RBM20_HUMAN
ID RBM20_HUMAN Reviewed; 1227 AA.
AC Q5T481; A6NIP5; B5A868; Q5JVI1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=RNA-binding protein 20 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 20 {ECO:0000305};
GN Name=RBM20 {ECO:0000303|PubMed:22466703, ECO:0000312|HGNC:HGNC:27424};
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], FUNCTION, VARIANT CMD1DD ALA-635, AND
RP CHARACTERIZATION OF VARIANT CMD1DD ALA-635.
RX PubMed=22466703; DOI=10.1038/nm.2693;
RA Guo W., Schafer S., Greaser M.L., Radke M.H., Liss M., Govindarajan T.,
RA Maatz H., Schulz H., Li S., Parrish A.M., Dauksaite V., Vakeel P.,
RA Klaassen S., Gerull B., Thierfelder L., Regitz-Zagrosek V., Hacker T.A.,
RA Saupe K.W., Dec G.W., Ellinor P.T., MacRae C.A., Spallek B., Fischer R.,
RA Perrot A., Ozcelik C., Saar K., Hubner N., Gotthardt M.;
RT "RBM20, a gene for hereditary cardiomyopathy, regulates titin splicing.";
RL Nat. Med. 18:766-773(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP TISSUE SPECIFICITY, AND VARIANTS CMD1DD GLN-634; HIS-636; SER-636; GLY-637
RP AND LEU-638.
RX PubMed=19712804; DOI=10.1016/j.jacc.2009.05.038;
RA Brauch K.M., Karst M.L., Herron K.J., de Andrade M., Pellikka P.A.,
RA Rodeheffer R.J., Michels V.V., Olson T.M.;
RT "Mutations in ribonucleic acid binding protein gene cause familial dilated
RT cardiomyopathy.";
RL J. Am. Coll. Cardiol. 54:930-941(2009).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23886709; DOI=10.1016/j.febslet.2013.07.018;
RA Filippello A., Lorenzi P., Bergamo E., Romanelli M.G.;
RT "Identification of nuclear retention domains in the RBM20 protein.";
RL FEBS Lett. 587:2989-2995(2013).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-679; SER-801;
RP SER-876; SER-980 AND SER-1060, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP FUNCTION, AND INTERACTION WITH U1 AND U2 U1 SMALL NUCLEAR RIBONUCLEOPROTEIN
RP COMPLEXES.
RX PubMed=24960161; DOI=10.1172/jci74523;
RA Maatz H., Jens M., Liss M., Schafer S., Heinig M., Kirchner M., Adami E.,
RA Rintisch C., Dauksaite V., Radke M.H., Selbach M., Barton P.J., Cook S.A.,
RA Rajewsky N., Gotthardt M., Landthaler M., Hubner N.;
RT "RNA-binding protein RBM20 represses splicing to orchestrate cardiac pre-
RT mRNA processing.";
RL J. Clin. Invest. 124:3419-3430(2014).
RN [7]
RP FUNCTION.
RX PubMed=27531932; DOI=10.1161/circresaha.116.309568;
RA Khan M.A., Reckman Y.J., Aufiero S., van den Hoogenhof M.M.,
RA van der Made I., Beqqali A., Koolbergen D.R., Rasmussen T.B.,
RA van der Velden J., Creemers E.E., Pinto Y.M.;
RT "RBM20 regulates circular RNA production from the titin gene.";
RL Circ. Res. 119:996-1003(2016).
RN [8]
RP FUNCTION.
RX PubMed=30948719; DOI=10.1038/s41467-019-09483-5;
RA Bertero A., Fields P.A., Ramani V., Bonora G., Yardimci G.G., Reinecke H.,
RA Pabon L., Noble W.S., Shendure J., Murry C.E.;
RT "Dynamics of genome reorganization during human cardiogenesis reveal an
RT RBM20-dependent splicing factory.";
RL Nat. Commun. 10:1538-1538(2019).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-635 SER-660;
RP SER-679; SER-742; SER-865; SER-876; SER-980; SER-1060; SER-1080; SER-1120
RP AND SER-1210, CHARACTERIZATION OF VARIANT CMD1DD ALA-635, AND MUTAGENESIS
RP OF SER-660; SER-679; GLU-685; SER-742; SER-876; SER-980; SER-1060;
RP SER-1080; SER-1120 AND SER-1210.
