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1. Full Text SUMO E3 ligase activity of TRIM proteins
by Chu, Y and Yang, X
Oncogene, ISSN 0950-9232, 03/2011, Volume 30, Issue 9, pp. 1108 - 1116
SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an... 
Mdm2 | TRIM proteins | sumoylation | SUMOE3 ligase | PML | p53 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PML NUCLEAR-BODIES | DNA-DAMAGE | REGULATES P53 | FAMILY PROTEINS | SUMO E3 ligase | UBIQUITIN LIGASES | CELL BIOLOGY | RET FINGER PROTEIN | ONCOLOGY | GENETICS & HEREDITY | TUMOR-SUPPRESSOR | C-JUN | Immunoprecipitation | Transcription Factors - chemistry | Humans | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Animals | Small Ubiquitin-Related Modifier Proteins - chemistry | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Sumoylation | RNA, Small Interfering | Ubiquitin-Protein Ligases - genetics | Microscopy, Fluorescence | Promyelocytic Leukemia Protein | Physiological aspects | Tumor suppressor genes | Research | Tumor proteins | Ligases | Proteins | Enzymes | Biochemistry | Cellular biology | Gene expression
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2. Full Text RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair
by Galanty, Yaron and Belotserkovskaya, Rimma and Coates, Julia and Jackson, Stephen P
Genes and Development, ISSN 0890-9369, 06/2012, Volume 26, Issue 11, pp. 1179 - 1195
Protein ubiquitylation and sumoylation play key roles in regulating cellular responses to DNA double-strand breaks (DSBs). Here, we show that human RNF4, a... 
RPA | Ubiquitin-proteasome system (UPS) | RAD51 | SUMO | RNF4 | DNA double-strand breaks (DSBs) | PROTEASOME ACTIVATOR PA28-GAMMA | DEVELOPMENTAL BIOLOGY | MAMMALIAN-CELLS | CELL BIOLOGY | ubiquitin-proteasome system (UPS) | DAMAGE RESPONSE | GENOMIC STABILITY | FANCONI-ANEMIA PATHWAY | CHROMATIN RETENTION | GENETICS & HEREDITY | HOMOLOGOUS RECOMBINATION | END RESECTION | PROTEINS | BINDING | DNA replication | Phosphorylation | Research | Ubiquitin-proteasome system | Analysis | Cellular control mechanisms | ubiquitin–proteasome system (UPS) | Research Paper
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3. Full Text Sumoylation of ABI5 by the Arabidopsis SUMO E3 Ligase SIZ1 Negatively Regulates Abscisic Acid Signaling
by Kenji Miura and Jiyoung Lee and Jing Bo Jin and Chan Yul Yoo and Tomoko Miura and Paul M. Hasegawa and Mark Estelle
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2009, Volume 106, Issue 13, pp. 5418 - 5423
SUMO (small ubiquitin-related modifier) conjugation (i.e., sumoylation) to protein substrates is a reversible posttranslational modification that regulates... 
Transcriptional regulatory elements | Plant growth regulators | Root growth | Genes | Germination | Gene expression regulation | Plants | Seedlings | Seed germination | Plant cells | Abscisic acid | Sumoylation | Signaling | SUMO | ABA | signaling | sumoylation | SEED-GERMINATION | GENETIC-ANALYSIS | PROTEIN | MULTIDISCIPLINARY SCIENCES | TRANSDUCTION | RESPONSES | SALICYLIC-ACID | GROWTH | abscisic acid | TRANSCRIPTION FACTOR | EXPRESSION | Arabidopsis Proteins - genetics | Arabidopsis Proteins - physiology | Basic-Leucine Zipper Transcription Factors - metabolism | Signal Transduction | Ligases - genetics | Ligases - metabolism | SUMO-1 Protein | Arabidopsis - metabolism | Arabidopsis Proteins - metabolism | Ubiquitin-Protein Ligases | Gene Expression Regulation, Plant | Abscisic Acid - metabolism | Ligases - physiology | Mutation | Plant Roots - growth & development | Ubiquitin | Arabidopsis | Ligases | Physiological aspects | Genetic aspects | Cellular signal transduction | Research | Properties | Biological Sciences
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4. Full Text SUMO E3 Ligase SlSIZ1 Facilitates Heat Tolerance in Tomato
by Zhang, Song and Wang, Shiju and Lv, Jinlian and Liu, Zhuangbin and Wang, Yong and Ma, Nana and Meng, Qingwei
Plant and Cell Physiology, ISSN 0032-0781, 01/2018, Volume 59, Issue 1, pp. 58 - 71
Abstract High temperature has become a major abiotic stress that limits crop productivity. Heat shock transcription factors (HSFs) and heat shock proteins... 
SUMO E3 ligase SlSIZ1 | Heat shock transcription factors (HSFs) | Heat stress | SUMOylation | Tomato | Heat shock proteins (HSPs) | SIZ1 | SHOCK TRANSCRIPTION FACTOR-1 | STRESS RESPONSE | PLANT SCIENCES | CELL BIOLOGY | HSP70 CHAPERONES | GENE | PROTEIN MODIFICATION | ARABIDOPSIS | ABSCISIC-ACID | EXPRESSION
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5. Full Text SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
by Yin, Yili and Seifert, Anne and Chua, Joy Shijia and Maure, Jean-Francxois and Golebiowski, Filip and Hay, Ronald T
Genes and Development, ISSN 0890-9369, 06/2012, Volume 26, Issue 11, pp. 1196 - 1208
Here we demonstrate that RNF4, a highly conserved small ubiquitin-like modifier (SUMO)-targeted ubiquitin E3 ligase, plays a critical role in the response of... 
SUMO | Ubiqutin | RNF4 | DNA damage | MDC1 | COMPLEX | DOUBLE-STRAND BREAKS | DEVELOPMENTAL BIOLOGY | SUMOYLATION | CELL BIOLOGY | REPAIR PROTEINS | ubiqutin | GENETICS & HEREDITY | UBIQUITYLATION | CHECKPOINT | END RESECTION | BINDING | CYCLE | Humans | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Rats | Homologous Recombination | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA Breaks, Double-Stranded | Transcription Factors - metabolism | Animals | DNA Repair | Cell Line, Tumor | Trans-Activators - metabolism | DNA Damage | HeLa Cells | Nuclear Proteins - genetics | Ubiquitin | Research | Gene expression | Genetic regulation | Structure | Research Paper
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6. Full Text A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen
by Sheng, Yi and Hong, Jenny H and Doherty, Ryan and Srikumar, Tharan and Shloush, Jonathan and Avvakumov, George V and Walker, John R and Xue, Sheng and Neculai, Dante and Wan, Janet W and Kim, Sung K and Arrowsmith, Cheryl H and Raught, Brian and Dhe-Paganon, Sirano
Molecular and Cellular Proteomics, ISSN 1535-9476, 08/2012, Volume 11, Issue 8, pp. 329 - 341
Here we describe a systematic structure-function analysis of the human ubiquitin (Ub) E2 conjugating proteins, consisting of the determination of 15 new... 
SYSTEM | ACTIVATION | MOLECULAR REPLACEMENT | SUMO | MECHANISM | PEPTIDE IDENTIFICATION | BIOCHEMICAL RESEARCH METHODS | HECT FAMILY | PROTEINS | POLYUBIQUITINATION | MASS-SPECTROMETRY | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Humans | Ubiquitin - chemistry | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Ubiquitin-Conjugating Enzymes - genetics | Phylogeny | Static Electricity | Ubiquitin-Protein Ligases - chemistry | Ubiquitin-Protein Ligases - classification | Blotting, Western | Ubiquitin-Conjugating Enzymes - chemistry | Sequence Homology, Amino Acid | Ubiquitination | Ubiquitin-Conjugating Enzymes - metabolism | Mass Spectrometry | Surface Properties | Protein Binding | Evolution, Molecular | Research
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7. Full Text The SLX4 Complex Is a SUMO E3 Ligase that Impacts on Replication Stress Outcome and Genome Stability
by Guervilly, Jean-Hugues and Takedachi, Arato and Naim, Valeria and Scaglione, Sarah and Chawhan, Charly and Lovera, Yoann and Despras, Emmanuelle and Kuraoka, Isao and Kannouche, Patricia and Rosselli, Filippo and Gaillard, Pierre-Henri L
Molecular Cell, ISSN 1097-2765, 01/2015, Volume 57, Issue 1, pp. 123 - 137
The SLX4 Fanconi anemia protein is a tumor suppressor that may act as a key regulator that engages the cell into specific genome maintenance pathways. Here, we... 
HOLLIDAY JUNCTION RESOLUTION | STRUCTURE-SPECIFIC ENDONUCLEASES | MITOSIS | PHOSPHORYLATION | HUMAN-CELLS | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORK COLLAPSE | MUS81-EME1 | DNA-REPAIR | FANCONI-ANEMIA | CELL BIOLOGY | Genomic Instability | Recombinases - genetics | Humans | Molecular Sequence Data | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Protein Interaction Domains and Motifs | Protein Subunits - genetics | Amino Acid Sequence | Recombinases - metabolism | Signal Transduction | Small Ubiquitin-Related Modifier Proteins - metabolism | Gene Expression Regulation | Ubiquitin-Protein Ligases - metabolism | DNA Replication | Ubiquitin-Conjugating Enzymes - genetics | DNA-Binding Proteins - genetics | Sequence Alignment | Ubiquitin-Conjugating Enzymes - metabolism | DNA Repair | Cell Line, Tumor | Protein Binding | Recombinant Fusion Proteins - genetics | Sumoylation | Genome | Ubiquitin-Protein Ligases - genetics | Ubiquitin | Sumo | Ligases | Genomics | Fanconi's anemia
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8. Full Text Salicylic acid‐mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase
by Lee, Jiyoung and Nam, Jaesung and Park, Hyeong Cheol and Na, Gunnam and Miura, Kenji and Jin, Jing Bo and Yoo, Chan Yul and Baek, Dongwon and Kim, Doh Hoon and Jeong, Jae Cheol and Kim, Donggiun and Lee, Sang Yeol and Salt, David E and Mengiste, Tesfaye and Gong, Qingqiu and Ma, Shisong and Bohnert, Hans J and Kwak, Sang‐Soo and Bressan, Ray A and Hasegawa, Paul M and Yun, Dae‐Jin
The Plant Journal, ISSN 0960-7412, 01/2007, Volume 49, Issue 1, pp. 79 - 90
Reversible modifications of target proteins by small ubiquitin‐like modifier (SUMO) proteins are involved in many cellular processes in yeast and animals. Yet... 
CC‐NBS‐type | systemic‐acquired resistance | TIR‐NBS‐type | gene | plant innate immunity | SIZ1 SUMO E3 ligase | salicylic acid | TIR-NBS-type R gene | Salicylic acid | Systemic-acquired resistance | Plant innate immunity | CC-NBS-type R gene | OF-FUNCTION MUTATION | DEFENSE RESPONSES | ACTIVATION | systemic-acquired resistance | PLANT-DISEASE RESISTANCE | SIGNALING COMPONENTS | SYSTEMIC ACQUIRED-RESISTANCE | CELL-DEATH | PLANT SCIENCES | PIAS PROTEINS | E3 LIGASE | PR GENE-EXPRESSION | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Salicylic Acid - metabolism | Ligases - genetics | Arabidopsis - immunology | Ligases - metabolism | Gene Expression Profiling | DNA-Binding Proteins - genetics | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | DNA-Binding Proteins - metabolism | Immunity, Innate - immunology | Gene Expression Regulation, Plant | Carboxylic Ester Hydrolases - genetics | Mutation | Carboxylic Ester Hydrolases - metabolism | Arabidopsis | Immunology | Gene expression | Molecular biology | Botany
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9. Full Text Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
by Reverter, David and Lima, Christopher D
Nature, ISSN 0028-0836, 06/2005, Volume 435, Issue 7042, pp. 687 - 692
SUMO-1 ( for small ubiquitin-related modifier) belongs to the ubiquitin (Ub) and ubiquitin-like (Ubl) protein family. SUMO conjugation occurs on specific... 
