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Entry version 182 (18 Sep 2019)
Sequence version 2 (27 Jul 2011)
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Protein

V(D)J recombination-activating protein 1

Gene

Rag1

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

Catalytic 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. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage 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 addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination. Mediates polyubiquitination of KPNA1.14 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Mg2+ or Mn2+.1 Publication

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 bindingi266Zinc 11 Publication1
Metal bindingi270Zinc 11 Publication1
Metal bindingi290Zinc 21 Publication1
Metal bindingi293Zinc 11 Publication1
Metal bindingi293Zinc 21 Publication1
Metal bindingi295Zinc 11 Publication1
Metal bindingi305Zinc 31 Publication1
Metal bindingi307Zinc 31 Publication1
Metal bindingi310Zinc 21 Publication1
Metal bindingi313Zinc 21 Publication1
Metal bindingi325Zinc 31 Publication1
Metal bindingi328Zinc 31 Publication1
Metal bindingi355Zinc 41 Publication1
Metal bindingi360Zinc 41 Publication1
Metal bindingi372Zinc 41 Publication1
Metal bindingi376Zinc 41 Publication1
Metal bindingi600Divalent metal cation; catalyticCurated1
Metal bindingi708Divalent metal cation; catalyticCurated1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei893Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site1
Metal bindingi962Divalent metal cation; catalyticCurated1

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 fingeri290 – 329RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri351 – 380RAG1-typePROSITE-ProRule annotationAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi389 – 456NBDPROSITE-ProRule annotationAdd BLAST68

<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, DNA-binding, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Transferase
Biological processDNA recombination, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.19 3474

<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 1
Short name:
RAG-1
Including the following 2 domains:
Endonuclease RAG1 (EC:3.1.-.-)
E3 ubiquitin-protein ligase RAG1 (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase RAG1Curated
<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:Rag1
<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:97848 Rag1

<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 display a severe combined immunodeficiency phenotype. The have a small lymphoid organs that do not contain mature B and T-lymphocytes. The arrest of B- and T-cell differentiation occurs at an early stage and correlates with the inability to perform V(D)J recombination. The frequency of homologous immunoglobulin pairing is much lower. No obvious neuroanatomical or behavioral abnormalities have been observed.1 Publication

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>Mutagenesisi233K → M: Abolishes autoubiquitination. 1 Publication1
Mutagenesisi307H → A: Displays lower E3 ligase activity and affects the joining step of V(D)J recombination. 1 Publication1
Mutagenesisi325C → G: Loss of E3 ligase activity and affects the joining step of V(D)J recombination. 2 Publications1
Mutagenesisi391R → A: Defects in converting nicked products to hairpins. 1 Publication1
Mutagenesisi391R → L: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication1
Mutagenesisi393R → A: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication1
Mutagenesisi401R → A: Allows robust hairpin activity. 1 Publication1
Mutagenesisi402R → A: Defects in converting nicked products to hairpins. 1 Publication1
Mutagenesisi405K → A: Reduced hairpin activity. 1 Publication1
Mutagenesisi406H → A: Allows robust hairpin activity. 1 Publication1
Mutagenesisi407R → A: Impairs DNA-binding and reduces hairpin formation without affecting nicking activity. 1 Publication1
Mutagenesisi443N → A: Impairs DNA-binding; when associated with A-445. 1 Publication1
Mutagenesisi445H → A: Impairs DNA-binding; when associated with A-443. 1 Publication1
Mutagenesisi546D → A: Loss of DNA-binding. 1
Mutagenesisi560D → A: Loss of DNA-binding. 1
Mutagenesisi597E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi600D → A: Loss of cleavage and strand transfer activities. 3 Publications1
Mutagenesisi600D → N: Loss of cleavage (both nicking and hairpin formation). 3 Publications1
Mutagenesisi707Y → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi708D → A: Loss of cleavage and strand transfer activities without affecting allelic exclusion. 4 Publications1
Mutagenesisi708D → N: Loss of cleavage (both nicking and hairpin formation). 4 Publications1
Mutagenesisi709E → A: Impaired cleavage (defective in hairpin formation). 1 Publication1
Mutagenesisi709E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi713R → A or C: Impaired cleavage (both nicking and hairpin formation). 1
Mutagenesisi719E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi725Y → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi760W → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi792D → N: Impaired cleavage. 1 Publication1
Mutagenesisi811E → A: Impaired cleavage. 1 Publication1
Mutagenesisi811E → Q: Loss of DNA-binding. 1 Publication1
Mutagenesisi893W → A: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi893W → F: Capable of nicking and retains some hairpinning. 1 Publication1
Mutagenesisi935Y → A, L or F: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi935Y → S or T: Capable of both nicking and hairpinning. 1 Publication1
Mutagenesisi938K → A: Capable of nicking but defective for hairpinning. 1
Mutagenesisi956W → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi959E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi962E → A or Q: Loss of cleavage (both nicking and hairpin formation). 3 Publications1
Mutagenesisi971F → A or W: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi972R → A: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi973K → A: Moderately defective with 56% of activity. 1 Publication1
Mutagenesisi986D → N: Impaired cleavage. 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_00000560051 – 1040V(D)J recombination-activating protein 1Add BLAST1040

