B.H., Hishiki T., Ohba K.,
Matsuyama T., Koyanagi Y., Tan Y.J., Sawasaki T., Chu J.J.,
Vasudevan S.G., Sano K., Yamamoto N.;
"Characterization of RyDEN (C19orf66) as an interferon-stimulated
cellular inhibitor against dengue virus replication.";
PLoS Pathog. 12:E1005357-E1005357(2016).
[47]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
PubMed=10499800; DOI=10.1016/S0092-8674(00)81517-2;
Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.;
"Recognition of polyadenylate RNA by the poly(A)-binding protein.";
Cell 98:835-845(1999).
[48]
STRUCTURE BY NMR OF 498-636, INTERACTION WITH GSPT1; PAIP1 AND PAIP2,
AND DOMAIN.
PubMed=11287632; DOI=10.1073/pnas.071024998;
Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I.,
Gehring K.;
"Structure and function of the C-terminal PABC domain of human
poly(A)-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001).
[49]
STRUCTURE BY NMR OF 541-623 IN COMPLEX WITH GSPT1.
Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I.,
Shimada I.;
"Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp
with chemical exchange using two overlapping motifs.";
Submitted (MAY-2009) to the PDB data bank.
[50]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 544-626 IN COMPLEX WITH
PAIP2, AND DOMAIN.
PubMed=20096703; DOI=10.1016/j.jmb.2010.01.032;
Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.;
"Molecular determinants of PAM2 recognition by the MLLE domain of
poly(A)-binding protein.";
J. Mol. Biol. 397:397-407(2010).
[51]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 543-621 IN COMPLEX WITH
LARP4B.
Grimm C., Pelz J.P.;
"LARP4B binds to the PABC1 MLLE domain via a variant PAM2 motif.";
Submitted (DEC-2010) to the PDB data bank.
[52]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 544-626 IN COMPLEX WITH
LARP4.
PubMed=21098120; DOI=10.1128/MCB.01162-10;
Yang R., Gaidamakov S.A., Xie J., Lee J., Martino L., Kozlov G.,
Crawford A.K., Russo A.N., Conte M.R., Gehring K., Maraia R.J.;
"La-related protein 4 binds poly(A), interacts with the poly(A)-
binding protein MLLE domain via a variant PAM2w motif, and can promote
mRNA stability.";
Mol. Cell. Biol. 31:542-556(2011).
-!- FUNCTION: Binds the poly(A) tail of mRNA, including that of its
own transcript. May be involved in cytoplasmic regulatory
processes of mRNA metabolism such as pre-mRNA splicing. Its
function in translational initiation regulation can either be
enhanced by PAIP1 or repressed by PAIP2. Can probably bind to
cytoplasmic RNA sequences other than poly(A) in vivo. Involved in
translationally coupled mRNA turnover. Implicated with other RNA-
binding proteins in the cytoplasmic deadenylation/translational
and decay interplay of the FOS mRNA mediated by the major coding-
region determinant of instability (mCRD) domain. Involved in
regulation of nonsense-mediated decay (NMD) of mRNAs containing
premature stop codons; for the recognition of premature
termination codons (PTC) and initiation of NMD a competitive
interaction between UPF1 and PABPC1 with the ribosome-bound
release factors is proposed. By binding to long poly(A) tails, may
protect them from uridylation by ZCCHC6/ZCCHC11 and hence
contribute to mRNA stability (PubMed:25480299). Positively
regulates the replication of dengue virus (DENV)
(PubMed:26735137). {ECO:0000269|PubMed:11051545,
ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:18447585,
ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:25480299,
ECO:0000269|PubMed:26735137}.
