Q15637 · SF01_HUMAN
- ProteinSplicing factor 1
- GeneSF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids639 (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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | ribosome | |
Cellular Component | spliceosomal complex | |
Cellular Component | U2AF complex | |
Molecular Function | identical protein binding | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | transcription corepressor activity | |
Molecular Function | zinc ion binding | |
Biological Process | Leydig cell differentiation | |
Biological Process | male sex determination | |
Biological Process | mRNA 3'-splice site recognition | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | negative regulation of smooth muscle cell proliferation | |
Biological Process | nuclear body organization | |
Biological Process | regulation of mRNA splicing, via spliceosome | |
Biological Process | regulation of steroid biosynthetic process | |
Biological Process | spliceosomal complex assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSplicing 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 accessionQ15637
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 15-17 | Abolishes interaction with U2AF2. | ||||
Sequence: KKR → EED | ||||||
Mutagenesis | 16-18 | Abolishes interaction with U2AF2. | ||||
Sequence: KRK → EDE | ||||||
Mutagenesis | 20 | Strongly decreases interaction with U2AF2 and spliceosome assembly. | ||||
Sequence: S → A | ||||||
Mutagenesis | 20 | Decreases interaction with U2AF2. | ||||
Sequence: S → T | ||||||
Mutagenesis | 21 | Decreases interaction with U2AF2 and spliceosome assembly. | ||||
Sequence: R → A | ||||||
Mutagenesis | 21 | No effect. | ||||
Sequence: R → K | ||||||
Mutagenesis | 22 | Abolishes interaction with U2AF2. | ||||
Sequence: W → A | ||||||
Mutagenesis | 22 | No effect. | ||||
Sequence: W → F | ||||||
Mutagenesis | 151 | Decreases RNA-binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 160 | Strongly reduces RNA-binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 184 | Abolishes RNA-binding. | ||||
Sequence: K → A | ||||||
Mutagenesis | 244 | Decreases RNA-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 247 | Decreases RNA-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 254 | Slightly decreases RNA-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 255 | Slightly decreases RNA-binding. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_017196 | 357 | ||||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 843 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, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000050129 | 2-639 | UniProt | Splicing factor 1 | |||
Sequence: ATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 14 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 20 | UniProt | Phosphoserine; by PKG | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 80 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 82 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 87 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 89 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 463 | UniProt | In isoform Q15637-6; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 467 | UniProt | In isoform Q15637-6; Omega-N-methylarginine | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-42 | Disordered | ||||
Sequence: MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPP | ||||||
Motif | 15-19 | Nuclear localization signal | ||||
Sequence: KKRKR | ||||||
Region | 65-94 | Disordered | ||||
Sequence: LRTGDLGIPPNPEDRSPSPEPIYNSEGKRL | ||||||
Domain | 141-222 | KH | ||||
Sequence: MIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQI | ||||||
Zinc finger | 277-296 | CCHC-type | ||||
Sequence: TVCTKCGGAGHIASDCKFQR | ||||||
Region | 325-639 | Disordered | ||||
Sequence: VPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN | ||||||
Compositional bias | 346-361 | Pro residues | ||||
Sequence: PAAPANNPPPPSLMST | ||||||
Compositional bias | 415-445 | Pro residues | ||||
Sequence: HNPNGPPPPWMQPPPPPMNQGPHPPGHHGPP | ||||||
Compositional bias | 472-518 | Pro residues | ||||
Sequence: PPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMA | ||||||
Compositional bias | 519-561 | Polar residues | ||||
Sequence: SSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQ | ||||||
Compositional bias | 564-610 | Pro residues | ||||
Sequence: PTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPS | ||||||
Compositional bias | 625-639 | Pro residues | ||||
Sequence: PFGMPPAPPPPPPQN |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q15637-1
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
- SynonymsSF1-HL1
- Length639
- Mass (Da)68,330
- Last updated2007-01-23 v4
- ChecksumEEBC6A02B29DAE4D
Q15637-2
- Name2
- SynonymsSF1-Bo, Bone
- Differences from canonical
- 597-639: YAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → IPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA
