Trim21

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. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses (By similarity).By similarity1 Publication

Catalytic activityⁱ

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	20 – 59	RING-typePROSITE-ProRule annotationAdd BLAST		40
Zinc fingerⁱ	96 – 127	B box-typePROSITE-ProRule annotationAdd BLAST		32

GO - Molecular functionⁱ

DNA binding Source: UniProtKB-KW
identical protein binding Source: MGI
RNA binding Source: UniProtKB-KW
ubiquitin-protein transferase activity Source: UniProtKB
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
innate immune response Source: MGI
negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
negative regulation of protein deubiquitination Source: UniProtKB
negative regulation of viral release from host cell Source: MGI
negative regulation of viral transcription Source: MGI
positive regulation of autophagy Source: UniProtKB
positive regulation of cell cycle Source: UniProtKB
positive regulation of DNA binding transcription factor activity Source: MGI
protein autoubiquitination Source: UniProtKB
protein destabilization Source: UniProtKB
protein monoubiquitination Source: UniProtKB
protein polyubiquitination Source: UniProtKB
protein trimerization Source: MGI
protein ubiquitination Source: UniProtKB
response to interferon-gamma Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Ribonucleoprotein, RNA-binding, Transferase
Biological process	Cell cycle, Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayⁱ	UPA00143

UniPathwayⁱ

UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 ubiquitin-protein ligase TRIM21 (EC:2.3.2.27) Alternative name(s): 52 kDa Ro protein 52 kDa ribonucleoprotein autoantigen Ro/SS-A RING-type E3 ubiquitin transferase TRIM21Curated Ro(SS-A) Sjoegren syndrome type A antigen Short name: SS-A Tripartite motif-containing protein 21
Gene namesⁱ	Name:Trim21 Synonyms:Ro52, Ssa1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Unplaced

Organism-specific databases

MGIⁱ	MGI:106657 Trim21

Keywords - Cellular componentⁱ

Cytoplasm, Cytoplasmic vesicle, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000056116	1 – 470	E3 ubiquitin-protein ligase TRIM21Add BLAST		470

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

EPDⁱ	Q62191
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q62191
PaxDbⁱ	Q62191
PeptideAtlas More...PeptideAtlasⁱ	Q62191
PRIDEⁱ	Q62191

PTM databases

PhosphoSitePlusⁱ	Q62191

PhosphoSitePlusⁱ

Q62191

Expressionⁱ

Inductionⁱ

Up-regulated by IFN.1 Publication

Gene expression databases

CleanExⁱ	MM_TRIM21

CleanExⁱ

MM_TRIM21

Interactionⁱ

Subunit structureⁱ

Homotrimer (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) (By similarity). Interacts (via C-terminus) with IRF8 (via C-terminus). Interacts with ULK1, BECN1 and with ATG8 family members, including GABARAP, GABARAPL1, GABARAPL2 and MAP1LC3C/LC3C. Interacts with TRIM21 and SQSTM1/sequestosome 1. Interacts with IRF3 (By similarity).By similarity1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Ddx41	Q91VN6	6	EBI-6840982,EBI-2551902

With

Entry

#Exp.

IntAct

Notes

Ddx41

Q91VN6

6

EBI-6840982,EBI-2551902

GO - Molecular functionⁱ

identical protein binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActⁱ	Q62191, 23 interactors
STRINGⁱ	10090.ENSMUSP00000033264

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	297 – 299	Combined sources	3
Beta strandⁱ	304 – 306	Combined sources	3
Beta strandⁱ	312 – 315	Combined sources	4
Beta strandⁱ	331 – 338	Combined sources	8
Beta strandⁱ	341 – 351	Combined sources	11
Beta strandⁱ	358 – 364	Combined sources	7
Turnⁱ	377 – 380	Combined sources	4
Beta strandⁱ	381 – 387	Combined sources	7
Beta strandⁱ	390 – 393	Combined sources	4
Beta strandⁱ	395 – 397	Combined sources	3
Beta strandⁱ	399 – 401	Combined sources	3
Beta strandⁱ	408 – 415	Combined sources	8
Turnⁱ	416 – 419	Combined sources	4
Beta strandⁱ	420 – 425	Combined sources	6
Turnⁱ	426 – 430	Combined sources	5
Beta strandⁱ	431 – 436	Combined sources	6
Beta strandⁱ	445 – 450	Combined sources	6
Beta strandⁱ	455 – 457	Combined sources	3
Beta strandⁱ	463 – 465	Combined sources	3

3D structure databases

ProteinModelPortalⁱ	Q62191
SMRⁱ	Q62191
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q62191

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	272 – 470	B30.2/SPRYPROSITE-ProRule annotationAdd BLAST		199

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	188 – 250	Sequence analysisAdd BLAST		63

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

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	20 – 59	RING-typePROSITE-ProRule annotationAdd BLAST		40
Zinc fingerⁱ	96 – 127	B box-typePROSITE-ProRule annotationAdd BLAST		32

Keywords - Domainⁱ

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG2177 Eukaryota ENOG4111G04 LUCA
HOGENOMⁱ	HOG000234134
HOVERGENⁱ	HBG001357
InParanoidⁱ	Q62191
PhylomeDBⁱ	Q62191

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00021 BBOX, 1 hit cd12900 SPRY_PRY_TRIM21, 1 hit
Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR001870 B30.2/SPRY IPR003879 Butyrophylin_SPRY IPR013320 ConA-like_dom_sf IPR006574 PRY IPR035831 PRY/SPRY_TRIM21 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13765 PRY, 1 hit PF00622 SPRY, 1 hit PF00643 zf-B_box, 1 hit PF00097 zf-C3HC4, 1 hit
PRINTSⁱ	PR01406 BBOXZNFINGER PR01407 BUTYPHLNCDUF
SMARTⁱ	View protein in SMART SM00336 BBOX, 1 hit SM00589 PRY, 1 hit SM00184 RING, 1 hit SM00449 SPRY, 1 hit
SUPFAMⁱ	SSF49899 SSF49899, 1 hit
PROSITEⁱ	View protein in PROSITE PS50188 B302_SPRY, 1 hit PS50119 ZF_BBOX, 1 hit PS00518 ZF_RING_1, 1 hit PS50089 ZF_RING_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q62191-1 [UniParc]FASTA Add 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
UniGeneⁱ	Mm.321227

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q62191	Trim21 protein		MOUSE		470
UPI000A314DA4		MUSCR		470
Uncharacterized protein		MOUSE		462

Protein	Similar proteins		Species	Score	Length
Q62191	E3 ubiquitin-protein ligase TRIM21	)	HUMAN		475
TRIM21 isoform 1		PANTR		475
UPI00045DF679		CHLSB		504
E3 ubiquitin-protein ligase TRIM21		MACMU		479
E3 ubiquitin-protein ligase TRIM21		MACFA		479
+136

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	Q62191, 23 interactors
STRINGⁱ	10090.ENSMUSP00000033264

PTM databases

PhosphoSitePlusⁱ	Q62191

PhosphoSitePlusⁱ

Q62191

Proteomic databases

EPDⁱ	Q62191
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q62191
PaxDbⁱ	Q62191
PeptideAtlas More...PeptideAtlasⁱ	Q62191
PRIDEⁱ	Q62191

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Organism-specific databases

MGIⁱ	MGI:106657 Trim21

Phylogenomic databases

eggNOGⁱ	KOG2177 Eukaryota ENOG4111G04 LUCA
HOGENOMⁱ	HOG000234134
HOVERGENⁱ	HBG001357
InParanoidⁱ	Q62191
PhylomeDBⁱ	Q62191

Enzyme and pathway databases

UniPathwayⁱ	UPA00143

UniPathwayⁱ

UPA00143

Miscellaneous databases

EvolutionaryTraceⁱ	Q62191
Protein Ontology More...PROⁱ	PR:Q62191
SOURCEⁱ	Search...

Gene expression databases

CleanExⁱ	MM_TRIM21

CleanExⁱ

MM_TRIM21

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00021 BBOX, 1 hit cd12900 SPRY_PRY_TRIM21, 1 hit
Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR001870 B30.2/SPRY IPR003879 Butyrophylin_SPRY IPR013320 ConA-like_dom_sf IPR006574 PRY IPR035831 PRY/SPRY_TRIM21 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13765 PRY, 1 hit PF00622 SPRY, 1 hit PF00643 zf-B_box, 1 hit PF00097 zf-C3HC4, 1 hit
PRINTSⁱ	PR01406 BBOXZNFINGER PR01407 BUTYPHLNCDUF
SMARTⁱ	View protein in SMART SM00336 BBOX, 1 hit SM00589 PRY, 1 hit SM00184 RING, 1 hit SM00449 SPRY, 1 hit
SUPFAMⁱ	SSF49899 SSF49899, 1 hit
PROSITEⁱ	View protein in PROSITE PS50188 B302_SPRY, 1 hit PS50119 ZF_BBOX, 1 hit PS00518 ZF_RING_1, 1 hit PS50089 ZF_RING_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RO52_MOUSE
Accessionⁱ	Q62191Primary (citable) accession number: Q62191
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	November 1, 1996
	Last modified:	March 28, 2018
	This is version 149 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q62191 (RO52_MOUSE)

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E3 ubiquitin-protein ligase TRIM21

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Coiled coil

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Phylogenomic databases

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