RING3 is linked to the Xenopus major histocompatibility complex.
Salter-Cid
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L
Department of Microbiology and Immunology, University of Miami School of Medicine, P. O. Box 016960 (R-138) Miami, FL 33101, USA.
Du Pasquier
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L
Flajnik
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004331:Drosophila melanogaster; D017344:Genes, Insect; D008040:Genetic Linkage; D006801:Humans; D008285:Major Histocompatibility Complex; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017346:Protein Serine-Threonine Kinases / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D014157:Transcription Factors; D014981:Xenopus / Q000235:genetics*; D029867:Xenopus Proteins; D000092468:Bromodomain Containing Proteins
D017346:Protein Serine-Threonine Kinases; D014157:Transcription Factors; D029867:Xenopus Proteins; C098415:BRD2 protein, human; D000092468:Bromodomain Containing Proteins; C490842:BRD2 protein, Xenopus