Q0VBL3 · RBM15_MOUSE
- ProteinRNA-binding protein 15
- GeneRbm15
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids962 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:29535189).
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189).
Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:29535189).
Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (By similarity).
Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (PubMed:17283045, PubMed:17376872, PubMed:18981216, PubMed:25468569).
Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (By similarity).
Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (PubMed:18981216).
Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (PubMed:25468569).
May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (By similarity).
High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (By similarity).
May be implicated in HOX gene regulation (By similarity).
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189).
Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:29535189).
Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (By similarity).
Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (PubMed:17283045, PubMed:17376872, PubMed:18981216, PubMed:25468569).
Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (By similarity).
Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (PubMed:18981216).
Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (PubMed:25468569).
May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (By similarity).
High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (By similarity).
May be implicated in HOX gene regulation (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear membrane | |
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | RNA N6-methyladenosine methyltransferase complex | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Biological Process | branching involved in blood vessel morphogenesis | |
Biological Process | dosage compensation by inactivation of X chromosome | |
Biological Process | negative regulation of myeloid cell differentiation | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | placenta blood vessel development | |
Biological Process | positive regulation of transcription of Notch receptor target | |
Biological Process | regulation of alternative mRNA splicing, via spliceosome | |
Biological Process | regulation of megakaryocyte differentiation | |
Biological Process | RNA methylation | |
Biological Process | spleen development | |
Biological Process | thrombopoietin-mediated signaling pathway | |
Biological Process | ventricular septum morphogenesis |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein 15
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ0VBL3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus membrane ; Peripheral membrane protein
Note: Colocalizes at the nuclear pore with DBP5 and NXF1.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethality around E9.5 (PubMed:17376872, PubMed:18981216).
Early embryos show growth retardation and incomplete closure of the notochord, as well as placental defects in the spongiotrophoblast and syncytiotrophoblast layers, resulting in an arrest of vascular branching morphogenesis (PubMed:18981216).
Conditional knockout mice lacking Rbm15 within the hematopoietic compartment display a loss of peripheral B-cells due to a block in pro/pre-B differentiation, as well as a myeloid and megakaryocytic expansion in spleen and bone marrow (PubMed:17376872).
Early embryos show growth retardation and incomplete closure of the notochord, as well as placental defects in the spongiotrophoblast and syncytiotrophoblast layers, resulting in an arrest of vascular branching morphogenesis (PubMed:18981216).
Conditional knockout mice lacking Rbm15 within the hematopoietic compartment display a loss of peripheral B-cells due to a block in pro/pre-B differentiation, as well as a myeloid and megakaryocytic expansion in spleen and bone marrow (PubMed:17376872).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 52 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000444611 | 1-962 | RNA-binding protein 15 | |||
Sequence: MRSAGREPLPRRSPRWRRASPLCETSAGWRVSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGERSKKLGGSGGSNGSSSGKTDSGGSRRSLHLDKSSSRGGSREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGVEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDAYAPSSSVVGTSVGSHRHAPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPPPLPRELERERDYPFYDRVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTENDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDTFGHRAPDPLRSARDRTPPLLYRDRDRDLYTDSDWVPPPPPVRERSARAATSAVTAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDRKNSASAERDRKHRTAAPTEGKNPLKKEDRSDGNAPSASTSSSKQKPPSQKQDGGTAPVAASSPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSATSDTAASTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRAKLVNSG | ||||||
Modified residue | 108 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 178 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 207 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 245 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 252 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 256 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 258 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 265 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 293 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 364 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 405 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 419 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 444 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 449 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 567 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 577 | Asymmetric dimethylarginine; alternate; by PRMT1 | ||||
Sequence: R | ||||||
Modified residue | 577 | Omega-N-methylarginine; alternate; by PRMT1 | ||||
Sequence: R | ||||||
Modified residue | 621 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 655 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 670 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 674 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 701 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 745 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 768 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 782 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 936 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Methylated at Arg-577 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.
Ubiquitinated by CNOT4 following methylation at Arg-577 by PRMT1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189).
The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189).
The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189).
Also a component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity).
Interacts with RBPJ (PubMed:17283045).
Interacts (via SPOC domain) with SETD1B (By similarity).
Interacts with NXF1, the interaction is required to promote mRNA export (By similarity).
Interacts with SF3B1 (By similarity).
The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189).
The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189).
Also a component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity).
Interacts with RBPJ (PubMed:17283045).
Interacts (via SPOC domain) with SETD1B (By similarity).
Interacts with NXF1, the interaction is required to promote mRNA export (By similarity).
Interacts with SF3B1 (By similarity).
