RAG2_MOUSE
ID RAG2_MOUSE Reviewed; 527 AA.
AC P21784;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=V(D)J recombination-activating protein 2;
DE Short=RAG-2;
GN Name=Rag2; Synonyms=Rag-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2360047; DOI=10.1126/science.2360047;
RA Oettinger M.A., Schatz D.G., Gorka C., Baltimore D.;
RT "RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J
RT recombination.";
RL Science 248:1517-1523(1990).
RN [2]
RP SEQUENCE REVISION TO 458.
RA Oettinger M.A., Schatz D.G., Gorka C., Baltimore D.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=1547487; DOI=10.1016/0092-8674(92)90029-c;
RA Shinkai Y., Rathbun G., Lam K.P., Oltz E.M., Stewart V., Mendelsohn M.,
RA Charron J., Datta M., Young F., Stall A.M., Alt F.W.;
RT "RAG-2-deficient mice lack mature lymphocytes owing to inability to
RT initiate V(D)J rearrangement.";
RL Cell 68:855-867(1992).
RN [4]
RP FUNCTION, AND INTERACTION WITH RAG1.
RX PubMed=8521468; DOI=10.1016/0092-8674(95)90116-7;
RA McBlane J.F., van Gent D.C., Ramsden D.A., Romeo C., Cuomo C.A.,
RA Gellert M., Oettinger M.A.;
RT "Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2
RT proteins and occurs in two steps.";
RL Cell 83:387-395(1995).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE RAG COMPLEX.
RX PubMed=9094713; DOI=10.1016/s0092-8674(00)80181-6;
RA Agrawal A., Schatz D.G.;
RT "RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA
RT containing signal ends in V(D)J recombination.";
RL Cell 89:43-53(1997).
RN [6]
RP IDENTIFICATION IN THE RAG COMPLEX.
RX PubMed=9184213; DOI=10.1093/emboj/16.10.2665;
RA van Gent D.C., Hiom K., Paull T.T., Gellert M.;
RT "Stimulation of V(D)J cleavage by high mobility group proteins.";
RL EMBO J. 16:2665-2670(1997).
RN [7]
RP MUTAGENESIS OF ASP-128; GLU-199; ASP-202; GLU-280; ASP-310; ASP-358 AND
RP ASP-374.
RX PubMed=10601032; DOI=10.1101/gad.13.23.3059;
RA Landree M.A., Wibbenmeyer J.A., Roth D.B.;
RT "Mutational analysis of RAG1 and RAG2 identifies three catalytic amino
RT acids in RAG1 critical for both cleavage steps of V(D)J recombination.";
RL Genes Dev. 13:3059-3069(1999).
RN [8]
RP FUNCTION, HISTONE-BINDING, AND MUTAGENESIS OF TYR-402; ASN-403; ASP-406 AND
RP GLU-407.
RX PubMed=16111638; DOI=10.1016/j.immuni.2005.07.004;
RA West K.L., Singha N.C., De Ioannes P., Lacomis L., Erdjument-Bromage H.,
RA Tempst P., Cortes P.;
RT "A direct interaction between the RAG2 C terminus and the core histones is
RT required for efficient V(D)J recombination.";
RL Immunity 23:203-212(2005).
RN [9]
RP DOMAIN PHD-TYPE ZINC-FINGER, ZINC-BINDING, HISTONE-BINDING, AND MUTAGENESIS
RP OF TYR-415; MET-443 AND TRP-453.
RX PubMed=18033247; DOI=10.1038/nature06431;
RA Matthews A.G., Kuo A.J., Ramon-Maiques S., Han S., Champagne K.S.,
RA Ivanov D., Gallardo M., Carney D., Cheung P., Ciccone D.N., Walter K.L.,
RA Utz P.J., Shi Y., Kutateladze T.G., Yang W., Gozani O., Oettinger M.A.;
RT "RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J
RT recombination.";
RL Nature 450:1106-1110(2007).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=18724932; DOI=10.1016/j.cell.2008.06.032;
RA Stetson D.B., Ko J.S., Heidmann T., Medzhitov R.;
RT "Trex1 prevents cell-intrinsic initiation of autoimmunity.";
RL Cell 134:587-598(2008).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF TRP-453.
RX PubMed=19524534; DOI=10.1016/j.molcel.2009.05.011;
RA Shimazaki N., Tsai A.G., Lieber M.R.;
RT "H3K4me3 stimulates the V(D)J RAG complex for both nicking and hairpinning
RT in trans in addition to tethering in cis: implications for
RT translocations.";
RL Mol. Cell 34:535-544(2009).
