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Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 37, pp. 15287 - 15300
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates... 
CONSERVED CYSTEINE | HUMAN PTS1 RECEPTOR | DOCKING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYCLING RECEPTOR | MACHINERY | MEMBRANE-PROTEIN | II SECRETION SYSTEM | AAA PEROXINS | TARGETING SIGNAL RECEPTOR | IMPORT RECEPTOR | Humans | Protein Multimerization | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Biological Transport | Gene Deletion | Receptors, Cytoplasmic and Nuclear - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Solubility | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Fusion Proteins - chemistry | Peroxisomes - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Models, Biological | Peroxisome-Targeting Signal 1 Receptor | Endopeptidase K - metabolism | Mutation | Intracellular Membranes - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Receptors, Cytoplasmic and Nuclear - metabolism | ubiquitylation (ubiquitination) | docking | PEX5 | peroxisome | translocation module | protein import | protein sorting | receptor recycling | PEX14 | Cell Biology
Journal Article
Nature (London), ISSN 1476-4687, 2004, Volume 431, Issue 7010, pp. 873 - 878
.... The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2... 
CORE | RECRUITMENT | TRANSCRIPTIONAL ACTIVATION | COMPLEX | LIGASE ACTIVITY | MULTIDISCIPLINARY SCIENCES | RAD6 | H3 LYSINE-27 METHYLATION | UBIQUITYLATION | RING FINGER PROTEINS | DROSOPHILA | Nuclear Proteins - isolation & purification | Nucleosomes - chemistry | Humans | Multiprotein Complexes | Ubiquitin - metabolism | Molecular Sequence Data | Drosophila melanogaster - genetics | Promoter Regions, Genetic - genetics | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Protein Subunits - isolation & purification | Repressor Proteins - isolation & purification | Response Elements - genetics | Nuclear Proteins - genetics | Proto-Oncogene Proteins - isolation & purification | Repressor Proteins - metabolism | Protein Subunits - genetics | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Cell Line | Catalytic Domain | Repressor Proteins - chemistry | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Nucleosomes - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Polycomb-Group Proteins | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - isolation & purification | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Homeodomain Proteins - genetics | Transcription Factors - metabolism | Polycomb Repressive Complex 2 | Animals | Polycomb Repressive Complex 1 | Transcription Factors - isolation & purification | Ubiquitin-Protein Ligases - isolation & purification | Protein Subunits - chemistry | Drosophila Proteins - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Proteins | Enzymes | Cell culture | Chromatin | Biochemistry
Journal Article
Molecular & cellular proteomics, ISSN 1535-9476, 11/2013, Volume 12, Issue 11, pp. 3184 - 3198
Protein-protein interactions can be modulated by the methylation of arginine residues... 
RNA-POLYMERASE-II | SYSTEM | RECRUITMENT | MESSENGER-RNA | BIOCHEMICAL RESEARCH METHODS | INTERACTION MAP | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | BINDING | NPL3 | SR-LIKE PROTEIN | Adaptor Proteins, Signal Transducing - chemistry | Ribonucleoprotein, U1 Small Nuclear - metabolism | RNA-Binding Proteins - genetics | Proteome - genetics | Saccharomyces cerevisiae - genetics | Molecular Sequence Data | Substrate Specificity | Proteome - chemistry | Protein Interaction Maps | Saccharomyces cerevisiae - metabolism | Tandem Mass Spectrometry | Ribonucleoprotein, U1 Small Nuclear - chemistry | Chromatography, Liquid | Protein-Arginine N-Methyltransferases - genetics | DEAD-box RNA Helicases - metabolism | Nuclear Proteins - genetics | DEAD-box RNA Helicases - chemistry | Protein-Arginine N-Methyltransferases - chemistry | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Repressor Proteins - chemistry | RNA-Binding Proteins - chemistry | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Ribonucleoprotein, U1 Small Nuclear - genetics | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Blotting, Western | Arginine - chemistry | Protein-Arginine N-Methyltransferases - metabolism | DEAD-box RNA Helicases - genetics | Two-Hybrid System Techniques | Adaptor Proteins, Signal Transducing - genetics | Proteomics | Saccharomyces cerevisiae Proteins - metabolism | Protein Processing, Post-Translational | Adaptor Proteins, Signal Transducing - metabolism | Methylation | Proteome - metabolism | Arginine - metabolism | RNA-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Research
Journal Article
PLoS pathogens, ISSN 1553-7374, 2013, Volume 9, Issue 9, p. e1003636
.... Moreover, 80% of potential EBNA 3A, 3B or 3C target genes were also targeted by EBNA 2, implicating extensive interplay between EBNA 2 and 3 proteins in cellular reprogramming... 
