Q07955 · SRSF1_HUMAN
- ProteinSerine/arginine-rich splicing factor 1
- GeneSRSF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | catalytic step 2 spliceosome | |
Cellular Component | cytoplasm | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA topoisomerase binding | |
Molecular Function | mRNA binding | |
Molecular Function | protein kinase B binding | |
Molecular Function | RNA binding | |
Biological Process | alternative mRNA splicing, via spliceosome | |
Biological Process | liver regeneration | |
Biological Process | mRNA 5'-splice site recognition | |
Biological Process | mRNA processing | |
Biological Process | mRNA splice site recognition | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | mRNA transport | |
Biological Process | oligodendrocyte differentiation | |
Biological Process | positive regulation of RNA splicing | |
Biological Process | regulation of RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/arginine-rich splicing factor 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ07955
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with dysmorphic facies and behavioral abnormalities (NEDFBA)
- Note
- DescriptionAn autosomal dominant disorder characterized by developmental delay, intellectual disability, speech delay, hypotonia, behavioral abnormalities, and non-specific dysmorphic facial features. Some patients have variable skeletal and cardiac anomalies.
- See alsoMIM:620489
Natural variants in NEDFBA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088937 | 24 | P>L | in NEDFBA; likely pathogenic | |
VAR_088938 | 28-248 | missing | in NEDFBA; likely pathogenic | |
VAR_088939 | 33-248 | missing | in NEDFBA; likely pathogenic | |
VAR_088940 | 40 | G>V | in NEDFBA; likely pathogenic | |
VAR_088941 | 44 | D>N | in NEDFBA; uncertain significance | |
VAR_088942 | 70 | A>T | in NEDFBA; likely pathogenic | |
VAR_088943 | 77-248 | missing | in NEDFBA; likely pathogenic | |
VAR_088944 | 84 | L>R | in NEDFBA; likely pathogenic | |
VAR_088945 | 160 | V>M | in NEDFBA; likely pathogenic | |
VAR_088946 | 183 | H>R | in NEDFBA; uncertain significance |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_088937 | 24 | in NEDFBA; likely pathogenic | |||
Sequence: P → L | ||||||
Natural variant | VAR_088938 | 28-248 | in NEDFBA; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088939 | 33-248 | in NEDFBA; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088940 | 40 | in NEDFBA; likely pathogenic | |||
Sequence: G → V | ||||||
Natural variant | VAR_088941 | 44 | in NEDFBA; uncertain significance | |||
Sequence: D → N | ||||||
Mutagenesis | 58-59 | In FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding. | ||||
Sequence: FV → SR | ||||||
Natural variant | VAR_088942 | 70 | in NEDFBA; likely pathogenic | |||
Sequence: A → T | ||||||
Natural variant | VAR_088943 | 77-248 | in NEDFBA; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088944 | 84 | in NEDFBA; likely pathogenic | |||
Sequence: L → R | ||||||
Natural variant | VAR_035488 | 89 | in a breast cancer sample; somatic mutation | |||
Sequence: P → S | ||||||
Mutagenesis | 93 | Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. | ||||
Sequence: R → A | ||||||
Mutagenesis | 97 | Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. | ||||
Sequence: R → A | ||||||
Mutagenesis | 109 | Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_088945 | 160 | in NEDFBA; likely pathogenic | |||
Sequence: V → M | ||||||
Mutagenesis | 162 | In AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. | ||||
Sequence: F → A | ||||||
Mutagenesis | 162 | Reduced nucleocytoplasmic shuttling; when associated with D-190. | ||||
Sequence: F → D | ||||||
Mutagenesis | 162-163 | In FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. | ||||
Sequence: FV → SR | ||||||
Mutagenesis | 180 | Reduced nucleocytoplasmic shuttling; when associated with D-162. | ||||
Sequence: F → D | ||||||
Mutagenesis | 182-199 | In MR-E; loss of ability to activate splicing. | ||||
Sequence: Missing | ||||||
Mutagenesis | 182-248 | In MR-B; strongly inhibits splicing. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_088946 | 183 | in NEDFBA; uncertain significance | |||
Sequence: H → R | ||||||
Mutagenesis | 192-199 | In MR-D; loss of ability to activate splicing. | ||||
Sequence: Missing | ||||||
Mutagenesis | 192-248 | In MR-A; loss of ability to activate splicing. | ||||
Sequence: Missing | ||||||
Mutagenesis | 199-224 | In RS-A; loss of ability to activate splicing but retains splice site switching. | ||||
Sequence: Missing | ||||||
Mutagenesis | 215-248 | In RS-C; loss of ability to activate splicing but retains splice site switching. | ||||
Sequence: Missing | ||||||
Mutagenesis | 226-248 | In RS-B; retains both splice activation and splice site switching activity. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 137 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000081911 | 2-248 | UniProt | Serine/arginine-rich splicing factor 1 | |||
Sequence: SGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 30 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 38 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 38 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 93 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 93 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 97 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 97 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 109 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 109 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 111 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 133 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 179 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 199 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 201 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 205 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 207 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 209 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 231 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 238 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of a ribonucleoprotein complex containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF (PubMed:24644279).