RN [12]
RP FUNCTION.
RX PubMed=19448632; DOI=10.1038/ni.1735;
RA Hewitt S.L., Yin B., Ji Y., Chaumeil J., Marszalek K., Tenthorey J.,
RA Salvagiotto G., Steinel N., Ramsey L.B., Ghysdael J., Farrar M.A.,
RA Sleckman B.P., Schatz D.G., Busslinger M., Bassing C.H., Skok J.A.;
RT "RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning
RT of immunoglobulin loci.";
RL Nat. Immunol. 10:655-664(2009).
RN [13]
RP INTERACTION WITH RAG1.
RX PubMed=19396172; DOI=10.1038/nsmb.1593;
RA Yin F.F., Bailey S., Innis C.A., Ciubotaru M., Kamtekar S., Steitz T.A.,
RA Schatz D.G.;
RT "Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that
RT mediates DNA synapsis.";
RL Nat. Struct. Mol. Biol. 16:499-508(2009).
RN [14]
RP STRUCTURE BY NMR OF 414-487 IN COMPLEX WITH ZINC, ZINC-BINDING,
RP PHOSPHOINOSITIDE-BINDING, AND MUTAGENESIS OF LYS-440; ARG-464 AND HIS-468.
RX PubMed=15964836; DOI=10.1074/jbc.m504731200;
RA Elkin S.K., Ivanov D., Ewalt M., Ferguson C.G., Hyberts S.G., Sun Z.Y.,
RA Prestwich G.D., Yuan J., Wagner G., Oettinger M.A., Gozani O.P.;
RT "A PHD finger motif in the C terminus of RAG2 modulates recombination
RT activity.";
RL J. Biol. Chem. 280:28701-28710(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 414-487 IN COMPLEX WITH ZINC AND
RP H3 PEPTIDE, DOMAIN PHD-TYPE ZINC-FINGER, ZINC-BINDING, HISTONE-BINDING, AND
RP MUTAGENESIS OF TYR-445.
RX PubMed=18025461; DOI=10.1073/pnas.0709170104;
RA Ramon-Maiques S., Kuo A.J., Carney D., Matthews A.G., Oettinger M.A.,
RA Gozani O., Yang W.;
RT "The plant homeodomain finger of RAG2 recognizes histone H3 methylated at
RT both lysine-4 and arginine-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18993-18998(2007).
CC -!- FUNCTION: Core component of the RAG complex, a multiprotein complex
CC that mediates the DNA cleavage phase during V(D)J recombination. V(D)J
CC recombination assembles a diverse repertoire of immunoglobulin and T-
CC cell receptor genes in developing B and T-lymphocytes through
CC rearrangement of different V (variable), in some cases D (diversity),
CC and J (joining) gene segments. DNA cleavage by the RAG complex occurs
CC in 2 steps: a first nick is introduced in the top strand immediately
CC upstream of the heptamer, generating a 3'-hydroxyl group that can
CC attack the phosphodiester bond on the opposite strand in a direct
CC transesterification reaction, thereby creating 4 DNA ends: 2 hairpin
CC coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin
CC structure plays an essential role in the V(D)J recombination reactions
CC and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3)
CC stimulates both the nicking and haipinning steps. The RAG complex also
CC plays a role in pre-B cell allelic exclusion, a process leading to
CC expression of a single immunoglobulin heavy chain allele to enforce
CC clonality and monospecific recognition by the B-cell antigen receptor
CC (BCR) expressed on individual B-lymphocytes. The introduction of DNA
CC breaks by the RAG complex on one immunoglobulin allele induces ATM-
CC dependent repositioning of the other allele to pericentromeric
CC heterochromatin, preventing accessibility to the RAG complex and
CC recombination of the second allele. In the RAG complex, RAG2 is not the
CC catalytic component but is required for all known catalytic activities
CC mediated by RAG1. It probably acts as a sensor of chromatin state that
CC recruits the RAG complex to H3K4me3. {ECO:0000269|PubMed:16111638,
CC ECO:0000269|PubMed:19448632, ECO:0000269|PubMed:19524534,
CC ECO:0000269|PubMed:2360047, ECO:0000269|PubMed:8521468,
CC ECO:0000269|PubMed:9094713}.
CC -!- SUBUNIT: Component of the RAG complex composed of core components RAG1
CC and RAG2, and associated component HMGB1 or HMGB2.