SIGNAL-BINDING-PROTEIN | RBP-J-KAPPA | GROWTH TRANSFORMATION | NUCLEAR ANTIGEN 3C | MICROBIOLOGY | TRANSFORMATION IN-VITRO | EBNA-2-MEDIATED TRANSACTIVATION | NUCLEAR-PROTEIN-2 ACIDIC DOMAIN | LONG-RANGE INTERACTION | VIROLOGY | BURKITTS-LYMPHOMA | LATENT MEMBRANE-PROTEIN | PARASITOLOGY | Protein-Tyrosine Kinases - metabolism | Humans | Epstein-Barr Virus Nuclear Antigens - chemistry | Viral Proteins - metabolism | Cellular Reprogramming | Alcohol Oxidoreductases - genetics | Cell Cycle Proteins - chemistry | Nerve Tissue Proteins - chemistry | Protein-Tyrosine Kinases - genetics | Protein-Tyrosine Kinases - chemistry | Cell Cycle Proteins - genetics | Nuclear Proteins - genetics | Binding Sites | Epstein-Barr Virus Nuclear Antigens - metabolism | Repressor Proteins - metabolism | Binding, Competitive | Recombinant Proteins - metabolism | Cell Line | Gene Targeting | Repressor Proteins - chemistry | Epstein-Barr Virus Nuclear Antigens - genetics | Viral Proteins - chemistry | Cell Cycle Proteins - metabolism | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Viral Proteins - genetics | Alcohol Oxidoreductases - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Epstein-Barr Virus Infections - pathology | Host-Pathogen Interactions | Nerve Tissue Proteins - metabolism | Enhancer Elements, Genetic | Alcohol Oxidoreductases - chemistry | Models, Biological | Herpesvirus 4, Human - metabolism | Epstein-Barr Virus Infections - metabolism | Transcription factors | Physiological aspects | Epstein-Barr virus | Genetic aspects | Research | Gene expression | Health aspects | Proteins | Medical research | Genomes | Genes
Journal Article
PloS one, ISSN 1932-6203, 2011, Volume 6, Issue 2, p. e17270
Background: The SMC5-6 protein complex is involved in the cellular response to DNA damage... 
RECOMBINATION | PROTEIN | GENE | ROLES | MULTIDISCIPLINARY SCIENCES | DNA-REPAIR | IDENTIFICATION | INHIBITOR | SUMO LIGASE | STATISTICAL-MODEL | Schizosaccharomyces pombe Proteins - chemistry | Melanoma-Specific Antigens - chemistry | Multigene Family | Protein Binding - genetics | Conserved Sequence - physiology | Saccharomyces cerevisiae - genetics | Humans | Molecular Sequence Data | Multiprotein Complexes - genetics | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Schizosaccharomyces - genetics | Sequence Homology | Multiprotein Complexes - metabolism | Schizosaccharomyces pombe Proteins - metabolism | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Repressor Proteins - chemistry | Schizosaccharomyces pombe Proteins - genetics | Chromosomal Proteins, Non-Histone - metabolism | Cell Cycle Proteins - metabolism | Models, Molecular | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Chromosomal Proteins, Non-Histone - genetics | Protein Interaction Mapping | Carrier Proteins - genetics | Schizosaccharomyces - metabolism | Multiprotein Complexes - chemistry | Carrier Proteins - metabolism | Models, Biological | Melanoma-Specific Antigens - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Chromosomal Proteins, Non-Histone - chemistry | Melanoma-Specific Antigens - genetics | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Family | DNA damage | Protein-protein interactions | Melanoma | Protein binding | Transcription factors | Yeast | Genomics | Steroidogenic factor 1 | Conservation | Genomes | Adipocytes | Hydrophobicity | Repressors | Evolutionary conservation | Transcription activation | Deoxyribonucleic acid--DNA | Antigens | Automation | Polypeptides | Melanoma-associated antigen | Mammals | Androgens | Molecular modelling | Mutagenesis | Site-directed mutagenesis | Proteomics | Ligands | Scientific imaging | Mutation | Protein interaction | Mass spectrometry | Deoxyribonucleic acid | DNA
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 489, Issue 7415, pp. 313 - 317
Cornelia de Lange syndrome (CdLS) is a dominantly inherited congenital malformation disorder, caused by mutations in the cohesin-loading protein NIPBL1,2 for nearly 60... 
