P32591 · SWI3_YEAST
- ProteinSWI/SNF complex subunit SWI3
- GeneSWI3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids825 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Miscellaneous
Present with 3150 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 | chromatin | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | SWI/SNF complex | |
Molecular Function | DNA binding | |
Molecular Function | histone binding | |
Biological Process | carbon catabolite activation of transcription from RNA polymerase II promoter | |
Biological Process | chromatin remodeling | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of mating type switching | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSWI/SNF complex subunit SWI3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32591
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 374 | Loss of DNA-binding. | ||||
Sequence: D → A | ||||||
Mutagenesis | 383 | Loss of DNA-binding; when associated with D-387. | ||||
Sequence: K → D | ||||||
Mutagenesis | 387 | Loss of DNA-binding; when associated with D-383. | ||||
Sequence: K → D | ||||||
Mutagenesis | 392 | Loss of DNA-binding. | ||||
Sequence: N → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 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_0000197123 | 1-825 | SWI/SNF complex subunit SWI3 | |||
Sequence: MENTLGEGSTVNASVDVDQHGNDNNSDSNANAAVAGVANTDTAGEESQQQDESLKDEATVPNTRDAESEAITVTAKQQPTMQANKLDSQETPSTEESRAQNVFGQDNEDSDNLFGETESSVSNNEANTPSIPTNPVDNENNKPAIKEDSTIQDSNGDVKNMEDVKIQKEEEPENNTVIEGVKEESQPDENTKEMDEVEEDDEDDDQPMISPDNSIFGDTKSESKQLGNTSSVANTPSEIPDAHKAEQEDIIEKTESVDKKVDSGEERNEQEREIMNDHSKSANPKKTTITRVEPETFEIPQAHEIVIPSYSKWFNLEKIHSIEVQSLPEFFTNRIPSKTPEVYMRYRNFMVNSYRLNPNEYFSVTTARRNVSGDAAALFRLHKFLTKWGLINYQVDSKLLPKNIEPPLTSQYSTRHDAPRGLFPFESYKPSVQLPDMAKLKKMMNTSDSESTLYKYLKESKRKYDEITHPPSTTDDENGDKNDNGGKMNNEVSTSTSMTGDANLLEEGETSRPLKKVKILEQIDENWSKEDLQKLLKGIQEFGADWYKVAKNVGNKSPEQCILRFLQLPIEDKFLYGDGNGKGDNDNGLGPLKYAPHLPFSKSENPVLSTIAFLVGLVNPKTVQSMTQRAIQSAESIKSQKEEISDQKPIEHIKEGSEIAISSLGYRSHIFATNEERQMNFLTNELIRLQMEKLDAKLNHLKKLEKFMELERKTLERQQENLLIQRLNFNQNSSKIVNVLSKCLNLISDSNINNSSVAEKEEIRSQIDHFKSMLSKPETLSIGKNPFNKPNIETGENHNGQSISNENDVKPISIEAPQFYRYWSA | ||||||
Modified residue | 88 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 185 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 235 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 657 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with RTT102, SWP82 and the N-terminus of SNF2. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32591 | RTT102 P53330 | 4 | EBI-18622, EBI-23637 | |
BINARY | P32591 | SNF2 P22082 | 10 | EBI-18622, EBI-17526 | |
BINARY | P32591 | SNF6 P18888 | 8 | EBI-18622, EBI-17550 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-47 | Polar residues | ||||
Sequence: MENTLGEGSTVNASVDVDQHGNDNNSDSNANAAVAGVANTDTAGEES | ||||||
Region | 1-285 | Disordered | ||||
