CHD4

From Wikipedia, the free encyclopedia
Jump to: navigation, search
CHD4
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CHD4, CHD-4, Mi-2b, Mi2-BETA, chromodomain helicase DNA binding protein 4, SIHIWES
External IDs MGI: 1344380 HomoloGene: 68175 GeneCards: CHD4
RNA expression pattern
PBB GE CHD4 201182 s at fs.png

PBB GE CHD4 201183 s at fs.png

PBB GE CHD4 201184 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001273
NM_001297553

NM_145979
NM_001346610

RefSeq (protein)

NP_001264
NP_001284482

NP_666091.1
NP_001333539
NP_666091

Location (UCSC) Chr 12: 6.57 – 6.61 Mb Chr 6: 125.1 – 125.13 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Chromodomain-helicase-DNA-binding protein 4 is an enzyme that in humans is encoded by the CHD4 gene.[3][4][5]

Function[edit]

The product of this gene belongs to the SNF2/RAD54 helicase family. It represents the main component of the nucleosome remodeling and deacetylase complex and plays an important role in epigenetic transcriptional repression. Patients with dermatomyositis develop antibodies against this protein.[5]

Interactions[edit]

CHD4 has been shown to interact with HDAC1,[6][7][8] Histone deacetylase 2,[8][9][10] MTA2,[6] SATB1[11] and Ataxia telangiectasia and Rad3 related.[10]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Seelig HP, Moosbrugger I, Ehrfeld H, Fink T, Renz M, Genth E (Oct 1995). "The major dermatomyositis-specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation". Arthritis and Rheumatism. 38 (10): 1389–99. doi:10.1002/art.1780381006. PMID 7575689. 
  4. ^ Seelig HP, Renz M, Targoff IN, Ge Q, Frank MB (Oct 1996). "Two forms of the major antigenic protein of the dermatomyositis-specific Mi-2 autoantigen". Arthritis and Rheumatism. 39 (10): 1769–71. doi:10.1002/art.1780391029. PMID 8843877. 
  5. ^ a b "Entrez Gene: CHD4 chromodomain helicase DNA binding protein 4". 
  6. ^ a b Yao YL, Yang WM (Oct 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". The Journal of Biological Chemistry. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132. 
  7. ^ Grozinger CM, Hassig CA, Schreiber SL (Apr 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proceedings of the National Academy of Sciences of the United States of America. 96 (9): 4868–73. doi:10.1073/pnas.96.9.4868. PMC 21783Freely accessible. PMID 10220385. 
  8. ^ a b Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (Oct 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. doi:10.1038/27699. PMID 9804427. 
  9. ^ Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R (Feb 2003). "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". The Journal of Biological Chemistry. 278 (9): 7234–9. doi:10.1074/jbc.M208992200. PMID 12493763. 
  10. ^ a b Schmidt DR, Schreiber SL (Nov 1999). "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4". Biochemistry. 38 (44): 14711–7. doi:10.1021/bi991614n. PMID 10545197. 
  11. ^ Yasui D, Miyano M, Cai S, Varga-Weisz P, Kohwi-Shigematsu T (Oct 2002). "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature. 419 (6907): 641–5. doi:10.1038/nature01084. PMID 12374985. 

External links[edit]

Further reading[edit]