CC {ECO:0000269|PubMed:15964836, ECO:0000269|PubMed:18025461,
CC ECO:0000269|PubMed:9094713, ECO:0000269|PubMed:9184213}.
CC -!- INTERACTION:
CC P21784; P15919: Rag1; NbExp=4; IntAct=EBI-7602123, EBI-7602168;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Maturing lymphoid cells.
CC -!- DOMAIN: The atypical PHD-type zinc finger recognizes and binds histone
CC H3 trimethylated on 'Lys-4' (H3K4me3). The presence Tyr-445 instead of
CC a carboxylate in classical PHD-type zinc fingers results in an enhanced
CC binding to H3K4me3 in presence of dimethylated on 'Arg-2' (H3R2me2)
CC rather than inhibited. The atypical PHD-type zinc finger also binds
CC various phosphoinositides, such as phosphatidylinositol 3,4-
CC bisphosphate binding (PtdIns(3,4)P2), phosphatidylinositol 3,5-
CC bisphosphate binding (PtdIns(3,5)P2), phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-
CC trisphosphate binding (PtdIns(3,4,5)P3). {ECO:0000269|PubMed:18025461,
CC ECO:0000269|PubMed:18033247}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but fail to produce mature B or
CC T-lymphocytes. Very immature lymphoid cells are present in primary
CC lymphoid organs. These cells do not rearrange their immunoglobulin or
CC T-cell receptor loci. Double knockout with TREX1 does not show a
CC visible phenotype. {ECO:0000269|PubMed:1547487,
CC ECO:0000269|PubMed:18724932}.
CC -!- SIMILARITY: Belongs to the RAG2 family. {ECO:0000305}.
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DR EMBL; M64796; AAB82302.1; -; mRNA.
DR CCDS; CCDS16462.1; -.
DR PIR; A34852; A34852.
DR RefSeq; NP_033046.1; NM_009020.3.
DR RefSeq; XP_017172095.1; XM_017316606.1.
DR PDB; 2JWO; NMR; -; A=414-487.
DR PDB; 2V83; X-ray; 2.40 A; A/B/C=414-487.
DR PDB; 2V85; X-ray; 2.00 A; A/B=414-487.
DR PDB; 2V86; X-ray; 2.05 A; A/B=414-487.
DR PDB; 2V87; X-ray; 1.80 A; A/B=414-487.
DR PDB; 2V88; X-ray; 2.00 A; A/B=414-487.
DR PDB; 2V89; X-ray; 1.10 A; A/B=414-487.
DR PDB; 4WWX; X-ray; 3.20 A; X/Y=2-350.
DR PDB; 5ZDZ; X-ray; 2.80 A; B/D=1-387.
DR PDB; 5ZE0; X-ray; 2.75 A; B/D=1-387.
DR PDB; 5ZE1; X-ray; 3.00 A; B/D=1-387.
DR PDB; 5ZE2; X-ray; 3.30 A; B/D=1-387.
DR PDB; 6CG0; EM; 3.17 A; B/D=1-520.
DR PDB; 6CIJ; EM; 3.90 A; B/D=1-520.
DR PDB; 6CIK; X-ray; 3.15 A; B/D=1-359.
DR PDB; 6CIL; X-ray; 4.15 A; B/D=1-359.
DR PDB; 6CIM; X-ray; 3.60 A; B/D=1-359.
DR PDB; 6OEM; EM; 3.60 A; B/D=1-527.
DR PDB; 6OEN; EM; 4.30 A; B/D=1-527.
DR PDB; 6OEO; EM; 3.69 A; B/D=1-527.
DR PDB; 6OEP; EM; 3.70 A; B/D=1-527.
DR PDB; 6OEQ; EM; 4.30 A; B/D=1-527.
DR PDB; 6OER; EM; 3.29 A; B/D=1-527.
DR PDB; 6OES; EM; 3.06 A; B/D=1-527.
DR PDB; 6OET; EM; 3.40 A; B/D=1-527.
DR PDB; 6V0V; EM; 3.61 A; B=1-520.
DR PDB; 6XNX; EM; 2.70 A; B/D=3-361.
DR PDB; 6XNY; EM; 2.90 A; B/D=3-361.
DR PDB; 6XNZ; EM; 3.80 A; B/D=3-361.
DR PDBsum; 2JWO; -.
DR PDBsum; 2V83; -.
DR PDBsum; 2V85; -.
