RBM20
entrez
282996
canonical
uniprot
Q5T481
canonical
ensembl
ENSG00000203867
resolver
ensp
ENSP00000358532
resolver
ensp
ENSP00000520684
resolver
enst
ENST00000369519
resolver
enst
ENST00000718239
resolver
genesymbol
RBM20
resolver
hgnc
HGNC:27424
resolver
uniprot
A6NIP5
resolver
uniprot
B5A868
resolver
uniprot
Q5JVI1
resolver
uniprot_entry
RBM20_HUMAN
resolver
uniprot_sec
A6NIP5
resolver
uniprot_sec
B5A868
resolver
uniprot_sec
Q5JVI1
resolver
amino_acid_sequence
MVLAAAMSQDADPSGPEQPDRVACSVPGARASPAPSGPRGMQQPPPPPQPPPPPQAGLPQIIQNAAKLLDKNPFSVSNPNPLLPSPASLQLAQLQAQLTLHRLKLAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVITGPHGHAGVPQHAAAIPSTRFPSNAIAFSPPSQTRGPGPSMNLPNQPPSAMVMHPFTGVMPQTPGQPAVILGIGKTGPAPATAGFYEYGKASSGQTYGPETDGQPGFLPSSASTSGSVTYEGHYSHTGQDGQAAFSKDFYGPNSQGSHVASGFPAEQAGGLKSEVGPLLQGTNSQWESPHGFSGQSKPDLTAGPMWPPPHNQPYELYDPEEPTSDRTPPSFGGRLNNSKQGFIGAGRRAKEDQALLSVRPLQAHELNDFHGVAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLVFSENAGIRCILGSAEGTLCASPNSTAVYNPAGNEDYASNLGTSYVPIPARSFTQSSPTFPLASVGTTFAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKSAVINGEKLLIRMSKRYKELQLKKPGKAVAAIIQDIHSQRERDMFREADRYGPERPRSRSPVSRSLSPRSHTPSFTSCSSSHSPPGPSRADWGNGRDSWEHSPYARREEERDPAPWRDNGDDKRDRMDPWAHDRKHHPRQLDKAELDERPEGGRPHREKYPRSGSPNLPHSVSSYKSREDGYYRKEPKAKSDKYLKQQQDAPGRSRRKDEARLRESRHPHPDDSGKEDGLGPKVTRAPEGAKAKQNEKNKTKRTDRDQEGADDRKENTMAENEAGKEEQEGMEESPQSVGRQEKEAEFSDPENTRTKKEQDWESESEAEGESWYPTNMEELVTVDEVGEEEDFIVEPDIPELEEIVPIDQKDKICPETCLCVTTTLDLDLAQDFPKEGVKAVGNGAAEISLKSPRELPSASTSCPSDMDVEMPGLNLDAERKPAESETGLSLEDSDCYEKEAKGVESSDVHPAPTVQQMSSPKPAEERARQPSPFVDDCKTRGTPEDGACEGSPLEEKASPPIETDLQNQACQEVLTPENSRYVEMKSLEVRSPEYTEVELKQPLSLPSWEPEDVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEETAKMSHCRSAVHYRNLQKYLSQLAEEGLKETEGADSPRPEDSGIVPRFERKKL
uniprot
proteins
disease_involvement
DISEASE: Cardiomyopathy, dilated, 1DD (CMD1DD) [MIM:613172]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:19712804, ECO:0000269|PubMed:20590677, ECO:0000269|PubMed:21846512, ECO:0000269|PubMed:22004663, ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23861363, ECO:0000269|PubMed:26604136, ECO:0000269|PubMed:27496873, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:30262925, ECO:0000269|PubMed:30871348, ECO:0000269|PubMed:30871351, ECO:0000269|PubMed:31583969, ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34021826, ECO:0000269|PubMed:34174465, ECO:0000269|PubMed:34322310, ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Left ventricular non-compaction (LVNCX): A form of left ventricular non-compaction, a cardiomyopathy due to myocardial morphogenesis arrest and characterized by a hypertrophic left ventricle, a severely thickened 2-layered myocardium, numerous prominent trabeculations, deep intertrabecular recesses, and poor systolic function. Clinical manifestations are variable. Some affected individuals experience no symptoms at all, others develop heart failure. In some cases, left ventricular non-compaction is associated with other congenital heart anomalies. The disease is caused by variants affecting the gene represented in this entry. {ECO:0000269|PubMed:32851336}.
