The human gene, DGLUCY, is highly conserved in mammals and birds.[6]Orthologs gathered from BLAST and BLAT searches reveal that the human DGLUCY mRNA sequence is conserved with a sequence identity of 98% in chimpanzees, 88% in mice, and 81% in platypus and chicken.[7][8] The following table contains a list orthologs that were gathered from BLAST searches. Sequence alignments were performed using blastn to derive sequence identity, score, and E-values between the human c14orf159 variant 1 mRNA and its orthologs.
The protein that the human gene DGLUCY encodes has been found to be highly conserved among mammals, birds, amphibians, fish, tunicates, cnidarians, and echinoderms. However, no protein orthologs have been found in nematodes, arthropods, fungi, protists, plants, bacteria, or archea. Fungi and bacteria contain the DUF1445 conserved domain which is found in human c14orf159 and its orthologs. BLAST and BLAT searches have been utilized to find orthologs to the c14orf159 protein. The following table lists protein orthologs for the human protein with sequence identity, sequence similarity, scores, and E-values derived from blastp sequence comparisons.[9]
Post-translational modifications are predicted for the protein DGLUCY. All predicted sites in human DGLUCY were compared to orthologs using multiple sequence alignments to determine likelihood of modification.[12][13][14][15][16]
^Mehrle A, Rosenfelder H. "RZPD CloneID DKFZp686J0759". LifeDB: Database for Localization, Interaction, Functional assays and Expression of Proteins. German Cancer Research Center.[permanent dead link]
^Prediction of glycosylation across the human proteome and the correlation to protein function. Gupta, R. and S. Brunak. Pacific Symposium on Biocomputing, 7:310-322, 2002 <http://www.cbs.dtu.dk/services/YinOYang/>.
^Locating proteins in the cell using TargetP, SignalP, and related tools Olof Emanuelsson, Søren Brunak, Gunnar von Heijne, Henrik Nielsen Nature Protocols 2, 953-971 (2007) http://www.cbs.dtu.dk/services/SignalP/.
^Scanning the available Dictyostelium discoideum proteome for O-linked GlcNAc glycosylation sites using neural networks. R. Gupta, E. Jung, A.A. Gooley, K.L. Williams, S. Brunak and J. Hansen. Glycobiology: 9(10):1009-22, 1999 http://www.cbs.dtu.dk/services/DictyOGlyc/.
^Analysis and prediction of mammalian protein glycation. Morten Bo Johansen, Lars Kiemer and Søren Brunak Glycobiology, 16:844-853, 2006 http://www.cbs.dtu.dk/services/NetGlycate/.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.