RX PubMed=35427468; DOI=10.1016/j.molcel.2022.03.024;
RA Vieira-Vieira C.H., Dauksaite V., Sporbert A., Gotthardt M., Selbach M.;
RT "Proteome-wide quantitative RNA-interactome capture identifies
RT phosphorylation sites with regulatory potential in RBM20.";
RL Mol. Cell 0:0-0(2022).
RN [10]
RP VARIANTS CMD1DD ILE-535; TRP-634; GLN-634; CYS-636; HIS-636 AND GLN-716.
RX PubMed=20590677; DOI=10.1111/j.1752-8062.2010.00198.x;
RA Li D., Morales A., Gonzalez-Quintana J., Norton N., Siegfried J.D.,
RA Hofmeyer M., Hershberger R.E.;
RT "Identification of novel mutations in RBM20 in patients with dilated
RT cardiomyopathy.";
RL Clin. Transl. Sci. 3:90-97(2010).
RN [11]
RP VARIANT CMD1DD GLY-637.
RX PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005;
RA Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A., Dauphin C.,
RA Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P., Seronde M.F.,
RA Faivre L., Eicher J.C., Rousson R.;
RT "Clinical and mutational spectrum in a cohort of 105 unrelated patients
RT with dilated cardiomyopathy.";
RL Eur. J. Med. Genet. 54:E570-E575(2011).
RN [12]
RP VARIANTS CMD1DD ILE-83; LEU-455; LEU-638; ASN-888; 1031-GLY--LEU-1227 DEL;
RP ARG-1081 AND LYS-1206.
RX PubMed=22004663; DOI=10.1016/j.hrthm.2011.10.016;
RA Refaat M.M., Lubitz S.A., Makino S., Islam Z., Frangiskakis J.M., Mehdi H.,
RA Gutmann R., Zhang M.L., Bloom H.L., MacRae C.A., Dudley S.C., Shalaby A.A.,
RA Weiss R., McNamara D.M., London B., Ellinor P.T.;
RT "Genetic variation in the alternative splicing regulator RBM20 is
RT associated with dilated cardiomyopathy.";
RL Heart Rhythm 9:390-396(2012).
RN [13]
RP VARIANT CMD1DD HIS-636.
RX PubMed=23861363; DOI=10.1161/circgenetics.113.000011;
RA Wells Q.S., Becker J.R., Su Y.R., Mosley J.D., Weeke P., D'Aoust L.,
RA Ausborn N.L., Ramirez A.H., Pfotenhauer J.P., Naftilan A.J., Markham L.,
RA Exil V., Roden D.M., Hong C.C.;
RT "Whole exome sequencing identifies a causal RBM20 mutation in a large
RT pedigree with familial dilated cardiomyopathy.";
RL Circ. Cardiovasc. Genet. 6:317-326(2013).
RN [14]
RP VARIANT CMD1DD LYS-913, CHARACTERIZATION OF VARIANT CMD1DD LYS-913, AND
RP FUNCTION.
RX PubMed=27496873; DOI=10.1093/cvr/cvw192;
RA Beqqali A., Bollen I.A., Rasmussen T.B., van den Hoogenhof M.M.,
RA van Deutekom H.W., Schafer S., Haas J., Meder B., Soerensen K.E.,
RA van Oort R.J., Mogensen J., Hubner N., Creemers E.E., van der Velden J.,
RA Pinto Y.M.;
RT "A mutation in the glutamate-rich region of RNA-binding motif protein 20
RT causes dilated cardiomyopathy through missplicing of titin and impaired
RT Frank-Starling mechanism.";
RL Cardiovasc. Res. 112:452-463(2016).
RN [15]
RP VARIANT CMD1DD SER-636, CHARACTERIZATION OF VARIANT CMD1DD SER-636, AND
RP FUNCTION.
RX PubMed=26604136; DOI=10.1093/hmg/ddv468;
RA Wyles S.P., Li X., Hrstka S.C., Reyes S., Oommen S., Beraldi R.,
RA Edwards J., Terzic A., Olson T.M., Nelson T.J.;
RT "Modeling structural and functional deficiencies of RBM20 familial dilated
RT cardiomyopathy using human induced pluripotent stem cells.";
RL Hum. Mol. Genet. 25:254-265(2016).
RN [16]
RP VARIANTS CMD1DD TRP-634 AND 1031-GLY--LEU-1227 DEL, CHARACTERIZATION OF
RP VARIANTS CMD1DD TRP-634 AND 1031-GLY--LEU-1227 DEL, AND FUNCTION.