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 | Basic and acidic residues | ||||
Sequence: MRSAGREPLPRRSPRWRR | ||||||
Region | 1-167 | Disordered | ||||
Sequence: MRSAGREPLPRRSPRWRRASPLCETSAGWRVSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGERSKKLGGSGGSNGSSSGKTDSGGSRRSLHLDKSSSRGGSREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGVE | ||||||
Compositional bias | 31-70 | Basic and acidic residues | ||||
Sequence: VSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGER | ||||||
Compositional bias | 76-92 | Polar residues | ||||
Sequence: GSGGSNGSSSGKTDSGG | ||||||
Compositional bias | 93-107 | Basic and acidic residues | ||||
Sequence: SRRSLHLDKSSSRGG | ||||||
Compositional bias | 108-157 | Polar residues | ||||
Sequence: SREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAAS | ||||||
Domain | 169-251 | RRM 1 | ||||
Sequence: KTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYV | ||||||
Region | 257-297 | Disordered | ||||
Sequence: RSPLDKDAYAPSSSVVGTSVGSHRHAPGGGGGQRSLSPGGA | ||||||
Domain | 373-450 | RRM 2 | ||||
Sequence: RTLFLGNLDITVTENDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKA | ||||||
Domain | 454-528 | RRM 3 | ||||
Sequence: TRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADT | ||||||
Region | 553-779 | Disordered | ||||
Sequence: GHRAPDPLRSARDRTPPLLYRDRDRDLYTDSDWVPPPPPVRERSARAATSAVTAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDRKNSASAERDRKHRTAAPTEGKNPLKKEDRSDGNAPSASTSSSKQKPPSQKQDGGTAPVA | ||||||
Compositional bias | 557-582 | Basic and acidic residues | ||||
Sequence: PDPLRSARDRTPPLLYRDRDRDLYTD | ||||||
Compositional bias | 610-752 | Basic and acidic residues | ||||
Sequence: LDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDRKNSASAERDRKHRTAAPTEGKNPLKKEDRSDG | ||||||
Compositional bias | 753-776 | Polar residues | ||||
Sequence: NAPSASTSSSKQKPPSQKQDGGTA | ||||||
Domain | 778-957 | SPOC | ||||
Sequence: VAASSPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSATSDTAASTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRAK | ||||||
Region | 866-885 | Disordered | ||||
Sequence: GSSDSRSSSSSATSDTAAST |
Sequence similarities
Belongs to the RRM Spen family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q0VBL3-1
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
- Length962
- Mass (Da)105,722
- Last updated2006-09-05 v1
- ChecksumD740EDBF23279C5D
Q0VBL3-2
- Name2
- Differences from canonical
- 956-962: AKLVNSG → GAS
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Basic and acidic residues | ||||
Sequence: MRSAGREPLPRRSPRWRR | ||||||
Compositional bias | 31-70 | Basic and acidic residues | ||||
Sequence: VSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGER | ||||||
Sequence conflict | 41 | in Ref. 1; BAD90348 | ||||
Sequence: R → P | ||||||
Compositional bias | 76-92 | Polar residues | ||||
Sequence: GSGGSNGSSSGKTDSGG | ||||||
Sequence conflict | 78 | in Ref. 4; BAE40192 | ||||
Sequence: G → S | ||||||
Compositional bias | 93-107 | Basic and acidic residues | ||||
Sequence: SRRSLHLDKSSSRGG | ||||||
Compositional bias | 108-157 | Polar residues | ||||
Sequence: SREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAAS | ||||||
Sequence conflict | 157 | in Ref. 4; BAE38672 | ||||
Sequence: S → A | ||||||
Compositional bias | 557-582 | Basic and acidic residues | ||||
Sequence: PDPLRSARDRTPPLLYRDRDRDLYTD | ||||||
Compositional bias | 610-752 | Basic and acidic residues | ||||
Sequence: LDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDRKNSASAERDRKHRTAAPTEGKNPLKKEDRSDG | ||||||
Sequence conflict | 619 | in Ref. 4; BAE40192 | ||||
Sequence: G → S | ||||||
Compositional bias | 753-776 | Polar residues | ||||
Sequence: NAPSASTSSSKQKPPSQKQDGGTA | ||||||
Alternative sequence | VSP_059625 | 956-962 | in isoform 2 | |||
Sequence: AKLVNSG → GAS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK220162 EMBL· GenBank· DDBJ | BAD90348.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC132405 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC028452 EMBL· GenBank· DDBJ | AAH28452.1 EMBL· GenBank· DDBJ | mRNA | ||
BC051409 EMBL· GenBank· DDBJ | AAH51409.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057038 EMBL· GenBank· DDBJ | AAH57038.1 EMBL· GenBank· DDBJ | mRNA | ||
BC080828 EMBL· GenBank· DDBJ | AAH80828.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC120590 EMBL· GenBank· DDBJ | AAI20591.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137741 EMBL· GenBank· DDBJ | AAI37742.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166271 EMBL· GenBank· DDBJ | BAE38672.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168242 EMBL· GenBank· DDBJ | BAE40192.1 EMBL· GenBank· DDBJ | mRNA |