RANBP2 | UBIQUITINATION | NUCLEOPORIN | DOMAIN | PROTEIN | SUMO CONJUGATION | ENZYME UBC9 | MULTIDISCIPLINARY SCIENCES | NUCLEAR-PORE COMPLEX | RANGAP1 | FAMILY | Amino Acid Sequence | Molecular Chaperones - metabolism | Nuclear Pore Complex Proteins - metabolism | Humans | Nuclear Pore Complex Proteins - chemistry | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | GTPase-Activating Proteins - chemistry | GTPase-Activating Proteins - metabolism | Molecular Chaperones - chemistry | Ubiquitin-Protein Ligases - chemistry | Ubiquitin-Conjugating Enzymes - chemistry | Multiprotein Complexes - metabolism | Multiprotein Complexes - chemistry | SUMO-1 Protein - chemistry | Ubiquitin-Conjugating Enzymes - metabolism | Protein Conformation | SUMO-1 Protein - metabolism | Binding Sites | Proteins | Binding sites | Crystal structure
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10. Full Text DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex
by Varejão, Nathalia and Ibars, Eva and Lascorz, Jara and Colomina, Neus and Torres‐Rosell, Jordi and Reverter, David
The EMBO Journal, ISSN 0261-4189, 06/2018, Volume 37, Issue 12, p. n/a
Modification of chromosomal proteins by conjugation to SUMO is a key step to cope with DNA damage and to maintain the integrity of the genome. The recruitment... 
E3 ligase activity | repair | SUMO | Smc5/6 complex | DNA | Nse2 | ylation | SUMOylation | DNA repair | RECOMBINATION | UBIQUITIN-CONJUGATING ENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | CORE COMPONENT | CELL BIOLOGY | MAINTENANCE | REPAIR | REPLICATION | INDUCED SUMOYLATION | BINDING | CONTRIBUTES | SUBUNIT | DNA, Fungal - genetics | Saccharomyces cerevisiae - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Multiprotein Complexes - genetics | DNA, Fungal - chemistry | Saccharomyces cerevisiae Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Saccharomyces cerevisiae - chemistry | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Multiprotein Complexes - chemistry | SUMO-1 Protein - chemistry | SUMO-1 Protein - genetics | DNA, Fungal - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Cell Cycle Proteins - genetics | Sumoylation | SUMO-1 Protein - metabolism | DNA Damage | Enzyme Activation | Ubiquitin-Protein Ligases - genetics | Saccharomyces cerevisiae Proteins - chemistry | Binding | Chromatin | Yeast | Cell survival | DNA damage | Activation | Genomes | Electrostatic properties | Molecular chains | Proteins | SUMO protein | Conjugation | Sensors | Repair | Damage | Viability | Ubiquitin-protein ligase | Deoxyribonucleic acid--DNA | DNA Replication, Repair & Recombination | Post-translational Modifications, Proteolysis & Proteomics | Structural Biology | 6 complex | Smc5
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11. Full Text PHD Domain-Mediated E3 Ligase Activity Directs Intramolecular Sumoylation of an Adjacent Bromodomain Required for Gene Silencing
by Ivanov, Alexey V and Peng, Hongzhuang and Yurchenko, Vyacheslav and Yap, Kyoko L and Negorev, Dmitri G and Schultz, David C and Psulkowski, Elyse and Fredericks, William J and White, David E and Maul, Gerd G and Sadofsky, Moshe J and Zhou, Ming-Ming and Rauscher, Frank J
Molecular Cell, ISSN 1097-2765, 12/2007, Volume 28, Issue 5, pp. 823 - 837
Tandem PHD and bromodomains are often found in chromatin-associated proteins and have been shown to cooperate in gene silencing. Each domain can bind... 
PROTEINS | DNA | LOCALIZATION | RECOGNITION | RING | BIOCHEMISTRY & MOLECULAR BIOLOGY | ZINC-FINGER PROTEINS | COMPLEXES | TRANSCRIPTIONAL REPRESSION | SUMO MODIFICATION | KAP-1 COREPRESSOR | BINDING | CONTRIBUTES | CELL BIOLOGY | Chromatin - metabolism | Autoantigens - metabolism | Mi-2 Nucleosome Remodeling and Deacetylase Complex | Saccharomyces cerevisiae - genetics | Humans | Protein Methyltransferases - genetics | RING Finger Domains | Tripartite Motif-Containing Protein 28 | Autoantigens - genetics | Bone Neoplasms - pathology | Protein Methyltransferases - metabolism | Repressor Proteins - antagonists & inhibitors | Bone Neoplasms - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Kidney - metabolism | Transcription, Genetic | Bone Neoplasms - genetics | DNA Helicases - genetics | Osteosarcoma - metabolism | Repressor Proteins - metabolism | DNA-Binding Proteins - antagonists & inhibitors | Histone Deacetylases - genetics | Small Ubiquitin-Related Modifier Proteins - metabolism | Cells, Cultured | Gene Expression Regulation | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Ubiquitin-Conjugating Enzymes - genetics | DNA-Binding Proteins - genetics | DNA Helicases - metabolism | Two-Hybrid System Techniques | Ubiquitin-Conjugating Enzymes - metabolism | Adenosine Triphosphatases - genetics | Protein Processing, Post-Translational | Osteosarcoma - genetics | Lysine - chemistry | Ubiquitin-Protein Ligases - genetics | Osteosarcoma - pathology | Saccharomyces cerevisiae - growth & development
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12. Full Text The ubiquitin E3 ligase RHA2b promotes degradation of MYB30 in abscisic acid signaling
by Zheng, Yuan and Chen, Zhaojin and Ma, Liang and Liao, Chancan
Plant Physiology, ISSN 0032-0889, 09/2018, Volume 178, Issue 1, pp. 428 - 440
The phytohormone abscisic acid (ABA) is critical for plants encountering abiotic stress. We reported previously that the Arabidopsis (Arabidopsis thaliana)... 
ARABIDOPSIS-THALIANA | PROTEIN PHOSPHATASES | SEED-GERMINATION | STRESS RESPONSES | SUMO | POSITIVE REGULATOR | PROTEASOME SYSTEM | TRANSCRIPTION FACTOR | SUMOYLATION | KINASE-PHOSPHATASE PAIR | PLANT SCIENCES | Abscisic acid | Physiological aspects | Cellular signal transduction | Observations | Ligases | Ubiquitin | Arabidopsis thaliana
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13. Full Text Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity
by Wright, Joshua D and MacE, Peter D and Day, Catherine L
Nature Structural and Molecular Biology, ISSN 1545-9993, 01/2016, Volume 23, Issue 1, pp. 45 - 52
RING-domain E3 ligases enhance transfer of ubiquitin to substrate proteins by stabilizing the RING-bound thioester-linked E2-ubiquitin conjugate in a defined... 
BINDING DOMAINS | COMPLEX | SUMO | POLYUBIQUITIN | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | BIOPHYSICS | STRUCTURAL BASIS | DEGRADATION | CHAINS | RNF111/ARKADIA | REVEALS | Aurora Kinase B - metabolism | Humans | Ubiquitin - chemistry | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Crystallography, X-Ray | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | RING Finger Domains | Ubiquitin-Protein Ligases - chemistry | Aurora Kinase B - chemistry | Models, Biological | Protein Binding | Protein Conformation | Ubiquitin | Physiological aspects | Research | Ligases | Protein binding | Enzymes | Biochemistry | Crystal structure
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