serw-MX  [xml]  

 DeCS Categories

D08 Enzymes and Coenzymes .
D08.811 Enzymes .
D08.811.464 Ligases .
D08.811.464.938 Ubiquitin-Protein Ligase Complexes .
D08.811.464.938.750 Ubiquitin-Protein Ligases .
D08.811.464.938.750.782 Tripartite Motif-Containing Protein 28 .
D12 Amino Acids, Peptides, and Proteins .
D12.776 Proteins .
D12.776.220 Cytoskeletal Proteins .
D12.776.220.909 Pyrin .
D12.776.260 DNA-Binding Proteins .
D12.776.260.703 Repressor Proteins .
D12.776.260.703.675 Tripartite Motif-Containing Protein 28 .
D12.776.624 Neoplasm Proteins .
D12.776.624.776 Tumor Suppressor Proteins .
D12.776.624.776.654 Promyelocytic Leukemia Protein .
D12.776.660 Nuclear Proteins .
D12.776.660.745 Promyelocytic Leukemia Protein .
D12.776.930 Transcription Factors .
D12.776.930.713 Promyelocytic Leukemia Protein .
D12.776.930.780 Repressor Proteins .
D12.776.930.780.911 Tripartite Motif-Containing Protein 28 .
D12.776.934 Tripartite Motif Proteins .
D12.776.934.500 Promyelocytic Leukemia Protein .
D12.776.934.750 Pyrin .
D12.776.934.875 Tripartite Motif-Containing Protein 28 .
G02 Chemical Phenomena .
G02.111 Biochemical Phenomena .
G02.111.694 Protein Multimerization .
 Synonyms & Historicals
Pyrin .
MEFV Protein .
Marenostrin .
Mediterranean Fever Protein .
TRIM20 Protein .
A tripartite motif protein that consists of an N-terminal pyrin domain, a central coiled-coil region and B-box type ZINC FINGER, and C-terminal regions that mediate homotrimerization and interactions with other proteins (the B30.2/SPRY DOMAIN). It is expressed primarily by mature GRANULOCYTES and associates with the cytoskeleton in the perinuclear area as well as AUTOPHAGOSOMES, where it co-ordinates the assembly of AUTOPHAGY-RELATED PROTEINS and degradation of INFLAMMASOME components. It functions in INNATE IMMUNITY and INFLAMMATION; mutations in the Pyrin protein (MEFV) gene are associated with FAMILIAL MEDITERRANEAN FEVER. .
Tripartite Motif-Containing Protein 28 .
TRIM28 Protein .
Tripartite Motif Containing Protein 28 .
A tripartite motif protein consisting of an N-terminal RING finger, two B-box type ZINC FINGERS, and C-terminal PHD domain. It functions as a transcriptional repressor by associating with Kruppel-association box domain (KRAB domain) transcription factors and has E3-SUMO-ligase activity towards itself and also sumoylates INTERFERON REGULATORY FACTOR-7 to reduce its activity as a transcriptional activator. It can also function as a ubiquitin protein ligase towards TUMOR SUPPRESSOR PROTEIN P53. .
Tripartite Motif Proteins .
RBCC Protein Family .
RBCC Proteins .
TRIM Protein Family .
TRIM Proteins .
Family, RBCC Protein .
Family, TRIM Protein .
Motif Proteins, Tripartite .
Protein Family, RBCC .
Protein Family, TRIM .
Proteins, RBCC .
Proteins, TRIM .
Proteins, Tripartite Motif .
A protein family defined by the presence of three ZINC FINGER domains, one of which is a RING FINGER DOMAIN, a coiled-coil region, and a highly variable C-terminal region. They function in many cellular processes including APOPTOSIS and CELL CYCLE regulation. .
Promyelocytic Leukemia Protein .
RNF71 Protein .
TRIM19 Protein .
A tripartite motif protein that contains three ZINC FINGERS, including a RING FINGER DOMAIN, at its N-terminal. Several nuclear and one cytoplasmic isoforms result from alternative splicing of the PML gene; most nuclear isoforms localize to subnuclear structures (PML nuclear bodies) that are disrupted in ACUTE PROMYELOCYTIC LEUKEMIA cells. .
Protein Multimerization .
Protein Dimerization .
Protein Heteromultimerizaton .
Protein Multimer Assembly .
Protein Trimerization .
Assembly, Protein Multimer .
Dimerization, Protein .
Heteromultimerizaton, Protein .
Heteromultimerizatons, Protein .
Multimer Assembly, Protein .
Multimerization, Protein .
Trimerization, Protein .
Protein Hybridization .
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. .