RBM4
entrez
5936
canonical
uniprot
Q9BWF3
canonical
ensembl
ENSG00000173933
resolver
ensp
ENSP00000309166
resolver
ensp
ENSP00000381680
resolver
ensp
ENSP00000413497
resolver
genesymbol
RBM4
resolver
genesymbol_syn
RBM4A
resolver
hgnc
HGNC:9901
resolver
uniprot
B3KUN0
resolver
uniprot
B4E1U0
resolver
uniprot
E7EQS3
resolver
uniprot
O02916
resolver
uniprot
Q4VC48
resolver
uniprot
Q6P1P2
resolver
uniprot
Q8WU85
resolver
uniprot_entry
RBM4_HUMAN
resolver
uniprot_sec
B3KUN0
resolver
uniprot_sec
B4E1U0
resolver
uniprot_sec
E7EQS3
resolver
uniprot_sec
O02916
resolver
uniprot_sec
Q4VC48
resolver
uniprot_sec
Q6P1P2
resolver
uniprot_sec
Q8WU85
resolver
amino_acid_sequence
MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKTSTKLHVGNISPTCTNKELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPIDRSGRVADLTEQYNEQYGAVRTPYTMSYGDSLYYNNAYGALDAYYKRCRAARSYEAVAAAAASVYNYAEQTLSQLPQVQNTAMASHLTSTSLDPYDRHLLPTSGAAATAAAAAAAAAAVTAASTSYYGRDRSPLRRATAPVPTVGEGYGYGHESELSQASAAARNSLYDMARYEREQYADRARYSAF
uniprot
proteins
function
FUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. {ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:16777844, ECO:0000269|PubMed:16934801, ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:21343338, ECO:0000269|PubMed:21518792, ECO:0000269|PubMed:37548402}.
uniprot
proteins
mass_dalton
40314
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="Y->A: Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115."; /evidence="ECO:0000269|PubMed:12628928"; MUTAGEN 39; /note="F->A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115."; /evidence="ECO:0000269|PubMed:12628928"; MUTAGEN 113; /note="Y->A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115."; /evidence="ECO:0000269|PubMed:12628928"; MUTAGEN 115; /note="F->A: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113."; /evidence="ECO:0000269|PubMed:12628928"; MUTAGEN 309; /note="S->A: Inhibits IRES-mediated mRNA translation. Does not inhibit interaction with EIF4A1. Inhibits localization in cytoplasm and cytoplasmic granules upon cell muscle differentiation. Inhibits negative regulation of translation involved in gene silencing by miRNA."; /evidence="ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:21518792
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-309 is induced upon cell muscle differentiation (By similarity). Phosphorylated. Phosphorylated in vitro on Ser-309 by SRPK1. Phosphorylation on Ser-309 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation. {ECO:0000250, ECO:0000269|PubMed:17284590}.
uniprot
proteins
pubmed
12469345
uniprot
proteins
pubmed
12628928
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16260624
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16777844
uniprot
proteins
pubmed
16907643
uniprot
proteins
pubmed
16934801
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17284590
uniprot
proteins
pubmed
17932509
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18708123
uniprot
proteins
pubmed
19561594
uniprot
proteins
pubmed
19801630
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21343338
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21518792
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
37548402
uniprot
proteins
pubmed
9169144
uniprot
proteins
sequence_length
364
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus speckle. Cytoplasm. Cytoplasmic granule. Note=Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation.
uniprot
proteins