RX PubMed=29895960; DOI=10.1038/s41598-018-26624-w;
RA Murayama R., Kimura-Asami M., Togo-Ohno M., Yamasaki-Kato Y., Naruse T.K.,
RA Yamamoto T., Hayashi T., Ai T., Spoonamore K.G., Kovacs R.J., Vatta M.,
RA Iizuka M., Saito M., Wani S., Hiraoka Y., Kimura A., Kuroyanagi H.;
RT "Phosphorylation of the RSRSP stretch is critical for splicing regulation
RT by RNA-Binding Motif Protein 20 (RBM20) through nuclear localization.";
RL Sci. Rep. 8:8970-8970(2018).
RN [17]
RP VARIANTS CMD1DD VAL-196; TRP-392; GLN-634; HIS-636; SER-636; LEU-638;
RP GLY-674; LYS-913 AND SER-1039.
RX PubMed=30871348; DOI=10.1161/circheartfailure.118.005700;
RA Hey T.M., Rasmussen T.B., Madsen T., Aagaard M.M., Harbo M., Moelgaard H.,
RA Moeller J.E., Eiskjaer H., Mogensen J.;
RT "Pathogenic RBM20-variants are associated with a severe disease expression
RT in male patients with dilated cardiomyopathy.";
RL Circ. Heart Fail. 12:e005700-e005700(2019).
RN [18]
RP VARIANTS CMD1DD ILE-535 AND GLN-716.
RX PubMed=30871351; DOI=10.1161/circheartfailure.118.005371;
RA Parikh V.N., Caleshu C., Reuter C., Lazzeroni L.C., Ingles J., Garcia J.,
RA McCaleb K., Adesiyun T., Sedaghat-Hamedani F., Kumar S., Graw S., Gigli M.,
RA Stolfo D., Dal Ferro M., Ing A.Y., Nussbaum R., Funke B., Wheeler M.T.,
RA Hershberger R.E., Cook S., Steinmetz L.M., Lakdawala N.K., Taylor M.R.G.,
RA Mestroni L., Merlo M., Sinagra G., Semsarian C., Meder B., Judge D.P.,
RA Ashley E.;
RT "Regional variation in RBM20 causes a highly penetrant arrhythmogenic
RT cardiomyopathy.";
RL Circ. Heart Fail. 12:e005371-e005371(2019).
RN [19]
RP VARIANT CMD1DD CYS-636, CHARACTERIZATION OF VARIANT CMD1DD CYS-636, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30262925; DOI=10.1038/s41436-018-0291-2;
RA Brodehl A., Ebbinghaus H., Gaertner-Rommel A., Stanasiuk C., Klauke B.,
RA Milting H.;
RT "Functional analysis of DES-p.L398P and RBM20-p.R636C.";
RL Genet. Med. 21:1246-1247(2019).
RN [20]
RP VARIANT CMD1DD LYS-905.
RX PubMed=31583969; DOI=10.1080/00015385.2019.1674490;
RA Robyns T., Willems R., Van Cleemput J., Jhangiani S., Muzny D., Gibbs R.,
RA Lupski J.R., Breckpot J., Devriendt K., Corveleyn A.;
RT "Whole exome sequencing in a large pedigree with DCM identifies a novel
RT mutation in RBM20.";
RL Acta Cardiol. 75:748-753(2020).
RN [21]
RP VARIANTS CMD1DD LEU-638 AND ALA-914, CHARACTERIZATION OF VARIANTS CMD1DD
RP LEU-638 AND ALA-914, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=32840935; DOI=10.1002/humu.24096;
RA Gaertner A., Klauke B., Felski E., Kassner A., Brodehl A., Gerdes D.,
RA Stanasiuk C., Ebbinghaus H., Schulz U., Dubowy K.O., Tiesmeier J.,
RA Laser K.T., Bante H., Bergau L., Sommer P., Fox H., Morshuis M.,
RA Gummert J., Milting H.;
RT "Cardiomyopathy-associated mutations in the RS domain affect nuclear
RT localization of RBM20.";
RL Hum. Mutat. 41:1931-1943(2020).
RN [22]
RP VARIANT CMD1DD SER-636, CHARACTERIZATION OF VARIANT CMD1DD SER-636, AND
RP SUBCELLULAR LOCATION.
RX PubMed=33188278; DOI=10.1038/s41591-020-1087-x;
RG Wanek Program Preclinical Pipeline;
RA Schneider J.W., Oommen S., Qureshi M.Y., Goetsch S.C., Pease D.R.,
RA Sundsbak R.S., Guo W., Sun M., Sun H., Kuroyanagi H., Webster D.A.,
RA Coutts A.W., Holst K.A., Edwards B.S., Newville N., Hathcock M.A.,
RA Melkamu T., Briganti F., Wei W., Romanelli M.G., Fahrenkrug S.C.,
RA Frantz D.E., Olson T.M., Steinmetz L.M., Carlson D.F., Nelson T.J.;
RT "Dysregulated ribonucleoprotein granules promote cardiomyopathy in RBM20
RT gene-edited pigs.";
RL Nat. Med. 26:1788-1800(2020).
