Q96I25 · SPF45_HUMAN
- ProteinSplicing factor 45
- GeneRBM17
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids401 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia.
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 | nucleoplasm | |
Cellular Component | spliceosomal complex | |
Molecular Function | RNA binding | |
Biological Process | alternative mRNA splicing, via spliceosome | |
Biological Process | mRNA cis splicing, via spliceosome |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSplicing factor 45
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96I25
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 319 | Impairs interaction with SF1; has minor effect on interaction with SF3B1 and U2AF2. | ||||
Sequence: D → A | ||||||
Mutagenesis | 319 | Abolishes interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. | ||||
Sequence: D → K | ||||||
Mutagenesis | 375 | Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. | ||||
Sequence: R → A | ||||||
Mutagenesis | 376 | Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 377 | Impairs interaction with SF1 and U2AF2 and abolishes interaction with SF3B1. Abolishes regulation of alternative splicing. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 311 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000081903 | 2-401 | UniProt | Splicing factor 45 | |||
Sequence: SLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKACFYNLDKFRVLDLAEQV | |||||||
Cross-link | 15 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 24 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 33 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 41 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 41 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 58 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 71 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 155 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 169 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 222 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 237 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 256 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 266 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 276 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 291 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 293 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binds SXL. Associates with the spliceosome. Interacts with SF3B1, SF1 and U2AF2.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 57-84 | Disordered | ||||
Sequence: LKRGGSSDDRQIVDTPPHVAAGLKDPVP | ||||||
Compositional bias | 114-170 | Basic and acidic residues | ||||
Sequence: RQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSM | ||||||
Region | 114-233 | Disordered | ||||
Sequence: RQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLAN | ||||||
Compositional bias | 183-202 | Basic and acidic residues | ||||
Sequence: EKDKELPRDFPYEEDSRPRS | ||||||
Domain | 235-283 | G-patch | ||||
Sequence: GGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDAT | ||||||
Domain | 306-385 | RRM | ||||
Sequence: VVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKAC |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length401
- Mass (Da)44,962
- Last updated2001-12-01 v1
- Checksum99FA8C5E5E998554
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 114-170 | Basic and acidic residues | ||||
Sequence: RQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSM | ||||||
Compositional bias | 183-202 | Basic and acidic residues | ||||
Sequence: EKDKELPRDFPYEEDSRPRS | ||||||
Sequence conflict | 214 | in Ref. 1; AAH09064 | ||||
Sequence: Y → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC007871 EMBL· GenBank· DDBJ | AAH07871.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009064 EMBL· GenBank· DDBJ | AAH09064.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039322 EMBL· GenBank· DDBJ | AAH39322.1 EMBL· GenBank· DDBJ | mRNA |