pubmed-article:15629158 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0080347 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C1421569 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C1421775 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:15629158 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:15629158 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:15629158 | pubmed:dateCreated | 2005-1-4 | lld:pubmed |
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pubmed-article:15629158 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15629158 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15629158 | pubmed:abstractText | Human ZNF295 protein harbors a BTB/POZ domain and multiple krüppel (C(2)H(2)) type zinc finger domains, and thus belongs to a family of POK (POZ and krüppel) transcription factor. We have identified many transcript variants generated by the alternative splicing in 5' non-coding exons, an intra-exonic splicing in a coding region, and the use of three polyadenylation signals in the 3' UTR. The intra-exonic splicing removes 603-bp coding sequence, and thus ZNF295 gene produces two protein isoforms: ZNF295L with 1066 amino acid residues and ZNF295S with 865 amino acid residues, containing 9 and 5 zinc finger domains, respectively. ZNF295 is ubiquitously expressed in human fetal and adult tissues. Analysis of transcription activity of ZNF295 using various promoter-reporters demonstrated that ZNF295 acts as a transcription repressor, and contains two separate regions for repression activity: the BTB/POZ domain and the central region between BTB/POZ and ZF domains. Both ZNF295L and ZNF295S could interact not only with themselves and each other, but also with another POK protein ZFP161 known to function as a transcription repressor and an activator. We postulated that ZNF295 may be involved in the bi-directional control of gene expression in concert with ZFP161. | lld:pubmed |
pubmed-article:15629158 | pubmed:language | eng | lld:pubmed |
pubmed-article:15629158 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15629158 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15629158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15629158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15629158 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15629158 | pubmed:month | Feb | lld:pubmed |
pubmed-article:15629158 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:15629158 | pubmed:author | pubmed-author:WangJunJ | lld:pubmed |
pubmed-article:15629158 | pubmed:author | pubmed-author:ShimizuNobuyo... | lld:pubmed |
pubmed-article:15629158 | pubmed:author | pubmed-author:KudohJunJ | lld:pubmed |
pubmed-article:15629158 | pubmed:author | pubmed-author:TakayanagiAts... | lld:pubmed |
pubmed-article:15629158 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15629158 | pubmed:day | 11 | lld:pubmed |
pubmed-article:15629158 | pubmed:volume | 327 | lld:pubmed |
pubmed-article:15629158 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15629158 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15629158 | pubmed:pagination | 615-27 | lld:pubmed |
pubmed-article:15629158 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:15629158 | pubmed:meshHeading | pubmed-meshheading:15629158... | lld:pubmed |
pubmed-article:15629158 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15629158 | pubmed:articleTitle | Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is directly associated with ZFP161. | lld:pubmed |
pubmed-article:15629158 | pubmed:affiliation | Department of Molecular Biology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan. | lld:pubmed |
pubmed-article:15629158 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15629158 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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