-!- SUBUNIT: May interact with SETX (PubMed:21700224). May form
homodimers. Component of a multisubunit autoregulatory
ribonucleoprotein complex (ARC), at least composed of IGF2BP1,
PABPC1 and CSDE1 (PubMed:16356927). Directly interacts with
IGF2BP1. Part of a complex associated with the FOS mCRD domain and
consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR
(PubMed:11051545). Interacts with the PABPC1-interacting motif-1
(PAM1) and -2 (PAM2) of PAIP1 and PAIP2 (PubMed:9548260,
PubMed:11172725, PubMed:11438674, PubMed:11997512,
PubMed:11287632, PubMed:20096703). Interacts with PAIP1 with a 1:1
stoichiometry and with PAIP2 with a 1:2 stoichiometry. The
interaction with CSDE1 is direct and RNA-independent. Found in a
mRNP complex with YBX2 (By similarity). Interacts with PAPD4/GLD2
(By similarity). Identified in the spliceosome C complex
(PubMed:11991638). Identified in a mRNP complex, at least composed
of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2,
PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-
dependent mRNP granule complex containing untranslated mRNAs.
Interacts with NFX1 (PubMed:17267499). Interacts with PIWIL1 (By
similarity). Interacts with AGO1, AGO2, GSPT1 and GSPT2
(PubMed:17932509, PubMed:18447585, Ref.49). Interacts with human
cytomegalovirus/HHV-5 protein UL69 (PubMed:20133758). Interacts
with LARP4B (Ref.51). Interacts (via the second and third RRM
domains and the C-terminus) with PAIP2B (via central acidic
portion and C-terminus) (PubMed:16804161, PubMed:11287632).
Interacts with LARP1 (PubMed:20430826, PubMed:24532714,
PubMed:25940091). Interacts with RYDEN (PubMed:26735137). Found in
a complex with RYDEN and LARP1 (PubMed:26735137). Interacts with
LARP4 (PubMed:21098120). Interacts with ZFC3H1 in a RNase-
sensitive manner (PubMed:27871484). Interacts with TRIM71 (via NHL
repeats) in an RNA-dependent manner (PubMed:23125361).
{ECO:0000250|UniProtKB:P29341, ECO:0000269|PubMed:11051545,
ECO:0000269|PubMed:11172725, ECO:0000269|PubMed:11287632,
ECO:0000269|PubMed:11438674, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:11997512, ECO:0000269|PubMed:15314026,
ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16804161,
ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:17267499,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17932509,
ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19029303,
ECO:0000269|PubMed:20096703, ECO:0000269|PubMed:20133758,
ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:20573744,
ECO:0000269|PubMed:21098120, ECO:0000269|PubMed:21700224,
ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:24532714,
ECO:0000269|PubMed:26735137, ECO:0000269|PubMed:27871484,
ECO:0000269|PubMed:9548260, ECO:0000269|Ref.49}.
-!- INTERACTION:
Q99700:ATXN2; NbExp=6; IntAct=EBI-81531, EBI-697691;
O00571:DDX3X; NbExp=10; IntAct=EBI-81531, EBI-353779;
P06730:EIF4E; NbExp=5; IntAct=EBI-81531, EBI-73440;
Q04637:EIF4G1; NbExp=4; IntAct=EBI-81531, EBI-73711;
P15170-2:GSPT1; NbExp=2; IntAct=EBI-81531, EBI-9094806;
Q8IYD1:GSPT2; NbExp=7; IntAct=EBI-81531, EBI-3869637;
Q14103-4:HNRNPD; NbExp=2; IntAct=EBI-81531, EBI-432545;
P35568:IRS1; NbExp=2; IntAct=EBI-81531, EBI-517592;
Q09161:NCBP1; NbExp=4; IntAct=EBI-81531, EBI-464743;
Q86U42:PABPN1; NbExp=2; IntAct=EBI-81531, EBI-1226435;
Q9H074:PAIP1; NbExp=13; IntAct=EBI-81531, EBI-81519;
Q9BPZ3:PAIP2; NbExp=5; IntAct=EBI-81531, EBI-2957445;
Q58A45:PAN3; NbExp=4; IntAct=EBI-81531, EBI-2513054;
Q96Q15:SMG1; NbExp=2; IntAct=EBI-81531, EBI-1049832;
Q8NDV7:TNRC6A; NbExp=3; IntAct=EBI-81531, EBI-2269715;
Q9UPQ9:TNRC6B; NbExp=3; IntAct=EBI-81531, EBI-947158;
Q9HCJ0:TNRC6C; NbExp=22; IntAct=EBI-81531, EBI-6507625;
P50616:TOB1; NbExp=4; IntAct=EBI-81531, EBI-723281;
Q14106:TOB2; NbExp=4; IntAct=EBI-81531, EBI-2562000;
Q9J0X9:UL54 (xeno); NbExp=3; IntAct=EBI-81531, EBI-7967856;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20573744,
ECO:0000269|PubMed:7908267, ECO:0000269|PubMed:9582337}. Nucleus
{ECO:0000269|PubMed:18799579, ECO:0000269|PubMed:9582337}.
