Rag1
entrez
19373
canonical
uniprot
P15919
canonical
ensembl
ENSMUSG00000061311
resolver
ensp
ENSMUSP00000077584
resolver
enst
ENSMUST00000078494
resolver
genesymbol
Rag1
resolver
uniprot
A2AVN8
resolver
uniprot
Q3TR87
resolver
uniprot_entry
Q3TR87_MOUSE
resolver
uniprot_entry
RAG1_MOUSE
resolver
uniprot_sec
A2AVN8
resolver
amino_acid_sequence
MAASLPSTLSFSSAPDEIQHPQIKFSEWKFKLFRVRSFEKAPEEAQKEKDSSEGKPYLEQSPVVPEKPGGQNSILTQRALKLHPKFSKKFHADGKSSDKAVHQARLRHFCRICGNRFKSDGHSRRYPVHGPVDAKTQSLFRKKEKRVTSWPDLIARIFRIDVKADVDSIHPTEFCHDCWSIMHRKFSSSHSQVYFPRKVTVEWHPHTPSCDICFTAHRGLKRKRHQPNVQLSKKLKTVLNHARRDRRKRTQARVSSKEVLKKISNCSKIHLSTKLLAVDFPAHFVKSISCQICEHILADPVETSCKHLFCRICILRCLKVMGSYCPSCRYPCFPTDLESPVKSFLNILNSLMVKCPAQDCNEEVSLEKYNHHVSSHKESKETLVHINKGGRPRQHLLSLTRRAQKHRLRELKIQVKEFADKEEGGDVKAVCLTLFLLALRARNEHRQADELEAIMQGRGSGLQPAVCLAIRVNTFLSCSQYHKMYRTVKAITGRQIFQPLHALRNAEKVLLPGYHPFEWQPPLKNVSSRTDVGIIDGLSGLASSVDEYPVDTIAKRFRYDSALVSALMDMEEDILEGMRSQDLDDYLNGPFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTVMRITIEHGSQNVKVFEEPKPNSELCCKPLCLMLADESDHETLTAILSPLIAEREAMKSSELTLEMGGIPRTFKFIFRGTGYDEKLVREVEGLEASGSVYICTLCDTTRLEASQNLVFHSITRSHAENLQRYEVWRSNPYHESVEELRDRVKGVSAKPFIETVPSIDALHCDIGNAAEFYKIFQLEIGEVYKHPNASKEERKRWQATLDKHLRKRMNLKPIMRMNGNFARKLMTQETVDAVCELIPSEERHEALRELMDLYLKMKPVWRSSCPAKECPESLCQYSFNSQRFAELLSTKFKYRYEGKITNYFHKTLAHVPEIIERDGSIGAWASEGNESGNKLFRRFRKMNARQSKCYEMEDVLKHHWLYTSKYLQKFMNAHNALKSSGFTMNSKETLGDPLGIEDSLESQDSMEF
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10678172, ECO:0000269|PubMed:12629039, ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:17028591, ECO:0000269|PubMed:19118899, ECO:0000269|PubMed:19396172, ECO:0000269|PubMed:19448632, ECO:0000269|PubMed:19524534, ECO:0000269|PubMed:20122409, ECO:0000269|PubMed:22157821, ECO:0000269|PubMed:2598259, ECO:0000269|PubMed:8521468, ECO:0000269|PubMed:9094713}.
