A0AV96 · RBM47_HUMAN
- ProteinRNA-binding protein 47
- GeneRBM47
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids593 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (PubMed:24038582, PubMed:24916387, PubMed:27050523, PubMed:30844405, PubMed:31358901, PubMed:34160127).
Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules (PubMed:24038582, PubMed:24916387, PubMed:30844405).
Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10 (PubMed:34160127).
Also involved in the alternative splicing of several genes including TJP1. Binds the pre-mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (PubMed:27050523, PubMed:31358901).
Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity).
Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules (PubMed:24038582, PubMed:24916387, PubMed:30844405).
Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10 (PubMed:34160127).
Also involved in the alternative splicing of several genes including TJP1. Binds the pre-mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (PubMed:27050523, PubMed:31358901).
Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apolipoprotein B mRNA editing enzyme complex | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | enzyme binding | |
Molecular Function | enzyme-substrate adaptor activity | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Biological Process | 3'-UTR-mediated mRNA stabilization | |
Biological Process | cytidine to uridine editing | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | mRNA processing | |
Biological Process | positive regulation of interleukin-10 production | |
Biological Process | positive regulation of type I interferon-mediated signaling pathway | |
Biological Process | regulation of alternative mRNA splicing, via spliceosome | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein 47
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0AV96
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 115 | Loss of function in regulation of alternative splicing. Loss of pre-mRNA binding activity. Decreased homodimerization. | ||||
Sequence: F → A | ||||||
Mutagenesis | 198 | Decreased function in regulation of alternative splicing. Decreased pre-mRNA binding. No effect on homodimerization. | ||||
Sequence: F → A | ||||||
Mutagenesis | 285 | Decreased function in regulation of alternative splicing. No effect on pre-mRNA binding. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_061832 | 538 | in dbSNP:rs35529250 | |||
Sequence: G → R | ||||||
Natural variant | VAR_054770 | 565 | in dbSNP:rs278981 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 820 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000307855 | 1-593 | UniProt | RNA-binding protein 47 | |||
Sequence: MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY | |||||||
Modified residue | 332 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 394 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 394 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 405 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 405 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 519 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated by interferon.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (PubMed:31358901).
Interacts with A1CF (PubMed:24916387).
Interacts with APOBEC1; form an mRNA editing complex (PubMed:24916387).
Interacts with RBPMS (PubMed:37548402).
Interacts with A1CF (PubMed:24916387).
Interacts with APOBEC1; form an mRNA editing complex (PubMed:24916387).
Interacts with RBPMS (PubMed:37548402).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | A0AV96 | C10orf55 Q5SWW7 | 3 | EBI-2823850, EBI-12809220 | |
BINARY | A0AV96 | C1orf94 Q6P1W5 | 3 | EBI-2823850, EBI-946029 | |
BINARY | A0AV96 | CAMK2A Q9UQM7 | 3 | EBI-2823850, EBI-1383687 | |
BINARY | A0AV96 | CELF5 Q8N6W0 | 3 | EBI-2823850, EBI-12139335 | |
BINARY | A0AV96 | FAM22F B7ZLH0 | 3 | EBI-2823850, EBI-10220102 | |
BINARY | A0AV96 | OTX2 P32243-2 | 3 | EBI-2823850, EBI-9087860 | |
BINARY | A0AV96 | PCBP3 P57721-2 | 3 | EBI-2823850, EBI-11983983 | |
BINARY | A0AV96 | PRR13 Q9NZ81 | 3 | EBI-2823850, EBI-740924 | |
BINARY | A0AV96 | RBFOX1 Q9NWB1-5 | 3 | EBI-2823850, EBI-12123390 | |
BINARY | A0AV96 | RBM46 Q8TBY0 | 2 | EBI-2823850, EBI-12068216 | |
BINARY | A0AV96 | ZNF385C Q66K41-2 | 3 | EBI-2823850, EBI-12055653 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MTAEDSTAAMSSDSAAGS | ||||||
Region | 1-25 | Disordered | ||||
Sequence: MTAEDSTAAMSSDSAAGSSAKVPEG | ||||||
Domain | 71-149 | RRM 1 | ||||
Sequence: CEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVD | ||||||
Domain | 151-233 | RRM 2 | ||||
Sequence: CRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEP | ||||||
Domain | 246-318 | RRM 3 | ||||
Sequence: KILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKP |
Domain
The RRM domains are required for mRNA stabilization.
Sequence similarities
Belongs to the RRM RBM47 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
A0AV96-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Synonymsh-isoform a
- Length593
- Mass (Da)64,099
- Last updated2010-11-30 v2
- ChecksumAEA061F89A68010B
A0AV96-2
- Name2
- Synonymsh-isoform b
- Differences from canonical
- 375-443: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MTAEDSTAAMSSDSAAGS | ||||||
Sequence conflict | 9 | in Ref. 1; AAM21973 | ||||
Sequence: A → T | ||||||
Sequence conflict | 97 | in Ref. 2; BAA91049 | ||||
Sequence: I → T | ||||||
Alternative sequence | VSP_028839 | 375-443 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 515 | in Ref. 1; AAM21972 | ||||
Sequence: G → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF261889 EMBL· GenBank· DDBJ | AAM21972.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF262323 EMBL· GenBank· DDBJ | AAM21973.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK000280 EMBL· GenBank· DDBJ | BAA91049.1 EMBL· GenBank· DDBJ | mRNA | ||
AC098869 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC112717 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC034402 EMBL· GenBank· DDBJ | AAH34402.1 EMBL· GenBank· DDBJ | mRNA | ||
BC126261 EMBL· GenBank· DDBJ | AAI26262.1 EMBL· GenBank· DDBJ | mRNA |