Rbm20
entrez
309544
canonical
uniprot
E9PT37
canonical
ensembl
ENSRNOG00000014705
resolver
ensp
ENSRNOP00000051570
resolver
ensp
ENSRNOP00000091922
resolver
enst
ENSRNOT00000054685
resolver
enst
ENSRNOT00000113904
resolver
genesymbol
Rbm20
resolver
uniprot
A0A8I6AGI3
resolver
uniprot
C1IEE3
resolver
uniprot_entry
A0A8I6AGI3_RAT
resolver
uniprot_entry
RBM20_RAT
resolver
uniprot_sec
C1IEE3
resolver
amino_acid_sequence
MVLAAAMSQDADPSGPEQPDRDACIVPGVQGPPAPQGQQGMQPLPPPLPPPPQPQSSLPQIIQNAAKLLDKNPFSVSSQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTTHGPTGVSQHAATVPSAHFPSTAIAFSPPSQAGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSIGKAGPTPATTGFYDYGKANPGQAYGSETEGQPGFLPASASAAASGGVTYEGHYSHTGQDGQATFSKDFYGPSAQGSHAAGGFPADQAGSMKGDVGGLLQGTNSQWERPSGFSGQNKADITAGPGLWAPPASQPYELYDPEEPTSDRAPPAFGSRLNNSKQGFNCSCRRTKEGQAMLSVRPLQGHQLNDFRGLAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSESAGLRSICATGEGTLSASANSTAVYNPTGNEDYTSTLGTSYAAIPTRAFAQSNPMFPSASSGTNFAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKPALINGEKLLIRMSTRYKELQLKKPGKNVAAIIQDIHSQRERCMLREADRYGPERPRSRSPMSRSLSPRSHSPPGPSRADWGNGRDSYAWRDEDRETVPRRENGEDKRDRLDVWAHDRKHYPRQLDKAELDERLEGGRGYREKYLKSGSPGPLHSASGYKGREDGYHRKETKAKLDKHPKQQQQDVPGRSRRKEEARLREPRHPHPEDSGKEEDLEPKVTRAPEGTKSKQSEKSKTKRADRDQEGADDKKEGRGAENEAGTEEQEGMEESPASVGTQQEGTESSDPENTRTKKGQDCDSGSEPEGDNWYPTNMEELVTVDEVGEEDFIMEPDIPELEEIVPIDQKDKILPEICPCVTATLGLDLAKDFTKQGETLGNGDAELSPKLPGQVPSTSTSCPNDTDMEMAGLNLDAERKPAESETGLSPEVSNCYEKEARGAEGSDVRLAPAAQRMSSPQPADERAQQSSPFLDDCKARGSPEDGPHEVSPLEEKASPTTESDLQSQACQENSRYTETRSLNSRSPEFTEAELKEPLSLPSWEPEVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEAAKVSHCRSTVHYRNLQKYLSQLAEEGLKETEGVDSPSPERSGIGPHLERKKL
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:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899, PubMed:27289039, PubMed:33805770, 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:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (PubMed:23307558, PubMed:24367651, PubMed:24960161, PubMed:25573899, PubMed:33805770, PubMed:35394688). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (PubMed:27289039). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23307558, ECO:0000269|PubMed:24367651, ECO:0000269|PubMed:24960161, ECO:0000269|PubMed:25573899, ECO:0000269|PubMed:27289039, ECO:0000269|PubMed:33805770, ECO:0000269|PubMed:35394688}.
uniprot
proteins
mass_dalton
130760
uniprot
proteins
mutagenesis
MUTAGEN 638; /note="S->A: Impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs. Decreased localization to the nucleus associated with an increased localization to cytoplasmic ribonucleoprotein granules."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 638; /note="S->D: Mimics phosphorylation; does not restore nuclear localization."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 640; /note="S->D: Mimics phosphorylation; does not restore nuclear localization."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 640; /note="S->G: Impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs. Decreased localization to the nucleus associated with an increased localization to cytoplasmic ribonucleoprotein granules."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 643; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 645; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 652; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 729; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 789; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 879; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 881; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 999; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1034; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1046; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1057; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1096; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1190; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688"; MUTAGEN 1192; /note="S->A: No effect; does not affect ability to regulate alternative splicing."; /evidence="ECO:0000269|PubMed:35394688
uniprot
proteins
post_translational_modification
PTM: Phosphorylation regulates the subcellular localization. Phosphorylation of Ser-638 and Ser-640 in the RS (arginine/serine-rich) region promotes nuclear localization of the protein (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:35394688}.
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
22466703
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23307558
uniprot
proteins
pubmed
24367651
uniprot
proteins
pubmed
24960161
uniprot
proteins
pubmed
25573899
uniprot
proteins
pubmed
27289039
uniprot
proteins
pubmed
33805770
uniprot
proteins
pubmed
35394688
uniprot
proteins
sequence_length
1207
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:23307558, ECO:0000269|PubMed:35394688}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {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 (By similarity). 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:35394688). {ECO:0000250|UniProtKB:Q5T481, ECO:0000269|PubMed:35394688}.
uniprot
proteins