Rbm20
entrez
73713
canonical
uniprot
Q3UQS8
canonical
ensembl
ENSMUSG00000043639
resolver
ensp
ENSMUSP00000129447
resolver
genesymbol
Rbm20
resolver
uniprot
E9PVK0
resolver
uniprot
Q8CFS9
resolver
uniprot_entry
RBM20_MOUSE
resolver
uniprot_sec
E9PVK0
resolver
uniprot_sec
Q8CFS9
resolver
amino_acid_sequence
MVLAVAMSQDADPSGPEQPDRDACVMPGVQGPSVPQGQQGMQPLPPPPPPQPQASLPQIIQNAAKLLDKSPFSVNNQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTAHGPTGVSQHAASVPSAHFPSTAIAFSPPSQTGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSLGKAGPTPATTGFYDYGKANSGQAYGSETEGQPGFLPASASATASGSMTYEGHYSHTGQDGQPAFSKDFYGPNAQGPHIAGGFPADQTGSMKGDVGGLLQGTNSQWERPPGFSGQNKPDITAGPSLWAPPASQPYELYDPEEPTSDRAPPAFGSRLNNSKQGFGCSCRRTKEGQAVLSVRPLQGHQLNDFRGLAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSESAGLRSIRASGEGTLSASANSTAVYNPTGNEDYTSNLGTSYAAIPTRAFAQSNPVFPSASSGTSFAAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKPAIINGEKLLIRMSTRYKELQLKKPGKNVAAIIQDIHSQRERDMLREADRYGPERPRSRSPMSRSLSPRSHSPPGPSRADWGNGRDSYAWRDEDRETVPRRENGEDKRDRLDVWAHDRKHYPRQLDKAELDERLEGGRGYREKYLKSGSPGPLHSVSGYKGREDGYHRKEPKAKLDKYPKQQPDVPGRSRRKEEARLREPRHPHPEDSGKAEDLEPKITRAPDGTKSKQSEKSKTKRADRDQEGADDKKESQLAENEAGAEEQEGMVGIQQEGTESCDPENTRTKKGQDCDSGSEPEGDNWYPTNMEELVTVDEVGEEDFIMEPDLPELEEIVPIDQKDKTLPKICTCVTATLGLDLAKDFTKQGETLGNGDAELSLKLPGQVPSTSASCPNDTDLEMPGLNLDAERKPAESETGLSLEVSNCYEKEARGEEDSDVSLAPAVQQMSSPQPADERARQSSPFLDDCKARGSPEDGSHEASPLEGKASPPTESDLQSQACRENPRYMEVKSLNVRSPEFTEAELKEPLSLPSWEPEVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEAAKVSHCRSTVHYRNLQKYLSQLAEEGLKETEGTDSPSPERGGIGPHLERKKL
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:24584570, PubMed:27630136, PubMed:29650543, PubMed:29895960, PubMed:33110103, PubMed:35041844, PubMed:35394688). 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:32187365). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (PubMed:27630136, PubMed:29895960, PubMed:33110103, PubMed:35041844). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (PubMed:37272356). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:E9PT37, ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:24584570, ECO:0000269|PubMed:27630136, ECO:0000269|PubMed:29650543, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:32187365, ECO:0000269|PubMed:33110103, ECO:0000269|PubMed:35041844, ECO:0000269|PubMed:35394688, ECO:0000269|PubMed:37272356}.
uniprot
proteins
mass_dalton
130124
uniprot
proteins
mutagenesis
MUTAGEN 523; /note="H->A: Strongly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 526; /note="N->A: Slightly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 537; /note="V->I: Slightly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 558; /note="Q->A: Does not affect pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 560; /note="F->A: Strongly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 577; /note="Q->A: Does not affect pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 591; /note="R->M: Slightly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 595; /note="R->M: Strongly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 596; /note="Y->A: Strongly reduced pre-mRNA-binding."; /evidence="ECO:0000269|PubMed:32187365"; MUTAGEN 636; /note="R->W: Impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs."; /evidence="ECO:0000269|PubMed:29895960"; MUTAGEN 637..639; /note="SRS->ARA: Abolished localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs."; /evidence="ECO:0000269|PubMed:29895960"; MUTAGEN 637; /note="S->A: Knockin mice show severe cardiac phenotypes, characterized by dilated cardiomyopathy and atrial fibrillation. Decreased localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs."; /evidence="ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:33110103, ECO:0000269|PubMed:35394688"; MUTAGEN 639; /note="S->A: Decreased localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs."; /evidence="ECO:0000269|PubMed:29895960"; MUTAGEN 639; /note="S->G: Knockin mice show severe cardiac phenotypes, characterized by dilated cardiomyopathy, leading to premature death. Decreased localization to the nucleus associated with an increased localization to cytoplasmic ribonucleoprotein granules."; /evidence="ECO:0000269|PubMed:35041844
uniprot
proteins
post_translational_modification
PTM: Phosphorylation regulates the subcellular localization. Phosphorylation of Ser-637 and Ser-639 in the RS (arginine/serine-rich) region promotes nuclear localization of the protein (PubMed:29895960, PubMed:35394688). In contrast, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:35394688}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22466703
uniprot
proteins
pubmed
23886709
uniprot
proteins
pubmed
24584570
uniprot
proteins
pubmed
27630136
uniprot
proteins
pubmed
29650543
uniprot
proteins
pubmed
29895960
uniprot
proteins
pubmed
32187365
uniprot
proteins
pubmed
33110103
uniprot
proteins
pubmed
35041844
uniprot
proteins
pubmed
35394688
uniprot
proteins
pubmed
37272356
uniprot
proteins
sequence_length
1199
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23886709, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:33110103, ECO:0000269|PubMed:35041844, ECO:0000269|PubMed:35394688}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:35041844, ECO:0000269|PubMed:35394688}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:35394688). Also localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role (PubMed:35394688). 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:29895960, PubMed:35394688). {ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:35394688}.
uniprot
proteins