Sequence: MENTLGEGSTVNASVDVDQHGNDNNSDSNANAAVAGVANTDTAGEESQQQDESLKDEATVPNTRDAESEAITVTAKQQPTMQANKLDSQETPSTEESRAQNVFGQDNEDSDNLFGETESSVSNNEANTPSIPTNPVDNENNKPAIKEDSTIQDSNGDVKNMEDVKIQKEEEPENNTVIEGVKEESQPDENTKEMDEVEEDDEDDDQPMISPDNSIFGDTKSESKQLGNTSSVANTPSEIPDAHKAEQEDIIEKTESVDKKVDSGEERNEQEREIMNDHSKSANPK | ||||||
Compositional bias | 48-63 | Basic and acidic residues | ||||
Sequence: QQQDESLKDEATVPNT | ||||||
Compositional bias | 65-140 | Polar residues | ||||
Sequence: DAESEAITVTAKQQPTMQANKLDSQETPSTEESRAQNVFGQDNEDSDNLFGETESSVSNNEANTPSIPTNPVDNEN | ||||||
Compositional bias | 158-189 | Basic and acidic residues | ||||
Sequence: VKNMEDVKIQKEEEPENNTVIEGVKEESQPDE | ||||||
Compositional bias | 190-208 | Acidic residues | ||||
Sequence: NTKEMDEVEEDDEDDDQPM | ||||||
Compositional bias | 212-237 | Polar residues | ||||
Sequence: DNSIFGDTKSESKQLGNTSSVANTPS | ||||||
Compositional bias | 241-280 | Basic and acidic residues | ||||
Sequence: DAHKAEQEDIIEKTESVDKKVDSGEERNEQEREIMNDHSK | ||||||
Domain | 305-402 | SWIRM | ||||
Sequence: IVIPSYSKWFNLEKIHSIEVQSLPEFFTNRIPSKTPEVYMRYRNFMVNSYRLNPNEYFSVTTARRNVSGDAAALFRLHKFLTKWGLINYQVDSKLLPK | ||||||
Compositional bias | 464-484 | Basic and acidic residues | ||||
Sequence: YDEITHPPSTTDDENGDKNDN | ||||||
Region | 464-509 | Disordered | ||||
Sequence: YDEITHPPSTTDDENGDKNDNGGKMNNEVSTSTSMTGDANLLEEGE | ||||||
Compositional bias | 485-504 | Polar residues | ||||
Sequence: GGKMNNEVSTSTSMTGDANL | ||||||
Domain | 522-573 | SANT | ||||
Sequence: QIDENWSKEDLQKLLKGIQEFGADWYKVAKNVGNKSPEQCILRFLQLPIEDK | ||||||
Region | 694-722 | Leucine-zipper | ||||
Sequence: LDAKLNHLKKLEKFMELERKTLERQQENL |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length825
- Mass (Da)92,926
- Last updated1993-10-01 v1
- ChecksumDBA2E2022F15F9A6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-47 | Polar residues | ||||
Sequence: MENTLGEGSTVNASVDVDQHGNDNNSDSNANAAVAGVANTDTAGEES | ||||||
Compositional bias | 48-63 | Basic and acidic residues | ||||
Sequence: QQQDESLKDEATVPNT | ||||||
Compositional bias | 65-140 | Polar residues | ||||
Sequence: DAESEAITVTAKQQPTMQANKLDSQETPSTEESRAQNVFGQDNEDSDNLFGETESSVSNNEANTPSIPTNPVDNEN | ||||||
Compositional bias | 158-189 | Basic and acidic residues | ||||
Sequence: VKNMEDVKIQKEEEPENNTVIEGVKEESQPDE | ||||||
Compositional bias | 190-208 | Acidic residues | ||||
Sequence: NTKEMDEVEEDDEDDDQPM | ||||||
Compositional bias | 212-237 | Polar residues | ||||
Sequence: DNSIFGDTKSESKQLGNTSSVANTPS | ||||||
Compositional bias | 241-280 | Basic and acidic residues | ||||
Sequence: DAHKAEQEDIIEKTESVDKKVDSGEERNEQEREIMNDHSK | ||||||
Compositional bias | 464-484 | Basic and acidic residues | ||||
Sequence: YDEITHPPSTTDDENGDKNDN | ||||||
Compositional bias | 485-504 | Polar residues | ||||
Sequence: GGKMNNEVSTSTSMTGDANL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M84390 EMBL· GenBank· DDBJ | AAA35136.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X56792 EMBL· GenBank· DDBJ | CAA40112.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49451 EMBL· GenBank· DDBJ | CAA89470.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006943 EMBL· GenBank· DDBJ | DAA08629.1 EMBL· GenBank· DDBJ | Genomic DNA |