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 in the presence of CDC34/UBCH3.2 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P15919

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

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PaxDbi
P15919

PRoteomics IDEntifications database

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PRIDEi
P15919

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15919

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

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PhosphoSitePlusi
P15919

<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 and central nervous system.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000061311 Expressed in 41 organ(s), highest expression level in thymus

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P15919 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

Homodimer.

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

Interacts with DCAF1, leading to recruitment of the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to ubiquitinate proteins and limit error-prone repair during V(D)J recombination.

6 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202574, 12 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P15919

Database of interacting proteins

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DIPi
DIP-48518N

Protein interaction database and analysis system

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IntActi
P15919, 5 interactors

Molecular INTeraction database

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MINTi
P15919

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000077584

<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

11040
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
P15919

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

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EvolutionaryTracei
P15919

<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

<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 RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity.1 Publication
The NBD (nonamer binding) DNA-binding domain mediates the specific binding to the nonamer RSS motif by forming a tightly interwoven homodimer that binds and synapses 2 nonamer elements, with each NBD making contact with both DNA molecules. Each RSS is composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either 12 bp or 23 bp.PROSITE-ProRule annotation1 Publication

<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 RAG1 family.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri290 – 329RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri351 – 380RAG1-typePROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IKNG Eukaryota
ENOG4110KH0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008679

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000232009

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15919

KEGG Orthology (KO)

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KOi
K10628

Identification of Orthologs from Complete Genome Data

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OMAi
GYHPFEW

Database of Orthologous Groups

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OrthoDBi
85196at2759

TreeFam database of animal gene trees

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TreeFami
TF331926

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024627 RAG1
IPR035714 RAG1_imp-bd
IPR019485 RAG1_Znf
IPR023336 RAG_nonamer-bd_dom
IPR036236 Znf_C2H2_sf
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The PANTHER Classification System

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PANTHERi
PTHR11539 PTHR11539, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12940 RAG1, 1 hit
PF12560 RAG1_imp_bd, 1 hit
PF00097 zf-C3HC4, 1 hit
PF10426 zf-RAG1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00184 RING, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57667 SSF57667, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51487 NBD, 1 hit
PS51765 ZF_RAG1, 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_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.

P15919-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASLPSTLS FSSAPDEIQH PQIKFSEWKF KLFRVRSFEK APEEAQKEKD
60 70 80 90 100
SSEGKPYLEQ SPVVPEKPGG QNSILTQRAL KLHPKFSKKF HADGKSSDKA
110 120 130 140 150
VHQARLRHFC RICGNRFKSD GHSRRYPVHG PVDAKTQSLF RKKEKRVTSW
160 170 180 190 200
PDLIARIFRI DVKADVDSIH PTEFCHDCWS IMHRKFSSSH SQVYFPRKVT
210 220 230 240 250
VEWHPHTPSC DICFTAHRGL KRKRHQPNVQ LSKKLKTVLN HARRDRRKRT
260 270 280 290 300
QARVSSKEVL KKISNCSKIH LSTKLLAVDF PAHFVKSISC QICEHILADP
310 320 330 340 350
VETSCKHLFC RICILRCLKV MGSYCPSCRY PCFPTDLESP VKSFLNILNS
360 370 380 390 400
LMVKCPAQDC NEEVSLEKYN HHVSSHKESK ETLVHINKGG RPRQHLLSLT
410 420 430 440 450
RRAQKHRLRE LKIQVKEFAD KEEGGDVKAV CLTLFLLALR ARNEHRQADE
460 470 480 490 500
LEAIMQGRGS GLQPAVCLAI RVNTFLSCSQ YHKMYRTVKA ITGRQIFQPL
510 520 530 540 550
HALRNAEKVL LPGYHPFEWQ PPLKNVSSRT DVGIIDGLSG LASSVDEYPV
560 570 580 590 600
DTIAKRFRYD SALVSALMDM EEDILEGMRS QDLDDYLNGP FTVVVKESCD
610 620 630 640 650
GMGDVSEKHG SGPAVPEKAV RFSFTVMRIT IEHGSQNVKV FEEPKPNSEL
660 670 680 690 700
CCKPLCLMLA DESDHETLTA ILSPLIAERE AMKSSELTLE MGGIPRTFKF
710 720 730 740 750
IFRGTGYDEK LVREVEGLEA SGSVYICTLC DTTRLEASQN LVFHSITRSH
760 770 780 790 800
AENLQRYEVW RSNPYHESVE ELRDRVKGVS AKPFIETVPS IDALHCDIGN
810 820 830 840 850
AAEFYKIFQL EIGEVYKHPN ASKEERKRWQ ATLDKHLRKR MNLKPIMRMN
860 870 880 890 900
GNFARKLMTQ ETVDAVCELI PSEERHEALR ELMDLYLKMK PVWRSSCPAK
910 920 930 940 950
ECPESLCQYS FNSQRFAELL STKFKYRYEG KITNYFHKTL AHVPEIIERD
960 970 980 990 1000
GSIGAWASEG NESGNKLFRR FRKMNARQSK CYEMEDVLKH HWLYTSKYLQ
1010 1020 1030 1040
KFMNAHNALK SSGFTMNSKE TLGDPLGIED SLESQDSMEF
Length:1,040
Mass (Da):119,185
Last modified:July 27, 2011 - 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:i7C2E6AD68DCBA081
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti609H → L in AAA40028 (PubMed:2598259).Curated1

