E3 ubiquitin-protein ligase TRIM21 (Protein name
), RO52_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
TRIM21(RNF81;RO52;SSA1);
Protein name:
E3 ubiquitin-protein ligase TRIM21;
Alternative:
52 kDa ribonucleoprotein autoantigen Ro/SS-A;52 kDa Ro protein;Ro(SS-A);RING finger protein 81;Tripartite motif-containing protein 21;Sjoegren syndrome type A antigen(SS-A);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts (via C-terminus) with IRF8 (via C-terminus) (By similarity). Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB, IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2 does not depend on an intact F-box domain. Interacts (via N-terminus and C-terminus) with DCP2 (via N-terminus and C-terminus).
Function:
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.
Subcellular Location:
Cytoplasm
Nucleus
Cytoplasm
P-body
Enters the nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-like structures in the cytoplasm, called cytoplasmic bodies (P-body) that are located underneath the plasma membrane and also diffusely in the cytoplasm and are highly motil in cells. Cytoplasmic bodies are located along the microtubules and do not share the same cytoplasmic bodies with TRIM5. Colocalizes with DCP2 in P-body.
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1);VARIANT ALA-52
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANT ARG-96
6.
"Isolation of human Sjogren syndrome type A antigen cDNA clone from HEp-2 cells, isolate 1." Chen Y.-J.
,
Fan Y.-H.
,
Chiou S.-H.
Submitted (2004-09) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: FUNCTION;AUTOUBIQUITINATION;MUTAGENESIS OF CYS-16
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Cited for: FUNCTION;AUTOUBIQUITINATION;DEUBIQUITINATION BY USP4;MUTAGENESIS OF CYS-16
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Cited for: FUNCTION;AUTOUBIQUITINATION;INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX;INTERACTION WITH SKP2; SKP1; CUL1 AND FBXW11
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Cited for: FUNCTION;INTERACTION WITH DCP2;SUBCELLULAR LOCATION
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Cited for: FUNCTION;SUBCELLULAR LOCATION;COILED-COIL DOMAIN;DOMAIN B30.2/SPRY
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Cited for: FUNCTION;INTERACTION WITH VCP;AUTOUBIQUITINATION;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;INTERACTION WITH IKBKB;MUTAGENESIS OF CYS-16
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]