DR PDBsum; 2V86; -.
DR PDBsum; 2V87; -.
DR PDBsum; 2V88; -.
DR PDBsum; 2V89; -.
DR PDBsum; 4WWX; -.
DR PDBsum; 5ZDZ; -.
DR PDBsum; 5ZE0; -.
DR PDBsum; 5ZE1; -.
DR PDBsum; 5ZE2; -.
DR PDBsum; 6CG0; -.
DR PDBsum; 6CIJ; -.
DR PDBsum; 6CIK; -.
DR PDBsum; 6CIL; -.
DR PDBsum; 6CIM; -.
DR PDBsum; 6OEM; -.
DR PDBsum; 6OEN; -.
DR PDBsum; 6OEO; -.
DR PDBsum; 6OEP; -.
DR PDBsum; 6OEQ; -.
DR PDBsum; 6OER; -.
DR PDBsum; 6OES; -.
DR PDBsum; 6OET; -.
DR PDBsum; 6V0V; -.
DR PDBsum; 6XNX; -.
DR PDBsum; 6XNY; -.
DR PDBsum; 6XNZ; -.
DR AlphaFoldDB; P21784; -.
DR SMR; P21784; -.
DR BioGRID; 202575; 2.
DR CORUM; P21784; -.
DR DIP; DIP-46179N; -.
DR IntAct; P21784; 4.
DR MINT; P21784; -.
DR STRING; 10090.ENSMUSP00000038204; -.
DR iPTMnet; P21784; -.
DR PhosphoSitePlus; P21784; -.
DR PaxDb; P21784; -.
DR PRIDE; P21784; -.
DR ProteomicsDB; 300390; -.
DR Antibodypedia; 26023; 274 antibodies from 33 providers.
DR DNASU; 19374; -.
DR Ensembl; ENSMUST00000044031; ENSMUSP00000038204; ENSMUSG00000032864.
DR Ensembl; ENSMUST00000111227; ENSMUSP00000106858; ENSMUSG00000032864.
DR GeneID; 19374; -.
DR KEGG; mmu:19374; -.
DR UCSC; uc008lhj.1; mouse.
DR CTD; 5897; -.
DR MGI; MGI:97849; Rag2.
DR VEuPathDB; HostDB:ENSMUSG00000032864; -.
DR eggNOG; ENOG502QVKU; Eukaryota.
DR GeneTree; ENSGT00390000012559; -.
DR HOGENOM; CLU_516740_0_0_1; -.
DR InParanoid; P21784; -.
DR OMA; WNSVVDC; -.
DR OrthoDB; 687724at2759; -.
DR PhylomeDB; P21784; -.
DR TreeFam; TF331236; -.
DR BioGRID-ORCS; 19374; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; P21784; -.
DR PRO; PR:P21784; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P21784; protein.
DR Bgee; ENSMUSG00000032864; Expressed in thymus and 23 other tissues.
DR ExpressionAtlas; P21784; baseline and differential.
DR Genevisible; P21784; MM.
DR GO; GO:0097519; C:DNA recombinase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:0002358; P:B cell homeostatic proliferation; IMP:MGI.
DR GO; GO:0002326; P:B cell lineage commitment; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IGI:MGI.
DR GO; GO:1904155; P:DN2 thymocyte differentiation; IMP:MGI.
DR GO; GO:0006310; P:DNA recombination; TAS:MGI.
DR GO; GO:0002313; P:mature B cell differentiation involved in immune response; ISO:MGI.
DR GO; GO:0033085; P:negative regulation of T cell differentiation in thymus; ISO:MGI.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:MGI.
DR GO; GO:0002331; P:pre-B cell allelic exclusion; IMP:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
DR GO; GO:0002360; P:T cell lineage commitment; IMP:MGI.
DR GO; GO:0033151; P:V(D)J recombination; IMP:UniProtKB.
DR CDD; cd15569; PHD_RAG2; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR004321; RAG2.
DR InterPro; IPR025162; RAG2_PHD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR10960; PTHR10960; 1.
DR Pfam; PF03089; RAG2; 1.
DR Pfam; PF13341; RAG2_PHD; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA recombination; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..527
FT /note="V(D)J recombination-activating protein 2"
FT /id="PRO_0000167138"
FT ZN_FING 416..484
FT /note="PHD-type; atypical"
FT REGION 359..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15964836,
FT ECO:0000269|PubMed:18025461"
FT MUTAGEN 128
FT /note="D->N: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 199
FT /note="E->Q: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 202
FT /note="D->N: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 280
FT /note="E->Q: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 310
FT /note="D->N: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 358
FT /note="D->N: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 374
FT /note="D->N: Does not affect the endonuclease activity of
FT the RAG complex."