RN [23]
RP INVOLVEMENT IN LEFT VENTRICULAR NON-COMPACTION (LVNCX), AND VARIANTS
RP HIS-636 AND GLY-637.
RX PubMed=32851336; DOI=10.1002/ped4.12183;
RA Sun Q., Guo J., Hao C., Guo R., Hu X., Chen Y., Yang W., Li W., Feng Y.;
RT "Whole-exome sequencing reveals two de novo variants in the RBM20 gene in
RT two Chinese patients with left ventricular non-compaction cardiomyopathy.";
RL Pediatr. Investig. 4:11-16(2020).
RN [24]
RP VARIANT CMD1DD TRP-634.
RX PubMed=34322310;
RA Liatakis I., Prappa E., Gouziouta A., Pantou M.P., Gourzi P., Vlachos K.,
RA Mililis P., Kariki O., Degiannis D., Efremidis M., Letsas K.P.;
RT "RBM20 mutation and ventricular arrhythmias in a young patient with dilated
RT cardiomyopathy: a case report.";
RL Am. J. Cardiovasc. Dis. 11:398-403(2021).
RN [25]
RP VARIANT CMD1DD TRP-634.
RX PubMed=34021826; DOI=10.1186/s43044-021-00165-6;
RA Das S., Seth S.;
RT "Familial dilated cardiomyopathy with RBM20 mutation in an Indian patient:
RT a case report.";
RL Egypt Heart J. 73:47-47(2021).
RN [26]
RP VARIANTS CMD1DD THR-52; SER-177; LEU-194; VAL-259; PRO-598 AND TRP-1057.
RX PubMed=34174465; DOI=10.1016/j.ejmg.2021.104278;
RA Robles-Mezcua A., Rodriguez-Miranda L., Morcillo-Hidalgo L.,
RA Jimenez-Navarro M., Garcia-Pinilla J.M.;
RT "Phenotype and progression among patients with dilated cardiomyopathy and
RT RBM20 mutations.";
RL Eur. J. Med. Genet. 64:104278-104278(2021).
RN [27]
RP VARIANT CMD1DD SER-636, CHARACTERIZATION OF VARIANT CMD1DD SER-636,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=34732726; DOI=10.1038/s41467-021-26623-y;
RA Fenix A.M., Miyaoka Y., Bertero A., Blue S.M., Spindler M.J., Tan K.K.B.,
RA Perez-Bermejo J.A., Chan A.H., Mayerl S.J., Nguyen T.D., Russell C.R.,
RA Lizarraga P.P., Truong A., So P.L., Kulkarni A., Chetal K., Sathe S.,
RA Sniadecki N.J., Yeo G.W., Murry C.E., Conklin B.R., Salomonis N.;
RT "Gain-of-function cardiomyopathic mutations in RBM20 rewire splicing
RT regulation and re-distribute ribonucleoprotein granules within processing
RT bodies.";
RL Nat. Commun. 12:6324-6324(2021).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing
CC of a subset of genes encoding key structural proteins involved in
CC cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH
CC (PubMed:22466703, PubMed:24960161, PubMed:27531932, PubMed:27496873,
CC PubMed:26604136, PubMed:29895960, PubMed:30948719, PubMed:32840935,
CC PubMed:35427468, PubMed:34732726). Acts as a repressor of mRNA
CC splicing: specifically binds the 5'UCUU-3' motif that is predominantly
CC found within intronic sequences of pre-mRNAs, leading to the exclusion
CC of specific exons in target transcripts (PubMed:24960161,
CC PubMed:30948719, PubMed:34732726). RBM20-mediated exon skipping is
CC hormone-dependent and is essential for TTN isoform transition in both
CC cardiac and skeletal muscles (PubMed:27531932, PubMed:30948719). RBM20-
CC mediated exon skipping of TTN provides substrates for the formation of
CC circular RNA (circRNAs) from the TTN transcripts (PubMed:27531932,
CC PubMed:34732726). Together with RBM24, promotes the expression of short
CC isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:E9PT37, ECO:0000269|PubMed:22466703,
CC ECO:0000269|PubMed:24960161, ECO:0000269|PubMed:26604136,
CC ECO:0000269|PubMed:27496873, ECO:0000269|PubMed:27531932,
CC ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:30948719,
CC ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:34732726,
CC ECO:0000269|PubMed:35427468}.
