3hm5

SANT domain of human DNA methyltransferase 1 associated protein 1SANT domain of human DNA methyltransferase 1 associated protein 1

Structural highlights

3hm5 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DMAP1_HUMAN Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Xin H, Yoon HG, Singh PB, Wong J, Qin J. Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells. J Biol Chem. 2004 Mar 5;279(10):9539-46. Epub 2003 Dec 9. PMID:14665632 doi:http://dx.doi.org/10.1074/jbc.M311587200
↑ Muromoto R, Sugiyama K, Takachi A, Imoto S, Sato N, Yamamoto T, Oritani K, Shimoda K, Matsuda T. Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1. J Immunol. 2004 Mar 1;172(5):2985-93. PMID:14978102
↑ Doyon Y, Selleck W, Lane WS, Tan S, Cote J. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. PMID:14966270
↑ Delgermaa L, Hayashi N, Dorjsuren D, Nomura T, Thuy le TT, Murakami S. Subcellular localization of RPB5-mediating protein and its putative functional partner. Mol Cell Biol. 2004 Oct;24(19):8556-66. PMID:15367675 doi:http://dx.doi.org/10.1128/MCB.24.19.8556-8566.2004

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OCA

[1] Xin H, Yoon HG, Singh PB, Wong J, Qin J. Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells. J Biol Chem. 2004 Mar 5;279(10):9539-46. Epub 2003 Dec 9. PMID:14665632 doi:http://dx.doi.org/10.1074/jbc.M311587200

[2] Muromoto R, Sugiyama K, Takachi A, Imoto S, Sato N, Yamamoto T, Oritani K, Shimoda K, Matsuda T. Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1. J Immunol. 2004 Mar 1;172(5):2985-93. PMID:14978102

[3] Doyon Y, Selleck W, Lane WS, Tan S, Cote J. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. PMID:14966270

[4] Delgermaa L, Hayashi N, Dorjsuren D, Nomura T, Thuy le TT, Murakami S. Subcellular localization of RPB5-mediating protein and its putative functional partner. Mol Cell Biol. 2004 Oct;24(19):8556-66. PMID:15367675 doi:http://dx.doi.org/10.1128/MCB.24.19.8556-8566.2004

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