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GeneQ17861672· pop 6· linked from 5 articles

Also 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
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].

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
View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Image
Protein CHD1 PDB 2b2t.png
Show 5 more facts
HomoloGene ID
68174
genomic end
98929007
genomic start
98190908
cytogenetic location
5q15-q21.1
Sources (4)

via Wikidata · CC0

~4 min read

Article

7 sections
Contents
  • 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.

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