Tag |
Content |
WERAM ID |
WERAM-Mum-0129 |
Ensembl Protein ID |
ENSMUSP00000106858.1 |
Uniprot Accession |
P21784; RAG2_MOUSE |
Genbank Protein ID |
NP_033046.1 |
Protein Name |
V(D)J recombination-activating protein 2 |
Genbank Nucleotide ID |
NM_009020.3 |
Gene Name |
RAG2 |
Ensembl Information |
|
Details |
Type |
Family |
Domain |
Substrates |
AA |
References (PMIDs) |
Me_Reader |
PHD |
PHD-type |
H3R2me2; K4me3 |
R |
22720264 |
|
Status |
Reviewed |
Classification |
Type |
Family |
E-value |
Score |
Start |
End |
Me_Reader |
PHD |
6.80e-09 |
37.3 |
418 |
483 |
|
Organism |
Mus musculus |
NCBI Taxa ID |
10090 |
Functional Description (View)Functional Description
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. |
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.
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Domain Profile |
Me_Reader PHD
PHD.txt 2 tiClvCgkddeg.......eke.....mvqCdeCd.dwfHlkCvklp...lsslpeg.kswyCpsCke 52 t+C++C ++d + + e m++C+++d +w+H++C++l+ l +l+eg +++yC+++++ ENSMUSP00000106858.1 418 TCCPTC-DVDINtwvpfysT-ElnkpaMIYCSHGDgHWVHAQCMDLEertLIHLSEGsNKYYCNEHVQ 483 79****.9999966666650.155566******9999**********8888888888678*****986 PP
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Protein Sequence (Fasta) | MSLQMVTVGH NIALIQPGFS LMNFDGQVFF FGQKGWPKRS CPTGVFHFDI KQNHLKLKPA 60 IFSKDSCYLP PLRYPATCSY KGSIDSDKHQ YIIHGGKTPN NELSDKIYIM SVACKNNKKV 120 TFRCTEKDLV GDVPEPRYGH SIDVVYSRGK SMGVLFGGRS YMPSTQRTTE KWNSVADCLP 180 HVFLIDFEFG CATSYILPEL QDGLSFHVSI ARNDTVYILG GHSLASNIRP ANLYRIRVDL 240 PLGTPAVNCT VLPGGISVSS AILTQTNNDE FVIVGGYQLE NQKRMVCSLV SLGDNTIEIS 300 EMETPDWTSD IKHSKIWFGS NMGNGTIFLG IPGDNKQAMS EAFYFYTLRC SEEDLSEDQK 360 IVSNSQTSTE DPGDSTPFED SEEFCFSAEA TSFDGDDEFD TYNEDDEDDE SVTGYWITCC 420 PTCDVDINTW VPFYSTELNK PAMIYCSHGD GHWVHAQCMD LEERTLIHLS EGSNKYYCNE 480 HVQIARALQT PKRNPPLQKP PMKSLHKKGS GKVLTPAKKS FLRRLFD 527Protein Fasta Sequence
>ENSMUSP00000106858.1|RAG2|Mus musculus MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPAIFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKVTFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEISEMETPDWTSDIKHSKIWFGSNMGNGTIFLGIPGDNKQAMSEAFYFYTLRCSEEDLSEDQKIVSNSQTSTEDPGDSTPFEDSEEFCFSAEATSFDGDDEFDTYNEDDEDDESVTGYWITCCPTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLEERTLIHLSEGSNKYYCNEHVQIARALQTPKRNPPLQKPPMKSLHKKGSGKVLTPAKKSFLRRLFD
