Q12186 · BBP_YEAST
- ProteinBranchpoint-bridging protein
- GeneMSL5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids476 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA.
Miscellaneous
Present with 4380 molecules/cell in log phase SD medium.
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 | commitment complex | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | mRNA binding | |
Molecular Function | pre-mRNA branch point binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | regulation of mRNA splicing, via spliceosome | |
Biological Process | spliceosomal complex assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBranchpoint-bridging protein
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ12186
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 60 | In MSL5-2; temperature-sensitive; growth defect; when associated with N-72 and S-155. | ||||
Sequence: R → G | ||||||
Mutagenesis | 72 | In MSL5-2; temperature-sensitive; growth defect; when associated with G-60 and S-155. | ||||
Sequence: I → N | ||||||
Mutagenesis | 155 | In MSL5-2; temperature-sensitive; growth defect; when associated with G-60 and N-72. | ||||
Sequence: P → S | ||||||
Mutagenesis | 195 | In MSL5-5; cold-sensitive; growth defect; when associated with V-258. | ||||
Sequence: V → D | ||||||
Mutagenesis | 230 | In msl-5; loss of function. | ||||
Sequence: G → S | ||||||
Mutagenesis | 258 | In MSL5-5; cold-sensitive; growth defect; when associated with D-195. | ||||
Sequence: E → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000234564 | 1-476 | Branchpoint-bridging protein | |||
Sequence: MSFRRINSRYFENRKGSSMEEKKAKVPPNVNLSLWRKNTVESDVHRFNSLPSKISGALTREQIYSYQVMFRIQEITIKLRTNDFVPPSRKNRSPSPPPVYDAQGKRTNTREQRYRKKLEDERIKLVEIALKTIPYFVPPDDYKRPTKFQDKYYIPVDQYPDVNFVGLLLGPRGRTLRKLQEDSNCKIAIRGRGSVKEGKNASDLPPGAMNFEDPLHCLIIADSEDKIQKGIKVCQNIVIKAVTSPEGQNDLKRGQLRELAELNGTLREDNRPCPICGLKDHKRYDCPNRKIPNIQGIVCKICGQTGHFSRDCNSSSQRMSRFDRNATVNNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLKFPASSRYAPSPSPPASHISRQAQNVTPTPPPGLTSSSFSSGVPGIAPPPLQSPPESEQPKFSLPPPPGMTTVQSSIAPPPGLSGPPGFSNNMGNDINKPTPPGLQGPPGL | ||||||
Modified residue | 93 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 95 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 100 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 382 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with MUD2 and PRP40. The proline-rich sequence of this protein interacts with the GYF domains of SMY2 and SYH1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12186 | MUD2 P36084 | 6 | EBI-34012, EBI-11612 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 83-110 | Disordered | ||||
Sequence: DFVPPSRKNRSPSPPPVYDAQGKRTNTR | ||||||
Domain | 153-219 | KH | ||||
Sequence: YIPVDQYPDVNFVGLLLGPRGRTLRKLQEDSNCKIAIRGRGSVKEGKNASDLPPGAMNFEDPLHCLI | ||||||
Zinc finger | 271-288 | CCHC-type 1 | ||||
Sequence: RPCPICGLKDHKRYDCPN | ||||||
Zinc finger | 297-314 | CCHC-type 2 | ||||
Sequence: IVCKICGQTGHFSRDCNS | ||||||
Compositional bias | 329-366 | Polar residues | ||||
Sequence: NNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLK | ||||||
Region | 329-476 | Disordered | ||||
Sequence: NNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLKFPASSRYAPSPSPPASHISRQAQNVTPTPPPGLTSSSFSSGVPGIAPPPLQSPPESEQPKFSLPPPPGMTTVQSSIAPPPGLSGPPGFSNNMGNDINKPTPPGLQGPPGL | ||||||
Compositional bias | 376-408 | Polar residues | ||||
Sequence: SPSPPASHISRQAQNVTPTPPPGLTSSSFSSGV | ||||||
Compositional bias | 412-432 | Pro residues | ||||
Sequence: APPPLQSPPESEQPKFSLPPP |
Sequence similarities
Belongs to the BBP/SF1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length476
- Mass (Da)53,034
- Last updated1996-11-01 v1
- ChecksumF94FF7175345C47D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 329-366 | Polar residues | ||||
Sequence: NNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLK | ||||||
Compositional bias | 376-408 | Polar residues | ||||
Sequence: SPSPPASHISRQAQNVTPTPPPGLTSSSFSSGV | ||||||
Compositional bias | 412-432 | Pro residues | ||||
Sequence: APPPLQSPPESEQPKFSLPPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X89514 EMBL· GenBank· DDBJ | CAA61695.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U53877 EMBL· GenBank· DDBJ | AAB82363.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73288 EMBL· GenBank· DDBJ | CAA97683.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09430.1 EMBL· GenBank· DDBJ | Genomic DNA |