https://gydb.org/index.php?action=history&feed=atom&title=HATd 2026-06-13T23:53:36Z Revision history for this page on the wiki MediaWiki 1.35.0 https://gydb.org/index.php?title=HATd&diff=1301&oldid=prev 2011-11-07T10:36:25Z

<p></p> <p><b>New page</b></p><div>''hATd'' dimerization domain is present in ZNF452/SCAND3 variants of [[SCAN/KRAB|SCAN/KRAB]] cellular integrases.<br /> <br /> [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=147706 ''hATd''] dimerization domain (pfam05699 in Conserved Domain Database) has been described in ''Activator'' (''Ac'') and ''Hermes'' TRs ([[literature:100840|Essers ''et al''. 2000]]; [[literature: |Michel ''et al''. 2003]]) belonging to ''hAT'' family of transposable elements. It was reported to be the most highly conserved region of ''hAT'' TRs and involved in the required TR oligomerization to assemble the transpososome (synaptic complex). Nevertheless, [[literature:30830|Hickman ''et al''. 2005]] argue that ''hATd'' domain is a misnomer (not involved in dimerization ) and according to ''Hermes'' structure features ''hATd'' conserved residues do not form an independent folding unit but have an important role in joining into a functional whole residues separated in sequence. <br /> <br /> The ''hATd'' domain has also been described in DREF factors (DNA replication related element binding factors) of ''Drosophila'' and humans ([[literature:100841|Hirose ''et al''. 1996]]; [[literature:|Esposito ''et al''. 1999]]; [[literature:100842|Ohshima ''et al''. 2003]]). DREF factors are transcriptional regulators and in humans the ''hATd'' domain has been reported to play an essential role in hDREFs self association, and also required for nuclear accumulation, DNA binding activity and granular pattern formation ([[literature:100843|Yamashita ''et al''. 2007]]).</div>

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