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Nucleotide Sequence (Fasta) | ACACTCTACC CTGCAGCCTT CAGCTTGGCA CAAACTAAAC AGTGACTCTT CCCCAAGTGC 60 CGAGTTTAAT TCCTGGCTTG GCCGAAAGGA TTCAGAGAGG GATAAGCAGC CCCTCTGGCC 120 TTCAGATAAA AGACCTATTC ACAATCAAAA ATGTCCCTGC AGATGGTAAC AGTGGGTCAT 180 AACATAGCCT TAATTCAACC AGGCTTCTCA CTTATGAATT TTGATGGCCA AGTTTTCTTC 240 TTTGGCCAGA AAGGCTGGCC TAAGAGATCC TGTCCTACTG GAGTCTTTCA TTTTGATATA 300 AAACAAAATC ATCTCAAACT GAAGCCTGCA ATCTTCTCTA AAGATTCCTG CTACCTCCCA 360 CCTCTTCGTT ATCCAGCTAC TTGCTCATAC AAAGGCAGCA TAGACTCTGA CAAGCATCAA 420 TATATCATTC ACGGAGGGAA AACACCAAAC AATGAGCTTT CCGATAAGAT TTATATCATG 480 TCTGTCGCTT GCAAGAATAA CAAAAAAGTT ACTTTCCGTT GCACAGAGAA AGACTTAGTA 540 GGAGATGTCC CTGAACCCAG ATACGGCCAT TCCATTGACG TGGTGTATAG TCGAGGGAAA 600 AGCATGGGTG TTCTCTTTGG AGGACGTTCA TACATGCCTT CTACCCAGAG AACCACAGAA 660 AAATGGAATA GTGTAGCTGA CTGCCTACCC CATGTTTTCT TGATAGATTT TGAATTTGGG 720 TGTGCTACAT CATATATTCT CCCAGAACTT CAGGATGGGC TGTCTTTTCA TGTTTCTATT 780 GCCAGAAACG ATACCGTTTA TATTTTGGGA GGACACTCAC TTGCCAGTAA TATACGCCCT 840 GCTAACTTGT ATAGAATAAG AGTGGACCTT CCCCTGGGTA CCCCAGCAGT GAATTGCACA 900 GTCTTGCCAG GAGGAATCTC TGTCTCCAGT GCAATCCTCA CTCAAACAAA CAATGATGAA 960 TTTGTTATTG TGGGTGGTTA TCAGCTGGAA AATCAGAAAA GGATGGTCTG CAGCCTTGTC 1020 TCTCTAGGGG ACAACACGAT TGAAATCAGT GAGATGGAGA CTCCTGACTG GACCTCAGAT 1080 ATTAAGCATA GCAAAATATG GTTTGGAAGC AACATGGGAA ACGGGACTAT TTTCCTTGGC 1140 ATACCAGGAG ACAATAAGCA GGCTATGTCA GAAGCATTCT ATTTCTATAC TTTGAGATGC 1200 TCTGAAGAGG ATTTGAGTGA AGATCAGAAA ATTGTCTCCA ACAGTCAGAC ATCAACAGAA 1260 GATCCTGGGG ACTCCACTCC CTTTGAAGAC TCAGAGGAAT TTTGTTTCAG TGCTGAAGCA 1320 ACCAGTTTTG ATGGTGACGA TGAATTTGAC ACCTACAATG AAGATGATGA AGATGACGAG 1380 TCTGTAACCG GCTACTGGAT AACATGTTGC CCTACTTGTG ATGTTGACAT CAATACCTGG 1440 GTTCCGTTCT ATTCAACGGA GCTCAATAAA CCCGCCATGA TCTATTGTTC TCATGGGGAT 1500 GGGCACTGGG TACATGCCCA GTGCATGGAT TTGGAAGAAC GCACACTCAT CCACTTGTCA 1560 GAAGGAAGCA ACAAGTATTA TTGCAATGAA CATGTACAGA TAGCAAGAGC ATTGCAAACT 1620 CCCAAAAGAA ACCCCCCCTT ACAAAAACCT CCAATGAAAT CCCTCCACAA AAAAGGCTCT 1680 GGGAAAGTCT TGACTCCTGC CAAGAAATCC TTCCTTAGAA GACTGTTTGA TTAATTTAGC 1740 AAAAGCCCCT CAGACTCAGG TATATTGCTC TCTGAATCTA CTTTCAATCA TAAACATTAT 1800 TTTGATTTTT GTTTACTGAA ATCTCTATGT TATGTTTTAG TTATGTGAAT TAAGTGC
1858Nucleotide Fasta Sequence
