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http://purl.uniprot.org/citations/17979886http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17979886http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17979886http://www.w3.org/2000/01/rdf-schema#comment"AlkB is an Escherichia coli protein that catalyses the oxidative demethylation of 1-methyladenine and 3-methylcytosine in DNA and RNA. The enzyme activity of AlkB is dependent on a 2-oxoglutarate- and Fe(II)-dependent (2OG-Fe[II]) oxygenase domain. Human AlkB homologues (hABH), hABH1, hABH2 and hABH3, which also possess the 2OG-Fe(II) oxygenase domain, have previously been identified. Recent bioinformatics analysis suggests the existence of an additional five ABH genes in humans. In this study, we identified the hABH4-hABH7 mRNAs and determined their expression in human tissues. Moreover, an hABH2 splice variant lacking the 2OG-Fe(II) oxygenase domain and a new gene, hABH8, were cloned from testis cDNA. hABH8 possesses not only the 2OG-Fe(II) oxygenase domain but both an RNA-binding motif and a methyl-transferase domain. mRNA of the eight hABH molecules was detected in the 16 normal human tissues examined. The sub-cellular localization of EmGFP-hABH8 was restricted to the cytoplasm. EmGFP-hABH1, 3, 4, 6 and 7 were localized in both the cytoplasm and nuclei. Interestingly, the EmGFP-hABH2 splice variant localized in nucleoplasm with a dot-like pattern. In some HeLa cells transfected with EmGFP-hABH5, dot-like fluorescence was also detected in the cytoplasm. These observations provide important information for the future annotation of the hABH family of molecules."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.org/dc/terms/identifier"doi:10.1111/j.1582-4934.2007.00094.x"xsd:string
http://purl.uniprot.org/citations/17979886http://purl.org/dc/terms/identifier"doi:10.1111/j.1582-4934.2007.00094.x"xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Konishi N."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Konishi N."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Furukawa T."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Furukawa T."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Tsujikawa K."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Tsujikawa K."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Tsuchiya M."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Tsuchiya M."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Makino Y."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Makino Y."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Arima H."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Arima H."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Kitae K."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Kitae K."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Koike K."xsd:string
http://purl.uniprot.org/citations/17979886http://purl.uniprot.org/core/author"Koike K."xsd:string