uniprot
proteins
function
FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH (PubMed:22466703, PubMed:24960161, PubMed:26604136, PubMed:27496873, PubMed:27531932, PubMed:29895960, PubMed:30948719, PubMed:32840935, PubMed:34732726, PubMed:35427468). Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts (PubMed:24960161, PubMed:30948719, PubMed:34732726). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (PubMed:27531932, PubMed:30948719). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (PubMed:27531932, PubMed:34732726). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:E9PT37, ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:24960161, ECO:0000269|PubMed:26604136, ECO:0000269|PubMed:27496873, ECO:0000269|PubMed:27531932, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:30948719, ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}.
uniprot
proteins
mass_dalton
134258
uniprot
proteins
mutagenesis
MUTAGEN 660; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-679; A-685; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 660; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-679, D-685, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 679; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-685; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 679; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-685, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 685; /note="E->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 685; /note="E->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 742; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-876; A-980; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 742; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-876, D-980, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 876; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-980; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 876; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-980, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 980; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-1060; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 980; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-1060, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1060; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1080; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1060; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1080, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1080; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1120 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1080; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1120 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1120; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1080 and A-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1120; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1080 and D-1210."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1210; /note="S->A: In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1080 and A-1120."; /evidence="ECO:0000269|PubMed:35427468"; MUTAGEN 1210; /note="S->D: In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1080 and D-1120."; /evidence="ECO:0000269|PubMed:35427468
uniprot
proteins
post_translational_modification
PTM: Phosphorylation regulates the subcellular localization (PubMed:35427468). Phosphorylation of Ser-635 and Ser-637 in the RS (arginine/serine-rich) region promotes nuclear localization of the protein (PubMed:35427468). In contrast, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (PubMed:35427468). {ECO:0000269|PubMed:35427468}.
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
19712804
uniprot
proteins
pubmed
20590677
uniprot
proteins
pubmed
21846512
uniprot
proteins
pubmed
22004663
uniprot
proteins
pubmed
22466703
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23861363
uniprot
proteins
pubmed
23886709
uniprot
proteins
pubmed
24960161
uniprot
proteins
pubmed
26604136
uniprot
proteins
pubmed
27496873
uniprot
proteins
pubmed
27531932
uniprot
proteins
pubmed
29895960
uniprot
proteins
pubmed
30262925
uniprot
proteins
pubmed
30871348
uniprot
proteins
pubmed
30871351
uniprot
proteins
pubmed
30948719
uniprot
proteins
pubmed
31583969
uniprot
proteins
pubmed
32840935
uniprot
proteins
pubmed
32851336
uniprot
proteins
pubmed
33188278
uniprot
proteins
pubmed
34021826
uniprot
proteins
pubmed
34174465
uniprot
proteins
pubmed
34322310
uniprot
proteins
pubmed
34732726
uniprot
proteins
pubmed
35427468
uniprot
proteins
sequence_length
1227
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:23886709, ECO:0000269|PubMed:30262925, ECO:0000269|PubMed:32840935, ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:33188278, PubMed:34732726, PubMed:35427468). Also localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role (PubMed:33188278, PubMed:34732726, PubMed:35427468). Subcellular localization is regulated by phosphorylation of different parts of the protein: while phosphorylation of the RS (arginine/serine-rich) region promotes nuclear localization, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (PubMed:35427468). {ECO:0000269|PubMed:33188278, ECO:0000269|PubMed:34732726, ECO:0000269|PubMed:35427468}.
uniprot
proteins