Q15637-3
- Name3
- SynonymsZFM1-A, ZFM1-ABCDEF
- Differences from canonical
- 587-639: PPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → RSIECLLCLLSLLTQLPLPLPKPGRQDPSPRRRWPEP
Q15637-4
- Name4
- SynonymsZFM1-B, ZFM1-ABCDF
Q15637-5
- Name5
Q15637-6
- Name6
- SynonymsZFM1-D, B6
- Differences from canonical
- 448-548: DQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQ → GKSVPGKYACGLWGLSPASRKRYDAATTYGHDA
- 555-639: PGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → QWAAPTPSLWSSSPMATTAAAASATPSAQQQYGFQYPLAMAAKIPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA
Q15637-7
- Name7
- Differences from canonical
- 1-26: Missing
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J792 | C9J792_HUMAN | SF1 | 62 | ||
F8WEV5 | F8WEV5_HUMAN | SF1 | 110 | ||
F8WEG7 | F8WEG7_HUMAN | SF1 | 51 | ||
A0A7P0T9U7 | A0A7P0T9U7_HUMAN | SF1 | 764 | ||
A0A9L9PXU0 | A0A9L9PXU0_HUMAN | SF1 | 54 | ||
A0A9L9PXR5 | A0A9L9PXR5_HUMAN | SF1 | 534 | ||
A0A9L9PXE4 | A0A9L9PXE4_HUMAN | SF1 | 763 | ||
H7BZT1 | H7BZT1_HUMAN | SF1 | 200 | ||
H7C561 | H7C561_HUMAN | SF1 | 608 | ||
H7C0N4 | H7C0N4_HUMAN | SF1 | 180 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045274 | 1-26 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008833 | 10 | in isoform 5 | |||
Sequence: L → LGKLGPPGLPPLPGPKGGFEPGPPPAPGPGAGLLAPGPPPPPPVGSMGALTAAFPFAALPPPPPPPPPPPPQQPPPPPPPPSPGASYPPPQPPPPPPLYQRVSPPQPPPPQPPRKDQQPGPAGGGG | ||||||
Sequence conflict | 269 | in Ref. 3; BAA05116/BAA05117 | ||||
Sequence: E → G | ||||||
Compositional bias | 346-361 | Pro residues | ||||
Sequence: PAAPANNPPPPSLMST | ||||||
Sequence conflict | 348 | in Ref. 2; AAB03514/AAB04033 | ||||
Sequence: A → R | ||||||
Sequence conflict | 377 | in Ref. 3; BAA05116/BAA05117 | ||||
Sequence: R → W | ||||||
Compositional bias | 415-445 | Pro residues | ||||
Sequence: HNPNGPPPPWMQPPPPPMNQGPHPPGHHGPP | ||||||
Alternative sequence | VSP_008834 | 448-548 | in isoform 6 | |||
Sequence: DQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQ → GKSVPGKYACGLWGLSPASRKRYDAATTYGHDA | ||||||
Compositional bias | 472-518 | Pro residues | ||||
Sequence: PPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMA | ||||||
Compositional bias | 519-561 | Polar residues | ||||
Sequence: SSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQ | ||||||
Alternative sequence | VSP_008835 | 528-548 | in isoform 4 and isoform 5 | |||
Sequence: NTTTTTTSAGTGSIPPWQQQQ → RSLPAAAMARAMRVRTFRAHW | ||||||
Alternative sequence | VSP_008836 | 549-639 | in isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008837 | 555-639 | in isoform 6 | |||
Sequence: PGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → QWAAPTPSLWSSSPMATTAAAASATPSAQQQYGFQYPLAMAAKIPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA | ||||||
Compositional bias | 564-610 | Pro residues | ||||
Sequence: PTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPS | ||||||
Sequence conflict | 570 | in Ref. 4; BAH11587 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_008838 | 587-639 | in isoform 3 | |||
Sequence: PPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → RSIECLLCLLSLLTQLPLPLPKPGRQDPSPRRRWPEP | ||||||
Sequence conflict | 591 | in Ref. 2; AAB04033 | ||||
Sequence: G → V | ||||||
Alternative sequence | VSP_008839 | 597-639 | in isoform 2 | |||
Sequence: YAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN → IPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA | ||||||
Sequence conflict | 623 | in Ref. 2; AAB04033 | ||||
Sequence: M → I | ||||||
Compositional bias | 625-639 | Pro residues | ||||
Sequence: PFGMPPAPPPPPPQN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y08765 EMBL· GenBank· DDBJ | CAA70018.1 EMBL· GenBank· DDBJ | mRNA | ||
Y08766 EMBL· GenBank· DDBJ | CAA70019.1 EMBL· GenBank· DDBJ | mRNA | ||
L49345 EMBL· GenBank· DDBJ | AAB03514.1 EMBL· GenBank· DDBJ | mRNA | ||
L49380 EMBL· GenBank· DDBJ | AAB04033.1 EMBL· GenBank· DDBJ | mRNA | ||
D26120 EMBL· GenBank· DDBJ | BAA05116.1 EMBL· GenBank· DDBJ | mRNA | ||
D26120 EMBL· GenBank· DDBJ | BAA05117.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293753 EMBL· GenBank· DDBJ | BAH11587.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001462 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000773 EMBL· GenBank· DDBJ | AAH00773.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC008080 EMBL· GenBank· DDBJ | AAH08080.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008724 EMBL· GenBank· DDBJ | AAH08724.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011657 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC020217 EMBL· GenBank· DDBJ | AAH20217.1 EMBL· GenBank· DDBJ | mRNA | ||
BC038446 EMBL· GenBank· DDBJ | AAH38446.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ000051 EMBL· GenBank· DDBJ | CAA03883.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ000052 EMBL· GenBank· DDBJ | CAA03883.1 EMBL· GenBank· DDBJ | Genomic DNA |