In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1. Interacts with CCNL1, CCNL2 and CDK11B (PubMed:18216018).
Interacts with RRP1B (PubMed:23604122).
Interacts (when phosphorylated in its RS domain) with TNPO3; promoting nuclear import (PubMed:24449914).
Interacts with ILDR1 (via C-terminus) and ILDR2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q07955 | CIR1 Q86X95 | 3 | EBI-398920, EBI-627102 | |
BINARY | Q07955 | CLK1 P49759-3 | 3 | EBI-398920, EBI-11981867 | |
BINARY | Q07955 | NFYA P23511 | 5 | EBI-398920, EBI-389739 | |
BINARY | Q07955 | NXF1 Q9UBU9 | 5 | EBI-398920, EBI-398874 | |
BINARY | Q07955 | RRP1B Q14684 | 6 | EBI-398920, EBI-372051 | |
BINARY | Q07955 | SNRNP70 P08621 | 5 | EBI-398920, EBI-1049228 | |
BINARY | Q07955 | SRPK1 Q96SB4 | 3 | EBI-398920, EBI-539478 | |
XENO | Q07955 | Srpk1 O70551 | 5 | EBI-398920, EBI-593343 | |
BINARY | Q07955 | SRPK2 P78362 | 3 | EBI-398920, EBI-593303 | |
XENO | Q07955 | Srpk2 O54781 | 3 | EBI-398920, EBI-593325 | |
BINARY | Q07955 | TRA2B P62995 | 3 | EBI-398920, EBI-725485 | |
BINARY | Q07955 | TRAF5 O00463 | 2 | EBI-398920, EBI-523498 | |
BINARY | Q07955 | U2AF1 Q01081 | 4 | EBI-398920, EBI-632461 | |
BINARY | Q07955 | U2AF2 P26368 | 3 | EBI-398920, EBI-742339 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-91 | RRM 1 | ||||
Sequence: CRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRS | ||||||
Region | 88-134 | Disordered | ||||
Sequence: FPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSW | ||||||
Domain | 121-195 | RRM 2 | ||||
Sequence: NRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVD | ||||||
Region | 191-248 | Disordered | ||||
Sequence: RVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT | ||||||
Region | 198-247 | Interaction with SAFB1 | ||||
Sequence: RSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSR | ||||||
Compositional bias | 205-225 | Basic residues | ||||
Sequence: SRSRSRSRSRSRSRSNSRSRS | ||||||
Compositional bias | 234-248 | Basic residues | ||||
Sequence: SPRYSPRHSRSRSRT |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q07955-1
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.
- NameASF-1
- Length248
- Mass (Da)27,745
- Last updated2007-01-23 v2
- ChecksumC28A0B2F112EA713
Q07955-2
- NameASF-2
- Differences from canonical
- 185-248: GETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT → FCLSNREKLPTSGLKLMGPEVQVMEDLDLEAVVVAEAVAEATAGVAVTPQGEAEDHHAILPVIADLALVHKMIGDTFCRTHVVYSFPLFSTIFSFFNSNCFVQNGLKC
Q07955-3
- NameASF-3
- NoteMay be due to intron retention.
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_005857 | 185-201 | in isoform ASF-3 | |||
Sequence: GETAYIRVKVDGPRSPS → VGYTRILFFDQNWIQWS | ||||||
Alternative sequence | VSP_005856 | 185-248 | in isoform ASF-2 | |||
Sequence: GETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT → FCLSNREKLPTSGLKLMGPEVQVMEDLDLEAVVVAEAVAEATAGVAVTPQGEAEDHHAILPVIADLALVHKMIGDTFCRTHVVYSFPLFSTIFSFFNSNCFVQNGLKC | ||||||
Alternative sequence | VSP_005858 | 202-248 | in isoform ASF-3 | |||
Sequence: Missing | ||||||
Compositional bias | 205-225 | Basic residues | ||||
Sequence: SRSRSRSRSRSRSRSNSRSRS | ||||||
Compositional bias | 234-248 | Basic residues | ||||
Sequence: SPRYSPRHSRSRSRT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M72709 EMBL· GenBank· DDBJ | AAA35565.1 EMBL· GenBank· DDBJ | mRNA | ||
M72709 EMBL· GenBank· DDBJ | AAA35564.1 EMBL· GenBank· DDBJ | mRNA | ||
M69040 EMBL· GenBank· DDBJ | AAA03476.1 EMBL· GenBank· DDBJ | mRNA | ||
AB062124 EMBL· GenBank· DDBJ | BAB93456.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312781 EMBL· GenBank· DDBJ | BAG35644.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94486.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010264 EMBL· GenBank· DDBJ | AAH10264.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033785 EMBL· GenBank· DDBJ | AAH33785.1 EMBL· GenBank· DDBJ | mRNA |