P32657 · CHD1_YEAST

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 nMATP

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site401-408ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular Componentmitochondrion
Cellular Componentnucleolar chromatin
Cellular Componentnucleus
Cellular ComponentSAGA complex
Cellular Componentsite of double-strand break
Cellular ComponentSLIK (SAGA-like) complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent activity, acting on DNA
Molecular FunctionATP-dependent chromatin remodeler activity
Molecular Functionchromatin binding
Molecular Functionchromatin DNA binding
Molecular FunctionDNA binding
Molecular Functionhelicase activity
Molecular Functionhistone binding
Molecular Functionmethylated histone binding
Molecular FunctionrDNA binding
Molecular Functiontranscription cis-regulatory region binding
Biological Processchromatin remodeling
Biological ProcessDNA double-strand break processing
Biological Processdouble-strand break repair via homologous recombination
Biological Processnegative regulation of DNA-templated DNA replication
Biological Processnucleosome organization
Biological Processregulation of chromatin organization
Biological Processregulation of transcription by RNA polymerase II
Biological Processregulation of transcriptional start site selection at RNA polymerase II promoter
Biological Processsister chromatid cohesion
Biological Processtermination of RNA polymerase I transcription
Biological Processtermination of RNA polymerase II transcription
Biological Processtranscription elongation by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chromo domain-containing protein 1
  • EC number
  • Alternative names
    • ATP-dependent helicase CHD1

Gene names

    • Name
      CHD1
    • ORF names
      SYGP-ORF4
    • Ordered locus names
      YER164W

Organism names

Accessions

  • Primary accession
    P32657
  • Secondary accessions
    • D3DM72

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis220No interaction with methylated histone H3 'K-4'.
Mutagenesis222Confers interaction with methylated histone H3 'K-4'.
Mutagenesis314No effect on interaction with methylated histone H3 'K-4'.
Mutagenesis316Disrupts interaction with methylated histone H3 'K-4'; abrogates histone acetylation activity of SLIK.

Variants

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The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00000802371-1468Chromo domain-containing protein 1
Modified residue36Phosphoserine
Modified residue72Phosphoserine
Modified residue987Phosphoserine
Modified residue989Phosphoserine
Cross-link1144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue1336Phosphoserine
Modified residue1364Phosphoserine
Modified residue1372Phosphoserine

Keywords

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

Family & Domains

Features

Showing features for region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region21-176Disordered
Compositional bias43-57Basic and acidic residues
Compositional bias58-86Acidic residues
Compositional bias116-139Polar residues
Compositional bias143-157Acidic residues
Domain195-257Chromo 1
Domain285-350Chromo 2
Domain388-562Helicase ATP-binding
Motif513-516DEAH box
Domain699-860Helicase C-terminal
Region974-1007Disordered
Compositional bias992-1007Basic and acidic residues
Compositional bias1220-1239Polar residues
Region1220-1247Disordered
Region1270-1378Disordered
Compositional bias1298-1313Polar residues
Compositional bias1331-1366Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,468
  • Mass (Da)
    168,241
  • Last updated
    1993-10-01 v1
  • Checksum
    78BDB74C7FEC6BE5
MAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDEDEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYKAILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEKHATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDLKYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRDDPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYLLSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMKALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRHTMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWSYSANFWPADVKSTKLMAMYDKITESQKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias43-57Basic and acidic residues
Compositional bias58-86Acidic residues
Compositional bias116-139Polar residues
Compositional bias143-157Acidic residues
Compositional bias992-1007Basic and acidic residues
Compositional bias1220-1239Polar residues
Compositional bias1298-1313Polar residues
Compositional bias1331-1366Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U18917
EMBL· GenBank· DDBJ
AAB64691.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006939
EMBL· GenBank· DDBJ
DAA07826.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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