Note=Localized in cytoplasmic mRNP granules containing
untranslated mRNAs (PubMed:17289661). Shuttles between the
cytoplasm and the nucleus (PubMed:9582337).
{ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:9582337}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11940-1; Sequence=Displayed;
Name=2;
IsoId=P11940-2; Sequence=VSP_009846;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus
(last 138 amino acids) regions interact with the PABPC1-
interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
{ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:11997512}.
-!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus
(last 138 amino acids) regions interact with the PABPC1-
interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.
{ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:20096703}.
-!- PTM: Phosphorylated by MAPKAPK2. {ECO:0000269|PubMed:12565831}.
-!- PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to
asymmetric dimethylarginine. {ECO:0000269|PubMed:11850402,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
-!- MISCELLANEOUS: Many viruses shutoff host mRNA translational
machinery by inhibiting cellular PABPC1 activity using different
mechanisms. Picornaviruses, caliciviruses or lentiviruses encode
proteases that cleave PABPC1 at several defined sites in the
proline-rich linker region between RRMs and the C-terminal domain.
Rotaviruses, gammherpesviruses and bunyamwera virus relocalize
PABPC1 from the cytoplasm to the nucleus thus altering its
function. Many of these viruses translate their mRNA in a PABPC1-
independent manner and are unaffected by host PABPC1 inhibition.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-!- CAUTION: Was termed (Ref.5) polyadenylate binding protein II.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00345; CAA68428.1; -; mRNA.
EMBL; U68104; AAD08718.1; -; Genomic_DNA.
EMBL; U68093; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68094; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68095; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68097; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68098; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68099; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68100; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68101; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68102; AAD08718.1; JOINED; Genomic_DNA.
EMBL; U68103; AAD08718.1; JOINED; Genomic_DNA.
EMBL; AP001205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015958; AAH15958.1; -; mRNA.
EMBL; BC023520; AAH23520.1; -; mRNA.
EMBL; Z48501; CAA88401.1; -; mRNA.
CCDS; CCDS6289.1; -. [P11940-1]
PIR; A93668; DNHUPA.
PIR; S52491; S52491.
RefSeq; NP_002559.2; NM_002568.3. [P11940-1]
RefSeq; XP_005250918.1; XM_005250861.2. [P11940-1]
UniGene; Hs.387804; -.
PDB; 1CVJ; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-190.
PDB; 1G9L; NMR; -; A=498-636.
PDB; 1JGN; NMR; -; A=544-636.
PDB; 1JH4; NMR; -; A=544-636.
PDB; 2K8G; NMR; -; A=90-182.
PDB; 2RQG; NMR; -; B=541-623.
PDB; 2RQH; NMR; -; B=541-623.
PDB; 2X04; X-ray; 1.49 A; A/B=545-619.
PDB; 3KTP; X-ray; 1.50 A; A=544-626.
PDB; 3KTR; X-ray; 1.70 A; A=544-626.
PDB; 3KUI; X-ray; 2.30 A; A=544-626.
PDB; 3KUJ; X-ray; 1.40 A; A=544-626.
PDB; 3KUR; X-ray; 2.50 A; A/B/C/D/E/F/G/H=544-617.
PDB; 3KUS; X-ray; 1.40 A; A/B=544-626.
PDB; 3KUT; X-ray; 1.50 A; A/B=544-626.
PDB; 3PKN; X-ray; 1.80 A; A=544-626.
PDB; 3PTH; X-ray; 1.70 A; A=543-621.