CC -!- SUBUNIT: Associates with components of the U1 and U2 U1 small nuclear
CC ribonucleoprotein complexes. {ECO:0000269|PubMed:24960161}.
CC -!- INTERACTION:
CC Q5T481; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11352885, EBI-739832;
CC Q5T481; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11352885, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130,
CC ECO:0000269|PubMed:23886709, ECO:0000269|PubMed:30262925,
CC ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:33188278,
CC ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}. Cytoplasm,
CC Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:33188278,
CC ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}. Note=The
CC active form that regulates alternative splicing localizes to the
CC nucleus (PubMed:35427468, PubMed:33188278, PubMed:34732726). Also
CC localizes to cytoplasmic ribonucleoprotein granules; localization to
CC cytoplasmic ribonucleoprotein granules plays an important regulatory
CC role (PubMed:35427468, PubMed:33188278, PubMed:34732726). Subcellular
CC localization is regulated by phosphorylation of different parts of the
CC protein: while phosphorylation of the RS (arginine/serine-rich) region
CC promotes nuclear localization, phosphorylation of the C-terminal
CC disordered region promotes localization to cytoplasmic
CC ribonucleoprotein granules (PubMed:35427468).
CC {ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34732726,
CC ECO:0000269|PubMed:35427468}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the heart (PubMed:19712804,
CC PubMed:23886709). Also expressed in skeletal muscle tissues, ovary,
CC small intestine and colon (PubMed:23886709).
CC {ECO:0000269|PubMed:19712804, ECO:0000269|PubMed:23886709}.
CC -!- PTM: Phosphorylation regulates the subcellular localization
CC (PubMed:35427468). Phosphorylation of Ser-635 and Ser-637 in the RS
CC (arginine/serine-rich) region promotes nuclear localization of the
CC protein (PubMed:35427468). In contrast, phosphorylation of the C-
CC terminal disordered region promotes localization to cytoplasmic
CC ribonucleoprotein granules (PubMed:35427468).
CC {ECO:0000269|PubMed:35427468}.
CC -!- DISEASE: Cardiomyopathy, dilated 1DD (CMD1DD) [MIM:613172]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:19712804,
CC ECO:0000269|PubMed:20590677, ECO:0000269|PubMed:21846512,
CC ECO:0000269|PubMed:22004663, ECO:0000269|PubMed:22466703,
CC ECO:0000269|PubMed:23861363, ECO:0000269|PubMed:26604136,
CC ECO:0000269|PubMed:27496873, ECO:0000269|PubMed:29895960,
CC ECO:0000269|PubMed:30262925, ECO:0000269|PubMed:30871348,
CC ECO:0000269|PubMed:30871351, ECO:0000269|PubMed:31583969,
CC ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:33188278,
CC ECO:0000269|PubMed:34021826, ECO:0000269|PubMed:34174465,
CC ECO:0000269|PubMed:34322310, ECO:0000269|PubMed:34732726,
CC ECO:0000269|PubMed:35427468}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Left ventricular non-compaction (LVNCX): A form of left
CC ventricular non-compaction, a cardiomyopathy due to myocardial
CC morphogenesis arrest and characterized by a hypertrophic left
CC ventricle, a severely thickened 2-layered myocardium, numerous
CC prominent trabeculations, deep intertrabecular recesses, and poor
CC systolic function. Clinical manifestations are variable. Some affected
CC individuals experience no symptoms at all, others develop heart
CC failure. In some cases, left ventricular non-compaction is associated
CC with other congenital heart anomalies. The disease is caused by
CC variants affecting the gene represented in this entry.
CC {ECO:0000269|PubMed:32851336}.
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DR EMBL; EU822950; ACF49364.1; -; mRNA.
DR EMBL; AL136368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44477.1; -.
DR RefSeq; NP_001127835.2; NM_001134363.2.
DR AlphaFoldDB; Q5T481; -.
DR BioGRID; 129433; 27.
DR IntAct; Q5T481; 11.
DR MINT; Q5T481; -.
DR STRING; 9606.ENSP00000358532; -.
DR GlyGen; Q5T481; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T481; -.
DR PhosphoSitePlus; Q5T481; -.
DR BioMuta; RBM20; -.
DR DMDM; 317373512; -.
DR EPD; Q5T481; -.
DR jPOST; Q5T481; -.