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
M29475 mRNA Translation: AAA40028.1
AL929569 Genomic DNA No translation available.
CH466519 Genomic DNA Translation: EDL27655.1
BC138342 mRNA Translation: AAI38343.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS16463.1

Protein sequence database of the Protein Information Resource

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PIRi
B33754

NCBI Reference Sequences

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RefSeqi
NP_033045.2, NM_009019.2
XP_006499075.1, XM_006499012.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000078494; ENSMUSP00000077584; ENSMUSG00000061311

Database of genes from NCBI RefSeq genomes

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GeneIDi
19373

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19373

UCSC genome browser

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UCSCi
uc008lhk.2 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
M29475 mRNA Translation: AAA40028.1
AL929569 Genomic DNA No translation available.
CH466519 Genomic DNA Translation: EDL27655.1
BC138342 mRNA Translation: AAI38343.1
CCDSiCCDS16463.1
PIRiB33754
RefSeqiNP_033045.2, NM_009019.2
XP_006499075.1, XM_006499012.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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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
1RMDX-ray2.10A265-380[»]
3GNAX-ray2.40A389-464[»]
3GNBX-ray3.00A389-464[»]
4WWXX-ray3.20B/E392-1008[»]
5ZDZX-ray2.80A/C384-1008[»]
5ZE0X-ray2.75A/C384-1008[»]
5ZE1X-ray3.00A/C384-1008[»]
5ZE2X-ray3.30A/C384-1008[»]
6CG0electron microscopy3.17A/C265-1039[»]
6CIJelectron microscopy3.90A/C265-1040[»]
6CIKX-ray3.15A/C384-1008[»]
6CILX-ray4.15A/C384-1008[»]
6CIMX-ray3.60A/C384-1008[»]
SMRiP15919
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi202574, 12 interactors
CORUMiP15919
DIPiDIP-48518N
IntActiP15919, 5 interactors
MINTiP15919
STRINGi10090.ENSMUSP00000077584

PTM databases

iPTMnetiP15919
PhosphoSitePlusiP15919

Proteomic databases

MaxQBiP15919
PaxDbiP15919
PRIDEiP15919

Genome annotation databases

EnsembliENSMUST00000078494; ENSMUSP00000077584; ENSMUSG00000061311
GeneIDi19373
KEGGimmu:19373
UCSCiuc008lhk.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5896
MGIiMGI:97848 Rag1

Phylogenomic databases

eggNOGiENOG410IKNG Eukaryota
ENOG4110KH0 LUCA
GeneTreeiENSGT00390000008679
HOGENOMiHOG000232009
InParanoidiP15919
KOiK10628
OMAiGYHPFEW
OrthoDBi85196at2759
TreeFamiTF331926

Enzyme and pathway databases

BRENDAi6.3.2.19 3474

Miscellaneous databases

EvolutionaryTraceiP15919

Protein Ontology

More...
PROi
PR:P15919

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000061311 Expressed in 41 organ(s), highest expression level in thymus
GenevisibleiP15919 MM

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR024627 RAG1
IPR035714 RAG1_imp-bd
IPR019485 RAG1_Znf
IPR023336 RAG_nonamer-bd_dom
IPR036236 Znf_C2H2_sf
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR11539 PTHR11539, 1 hit
PfamiView protein in Pfam
PF12940 RAG1, 1 hit
PF12560 RAG1_imp_bd, 1 hit
PF00097 zf-C3HC4, 1 hit
PF10426 zf-RAG1, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS51487 NBD, 1 hit
PS51765 ZF_RAG1, 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 nameiRAG1_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: P15919
Secondary accession number(s): A2AVN8
<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: April 1, 1990
Last sequence update: July 27, 2011
Last modified: September 18, 2019
This is version 182 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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