Rag2
entrez
19374
canonical
uniprot
P21784
canonical
ensembl
ENSMUSG00000032864
resolver
ensp
ENSMUSP00000038204
resolver
ensp
ENSMUSP00000106858
resolver
enst
ENSMUST00000044031
resolver
enst
ENSMUST00000111227
resolver
genesymbol
Rag2
resolver
genesymbol_syn
Rag-2
resolver
uniprot
Q542D1
resolver
uniprot_entry
Q542D1_MOUSE
resolver
uniprot_entry
RAG2_MOUSE
resolver
amino_acid_sequence
MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPAIFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKVTFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEISEMETPDWTSDIKHSKIWFGSNMGNGTIFLGIPGDNKQAMSEAFYFYTLRCSEEDLSEDQKIVSNSQTSTEDPGDSTPFEDSEEFCFSAEATSFDGDDEFDTYNEDDEDDESVTGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARALQTPKRNPPLQKPPMKSLHKKGSGKVLTPAKKSFLRRLFD
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:16111638, ECO:0000269|PubMed:19448632, ECO:0000269|PubMed:19524534, ECO:0000269|PubMed:2360047, ECO:0000269|PubMed:8521468, ECO:0000269|PubMed:9094713}.
uniprot
proteins
mass_dalton
59074
uniprot
proteins
mutagenesis
MUTAGEN 128; /note="D->N: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 199; /note="E->Q: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 202; /note="D->N: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 280; /note="E->Q: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 310; /note="D->N: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 358; /note="D->N: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 374; /note="D->N: Does not affect the endonuclease activity of the RAG complex."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 402; /note="Y->A: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:16111638"; MUTAGEN 403; /note="N->A: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:16111638"; MUTAGEN 406; /note="D->A: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:16111638"; MUTAGEN 407; /note="E->A: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:16111638"; MUTAGEN 408; /note="D->A: Induces a slight reduction in V(D)J recombination without affecting interaction with histones."; MUTAGEN 415; /note="Y->A: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding."; /evidence="ECO:0000269|PubMed:18033247"; MUTAGEN 440; /note="K->A: Binds PtdIns(4,5)P2 at wild-type level."; /evidence="ECO:0000269|PubMed:15964836"; MUTAGEN 443; /note="M->A: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding."; /evidence="ECO:0000269|PubMed:18033247"; MUTAGEN 445; /note="Y->A,D: Still binds H3K4me3 and H3R2me2 but with reduced affinity."; /evidence="ECO:0000269|PubMed:18025461"; MUTAGEN 453; /note="W->R: Abolishes binding to H3K4me3 without affecting phosphoinositide-binding. Impairs enzymatic activity of the RAG complex."; /evidence="ECO:0000269|PubMed:18033247, ECO:0000269|PubMed:19524534"; MUTAGEN 464; /note="R->A: Leads to a strong reduction in PtdIns(4,5)P2-binding."; /evidence="ECO:0000269|PubMed:15964836"; MUTAGEN 468; /note="H->A: Leads to a strong reduction in PtdIns(4,5)P2-binding."; /evidence="ECO:0000269|PubMed:15964836
uniprot
proteins
protein_family
RAG2 family
uniprot
proteins
pubmed
10601032
uniprot
proteins
pubmed
1547487
uniprot
proteins
pubmed
15964836
uniprot
proteins
pubmed
16111638
uniprot
proteins
pubmed
18025461
uniprot
proteins
pubmed
18033247
uniprot
proteins
pubmed
18724932
uniprot
proteins
pubmed
19396172
uniprot
proteins
pubmed
19448632
uniprot
proteins
pubmed
19524534
uniprot
proteins
pubmed
2360047
uniprot
proteins
pubmed
8521468
uniprot
proteins
pubmed
9094713
uniprot
proteins
pubmed
9184213
uniprot
proteins
sequence_length
527
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus.
uniprot
proteins