G5EF53 · SWSN4_CAEEL
- ProteinSWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- Geneswsn-4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology) (By similarity).
Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity).
Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain (PubMed:34473995).
Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad (PubMed:24402584).
Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23 (PubMed:27207389).
Required during mitosis for asymmetric cell division of T blast cells (PubMed:11030341).
Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity).
Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain (PubMed:34473995).
Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad (PubMed:24402584).
Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23 (PubMed:27207389).
Required during mitosis for asymmetric cell division of T blast cells (PubMed:11030341).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | SWI/SNF complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent activity, acting on DNA | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | histone binding | |
Molecular Function | hydrolase activity | |
Biological Process | chromatin remodeling | |
Biological Process | gonad development | |
Biological Process | positive regulation of double-strand break repair | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of G1/S transition of mitotic cell cycle | |
Biological Process | regulation of mitotic metaphase/anaphase transition | |
Biological Process | regulation of nucleotide-excision repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionG5EF53
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi knockdown results in 100% embryonic lethality (PubMed:24402584).
When RNAi is restricted to mesodermal cells of the MS, C and D lineages, which include the somatic gonadal precursor cells, results in gonadogenesis defects with increased expression of the head mesodermal cell marker arg-1 in somatic gonadal precursor cells (PubMed:24402584).
When RNAi is restricted to mesodermal cells of the MS, C and D lineages, which include the somatic gonadal precursor cells, results in gonadogenesis defects with increased expression of the head mesodermal cell marker arg-1 in somatic gonadal precursor cells (PubMed:24402584).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 346 | In sy598; enhances the multivulval phenotype of let-23(sa62) mutants. | ||||
Sequence: D → N | ||||||
Mutagenesis | 673 | In os13; temperature-sensitive hypomorphic mutation with weak embryonic lethality which disrupts asymmetric division of T blast cells resulting in a phasmid socket absent phenotype in addition to egg-laying defectivness, protrusive vulva and other vulval developmental defects and which exacerbates the reduced vulval induction phenotype of let-23(sy1) mutants; when associated with F-697. | ||||
Sequence: T → I | ||||||
Mutagenesis | 697 | In os13; temperature-sensitive hypomorphic mutation with weak embryonic lethality which disrupts asymmetric division of T blast cells resulting in a phasmid socket absent phenotype in addition to egg-laying defectiveness, protrusive vulva and other vulval developmental defects and which exacerbates the reduced vulval induction phenotype of let-23(sy1) mutants; when associated with I-673. | ||||
Sequence: L → P | ||||||
Mutagenesis | 1263 | No obvious defects in viability, growth, development or brood size in vivo. Significantly enhances lethality of pbrm-1 RNAi knock-down. Enhances brood size reduction phenotype in a pbrm-1 mutant background. | ||||
