Q62191 (RO52_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 115. History...
Names and origin
|Protein names||Recommended name:|
E3 ubiquitin-protein ligase TRIM21
52 kDa Ro protein
52 kDa ribonucleoprotein autoantigen Ro/SS-A
Sjoegren syndrome type A antigen
Tripartite motif-containing protein 21
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||470 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. Ref.2
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) By similarity. Interacts (via C-terminus) with IRF8 (via C-terminus). Ref.2
Cytoplasm. Nucleus. Cytoplasm › P-body By similarity. Note: Enters the nucleus upon exposure to nitric oxide By similarity. 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. Ref.2
Up-regulated by IFN. Ref.2
The coiled-coil is necessary for the cytoplasmic localization. The B30.2/SPRY domain is necessary for the cytoplasmic localization, the interaction with IRF3 and for the IRF3-driven interferon beta promoter activity. The RING-type zinc finger is necessary for ubiquitination and for the IRF3-driven interferon beta promoter activity. Interacts with SKP2 and CUL1 in a RING finger-independent manner By similarity.
Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization By similarity. Autoubiquitinated.
Belongs to the TRIM/RBCC family.
Contains 1 B box-type zinc finger.
Contains 1 B30.2/SPRY domain.
Contains 1 RING-type zinc finger.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 470||470||E3 ubiquitin-protein ligase TRIM21||PRO_0000056116|
|Domain||272 – 470||199||B30.2/SPRY|
|Zinc finger||20 – 59||40||RING-type|
|Zinc finger||96 – 127||32||B box-type|
|Coiled coil||188 – 250||63||Potential|
Helix Strand Turn
|Helix||297 – 299||3|
|Beta strand||304 – 306||3|
|Beta strand||312 – 315||4|
|Beta strand||331 – 338||8|
|Beta strand||341 – 351||11|
|Beta strand||358 – 364||7|
|Turn||377 – 380||4|
|Beta strand||381 – 387||7|
|Beta strand||390 – 393||4|
|Beta strand||395 – 397||3|
|Beta strand||399 – 401||3|
|Beta strand||408 – 415||8|
|Turn||416 – 419||4|
|Beta strand||420 – 425||6|
|Turn||426 – 430||5|
|Beta strand||431 – 436||6|
|Beta strand||445 – 450||6|
|Beta strand||455 – 457||3|
|Beta strand||463 – 465||3|
|||"Structural differences between the human and mouse 52-kD Ro autoantigens associated with poorly conserved autoantibody activity across species."|
Keech C.L., Gordon T.P., McCluskey J.
Clin. Exp. Immunol. 104:255-263(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
|||"Autoantigen Ro52 is an interferon inducible E3 ligase that ubiquitinates IRF-8 and enhances cytokine expression in macrophages."|
Kong H.J., Anderson D.E., Lee C.H., Jang M.K., Tamura T., Tailor P., Cho H.K., Cheong J., Xiong H., Morse H.C. III, Ozato K.
J. Immunol. 179:26-30(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 226-237; 242-252; 298-308 AND 329-340, FUNCTION, INTERACTION WITH IRF8, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, INDUCTION, MASS SPECTROMETRY.
|+||Additional computationally mapped references.|
|L27990 mRNA. Translation: AAB51154.1.|
3D structure databases
|SMR||Q62191. Positions 4-78, 95-131, 291-468. |
Protein-protein interaction databases
|IntAct||Q62191. 21 interactions.|
Protocols and materials databases
|MGI||MGI:106657. Trim21. |
Enzyme and pathway databases
Gene expression databases
Family and domain databases
|Gene3D||126.96.36.199. 1 hit. |
188.8.131.52. 1 hit.
|InterPro||IPR001870. B30.2/SPRY. |
|Pfam||PF13765. PRY. 1 hit. |
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
|PRINTS||PR01406. BBOXZNFINGER. |
|SMART||SM00336. BBOX. 1 hit. |
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
|SUPFAM||SSF49899. SSF49899. 1 hit. |
|PROSITE||PS50188. B302_SPRY. 1 hit. |
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
|Accession||Primary (citable) accession number: Q62191|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|