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Entry version 160 (16 Oct 2019)
Sequence version 2 (15 Jul 1998)
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Protein

V(D)J recombination-activating protein 2

Gene

Rag2

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

Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi419Zinc 12 Publications1
Metal bindingi423Zinc 12 Publications1
Metal bindingi446Zinc 22 Publications1
Metal bindingi452Zinc 22 Publications1
Metal bindingi455Zinc 12 Publications1
Metal bindingi458Zinc 12 Publications1
Metal bindingi478Zinc 22 Publications1
Metal bindingi481Zinc 22 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri416 – 484PHD-type; atypicalAdd BLAST69

<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

GO - Biological processi

<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 functionChromatin regulator
Biological processDNA recombination
LigandMetal-binding, Zinc

<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_and_taxonomy_section">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:
V(D)J recombination-activating protein 2
Short name:
RAG-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Rag2
Synonyms:Rag-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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: Chromosome 2

Organism-specific databases

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

More...
MGIi
MGI:97849 Rag2

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are viable but fail to produce mature B or T-lymphocytes. Very immature lymphoid cells are present in primary lymphoid organs. These cells do not rearrange their immunoglobulin or T-cell receptor loci. Double knockout with TREX1 does not show a visible phenotype.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi128D → N: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi199E → Q: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi202D → N: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi280E → Q: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi310D → N: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi358D → N: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi374D → N: Does not affect the endonuclease activity of the RAG complex. 1 Publication1
Mutagenesisi402Y → A: Reduced interaction with histones. 1 Publication1
Mutagenesisi403N → A: Reduced interaction with histones. 1 Publication1
Mutagenesisi406D → A: Reduced interaction with histones. 1 Publication1
Mutagenesisi407E → A: Reduced interaction with histones. 1 Publication1
Mutagenesisi408D → A: Induces a slight reduction in V(D)J recombination without affecting interaction with histones. 1
Mutagenesisi415Y → A: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding. 1 Publication1
Mutagenesisi440K → A: Binds PtdIns(4,5)P2 at wild-type level. 1 Publication1
Mutagenesisi443M → A: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding. 1 Publication1
Mutagenesisi445Y → A or D: Still binds H3K4me3 and H3R2me2 but with reduced affinity. 1 Publication1
Mutagenesisi453W → R: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding. Impairs enzymatic activity of the RAG complex. 2 Publications1
Mutagenesisi464R → A: Leads to a strong reduction in PtdIns(4,5)P2-binding. 1 Publication1
Mutagenesisi468H → A: Leads to a strong reduction in PtdIns(4,5)P2-binding. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001671381 – 527V(D)J recombination-activating protein 2Add BLAST527

Proteomic databases

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

More...
PaxDbi
P21784

PRoteomics IDEntifications database

More...
PRIDEi
P21784

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P21784

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

More...
PhosphoSitePlusi
P21784

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Maturing lymphoid cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000032864 Expressed in 43 organ(s), highest expression level in thymus

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P21784 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P21784 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P159194EBI-7602123,EBI-7602168

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202575, 1 interactor

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P21784

Database of interacting proteins

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DIPi
DIP-46179N

Protein interaction database and analysis system

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IntActi
P21784, 4 interactors

Molecular INTeraction database

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MINTi
P21784

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000038204

<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

1527
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

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SMRi
P21784

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21784

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi352 – 410Asp/Glu-rich (acidic)Add BLAST59

<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 atypical PHD-type zinc finger recognizes and binds histone H3 trimethylated on 'Lys-4' (H3K4me3). The presence Tyr-445 instead of a carboxylate in classical PHD-type zinc fingers results in an enhanced binding to H3K4me3 in presence of dimethylated on 'Arg-2' (H3R2me2) rather than inhibited. The atypical PHD-type zinc finger also binds various phosphoinositides, such as phosphatidylinositol 3,4-bisphosphate binding (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate binding (PtdIns(3,5)P2), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate binding (PtdIns(3,4,5)P3).2 Publications

<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 RAG2 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri416 – 484PHD-type; atypicalAdd BLAST69

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IJ5S Eukaryota
ENOG4110081 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000012559

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000237346

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21784

KEGG Orthology (KO)

More...
KOi
K10988

Identification of Orthologs from Complete Genome Data

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OMAi
PTGVFHF

Database of Orthologous Groups

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OrthoDBi
687724at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P21784

TreeFam database of animal gene trees

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TreeFami
TF331236

Family and domain databases

Conserved Domains Database

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CDDi
cd15569 PHD_RAG2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.120.10.80, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011043 Gal_Oxase/kelch_b-propeller
IPR015915 Kelch-typ_b-propeller
IPR004321 RAG2
IPR025162 RAG2_PHD
IPR011011 Znf_FYVE_PHD

The PANTHER Classification System

More...
PANTHERi
PTHR10960 PTHR10960, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03089 RAG2, 1 hit
PF13341 RAG2_PHD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50965 SSF50965, 1 hit
SSF57903 SSF57903, 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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P21784-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLQMVTVGH NIALIQPGFS LMNFDGQVFF FGQKGWPKRS CPTGVFHFDI
60 70 80 90 100
KQNHLKLKPA IFSKDSCYLP PLRYPATCSY KGSIDSDKHQ YIIHGGKTPN
110 120 130 140 150
NELSDKIYIM SVACKNNKKV TFRCTEKDLV GDVPEPRYGH SIDVVYSRGK
160 170 180 190 200
SMGVLFGGRS YMPSTQRTTE KWNSVADCLP HVFLIDFEFG CATSYILPEL
210 220 230 240 250
QDGLSFHVSI ARNDTVYILG GHSLASNIRP ANLYRIRVDL PLGTPAVNCT
260 270 280 290 300
VLPGGISVSS AILTQTNNDE FVIVGGYQLE NQKRMVCSLV SLGDNTIEIS
310 320 330 340 350
EMETPDWTSD IKHSKIWFGS NMGNGTIFLG IPGDNKQAMS EAFYFYTLRC
360 370 380 390 400
SEEDLSEDQK IVSNSQTSTE DPGDSTPFED SEEFCFSAEA TSFDGDDEFD
410 420 430 440 450
TYNEDDEDDE SVTGYWITCC PTCDVDINTW VPFYSTELNK PAMIYCSHGD
460 470 480 490 500
GHWVHAQCMD LEERTLIHLS EGSNKYYCNE HVQIARALQT PKRNPPLQKP
510 520
PMKSLHKKGS GKVLTPAKKS FLRRLFD
Length:527
Mass (Da):59,074
Last modified:July 15, 1998 - v2
<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:i51086F95A4A664A7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M64796 mRNA Translation: AAB82302.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS16462.1

Protein sequence database of the Protein Information Resource

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PIRi
A34852

NCBI Reference Sequences

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RefSeqi
NP_033046.1, NM_009020.3
XP_017172095.1, XM_017316606.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000044031; ENSMUSP00000038204; ENSMUSG00000032864
ENSMUST00000111227; ENSMUSP00000106858; ENSMUSG00000032864

Database of genes from NCBI RefSeq genomes

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GeneIDi
19374

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:19374

UCSC genome browser

More...
UCSCi
uc008lhj.1 mouse

<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
M64796 mRNA Translation: AAB82302.1
CCDSiCCDS16462.1
PIRiA34852
RefSeqiNP_033046.1, NM_009020.3
XP_017172095.1, XM_017316606.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JWONMR-A414-487[»]
2V83X-ray2.40A/B/C414-487[»]
2V85X-ray2.00A/B414-487[»]
2V86X-ray2.05A/B414-487[»]
2V87X-ray1.80A/B414-487[»]
2V88X-ray2.00A/B414-487[»]
2V89X-ray1.10A/B414-487[»]
4WWXX-ray3.20X/Y2-350[»]
5ZDZX-ray2.80B/D1-387[»]
5ZE0X-ray2.75B/D1-387[»]
5ZE1X-ray3.00B/D1-387[»]
5ZE2X-ray3.30B/D1-387[»]
6CG0electron microscopy3.17B/D1-520[»]
6CIJelectron microscopy3.90B/D1-520[»]
6CIKX-ray3.15B/D1-359[»]
6CILX-ray4.15B/D1-359[»]
6CIMX-ray3.60B/D1-359[»]
SMRiP21784
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi202575, 1 interactor
CORUMiP21784
DIPiDIP-46179N
IntActiP21784, 4 interactors
MINTiP21784
STRINGi10090.ENSMUSP00000038204

PTM databases

iPTMnetiP21784
PhosphoSitePlusiP21784

Proteomic databases

PaxDbiP21784
PRIDEiP21784

Genome annotation databases

EnsembliENSMUST00000044031; ENSMUSP00000038204; ENSMUSG00000032864
ENSMUST00000111227; ENSMUSP00000106858; ENSMUSG00000032864
GeneIDi19374
KEGGimmu:19374
UCSCiuc008lhj.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5897
MGIiMGI:97849 Rag2

Phylogenomic databases

eggNOGiENOG410IJ5S Eukaryota
ENOG4110081 LUCA
GeneTreeiENSGT00390000012559
HOGENOMiHOG000237346
InParanoidiP21784
KOiK10988
OMAiPTGVFHF
OrthoDBi687724at2759
PhylomeDBiP21784
TreeFamiTF331236

Miscellaneous databases

EvolutionaryTraceiP21784

Protein Ontology

More...
PROi
PR:P21784

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000032864 Expressed in 43 organ(s), highest expression level in thymus
ExpressionAtlasiP21784 baseline and differential
GenevisibleiP21784 MM

Family and domain databases

CDDicd15569 PHD_RAG2, 1 hit
Gene3Di2.120.10.80, 1 hit
InterProiView protein in InterPro
IPR011043 Gal_Oxase/kelch_b-propeller
IPR015915 Kelch-typ_b-propeller
IPR004321 RAG2
IPR025162 RAG2_PHD
IPR011011 Znf_FYVE_PHD
PANTHERiPTHR10960 PTHR10960, 1 hit
PfamiView protein in Pfam
PF03089 RAG2, 1 hit
PF13341 RAG2_PHD, 1 hit
SUPFAMiSSF50965 SSF50965, 1 hit
SSF57903 SSF57903, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiRAG2_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: P21784
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 15, 1998
Last modified: October 16, 2019
This is version 160 of the entry and version 2 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, Complete proteome, Reference proteome

Documents

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