Sequence: N → A | ||||||
Mutagenesis | 1264-1265 | Modest effect on worm viability. Significantly enhances lethality of pbrm-1 RNAi knock-down. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458465 | 1-1474 | SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4 | |||
Sequence: MSGRPAFEQFTAQPPQPAGEVVAQQAGDGAQGQELTISKLENAITSMEEQGLQNDHRHAKAVLLKQKLQSGLPDAVPGQENGGNQQITPAQLNQLRAQVSAYRLLARNEQVPANLIADAVMLRPKVTTLLPEPYEYPGEAENGEKLPYDLMKIFNLHQIRCNRPTTISVPSGIDPVGMLKQRENMIQNRIGLRMKLLNNLPADIPDHMKLKAEIELRALRLVNLQTQVRSEVMACLKRDTTLETALNPYAYRRTKRQSLREARVTEKLEKQQKMEQERKRRQKHTDLMQAIIQHGKEFKEYHRNNLLKMAKSRKAVMTYHQNNERERKKDEIRNEKLRMQKLMQEDEEGYRALLDEKKDQRLVYLLQQTDEYVDSLCSLVRQHQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTGKALTGDQAPKTEEIEFWLETHPEYEIVPRDQLSDDEEEEEEEAPVEPEEEKDDQYAGMDEETKAKMILEKARNEEDEYDQKTKKQMADYYATAHKIKEKVVKQHTTMGGGDPNLLLKPYQIKGLEWMVSLYNNNLNGILADEMGLGKTIQTISLVTYLMEVKQNNGPYLVIVPLSTLSNWQNEFAKWAPSVTTIIYKGTKDARRRVEGQIRKGAFNVLMTTYEYVIKEKALLGKIRWKYMIIDEGHRLKNHNCKLTLMLNGFFHAQHRLLLTGTPLQNKLPELWALLNFLLPSIFSSCGTFEQWFNAPFATTGEKVELNQEETMLIIRRLHKVLRPFLLRRLKKEVESQLPDKTEYVIKCDQSALQKVIYRHMQKGLLLDAKMSSGARSLMNTVVHLRKLCNHPFLFPNIEDSCRAYWKVNEVNGTDLMRVAGKLELLDRILPKLKATGHRILMFFQMTSMMNIFEDFLNFRRYTYLRLDGSTKPDERGDLLTQFNAPNSDLFLFMLSTRAGGLGLNLQTADTVIIFDSDWNPHQDMQAQDRAHRIGQKKEVRVLRLITANSVEEKILAAARYKLNVDEKVIQAGKFDQRSTGAERKQMLEQIIQADGEEEEEEEVPDDETVNQMVARSEEEFNIFQSMDIDRRREEANQLHRKPRLLEEHEIPDDILKLSFDYEEMERAREEGREVVDQTPNQRRRRREVDYSSDLLSDEQFMKQVEEVEDENNQAVAERKKQRKRKMAGLDENDDSMDDVVLQHKKKKTDPELAEKINEMLDVILEYKNEDGELIADVFQTLPTRKELPDYYQVISKPMDFDRINKKIETGRYTVMEELNDDMNLLVNNAQTYNEEGSEIYVSSETIGKLWKEQYDKFMNPPKPVEEPVKKKEPSTPSTSSSRPSTSGTPSVSDLQRTQQATAQQMLMLMTHMQSLPPAQAQQFQQALMTQTGGNQALMLQYMQSAMLAQRAQASTKVTPKKDEKKETSSSVKTEEAKKDDEPSTSSASAPPPKKKKESEDSEDPMEEDEEEEIIGQKKEPASSRRKSRPTRRFSNEDEEEEDDE |
Proteomic databases
Expression
Developmental stage
In L1 larvae ubiquitously expressed (at protein level) (PubMed:11030341, PubMed:27207389).
At later stages expressed in dividing vulval cells of the P lineage, hyp7 syncytia and ventral cord neurons (PubMed:11030341, PubMed:27207389).
In L4 larvae expression declines substantially after completion of vulval induction (PubMed:27207389).
At later stages expressed in dividing vulval cells of the P lineage, hyp7 syncytia and ventral cord neurons (PubMed:11030341, PubMed:27207389).
In L4 larvae expression declines substantially after completion of vulval induction (PubMed:27207389).
Gene expression databases
Interaction
Subunit
Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes (By similarity).
The canonical SWI/SNF complex contains the catalytic subunit swsn-4, core subunits swsn-1 and swsn-5, and accessory subunits swsn-3, swsn-6, swsn-9, either phf-10 or dpff-1, and either ham-3/swsn-2.1 or swsn-2.2 (By similarity).
BAF complexes additionally contain let-526, while PBAF complexes contain swsn-7 and pbrm-1 (By similarity).
swsn-9 shows similarity to both BRD7 and BRD9, mammalian BAF and PBAF components respectively, and may be a component of both BAF and PBAF (Probable). Interacts (via Bromo domain) with histone H3 (via N-terminal tail mono-acetylated on 'Lys-15'); the interaction is direct (PubMed:34473995).
The canonical SWI/SNF complex contains the catalytic subunit swsn-4, core subunits swsn-1 and swsn-5, and accessory subunits swsn-3, swsn-6, swsn-9, either phf-10 or dpff-1, and either ham-3/swsn-2.1 or swsn-2.2 (By similarity).
BAF complexes additionally contain let-526, while PBAF complexes contain swsn-7 and pbrm-1 (By similarity).
