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Q62191 (RO52_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM21

EC=6.3.2.-
Alternative name(s):
52 kDa Ro protein
52 kDa ribonucleoprotein autoantigen Ro/SS-A
Ro(SS-A)
Sjoegren syndrome type A antigen
Short name=SS-A
Tripartite motif-containing protein 21
Gene names
Name:Trim21
Synonyms:Ro52, Ssa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-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

Induction

Up-regulated by IFN. Ref.2

Domain

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.

Post-translational modification

Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization By similarity. Autoubiquitinated.

Sequence similarities

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.

Ontologies

Keywords
   Biological processCell cycle
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
Zinc-finger
   LigandDNA-binding
Metal-binding
RNA-binding
Zinc
   Molecular functionLigase
Ribonucleoprotein
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from sequence or structural similarity. Source: UniProtKB

protein monoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein polyubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23222971. Source: IntAct

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ddx41Q91VN66EBI-6840982,EBI-2551902

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470E3 ubiquitin-protein ligase TRIM21
PRO_0000056116

Regions

Domain272 – 470199B30.2/SPRY
Zinc finger20 – 5940RING-type
Zinc finger96 – 12732B box-type
Coiled coil188 – 25063 Potential

Secondary structure

.................................. 470
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62191 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 393AE5AFD254855B

FASTA47054,175
        10         20         30         40         50         60 
MSPSTTSKMS LEKMWEEVTC SICLDPMVEP MSIECGHCFC KECIFEVGKN GGSSCPECRQ 

        70         80         90        100        110        120 
QFLLRNLRPN RHIANMVENL KQIAQNTKKS TQETHCMKHG EKLHLFCEED GQALCWVCAQ 

       130        140        150        160        170        180 
SGKHRDHTRV PIEEAAKVYQ EKIHVVLEKL RKGKELAEKM EMDLTMQRTD WKRNIDTQKS 

       190        200        210        220        230        240 
RIHAEFALQN SLLAQEEQRQ LQRLEKDQRE YLRLLGKKEA ELAEKNQALQ ELISELERRI 

       250        260        270        280        290        300 
RGSELELLQE VRIILERSGS WNLDTLDIDA PDLTSTCPVP GRKKMLRTCW VHITLDRNTA 

       310        320        330        340        350        360 
NSWLIISKDR RQVRMGDTHQ NVSDNKERFS NYPMVLGAQR FSSGKMYWEV DVTQKEAWDL 

       370        380        390        400        410        420 
GVCRDSVQRK GQFSLSPENG FWTIWLWQDS YEAGTSPQTT LHIQVPPCQI GIFVDYEAGV 

       430        440        450        460        470 
VSFYNITDHG SLIYTFSECV FAGPLRPFFN VGFNYSGGNA APLKLCPLKM 

« Hide

References

[1]"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].
Tissue: Macrophage.
[2]"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, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27990 mRNA. Translation: AAB51154.1.
UniGeneMm.321227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VOKX-ray1.30A/B291-470[»]
3ZO0X-ray1.99B291-470[»]
ProteinModelPortalQ62191.
SMRQ62191. Positions 4-78, 95-131, 291-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62191. 21 interactions.

PTM databases

PhosphoSiteQ62191.

Proteomic databases

PaxDbQ62191.
PRIDEQ62191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:106657. Trim21.

Phylogenomic databases

eggNOGNOG276395.
HOGENOMHOG000234134.
HOVERGENHBG001357.
InParanoidQ62191.
PhylomeDBQ62191.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

CleanExMM_TRIM21.
GenevestigatorQ62191.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PRINTSPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ62191.
PROQ62191.
SOURCESearch...

Entry information

Entry nameRO52_MOUSE
AccessionPrimary (citable) accession number: Q62191
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot