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UniProtKB - Q62191 (RO52_MOUSE)

Entry version 161 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

E3 ubiquitin-protein ligase TRIM21

Gene

Trim21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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) (PubMed:17579016). Represses the innate antiviral response by facilitating the formation of the NMI-IFI35 complex through 'Lys-63'-linked ubiquitination of NMI (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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

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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri20 – 59RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri96 – 127B box-typePROSITE-ProRule annotationAdd BLAST32

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Ribonucleoprotein, RNA-binding, Transferase
Biological processCell cycle, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-3134975, Regulation of innate immune responses to cytosolic DNA
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Trim21
Synonyms:Ro52, Ssa1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:106657, Trim21

<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

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000561161 – 470E3 ubiquitin-protein ligase TRIM21Add BLAST470

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		Q62191

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q62191

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q62191

PeptideAtlas

More...PeptideAtlasi		Q62191

PRoteomics IDEntifications database

More...PRIDEi		Q62191

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		301631

PTM databases

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q62191

<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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by IFN.1 Publication

<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>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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) (PubMed:17579016).

Interacts (via the SPRY domain) with NMI (via coiled-coil domain); the interaction promotes 'Lys-63'-linked ubiquitination of NMI (By similarity).

Interacts with IFI35 and NMI; the interaction facilitates NMI-IFI35 complex formation (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q62191, 24 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000033264

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q62191, protein

<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

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q62191

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q62191

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini272 – 470B30.2/SPRYPROSITE-ProRule annotationAdd BLAST199

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili188 – 250Sequence analysisAdd BLAST63

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The coiled-coil is necessary for the cytoplasmic localization.By similarity
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. The RING-type zinc finger is necessary for ubiquitination of NMI.By similarity
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 B30.2/SPRY domain is necessary for the interaction with NMI.By similarity

<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

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri20 – 59RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri96 – 127B box-typePROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2177, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q62191

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q62191

Family and domain databases

Conserved Domains Database

More...CDDi		cd12900, SPRY_PRY_TRIM21, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.120.920, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01406, BBOXZNFINGER
PR01407, BUTYPHLNCDUF

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00336, BBOX, 1 hit
SM00589, PRY, 1 hit
SM00184, RING, 1 hit
SM00449, SPRY, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49899, SSF49899, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i393AE5AFD254855B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U7K7Q3U7K7_MOUSE
E3 ubiquitin-protein ligase TRIM21
Trim21
462Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L27990 mRNA Translation: AAB51154.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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

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 entryMethodResolution (Å)ChainPositionsPDBsum
2VOKX-ray1.30A/B291-470[»]
3ZO0X-ray1.99B291-470[»]
SMRiQ62191
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ62191, 24 interactors
STRINGi10090.ENSMUSP00000033264

PTM databases

PhosphoSitePlusiQ62191

Proteomic databases

EPDiQ62191
MaxQBiQ62191
PaxDbiQ62191
PeptideAtlasiQ62191
PRIDEiQ62191
ProteomicsDBi301631

Organism-specific databases

MGIiMGI:106657, Trim21

Phylogenomic databases

eggNOGiKOG2177, Eukaryota
InParanoidiQ62191
PhylomeDBiQ62191

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-MMU-3134975, Regulation of innate immune responses to cytosolic DNA
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Trim21, mouse
EvolutionaryTraceiQ62191

Protein Ontology

More...PROi		PR:Q62191
RNActiQ62191, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

CDDicd12900, SPRY_PRY_TRIM21, 1 hit
Gene3Di2.60.120.920, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
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
PfamiView protein in Pfam
PF13765, PRY, 1 hit
PF00622, SPRY, 1 hit
PF00643, zf-B_box, 1 hit
PF00097, zf-C3HC4, 1 hit
PRINTSiPR01406, BBOXZNFINGER
PR01407, BUTYPHLNCDUF
SMARTiView protein in SMART
SM00336, BBOX, 1 hit
SM00589, PRY, 1 hit
SM00184, RING, 1 hit
SM00449, SPRY, 1 hit
SUPFAMiSSF49899, SSF49899, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRO52_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q62191
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 7, 2021
This is version 161 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Keywords - Technical termi

3D-structure, 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
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