uniprot
proteins
mass_dalton
119185
uniprot
proteins
mutagenesis
MUTAGEN 233; /note="K->M: Abolishes autoubiquitination."; /evidence="ECO:0000269|PubMed:14671314"; MUTAGEN 307; /note="H->A: Displays lower E3 ligase activity and affects the joining step of V(D)J recombination."; /evidence="ECO:0000269|PubMed:20122409"; MUTAGEN 325; /note="C->G: Loss of E3 ligase activity and affects the joining step of V(D)J recombination."; /evidence="ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:20122409"; MUTAGEN 391; /note="R->A: Defects in converting nicked products to hairpins."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 391; /note="R->L: Impairs DNA-binding and hairpin formation while maintaining some nicking activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 393; /note="R->A: Impairs DNA-binding and hairpin formation while maintaining some nicking activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 401; /note="R->A: Allows robust hairpin activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 402; /note="R->A: Defects in converting nicked products to hairpins."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 405; /note="K->A: Reduced hairpin activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 406; /note="H->A: Allows robust hairpin activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 407; /note="R->A: Impairs DNA-binding and reduces hairpin formation without affecting nicking activity."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 443; /note="N->A: Impairs DNA-binding; when associated with A-445."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 445; /note="H->A: Impairs DNA-binding; when associated with A-443."; /evidence="ECO:0000269|PubMed:19396172"; MUTAGEN 546; /note="D->A: Loss of DNA-binding."; MUTAGEN 560; /note="D->A: Loss of DNA-binding."; MUTAGEN 597; /note="E->Q: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 600; /note="D->A: Loss of cleavage and strand transfer activities."; /evidence="ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10601033, ECO:0000269|PubMed:10678172"; MUTAGEN 600; /note="D->N: Loss of cleavage (both nicking and hairpin formation)."; /evidence="ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10601033, ECO:0000269|PubMed:10678172"; MUTAGEN 707; /note="Y->A: Deficient in both nicking and hairpin formation."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 708; /note="D->A: Loss of cleavage and strand transfer activities without affecting allelic exclusion."; /evidence="ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10601033, ECO:0000269|PubMed:10678172, ECO:0000269|PubMed:19448632"; MUTAGEN 708; /note="D->N: Loss of cleavage (both nicking and hairpin formation)."; /evidence="ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10601033, ECO:0000269|PubMed:10678172, ECO:0000269|PubMed:19448632"; MUTAGEN 709; /note="E->A: Impaired cleavage (defective in hairpin formation)."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 709; /note="E->Q: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 713; /note="R->A,C: Impaired cleavage (both nicking and hairpin formation)."; MUTAGEN 719; /note="E->Q: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 725; /note="Y->A: Deficient in both nicking and hairpin formation."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 760; /note="W->A: Deficient in both nicking and hairpin formation."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 792; /note="D->N: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 811; /note="E->A: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 811; /note="E->Q: Loss of DNA-binding."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 893; /note="W->A: Capable of nicking but defective for hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 893; /note="W->F: Capable of nicking and retains some hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 935; /note="Y->A,L,F: Capable of nicking but defective for hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 935; /note="Y->S,T: Capable of both nicking and hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 938; /note="K->A: Capable of nicking but defective for hairpinning."; MUTAGEN 956; /note="W->A: Deficient in both nicking and hairpin formation."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 959; /note="E->Q: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032"; MUTAGEN 962; /note="E->A,Q: Loss of cleavage (both nicking and hairpin formation)."; /evidence="ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10601033, ECO:0000269|PubMed:17028591"; MUTAGEN 971; /note="F->A,W: Capable of nicking but defective for hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 972; /note="R->A: Capable of nicking but defective for hairpinning."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 973; /note="K->A: Moderately defective with 56% of activity."; /evidence="ECO:0000269|PubMed:17028591"; MUTAGEN 986; /note="D->N: Impaired cleavage."; /evidence="ECO:0000269|PubMed:10601032
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated in the presence of CDC34/UBCH3. {ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:19118899}.
uniprot
proteins
protein_family
RAG1 family
uniprot
proteins
pubmed
10601032
uniprot
proteins
pubmed
10601033
uniprot
proteins
pubmed
10678172
uniprot
proteins
pubmed
12629039
uniprot
proteins
pubmed
14671314
uniprot
proteins
pubmed
1547488
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17028591
uniprot
proteins
pubmed
19118899
uniprot
proteins
pubmed
19396172
uniprot
proteins
pubmed
19448632
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19524534
uniprot
proteins
pubmed
20122409
uniprot
proteins
pubmed
22157821
uniprot
proteins
pubmed
2598259
uniprot
proteins
pubmed
8284210
uniprot
proteins
pubmed
8521468
uniprot
proteins
pubmed
9094713
uniprot
proteins
pubmed
9184213
uniprot
proteins
pubmed
9228952
uniprot
proteins
sequence_length
1040
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820, ECO:0000269|PubMed:8284210}.
uniprot
proteins