DR MassIVE; Q5T481; -.
DR MaxQB; Q5T481; -.
DR PaxDb; Q5T481; -.
DR PeptideAtlas; Q5T481; -.
DR PRIDE; Q5T481; -.
DR ProteomicsDB; 64438; -.
DR Antibodypedia; 50051; 100 antibodies from 21 providers.
DR DNASU; 282996; -.
DR Ensembl; ENST00000369519.4; ENSP00000358532.3; ENSG00000203867.8.
DR GeneID; 282996; -.
DR KEGG; hsa:282996; -.
DR MANE-Select; ENST00000369519.4; ENSP00000358532.3; NM_001134363.3; NP_001127835.2.
DR UCSC; uc001kzf.2; human.
DR CTD; 282996; -.
DR DisGeNET; 282996; -.
DR GeneCards; RBM20; -.
DR GeneReviews; RBM20; -.
DR HGNC; HGNC:27424; RBM20.
DR HPA; ENSG00000203867; Tissue enhanced (heart muscle, pancreas, skeletal muscle).
DR MalaCards; RBM20; -.
DR MIM; 613171; gene.
DR MIM; 613172; phenotype.
DR neXtProt; NX_Q5T481; -.
DR OpenTargets; ENSG00000203867; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA134934622; -.
DR VEuPathDB; HostDB:ENSG00000203867; -.
DR eggNOG; ENOG502QW62; Eukaryota.
DR GeneTree; ENSGT01030000234642; -.
DR HOGENOM; CLU_007364_0_0_1; -.
DR InParanoid; Q5T481; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q5T481; -.
DR TreeFam; TF333921; -.
DR PathwayCommons; Q5T481; -.
DR SignaLink; Q5T481; -.
DR BioGRID-ORCS; 282996; 9 hits in 1076 CRISPR screens.
DR ChiTaRS; RBM20; human.
DR GenomeRNAi; 282996; -.
DR Pharos; Q5T481; Tbio.
DR PRO; PR:Q5T481; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T481; protein.
DR Bgee; ENSG00000203867; Expressed in left ventricle myocardium and 128 other tissues.
DR Genevisible; Q5T481; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990935; F:splicing factor binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060914; P:heart formation; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12685; RRM_RBM20; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034791; RBM20.
DR InterPro; IPR034790; RBM20_RRM.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15592:SF11; PTHR15592:SF11; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Cardiomyopathy; Cytoplasm; Disease variant; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..1227
FT /note="RNA-binding protein 20"
FT /id="PRO_0000328824"
FT DOMAIN 518..593
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 409..443
FT /note="U1-type"
FT /evidence="ECO:0000255"
FT ZN_FING 1161..1192
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..655
FT /note="RS"
FT /evidence="ECO:0000305|PubMed:23886709"
FT REGION 977..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQS8"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQS8"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT37"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35427468"
FT VARIANT 52
FT /note="P -> T (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086515"
FT VARIANT 83
FT /note="L -> I (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22004663"
FT /id="VAR_086516"
FT VARIANT 173
FT /note="P -> T (in dbSNP:rs7908490)"
FT /id="VAR_042532"
FT VARIANT 177
FT /note="T -> S (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086517"
FT VARIANT 194
FT /note="M -> L (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086518"
FT VARIANT 196
FT /note="M -> V (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30871348"
FT /id="VAR_086519"
FT VARIANT 259
FT /note="G -> V (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086520"
FT VARIANT 392
FT /note="R -> W (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30871348"
FT /id="VAR_086521"
FT VARIANT 455
FT /note="S -> L (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22004663"
FT /id="VAR_086522"
FT VARIANT 535
FT /note="V -> I (in CMD1DD; dbSNP:rs183007628)"
FT /evidence="ECO:0000269|PubMed:20590677,
FT ECO:0000269|PubMed:30871351"
FT /id="VAR_068802"
FT VARIANT 598
FT /note="Q -> P (in CMD1DD)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086523"
FT VARIANT 634
FT /note="R -> Q (in CMD1DD; dbSNP:rs267607001)"
FT /evidence="ECO:0000269|PubMed:19712804,
FT ECO:0000269|PubMed:20590677, ECO:0000269|PubMed:30871348"
FT /id="VAR_063092"
FT VARIANT 634
FT /note="R -> W (in CMD1DD; impaired mRNA splicing of TTN
FT (Titin) mRNA; dbSNP:rs796734066)"
FT /evidence="ECO:0000269|PubMed:20590677,
FT ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:34021826,
FT ECO:0000269|PubMed:34322310"
FT /id="VAR_068803"
FT VARIANT 635
FT /note="S -> A (in CMD1DD; causes the formation of anomalous
FT isoforms in TTN (Titin); impaired localization to the
FT nucleus, leading to mislocalization to the cytoplasm)"
FT /evidence="ECO:0000269|PubMed:22466703,
FT ECO:0000269|PubMed:35427468"
FT /id="VAR_068804"
FT VARIANT 636
FT /note="R -> C (in CMD1DD; impaired localization to the
FT nucleus, leading to mislocalization to the cytoplasm;
FT dbSNP:rs267607002)"
FT /evidence="ECO:0000269|PubMed:20590677,
FT ECO:0000269|PubMed:30262925"
FT /id="VAR_068805"
FT VARIANT 636
FT /note="R -> H (in CMD1DD; also found in patients with left
FT ventricular non-compaction; dbSNP:rs267607004)"
FT /evidence="ECO:0000269|PubMed:19712804,
FT ECO:0000269|PubMed:20590677, ECO:0000269|PubMed:23861363,
FT ECO:0000269|PubMed:30871348, ECO:0000269|PubMed:32851336"
FT /id="VAR_063093"
FT VARIANT 636
FT /note="R -> S (in CMD1DD; impaired splicing of target
