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Q62191

- RO52_MOUSE

UniProt

Q62191 - RO52_MOUSE

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Protein

E3 ubiquitin-protein ligase TRIM21

Gene

Trim21

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 5940RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 12732B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  3. negative regulation of protein deubiquitination Source: UniProtKB
  4. positive regulation of cell cycle Source: UniProtKB
  5. protein autoubiquitination Source: UniProtKB
  6. protein destabilization Source: UniProtKB
  7. protein monoubiquitination Source: UniProtKB
  8. protein polyubiquitination Source: UniProtKB
  9. protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Ribonucleoprotein

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Trim21
Synonyms:Ro52, Ssa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:106657. Trim21.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. 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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470E3 ubiquitin-protein ligase TRIM21PRO_0000056116Add
BLAST

Post-translational modificationi

Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization (By similarity). Autoubiquitinated.By similarity1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ62191.
PaxDbiQ62191.
PRIDEiQ62191.

PTM databases

PhosphoSiteiQ62191.

Expressioni

Inductioni

Up-regulated by IFN.1 Publication

Gene expression databases

CleanExiMM_TRIM21.
GenevestigatoriQ62191.

Interactioni

Subunit structurei

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).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Ddx41Q91VN66EBI-6840982,EBI-2551902

Protein-protein interaction databases

IntActiQ62191. 21 interactions.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi297 – 2993Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi331 – 3388Combined sources
Beta strandi341 – 35111Combined sources
Beta strandi358 – 3647Combined sources
Turni377 – 3804Combined sources
Beta strandi381 – 3877Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi408 – 4158Combined sources
Turni416 – 4194Combined sources
Beta strandi420 – 4256Combined sources
Turni426 – 4305Combined sources
Beta strandi431 – 4366Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi455 – 4573Combined sources
Beta strandi463 – 4653Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VOKX-ray1.30A/B291-470[»]
3ZO0X-ray1.99B291-470[»]
ProteinModelPortaliQ62191.
SMRiQ62191. Positions 4-78, 94-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62191.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 470199B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili188 – 25063Sequence AnalysisAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 5940RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 12732B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG276395.
HOGENOMiHOG000234134.
HOVERGENiHBG001357.
InParanoidiQ62191.
PhylomeDBiQ62191.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PRINTSiPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62191-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPSTTSKMS LEKMWEEVTC SICLDPMVEP MSIECGHCFC KECIFEVGKN
60 70 80 90 100
GGSSCPECRQ QFLLRNLRPN RHIANMVENL KQIAQNTKKS TQETHCMKHG
110 120 130 140 150
EKLHLFCEED GQALCWVCAQ SGKHRDHTRV PIEEAAKVYQ EKIHVVLEKL
160 170 180 190 200
RKGKELAEKM EMDLTMQRTD WKRNIDTQKS RIHAEFALQN SLLAQEEQRQ
210 220 230 240 250
LQRLEKDQRE YLRLLGKKEA ELAEKNQALQ ELISELERRI RGSELELLQE
260 270 280 290 300
VRIILERSGS WNLDTLDIDA PDLTSTCPVP GRKKMLRTCW VHITLDRNTA
310 320 330 340 350
NSWLIISKDR RQVRMGDTHQ NVSDNKERFS NYPMVLGAQR FSSGKMYWEV
360 370 380 390 400
DVTQKEAWDL GVCRDSVQRK GQFSLSPENG FWTIWLWQDS YEAGTSPQTT
410 420 430 440 450
LHIQVPPCQI GIFVDYEAGV VSFYNITDHG SLIYTFSECV FAGPLRPFFN
460 470
VGFNYSGGNA APLKLCPLKM
Length:470
Mass (Da):54,175
Last modified:November 1, 1996 - v1
Checksum:i393AE5AFD254855B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27990 mRNA. Translation: AAB51154.1.
UniGeneiMm.321227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27990 mRNA. Translation: AAB51154.1 .
UniGenei Mm.321227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VOK X-ray 1.30 A/B 291-470 [» ]
3ZO0 X-ray 1.99 B 291-470 [» ]
ProteinModelPortali Q62191.
SMRi Q62191. Positions 4-78, 94-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q62191. 21 interactions.

PTM databases

PhosphoSitei Q62191.

Proteomic databases

MaxQBi Q62191.
PaxDbi Q62191.
PRIDEi Q62191.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:106657. Trim21.

Phylogenomic databases

eggNOGi NOG276395.
HOGENOMi HOG000234134.
HOVERGENi HBG001357.
InParanoidi Q62191.
PhylomeDBi Q62191.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei Q62191.
PROi Q62191.
SOURCEi Search...

Gene expression databases

CleanExi MM_TRIM21.
Genevestigatori Q62191.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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 ]
Pfami PF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
PRINTSi PR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTi SM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiRO52_MOUSE
AccessioniPrimary (citable) accession number: Q62191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3