PDB; 4F02; X-ray; 2.00 A; A/D=1-190.
PDB; 4F25; X-ray; 1.90 A; A=99-199.
PDB; 4F26; X-ray; 2.00 A; A=99-199.
PDB; 5DX1; X-ray; 1.93 A; F/G/H/I=449-466.
PDB; 5DX8; X-ray; 1.94 A; E/F/G/H=449-466.
PDB; 5DXA; X-ray; 2.07 A; F/G/I=449-466.
PDB; 5LGP; X-ray; 2.04 A; E/F/G/H=447-458.
PDB; 5LGQ; X-ray; 2.11 A; E/F/G/H=456-466.
PDB; 5LGR; X-ray; 2.00 A; E/F/G/H=447-458.
PDB; 5LGS; X-ray; 2.10 A; E/F/G/H=456-464.
PDBsum; 1CVJ; -.
PDBsum; 1G9L; -.
PDBsum; 1JGN; -.
PDBsum; 1JH4; -.
PDBsum; 2K8G; -.
PDBsum; 2RQG; -.
PDBsum; 2RQH; -.
PDBsum; 2X04; -.
PDBsum; 3KTP; -.
PDBsum; 3KTR; -.
PDBsum; 3KUI; -.
PDBsum; 3KUJ; -.
PDBsum; 3KUR; -.
PDBsum; 3KUS; -.
PDBsum; 3KUT; -.
PDBsum; 3PKN; -.
PDBsum; 3PTH; -.
PDBsum; 4F02; -.
PDBsum; 4F25; -.
PDBsum; 4F26; -.
PDBsum; 5DX1; -.
PDBsum; 5DX8; -.
PDBsum; 5DXA; -.
PDBsum; 5LGP; -.
PDBsum; 5LGQ; -.
PDBsum; 5LGR; -.
PDBsum; 5LGS; -.
ProteinModelPortal; P11940; -.
SMR; P11940; -.
BioGrid; 117939; 252.
CORUM; P11940; -.
DIP; DIP-31613N; -.
ELM; P11940; -.
IntAct; P11940; 114.
MINT; P11940; -.
STRING; 9606.ENSP00000313007; -.
BindingDB; P11940; -.
ChEMBL; CHEMBL1293286; -.
iPTMnet; P11940; -.
PhosphoSitePlus; P11940; -.
SwissPalm; P11940; -.
BioMuta; PABPC1; -.
DMDM; 3183544; -.
EPD; P11940; -.
MaxQB; P11940; -.
PaxDb; P11940; -.
PeptideAtlas; P11940; -.
PRIDE; P11940; -.
DNASU; 26986; -.
Ensembl; ENST00000318607; ENSP00000313007; ENSG00000070756. [P11940-1]
GeneID; 26986; -.
KEGG; hsa:26986; -.
UCSC; uc003yjs.2; human. [P11940-1]
CTD; 26986; -.
DisGeNET; 26986; -.
EuPathDB; HostDB:ENSG00000070756.13; -.
GeneCards; PABPC1; -.
HGNC; HGNC:8554; PABPC1.
HPA; CAB011536; -.
HPA; HPA045423; -.
HPA; HPA067156; -.
MIM; 604679; gene.
neXtProt; NX_P11940; -.
OpenTargets; ENSG00000070756; -.
PharmGKB; PA32880; -.
eggNOG; KOG0123; Eukaryota.
eggNOG; ENOG410XR5X; LUCA.
GeneTree; ENSGT00760000118913; -.
HOGENOM; HOG000217922; -.
HOVERGEN; HBG002295; -.
InParanoid; P11940; -.
KO; K13126; -.
OMA; RAAYYPA; -.
OrthoDB; EOG091G03ZE; -.
PhylomeDB; P11940; -.
TreeFam; TF300458; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-429947; Deadenylation of mRNA.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; P11940; -.
ChiTaRS; PABPC1; human.
EvolutionaryTrace; P11940; -.
GeneWiki; PABPC1; -.
GenomeRNAi; 26986; -.
PMAP-CutDB; P11940; -.