FT mRNAs, such as TTN, CAMK2D and CACNA1C; decreased
FT localization to the nucleus associated with relocalization
FT to P-body and stress granules; dbSNP:rs267607002)"
FT /evidence="ECO:0000269|PubMed:19712804,
FT ECO:0000269|PubMed:26604136, ECO:0000269|PubMed:30871348,
FT ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34732726"
FT /id="VAR_063094"
FT VARIANT 637
FT /note="S -> G (in CMD1DD; also found in patients with left
FT ventricular non-compaction; dbSNP:rs267607005)"
FT /evidence="ECO:0000269|PubMed:19712804,
FT ECO:0000269|PubMed:21846512, ECO:0000269|PubMed:32851336"
FT /id="VAR_063095"
FT VARIANT 638
FT /note="P -> L (in CMD1DD; impaired localization to the
FT nucleus, leading to mislocalization to the cytoplasm;
FT dbSNP:rs267607003)"
FT /evidence="ECO:0000269|PubMed:19712804,
FT ECO:0000269|PubMed:22004663, ECO:0000269|PubMed:30871348,
FT ECO:0000269|PubMed:32840935"
FT /id="VAR_063096"
FT VARIANT 674
FT /note="D -> G (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30871348"
FT /id="VAR_086524"
FT VARIANT 716
FT /note="R -> Q (in CMD1DD; dbSNP:rs375798246)"
FT /evidence="ECO:0000269|PubMed:20590677,
FT ECO:0000269|PubMed:30871351"
FT /id="VAR_068806"
FT VARIANT 768
FT /note="S -> W (in dbSNP:rs1417635)"
FT /id="VAR_042533"
FT VARIANT 888
FT /note="D -> N (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22004663"
FT /id="VAR_086525"
FT VARIANT 905
FT /note="M -> K (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31583969"
FT /id="VAR_086526"
FT VARIANT 913
FT /note="E -> K (in CMD1DD; decreased stability; impaired
FT mRNA splicing of target mRNAs)"
FT /evidence="ECO:0000269|PubMed:27496873,
FT ECO:0000269|PubMed:30871348"
FT /id="VAR_086527"
FT VARIANT 914
FT /note="V -> A (in CMD1DD; impaired mRNA splicing of target
FT mRNAs; does not affect nuclear localization)"
FT /evidence="ECO:0000269|PubMed:32840935"
FT /id="VAR_086528"
FT VARIANT 1031..1227
FT /note="Missing (in CMD1DD; impaired mRNA splicing of TTN
FT (Titin) mRNA)"
FT /evidence="ECO:0000269|PubMed:22004663,
FT ECO:0000269|PubMed:29895960"
FT /id="VAR_086529"
FT VARIANT 1039
FT /note="P -> S (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30871348"
FT /id="VAR_086530"
FT VARIANT 1057
FT /note="R -> W (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:34174465"
FT /id="VAR_086531"
FT VARIANT 1081
FT /note="P -> R (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22004663"
FT /id="VAR_086532"
FT VARIANT 1206
FT /note="E -> K (in CMD1DD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:22004663"
FT /id="VAR_086533"
FT MUTAGEN 660
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-679; A-685; A-742; A-
FT 876; A-980; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 660
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-679, D-685, D-742, D-876, D-980, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 679
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-685; A-742; A-
FT 876; A-980; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 679
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-685, D-742, D-876, D-980, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 685
FT /note="E->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-742; A-
FT 876; A-980; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 685
FT /note="E->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-742, D-876, D-980, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 742
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 876; A-980; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 742
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-876, D-980, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 876
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-980; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 876
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-980, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 980
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-876; A-1060; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 980
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-876, D-
FT 1060, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1060
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-876; A-980; A-1080; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1060
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-876, D-
FT 980, D-1080, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1080
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-876; A-980; A-1060; A-1120 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1080
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-876, D-
FT 980, D-1060, D-1120 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1120
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-876; A-980; A-1060; A-1080 and A-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1120
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-876, D-
FT 980, D-1060, D-1080 and D-1210."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1210
FT /note="S->A: In A10 mutant; does not affect nuclear
FT localization; when associated with A-660; A-679; A-685; A-
FT 742; A-876; A-980; A-1060; A-1080 and A-1120."
