1997
DOI: 10.1016/s0378-1119(96)00701-9
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The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals

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Cited by 43 publications
(81 citation statements)
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“…In solution, purifi ed ERH protein forms homodimers, suggesting ERH might function as a dimer in cell. The Drosophila E(r) protein can be phosphorylated by casein kinase II (CKII) in vitro (Gelsthorpe et al, 1997), and mutations in E(r) at two CKII consensus sites T18 and S24 compromise E(r) function in vivo (Gelsthorpe et al, 2006). Although it remains to be determined whether CKII also phosphorylates ERH in mammalian cells, mass-spectrometry data indicate that S24 might be a major phosphorylation site on human ERH.…”
Section: Structure and Regulation Of Erhmentioning
confidence: 99%
“…In solution, purifi ed ERH protein forms homodimers, suggesting ERH might function as a dimer in cell. The Drosophila E(r) protein can be phosphorylated by casein kinase II (CKII) in vitro (Gelsthorpe et al, 1997), and mutations in E(r) at two CKII consensus sites T18 and S24 compromise E(r) function in vivo (Gelsthorpe et al, 2006). Although it remains to be determined whether CKII also phosphorylates ERH in mammalian cells, mass-spectrometry data indicate that S24 might be a major phosphorylation site on human ERH.…”
Section: Structure and Regulation Of Erhmentioning
confidence: 99%
“…3 ER is a highly conserved protein that has been found in plants, animals and protists, but has yet to be found in fungi. 2 ER is 76% identical to the ER homologue, ERH, of vertebrates, 49% identical to the C. elegans ERH and 40% identical to the plant (Arabidopsis) ERH. 2 The vertebrate ER homologues are very highly conserved.…”
Section: Introductionmentioning
confidence: 98%
“…1,2 An examination of the amino acid sequence does not reveal any motifs that indicate a putative function or mode of regulation of the protein other than two conserved casein kinase II sites. 3 A mutagenic analysis of these sites indicate that they are important in the regulation of the activity of ER.…”
Section: Introductionmentioning
confidence: 99%
“…The high conservation of e(r) suggests that it encodes a vital function, 3 however previous mutagenic analyses revealed that e(r) hypomorphic mutations were viable, fertile, and morphologically wild-type and provide no compelling argument for the high conservation of the gene. 2,7 Data from the current study indicate that in Drosophila melanogaster, deficiencies of the e(r) gene are viable and morphologically wild-type, but that the null males and females have a decreased viability and that the females have a decreased fertility.…”
Section: Discussionmentioning
confidence: 96%
“…2 Subsequent studies revealed that the gene is highly conserved, present in species as diverse as insects, vertebrates, higher plants, and slime molds. 3 Current BLAST 4 searches have also identified the gene in protists, nematodes, flatworms, but not yeasts (S. I. Tsubota, unpublished data). Studies in Xenopus revealed that ER is nuclearly localized and binds to the transcription factor, DCoH/PCD (dimerization cofactor of HNF1/pterin-4a-carbinolamine dehydratase), and thus may be acting as a transcription cofactor of the HNF1 homeobox transcription factor.…”
Section: Introductionmentioning
confidence: 99%