FT /evidence="ECO:0000269|PubMed:10601032"
FT MUTAGEN 402
FT /note="Y->A: Reduced interaction with histones."
FT /evidence="ECO:0000269|PubMed:16111638"
FT MUTAGEN 403
FT /note="N->A: Reduced interaction with histones."
FT /evidence="ECO:0000269|PubMed:16111638"
FT MUTAGEN 406
FT /note="D->A: Reduced interaction with histones."
FT /evidence="ECO:0000269|PubMed:16111638"
FT MUTAGEN 407
FT /note="E->A: Reduced interaction with histones."
FT /evidence="ECO:0000269|PubMed:16111638"
FT MUTAGEN 408
FT /note="D->A: Induces a slight reduction in V(D)J
FT recombination without affecting interaction with histones."
FT MUTAGEN 415
FT /note="Y->A: Abolishes binding to H3K4me3 without affecting
FT phosphoinositide-binding."
FT /evidence="ECO:0000269|PubMed:18033247"
FT MUTAGEN 440
FT /note="K->A: Binds PtdIns(4,5)P2 at wild-type level."
FT /evidence="ECO:0000269|PubMed:15964836"
FT MUTAGEN 443
FT /note="M->A: Abolishes binding to H3K4me3 without affecting
FT phosphoinositide-binding."
FT /evidence="ECO:0000269|PubMed:18033247"
FT MUTAGEN 445
FT /note="Y->A,D: Still binds H3K4me3 and H3R2me2 but with
FT reduced affinity."
FT /evidence="ECO:0000269|PubMed:18025461"
FT MUTAGEN 453
FT /note="W->R: Abolishes binding to H3K4me3 without affecting
FT phosphoinositide-binding. Impairs enzymatic activity of the
FT RAG complex."
FT /evidence="ECO:0000269|PubMed:18033247,
FT ECO:0000269|PubMed:19524534"
FT MUTAGEN 464
FT /note="R->A: Leads to a strong reduction in PtdIns(4,5)P2-
FT binding."
FT /evidence="ECO:0000269|PubMed:15964836"
FT MUTAGEN 468
FT /note="H->A: Leads to a strong reduction in PtdIns(4,5)P2-
FT binding."
FT /evidence="ECO:0000269|PubMed:15964836"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6XNX"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6OER"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6CG0"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6XNX"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6OER"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6XNX"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5ZE0"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6CG0"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5ZE0"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4WWX"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6XNX"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6XNX"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6XNX"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6XNX"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6XNY"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5ZE0"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6XNX"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6XNY"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:6XNX"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:2V89"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:2V89"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2JWO"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2V89"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:2V89"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:2JWO"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:2V89"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:2V89"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:2V89"
FT TURN 479..483
FT /evidence="ECO:0007829|PDB:2V89"
SQ SEQUENCE 527 AA; 59074 MW; 51086F95A4A664A7 CRC64;
MSLQMVTVGH NIALIQPGFS LMNFDGQVFF FGQKGWPKRS CPTGVFHFDI KQNHLKLKPA
IFSKDSCYLP PLRYPATCSY KGSIDSDKHQ YIIHGGKTPN NELSDKIYIM SVACKNNKKV
TFRCTEKDLV GDVPEPRYGH SIDVVYSRGK SMGVLFGGRS YMPSTQRTTE KWNSVADCLP
HVFLIDFEFG CATSYILPEL QDGLSFHVSI ARNDTVYILG GHSLASNIRP ANLYRIRVDL
PLGTPAVNCT VLPGGISVSS AILTQTNNDE FVIVGGYQLE NQKRMVCSLV SLGDNTIEIS
EMETPDWTSD IKHSKIWFGS NMGNGTIFLG IPGDNKQAMS EAFYFYTLRC SEEDLSEDQK
IVSNSQTSTE DPGDSTPFED SEEFCFSAEA TSFDGDDEFD TYNEDDEDDE SVTGYWITCC
PTCDVDINTW VPFYSTELNK PAMIYCSHGD GHWVHAQCMD LEERTLIHLS EGSNKYYCNE
HVQIARALQT PKRNPPLQKP PMKSLHKKGS GKVLTPAKKS FLRRLFD