FT /evidence="ECO:0000269|PubMed:35427468"
FT MUTAGEN 1210
FT /note="S->D: In D10 mutant; mimics phosphorylation; does
FT not prevent nuclear localization but induces increased
FT localization to cytoplasmic ribonucleoprotein granules;
FT when associated with D-660, D-679, D-685, D-742, D-876, D-
FT 980, D-1060, D-1080 and D-1120."
FT /evidence="ECO:0000269|PubMed:35427468"
SQ SEQUENCE 1227 AA; 134258 MW; 24EFF5CE6E5FDFD4 CRC64;
MVLAAAMSQD ADPSGPEQPD RVACSVPGAR ASPAPSGPRG MQQPPPPPQP PPPPQAGLPQ
IIQNAAKLLD KNPFSVSNPN PLLPSPASLQ LAQLQAQLTL HRLKLAQTAV TNNTAAATVL
NQVLSKVAMS QPLFNQLRHP SVITGPHGHA GVPQHAAAIP STRFPSNAIA FSPPSQTRGP
GPSMNLPNQP PSAMVMHPFT GVMPQTPGQP AVILGIGKTG PAPATAGFYE YGKASSGQTY
GPETDGQPGF LPSSASTSGS VTYEGHYSHT GQDGQAAFSK DFYGPNSQGS HVASGFPAEQ
AGGLKSEVGP LLQGTNSQWE SPHGFSGQSK PDLTAGPMWP PPHNQPYELY DPEEPTSDRT
PPSFGGRLNN SKQGFIGAGR RAKEDQALLS VRPLQAHELN DFHGVAPLHL PHICSICDKK
VFDLKDWELH VKGKLHAQKC LVFSENAGIR CILGSAEGTL CASPNSTAVY NPAGNEDYAS
NLGTSYVPIP ARSFTQSSPT FPLASVGTTF AQRKGAGRVV HICNLPEGSC TENDVINLGL
PFGKVTNYIL MKSTNQAFLE MAYTEAAQAM VQYYQEKSAV INGEKLLIRM SKRYKELQLK
KPGKAVAAII QDIHSQRERD MFREADRYGP ERPRSRSPVS RSLSPRSHTP SFTSCSSSHS
PPGPSRADWG NGRDSWEHSP YARREEERDP APWRDNGDDK RDRMDPWAHD RKHHPRQLDK
AELDERPEGG RPHREKYPRS GSPNLPHSVS SYKSREDGYY RKEPKAKSDK YLKQQQDAPG
RSRRKDEARL RESRHPHPDD SGKEDGLGPK VTRAPEGAKA KQNEKNKTKR TDRDQEGADD
RKENTMAENE AGKEEQEGME ESPQSVGRQE KEAEFSDPEN TRTKKEQDWE SESEAEGESW
YPTNMEELVT VDEVGEEEDF IVEPDIPELE EIVPIDQKDK ICPETCLCVT TTLDLDLAQD
FPKEGVKAVG NGAAEISLKS PRELPSASTS CPSDMDVEMP GLNLDAERKP AESETGLSLE
DSDCYEKEAK GVESSDVHPA PTVQQMSSPK PAEERARQPS PFVDDCKTRG TPEDGACEGS
PLEEKASPPI ETDLQNQACQ EVLTPENSRY VEMKSLEVRS PEYTEVELKQ PLSLPSWEPE
DVFSELSIPL GVEFVVPRTG FYCKLCGLFY TSEETAKMSH CRSAVHYRNL QKYLSQLAEE
GLKETEGADS PRPEDSGIVP RFERKKL