SISTER-CHROMATID COHESION | NIPPED-B | COMPLEX | NIPBL | HUMAN GENOME | RNA-SEQ | MULTIDISCIPLINARY SCIENCES | X-CHROMOSOME-INACTIVATION | S-PHASE | PROTEINS | BINDING | Chromatin - metabolism | Chondroitin Sulfate Proteoglycans - chemistry | Humans | Crystallography, X-Ray | Male | Phosphoproteins - metabolism | Cell Cycle Proteins - chemistry | Chromatin Immunoprecipitation | Repressor Proteins - deficiency | De Lange Syndrome - metabolism | Fibroblasts | Female | Transcription, Genetic | Acetylation | Binding Sites | Repressor Proteins - metabolism | De Lange Syndrome - genetics | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histone Deacetylases - genetics | Cell Cycle Proteins - metabolism | Chondroitin Sulfate Proteoglycans - metabolism | Histone Deacetylases - chemistry | Histone Deacetylases - deficiency | Mutant Proteins - genetics | Prophase | Models, Molecular | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Mutation - genetics | Proteins - genetics | Mutant Proteins - chemistry | Protein Conformation | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Anaphase | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Genetics | De Lange syndrome | Genetic aspects | Research | Mutation (Biology) | Proteins | Cell culture | Genes | Cell cycle | Mutation | Females | Chromosomes | Crystal structure | Chromatin | Repressor Proteins | Life Sciences | Phosphoproteins | Chromosomal Proteins, Non-Histone | Histone Deacetylases | De Lange Syndrome | Chondroitin Sulfate Proteoglycans | Nuclear Proteins | Mutant Proteins | Adaptor Proteins, Signal Transducing | Development Biology | Cell Cycle Proteins
Journal Article
Nature structural & molecular biology, ISSN 1545-9985, 2018, Volume 25, Issue 2, pp. 154 - 162
Journal Article
RNA Biology, ISSN 1547-6286, 07/2011, Volume 8, Issue 4, pp. 552 - 556
The unconventional splicing of Hac1 by the ribonuclease Ire1 is a key event in the activation of the unfolded protein response (UPR... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | XBP1 | Intron | Splicing | RNA structure | HAC1 | Unfolded protein response | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | XBP1 MESSENGER-RNA | ENDOPLASMIC-RETICULUM STRESS | IRE1P | unfolded protein response | intron | GENE | SEQUENCE | splicing | TRANSCRIPTION FACTOR | Fungal Proteins - chemistry | Transcription Factors - chemistry | Membrane Glycoproteins - metabolism | Saccharomyces cerevisiae - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Membrane Glycoproteins - chemistry | X-Box Binding Protein 1 | RNA - genetics | Saccharomyces cerevisiae - metabolism | RNA Splicing | RNA, Fungal - genetics | Nucleic Acid Conformation | Protein-Serine-Threonine Kinases - metabolism | Gene Expression Regulation, Fungal | Repressor Proteins - chemistry | Unfolded Protein Response - genetics | Introns | RNA, Fungal - chemistry | Protein Splicing | Protein-Serine-Threonine Kinases - genetics | Repressor Proteins - genetics | Basic-Leucine Zipper Transcription Factors - genetics | Drosophila Proteins - chemistry | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | RNA - chemistry | DNA-Binding Proteins - chemistry | Regulatory Factor X Transcription Factors | Protein Folding | Membrane Glycoproteins - genetics | Sequence Alignment | Animals | Basic-Leucine Zipper Transcription Factors - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein-Serine-Threonine Kinases - chemistry | Drosophila Proteins - genetics | Caenorhabditis elegans Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Life Sciences | RNA Families
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase
Journal Article