swsn-9 shows similarity to both BRD7 and BRD9, mammalian BAF and PBAF components respectively, and may be a component of both BAF and PBAF (Probable). Interacts (via Bromo domain) with histone H3 (via N-terminal tail mono-acetylated on 'Lys-15'); the interaction is direct (PubMed:34473995).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 86-121 | QLQ | ||||
Sequence: QITPAQLNQLRAQVSAYRLLARNEQVPANLIADAVM | ||||||
Region | 263-283 | Disordered | ||||
Sequence: RVTEKLEKQQKMEQERKRRQK | ||||||
Domain | 272-344 | HSA | ||||
Sequence: QKMEQERKRRQKHTDLMQAIIQHGKEFKEYHRNNLLKMAKSRKAVMTYHQNNERERKKDEIRNEKLRMQKLMQ | ||||||
Compositional bias | 383-417 | Basic and acidic residues | ||||
Sequence: HQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTG | ||||||
Region | 383-427 | Disordered | ||||
Sequence: HQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTGKALTGDQAPK | ||||||
Region | 442-475 | Disordered | ||||
Sequence: EIVPRDQLSDDEEEEEEEAPVEPEEEKDDQYAGM | ||||||
Compositional bias | 447-472 | Acidic residues | ||||
Sequence: DQLSDDEEEEEEEAPVEPEEEKDDQY | ||||||
Domain | 545-710 | Helicase ATP-binding | ||||
Sequence: VSLYNNNLNGILADEMGLGKTIQTISLVTYLMEVKQNNGPYLVIVPLSTLSNWQNEFAKWAPSVTTIIYKGTKDARRRVEGQIRKGAFNVLMTTYEYVIKEKALLGKIRWKYMIIDEGHRLKNHNCKLTLMLNGFFHAQHRLLLTGTPLQNKLPELWALLNFLLPS | ||||||
Motif | 660-663 | DEAH box | ||||
Sequence: DEGH | ||||||
Domain | 854-1005 | Helicase C-terminal | ||||
Sequence: LLDRILPKLKATGHRILMFFQMTSMMNIFEDFLNFRRYTYLRLDGSTKPDERGDLLTQFNAPNSDLFLFMLSTRAGGLGLNLQTADTVIIFDSDWNPHQDMQAQDRAHRIGQKKEVRVLRLITANSVEEKILAAARYKLNVDEKVIQAGKFD | ||||||
Region | 1098-1119 | Disordered | ||||
Sequence: REEGREVVDQTPNQRRRRREVD | ||||||
Region | 1136-1161 | Disordered | ||||
Sequence: EVEDENNQAVAERKKQRKRKMAGLDE | ||||||
Domain | 1200-1270 | Bromo | ||||
Sequence: DGELIADVFQTLPTRKELPDYYQVISKPMDFDRINKKIETGRYTVMEELNDDMNLLVNNAQTYNEEGSEIY | ||||||
Region | 1207-1270 | Interacts with histone H3 | ||||
Sequence: VFQTLPTRKELPDYYQVISKPMDFDRINKKIETGRYTVMEELNDDMNLLVNNAQTYNEEGSEIY | ||||||
Region | 1287-1326 | Disordered | ||||
Sequence: FMNPPKPVEEPVKKKEPSTPSTSSSRPSTSGTPSVSDLQR | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: MNPPKPVEEPVKKKE | ||||||
Compositional bias | 1303-1326 | Polar residues | ||||
Sequence: PSTPSTSSSRPSTSGTPSVSDLQR | ||||||
Region | 1382-1474 | Disordered | ||||
Sequence: QASTKVTPKKDEKKETSSSVKTEEAKKDDEPSTSSASAPPPKKKKESEDSEDPMEEDEEEEIIGQKKEPASSRRKSRPTRRFSNEDEEEEDDE | ||||||
Compositional bias | 1386-1412 | Basic and acidic residues | ||||
Sequence: KVTPKKDEKKETSSSVKTEEAKKDDEP |
Domain
The Bromo domain directly and selectively associates with the N-terminal tail of histone H3 mono-acetylated on 'Lys-15'.
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,474
- Mass (Da)170,612
- Last updated2011-12-14 v1
- ChecksumAEB80E0926E09D5E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 383-417 | Basic and acidic residues | ||||
Sequence: HQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTG | ||||||
Compositional bias | 447-472 | Acidic residues | ||||
Sequence: DQLSDDEEEEEEEAPVEPEEEKDDQY | ||||||
Compositional bias | 1288-1302 | Basic and acidic residues | ||||
Sequence: MNPPKPVEEPVKKKE | ||||||
Compositional bias | 1303-1326 | Polar residues | ||||
Sequence: PSTPSTSSSRPSTSGTPSVSDLQR | ||||||
Compositional bias | 1386-1412 | Basic and acidic residues | ||||
Sequence: KVTPKKDEKKETSSSVKTEEAKKDDEP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF230280 EMBL· GenBank· DDBJ | AAG16655.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284604 EMBL· GenBank· DDBJ | CAA92768.1 EMBL· GenBank· DDBJ | Genomic DNA |