CHD1

From Wikipedia, the free encyclopedia


Chromodomain helicase DNA binding protein 1
PDB rendering based on 2b2t.
Available structures: 2b2t, 2b2u, 2b2v, 2b2w, 2b2y
Identifiers
Symbol(s) CHD1; DKFZp686E2337
External IDs OMIM: 602118 MGI88393 HomoloGene86052
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1105 12648
Ensembl ENSG00000153922 ENSMUSG00000023852
Uniprot O14646 Q14BJ0
Refseq NM_001270 (mRNA)
NP_001261 (protein)
NM_007690 (mRNA)
NP_031716 (protein)
Location Chr 5: 98.22 - 98.29 Mb Chr 17: 15.41 - 15.48 Mb
Pubmed search [1] [2]

Chromodomain helicase DNA binding protein 1, also known as CHD1, is a human gene.[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.[1]

[edit] References

[edit] Further reading

  • Stokes DG, Perry RP (1995). "DNA-binding and chromatin localization properties of CHD1.". Mol. Cell. Biol. 15 (5): 2745–53. PMID 7739555. 
  • Delmas V, Stokes DG, Perry RP (1993). "A mammalian DNA-binding protein that contains a chromodomain and an SNF2/SWI2-like helicase domain.". Proc. Natl. Acad. Sci. U.S.A. 90 (6): 2414–8. PMID 8460153. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548. 
  • Woodage T, Basrai MA, Baxevanis AD, et al. (1997). "Characterization of the CHD family of proteins.". Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11472–7. PMID 9326634. 
  • Kelley DE, Stokes DG, Perry RP (1999). "CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin.". Chromosoma 108 (1): 10–25. PMID 10199952. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Salomon AR, Ficarro SB, Brill LM, et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. doi:10.1073/pnas.2436191100. PMID 12522270. 
  • Tai HH, Geisterfer M, Bell JC, et al. (2003). "CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins.". Biochem. Biophys. Res. Commun. 308 (1): 170–6. PMID 12890497. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
  • Sims RJ, Chen CF, Santos-Rosa H, et al. (2006). "Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains.". J. Biol. Chem. 280 (51): 41789–92. doi:10.1074/jbc.C500395200. PMID 16263726. 
  • Flanagan JF, Mi LZ, Chruszcz M, et al. (2006). "Double chromodomains cooperate to recognize the methylated histone H3 tail.". Nature 438 (7071): 1181–5. doi:10.1038/nature04290. PMID 16372014. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 
  • Okuda M, Horikoshi M, Nishimura Y (2007). "Structural polymorphism of chromodomains in Chd1.". J. Mol. Biol. 365 (4): 1047–62. doi:10.1016/j.jmb.2006.10.039. PMID 17098252. 
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.