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CHD3
Introduction
Chromodomain-helicase-DNA-binding protein 3 is an enzyme that in humans is encoded by the CHD3 gene.[1][2][3]
Function
Function
This gene encodes a member of the CHD family of proteins which are characterized by the presence of chromo (chromatin organization modifier) domains and SNF2-related helicase/ATPase domains. This protein is one of the components of a histone deacetylase complex referred to as the Mi-2/NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromatin remodeling is essential for many processes including transcription. Autoantibodies against this protein are found in a subset of patients with dermatomyositis. Three alternatively spliced transcripts encoding different isoforms have been described.[3]
Mutations in CHD3 cause a neurodevelopmental syndrome with macrocephaly and impaired speech and language.[4]
References
References
- β Woodage T, Basrai MA, Baxevanis AD, Hieter P, Collins FS (Oct 1997). “Characterization of the CHD family of proteins”. Proceedings of the National Academy of Sciences of the United States of America. 94 (21): 11472β7. doi:10.1073/pnas.94.21.11472. PMCΒ 23509. PMIDΒ 9326634.
- β Ge Q, Nilasena DS, O’Brien CA, Frank MB, Targoff IN (Oct 1995). “Molecular analysis of a major antigenic region of the 240-kD protein of Mi-2 autoantigen”. The Journal of Clinical Investigation. 96 (4): 1730β7. doi:10.1172/JCI118218. PMCΒ 185809. PMIDΒ 7560064.
- β 3.0 3.1 “Entrez Gene: CHD3 chromodomain helicase DNA binding protein 3”.
- β Snijders Blok L, Rousseau J, Twist J, Ehresmann S, Takaku M, Venselaar H, et al. (November 2018). “CHD3 helicase domain mutations cause a neurodevelopmental syndrome with macrocephaly and impaired speech and language”. Nature Communications. 9 (1): 4619. doi:10.1038/s41467-018-06014-6. PMIDΒ 30397230.
- β 5.0 5.1 Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (Oct 1998). “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex”. Nature. 395 (6705): 917β21. doi:10.1038/27699. PMIDΒ 9804427.
- β Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb 2002). “Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)”. Molecular and Cellular Biology. 22 (3): 835β48. doi:10.1128/mcb.22.3.835-848.2002. PMCΒ 133546. PMIDΒ 11784859.
- β 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): 7234β9. doi:10.1074/jbc.M208992200. PMIDΒ 12493763.
- β Hakimi MA, Bochar DA, Schmiesing JA, Dong Y, Barak OG, Speicher DW, Yokomori K, Shiekhattar R (Aug 2002). “A chromatin remodelling complex that loads cohesin onto human chromosomes”. Nature. 418 (6901): 994β8. doi:10.1038/nature01024. PMIDΒ 12198550.
- β Lemos TA, Passos DO, Nery FC, Kobarg J (Jan 2003). “Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3”. FEBS Letters. 533 (1β3): 14β20. doi:10.1016/s0014-5793(02)03737-7. PMIDΒ 12505151.
- β Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, ToksΓΆz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). “A human protein-protein interaction network: a resource for annotating the proteome”. Cell. 122 (6): 957β68. doi:10.1016/j.cell.2005.08.029. PMIDΒ 16169070.
External links
External links
- Human CHD3 genome location and CHD3 gene details page in the UCSC Genome Browser.
Further reading
Further reading
- Bowen NJ, Fujita N, Kajita M, Wade PA (Mar 2004). “Mi-2/NuRD: multiple complexes for many purposes”. Biochimica et Biophysica Acta. 1677 (1β3): 52β7. doi:10.1016/j.bbaexp.2003.10.010. PMIDΒ 15020045.
- Gieser L, Swaroop A (Jul 1992). “Expressed sequence tags and chromosomal localization of cDNA clones from a subtracted retinal pigment epithelium library”. Genomics. 13 (3): 873β6. doi:10.1016/0888-7543(92)90173-P. PMIDΒ 1639417.
- 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): 1389β99. doi:10.1002/art.1780381006. PMIDΒ 7575689.
- 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): 1769β71. doi:10.1002/art.1780391029. PMIDΒ 8843877.
- Bonaldo MF, Lennon G, Soares MB (Sep 1996). “Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Research. 6 (9): 791β806. doi:10.1101/gr.6.9.791. PMIDΒ 8889548.
- Aubry F, MattΓ©i MG, Galibert F (Jun 1998). “Identification of a human 17p-located cDNA encoding a protein of the Snf2-like helicase family”. European Journal of Biochemistry / FEBS. 254 (3): 558β64. doi:10.1046/j.1432-1327.1998.2540558.x. PMIDΒ 9688266.
- Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (Oct 1998). “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex”. Nature. 395 (6705): 917β21. doi:10.1038/27699. PMIDΒ 9804427.
- Kleiderlein JJ, Nisson PE, Jessee J, Li WB, Becker KG, Derby ML, Ross CA, Margolis RL (Dec 1998). “CCG repeats in cDNAs from human brain”. Human Genetics. 103 (6): 666β73. doi:10.1007/s004390050889. PMIDΒ 9921901.
- Kim J, Sif S, Jones B, Jackson A, Koipally J, Heller E, Winandy S, Viel A, Sawyer A, Ikeda T, Kingston R, Georgopoulos K (Mar 1999). “Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes”. Immunity. 10 (3): 345β55. doi:10.1016/S1074-7613(00)80034-5. PMIDΒ 10204490.
- Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (Sep 1999). “Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation”. Nature Genetics. 23 (1): 62β6. doi:10.1038/12664. PMIDΒ 10471500.
- Cousin P, Billotte J, Chaubert P, Shaw P (Jan 2000). “Physical map of 17p13 and the genes adjacent to p53”. Genomics. 63 (1): 60β8. doi:10.1006/geno.1999.6062. PMIDΒ 10662545.
- Minty A, Dumont X, Kaghad M, Caput D (Nov 2000). “Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif”. The Journal of Biological Chemistry. 275 (46): 36316β23. doi:10.1074/jbc.M004293200. PMIDΒ 10961991.
- Schultz DC, Friedman JR, Rauscher FJ (Feb 2001). “Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD”. Genes & Development. 15 (4): 428β43. doi:10.1101/gad.869501. PMCΒ 312636. PMIDΒ 11230151.
- 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): 641β5. doi:10.1038/nature01084. PMIDΒ 12374985.
- Lemos TA, Passos DO, Nery FC, Kobarg J (Jan 2003). “Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3”. FEBS Letters. 533 (1β3): 14β20. doi:10.1016/S0014-5793(02)03737-7. PMIDΒ 12505151.
- Fujita N, Jaye DL, Kajita M, Geigerman C, Moreno CS, Wade PA (Apr 2003). “MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer”. Cell. 113 (2): 207β19. doi:10.1016/S0092-8674(03)00234-4. PMIDΒ 12705869.
- Lee BH, Yoshimatsu K, Maeda A, Ochiai K, Morimatsu M, Araki K, Ogino M, Morikawa S, Arikawa J (Dec 2003). “Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules”. Virus Research. 98 (1): 83β91. doi:10.1016/j.virusres.2003.09.001. PMIDΒ 14609633.
