P32657 · CHD1_YEAST
- ProteinChromo domain-containing protein 1
- GeneCHD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1468 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. It recognizes H3K4me. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Acts in opposition to the FACT complex in regulating polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the pol I transcription termination step. Negatively regulates DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome.
Miscellaneous
Present with 1620 molecules/cell in log phase SD medium.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
10.2 nM | ATP |
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromo domain-containing protein 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32657
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 220 | No interaction with methylated histone H3 'K-4'. | ||||
Sequence: E → L or W | ||||||
Mutagenesis | 222 | Confers interaction with methylated histone H3 'K-4'. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 314 | No effect on interaction with methylated histone H3 'K-4'. | ||||
Sequence: L → Y | ||||||
Mutagenesis | 316 | Disrupts interaction with methylated histone H3 'K-4'; abrogates histone acetylation activity of SLIK. | ||||
Sequence: Y → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080237 | 1-1468 | Chromo domain-containing protein 1 | |||
Sequence: MAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDEDEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYKAILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEKHATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDLKYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRDDPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYLLSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMKALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRHTMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWSYSANFWPADVKSTKLMAMYDKITESQKK | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 72 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 987 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 989 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1144 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 1336 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1364 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1372 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Interacts with RTF1, SPT5 and with the FACT subunits POB3 and SPT16.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 21-176 | Disordered | ||||
Sequence: RSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDEDEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDF | ||||||
Compositional bias | 43-57 | Basic and acidic residues | ||||
Sequence: DNIKQSRRKRMTTIE | ||||||
Compositional bias | 58-86 | Acidic residues | ||||
Sequence: DDEDEFEDEEGEEDSGEDEDEEDFEEDDD | ||||||
Compositional bias | 116-139 | Polar residues | ||||
Sequence: EKQSTVKIPTRFSNRQNKTVNYNI | ||||||
Compositional bias | 143-157 | Acidic residues | ||||
Sequence: DDDLLESEDDYGSEE | ||||||
Domain | 195-257 | Chromo 1 | ||||
Sequence: KVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVR | ||||||
Domain | 285-350 | Chromo 2 | ||||
Sequence: HVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQY | ||||||
Domain | 388-562 | Helicase ATP-binding | ||||
Sequence: AFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPG | ||||||
Motif | 513-516 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 699-860 | Helicase C-terminal | ||||
Sequence: LLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEP | ||||||
Region | 974-1007 | Disordered | ||||
Sequence: IKNSVNGDGTAANSDSDDDSTSRSSRRRARANDM | ||||||
Compositional bias | 992-1007 | Basic and acidic residues | ||||
Sequence: DSTSRSSRRRARANDM | ||||||
Compositional bias | 1220-1239 | Polar residues | ||||
Sequence: AKKSASSSDTTPTPSKKGKG | ||||||
Region | 1220-1247 | Disordered | ||||
Sequence: AKKSASSSDTTPTPSKKGKGITGSSKKV | ||||||
Region | 1270-1378 | Disordered | ||||
Sequence: TKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMKALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDC | ||||||
Compositional bias | 1298-1313 | Polar residues | ||||
Sequence: SKSMTPEITSSEPANG | ||||||
Compositional bias | 1331-1366 | Polar residues | ||||
Sequence: NNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAH |
Domain
The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3).
The CHD1 helical C-terminal domain (CHCT) binds DNA and nucleosomes.
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,468
- Mass (Da)168,241
- Last updated1993-10-01 v1
- Checksum78BDB74C7FEC6BE5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 43-57 | Basic and acidic residues | ||||
Sequence: DNIKQSRRKRMTTIE | ||||||
Compositional bias | 58-86 | Acidic residues | ||||
Sequence: DDEDEFEDEEGEEDSGEDEDEEDFEEDDD | ||||||
Compositional bias | 116-139 | Polar residues | ||||
Sequence: EKQSTVKIPTRFSNRQNKTVNYNI | ||||||
Compositional bias | 143-157 | Acidic residues | ||||
Sequence: DDDLLESEDDYGSEE | ||||||
Compositional bias | 992-1007 | Basic and acidic residues | ||||
Sequence: DSTSRSSRRRARANDM | ||||||
Compositional bias | 1220-1239 | Polar residues | ||||
Sequence: AKKSASSSDTTPTPSKKGKG | ||||||
Compositional bias | 1298-1313 | Polar residues | ||||
Sequence: SKSMTPEITSSEPANG | ||||||
Compositional bias | 1331-1366 | Polar residues | ||||
Sequence: NNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U18917 EMBL· GenBank· DDBJ | AAB64691.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07826.1 EMBL· GenBank· DDBJ | Genomic DNA |