RBPMS
entrez
11030
canonical
uniprot
Q93062
canonical
ensembl
ENSG00000157110
resolver
ensp
ENSP00000287771
resolver
ensp
ENSP00000318102
resolver
ensp
ENSP00000340176
resolver
ensp
ENSP00000380486
resolver
ensp
ENSP00000428675
resolver
ensp
ENSP00000645036
resolver
ensp
ENSP00000645037
resolver
ensp
ENSP00000645038
resolver
ensp
ENSP00000645043
resolver
ensp
ENSP00000724574
resolver
ensp
ENSP00000724578
resolver
ensp
ENSP00000724580
resolver
ensp
ENSP00000743138
resolver
enst
ENST00000517860
resolver
genesymbol
RBPMS
resolver
genesymbol_syn
HERMES
resolver
hgnc
HGNC:19097
resolver
uniprot
B4E3T4
resolver
uniprot
D3DSU9
resolver
uniprot
F6T586
resolver
uniprot
Q92516
resolver
uniprot
Q92517
resolver
uniprot
Q92518
resolver
uniprot
Q96J26
resolver
uniprot_entry
B4E3T4_HUMAN
resolver
uniprot_entry
F6T586_HUMAN
resolver
uniprot_entry
RBPMS_HUMAN
resolver
uniprot_sec
D3DSU9
resolver
uniprot_sec
Q92516
resolver
uniprot_sec
Q92517
resolver
uniprot_sec
Q92518
resolver
uniprot_sec
Q96J26
resolver
amino_acid_sequence
MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSEATSQGWKSRQFC
uniprot
proteins
function
FUNCTION: [Isoform A]: RNA binding protein that mediates the regulation of pre-mRNA alternative splicing (AS) (PubMed:24860013, PubMed:26347403). Acts either as activator (FLNB, HSPG2, LIPA1, MYOCD, PTPRF and PPFIBP1) or repressor (TPM1, ACTN1, ITGA7, PIEZO1, LSM14B, MBNL1 and MBML2) of splicing events on specific pre-mRNA targets (By similarity). Together with RNA binding proteins RBFOX2 and MBNL1/2, activates a splicing program associated with differentiated contractile vascular smooth muscle cells (SMC) by regulating AS of numerous pre-mRNA involved in actin cytoskeleton and focal adhesion machineries, suggesting a role in promoting a cell differentiated state (By similarity). Binds to introns, exons and 3'-UTR associated with tandem CAC trinucleotide motifs separated by a variable spacer region, at a minimum as a dimer. The minimal length of RNA required for RBPMS-binding tandem CAC motifs is 15 nt, with spacing ranging from 1 to 9 nt. Can also bind to CA dinucleotide repeats (PubMed:24860013, PubMed:26347403). Mediates repression of TPM1 exon 3 by binding to CAC tandem repeats in the flanking intronic regions, followed by higher-order oligomerization and heterotypic interactions with other splicing regulators including MBNL1 and RBFOX2, which prevents assembly of ATP-dependent splicing complexes (By similarity). {ECO:0000250|UniProtKB:A0A8I6G705, ECO:0000269|PubMed:24860013, ECO:0000269|PubMed:26347403}.; FUNCTION: [Isoform C]: Acts as a regulator of pre-mRNA alternative splicing (AS) (By similarity). Binds mRNA (PubMed:17099224). Regulates AS of ACTN1, FLNB, although with lower efficiency than isoform A / RBPMSA (By similarity). Acts as coactivator of SMAD transcriptional activity in a TGFB1-dependent manner, possibly through increased phosphorylation of SMAD2 and SMAD3 at the C-terminal SSXS regions and promotion of the nuclear accumulation of SMAD proteins (PubMed:17099224). {ECO:0000250|UniProtKB:A0A8I6G705, ECO:0000269|PubMed:17099224}.
uniprot
proteins
mass_dalton
21802
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="F->A: Abolishes RNA binding."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 36..38; /note="KPR->EPE: Impairs dimerization and RNA binding."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 65; /note="F->A: Abolishes RNA binding."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 97; /note="E->A: Abolishes RNA binding; when associated with A-100."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 100; /note="K->A: Abolishes RNA binding; when associated with A-97."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 100; /note="K->E: Abolishes RNA binding."; /evidence="ECO:0000269|PubMed:26347403"; MUTAGEN 103..104; /note="TK->AA: Abolishes RNA binding."; /evidence="ECO:0000269|PubMed:26347403
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17099224
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24860013
uniprot
proteins
pubmed
26347403
uniprot
proteins
pubmed
8855282
uniprot
proteins
sequence_length
196
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:24860013}. Cytoplasm {ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:24860013}. Cytoplasm, Stress granule {ECO:0000269|PubMed:24860013}. Cytoplasm, P-body {ECO:0000269|PubMed:26347403}. Note=Localized to cytoplasmic stress granules after oxidative stress (PubMed:24860013). Translocates into cytoplasmic stress granules that probably corresponds to P-bodies in response to oxidative stress (PubMed:26347403). {ECO:0000269|PubMed:24860013, ECO:0000269|PubMed:26347403}.
uniprot
proteins