CHD1
Sign in to saveAlso known as chromodomain helicase DNA binding protein 1, PILBOS, CHD-1
The Chromodomain-Helicase DNA-binding 1 is a protein that, in humans, is encoded by the CHD1 gene. CHD1 is a chromatin remodeling protein that is widely conserved across many eukaryotic organisms, from yeast to humans. CHD1 is named for three of its protein domains: two tandem chromodomains, its ATPase catalytic domain, and its DNA-binding domain (Figure 1).
Gene data
CHD1- Name
- chromodomain helicase DNA binding protein 1
- Type
- protein-coding
- Position
- 98,853,985–98,929,007 (−)
- Aliases
- CHD-1, PILBOS
- Ensembl
- ENSG00000153922
- RefSeq RNA
- NM_001270.4, NM_001364113.3, NM_001376194.2, NR_157078.3, NR_157079.3
- RefSeq protein
- NP_001261.2, NP_001351042.1, NP_001363123.1, XP_024310112.1, XP_024310113.1
The CHD family of proteins is characterized by the presence of chromo (chromatin organization modifier) domains and SNF2-related helicase/ATPase domains. CHD genes alter gene expression possibly by modification of chromatin structure thus altering access of the transcriptional apparatus to its chromosomal DNA template. [provided by RefSeq, Jul 2008].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Gene · Ensembl
chromodomain helicase DNA binding protein 1
- Symbol
- CHD1
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 5:98,853,985-98,929,627
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Image
- Protein CHD1 PDB 2b2t.png
Show 5 more facts
- HomoloGene ID
- 68174
- exact match
- identifiers.org/ncbigene/1105
- genomic end
- 98929007
- genomic start
- 98190908
- cytogenetic location
- 5q15-q21.1
Sources (4)
via Wikidata · CC0
~4 min read
Article
7 sectionsContents
- Structure
- Function
- Interactions
- Clinical significance
- References
- Further reading
- External links
The Chromodomain-Helicase DNA-binding 1 is a protein that, in humans, is encoded by the CHD1 gene. CHD1 is a chromatin remodeling protein that is widely conserved across many eukaryotic organisms, from yeast to humans. CHD1 is named for three of its protein domains: two tandem chromodomains, its ATPase catalytic domain, and its DNA-binding domain (Figure 1).
The CHD1 remodeler binds nucleosomes and induces local changes in nucleosome positioning through ATP hydrolysis coupled to DNA translocation of the DNA across the histone proteins. The catalytic domain of CHD1, which is highly conserved across all nucleosome remodelers, is a two-lobed structure. CHD1 relies on the DNA-binding domain, which binds DNA in a sequence non-specific manner, to help regulate spacing.