PRO; PR:P11940; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000070756; -.
CleanEx; HS_PABPC1; -.
ExpressionAtlas; P11940; baseline and differential.
Genevisible; P11940; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:MGI.
GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:CAFA.
GO; GO:0008494; F:translation activator activity; TAS:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; TAS:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
Gene3D; 3.30.70.330; -; 4.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR036053; PABP-dom.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 3.
SUPFAM; SSF54928; SSF54928; 2.
SUPFAM; SSF63570; SSF63570; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Methylation; mRNA processing;
mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Spliceosome.
CHAIN 1 636 Polyadenylate-binding protein 1.
/FTId=PRO_0000081698.
DOMAIN 11 89 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 99 175 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 191 268 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 294 370 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 542 619 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
REGION 166 289 CSDE1-binding.
COMPBIAS 495 501 Poly-Ala.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 299 299 N6-methyllysine. {ECO:0000269|Ref.7}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 319 319 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 385 385 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 419 419 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 432 432 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 436 436 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 455 455 Omega-N-methylated arginine; by CARM1;
partial. {ECO:0000305|PubMed:11850402}.
MOD_RES 460 460 Omega-N-methylated arginine; by CARM1;
partial. {ECO:0000305|PubMed:11850402}.
MOD_RES 475 475 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P29341}.
MOD_RES 481 481 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 493 493 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 493 493 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
MOD_RES 493 493 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
MOD_RES 506 506 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 512 512 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 518 518 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 447 535 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_009846.
MUTAGEN 455 455 R->A: Greatly reduces methylation by
CARM1 (in vitro); when associated with A-
460. {ECO:0000269|PubMed:11850402}.
MUTAGEN 460 460 R->A: Greatly reduces methylation by
CARM1 (in vitro); when associated with A-
455. {ECO:0000269|PubMed:11850402}.
CONFLICT 211 213 Missing (in Ref. 1; CAA68428).
{ECO:0000305}.
CONFLICT 410 410 M -> I (in Ref. 5; CAA88401).
{ECO:0000305}.
CONFLICT 428 428 I -> V (in Ref. 1; CAA68428).
{ECO:0000305}.
STRAND 12 17 {ECO:0000244|PDB:4F02}.
HELIX 24 31 {ECO:0000244|PDB:4F02}.
HELIX 32 34 {ECO:0000244|PDB:4F02}.
STRAND 37 44 {ECO:0000244|PDB:4F02}.
TURN 46 48 {ECO:0000244|PDB:4F02}.
STRAND 51 61 {ECO:0000244|PDB:4F02}.
HELIX 62 72 {ECO:0000244|PDB:4F02}.
STRAND 83 86 {ECO:0000244|PDB:4F02}.
HELIX 92 96 {ECO:0000244|PDB:4F02}.
STRAND 100 105 {ECO:0000244|PDB:4F25}.
HELIX 112 119 {ECO:0000244|PDB:4F25}.
HELIX 120 122 {ECO:0000244|PDB:4F25}.
STRAND 125 133 {ECO:0000244|PDB:4F25}.
STRAND 136 146 {ECO:0000244|PDB:4F25}.
HELIX 148 158 {ECO:0000244|PDB:4F25}.
STRAND 161 163 {ECO:0000244|PDB:2K8G}.
STRAND 169 174 {ECO:0000244|PDB:4F25}.
HELIX 176 183 {ECO:0000244|PDB:4F02}.
HELIX 547 551 {ECO:0000244|PDB:3KUJ}.
HELIX 555 557 {ECO:0000244|PDB:3KUJ}.
HELIX 558 573 {ECO:0000244|PDB:3KUJ}.
TURN 575 577 {ECO:0000244|PDB:3KUJ}.
HELIX 578 585 {ECO:0000244|PDB:3KUJ}.
HELIX 590 598 {ECO:0000244|PDB:3KUJ}.
HELIX 600 619 {ECO:0000244|PDB:3KUJ}.
TURN 623 625 {ECO:0000244|PDB:1JGN}.
STRAND 628 630 {ECO:0000244|PDB:1G9L}.
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


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