>ENSMUSP00000106858.1|PHD|Mus musculus ACACTCTACCCTGCAGCCTTCAGCTTGGCACAAACTAAACAGTGACTCTTCCCCAAGTGCCGAGTTTAATTCCTGGCTTGGCCGAAAGGATTCAGAGAGGGATAAGCAGCCCCTCTGGCCTTCAGATAAAAGACCTATTCACAATCAAAAATGTCCCTGCAGATGGTAACAGTGGGTCATAACATAGCCTTAATTCAACCAGGCTTCTCACTTATGAATTTTGATGGCCAAGTTTTCTTCTTTGGCCAGAAAGGCTGGCCTAAGAGATCCTGTCCTACTGGAGTCTTTCATTTTGATATAAAACAAAATCATCTCAAACTGAAGCCTGCAATCTTCTCTAAAGATTCCTGCTACCTCCCACCTCTTCGTTATCCAGCTACTTGCTCATACAAAGGCAGCATAGACTCTGACAAGCATCAATATATCATTCACGGAGGGAAAACACCAAACAATGAGCTTTCCGATAAGATTTATATCATGTCTGTCGCTTGCAAGAATAACAAAAAAGTTACTTTCCGTTGCACAGAGAAAGACTTAGTAGGAGATGTCCCTGAACCCAGATACGGCCATTCCATTGACGTGGTGTATAGTCGAGGGAAAAGCATGGGTGTTCTCTTTGGAGGACGTTCATACATGCCTTCTACCCAGAGAACCACAGAAAAATGGAATAGTGTAGCTGACTGCCTACCCCATGTTTTCTTGATAGATTTTGAATTTGGGTGTGCTACATCATATATTCTCCCAGAACTTCAGGATGGGCTGTCTTTTCATGTTTCTATTGCCAGAAACGATACCGTTTATATTTTGGGAGGACACTCACTTGCCAGTAATATACGCCCTGCTAACTTGTATAGAATAAGAGTGGACCTTCCCCTGGGTACCCCAGCAGTGAATTGCACAGTCTTGCCAGGAGGAATCTCTGTCTCCAGTGCAATCCTCACTCAAACAAACAATGATGAATTTGTTATTGTGGGTGGTTATCAGCTGGAAAATCAGAAAAGGATGGTCTGCAGCCTTGTCTCTCTAGGGGACAACACGATTGAAATCAGTGAGATGGAGACTCCTGACTGGACCTCAGATATTAAGCATAGCAAAATATGGTTTGGAAGCAACATGGGAAACGGGACTATTTTCCTTGGCATACCAGGAGACAATAAGCAGGCTATGTCAGAAGCATTCTATTTCTATACTTTGAGATGCTCTGAAGAGGATTTGAGTGAAGATCAGAAAATTGTCTCCAACAGTCAGACATCAACAGAAGATCCTGGGGACTCCACTCCCTTTGAAGACTCAGAGGAATTTTGTTTCAGTGCTGAAGCAACCAGTTTTGATGGTGACGATGAATTTGACACCTACAATGAAGATGATGAAGATGACGAGTCTGTAACCGGCTACTGGATAACATGTTGCCCTACTTGTGATGTTGACATCAATACCTGGGTTCCGTTCTATTCAACGGAGCTCAATAAACCCGCCATGATCTATTGTTCTCATGGGGATGGGCACTGGGTACATGCCCAGTGCATGGATTTGGAAGAACGCACACTCATCCACTTGTCAGAAGGAAGCAACAAGTATTATTGCAATGAACATGTACAGATAGCAAGAGCATTGCAAACTCCCAAAAGAAACCCCCCCTTACAAAAACCTCCAATGAAATCCCTCCACAAAAAAGGCTCTGGGAAAGTCTTGACTCCTGCCAAGAAATCCTTCCTTAGAAGACTGTTTGATTAATTTAGCAAAAGCCCCTCAGACTCAGGTATATTGCTCTCTGAATCTACTTTCAATCATAAACATTATTTTGATTTTTGTTTACTGAAATCTCTATGTTATGTTTTAGTTATGTGAATTAAGTGC
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Sequence Source |
Ensembl |
Keyword |
KW-0002--3D-structure KW-0156--Chromatin regulator KW-0181--Complete proteome KW-0233--DNA recombination KW-0479--Metal-binding KW-0539--Nucleus KW-1185--Reference proteome KW-0862--Zinc KW-0863--Zinc-finger --
|
Interpro |
IPR011043--Gal_Oxase/kelch_b-propeller IPR015915--Kelch-typ_b-propeller IPR004321--RAG2 IPR025162--RAG2_PHD IPR011011--Znf_FYVE_PHD
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PROSITE |
|
Pfam |
PF03089--RAG2 PF13341--RAG2_PHD
|
Gene Ontology |
GO:0005634--C:nucleus GO:0003682--F:chromatin binding GO:0003677--F:DNA binding GO:0035064--F:methylated histone binding GO:0035091--F:phosphatidylinositol binding GO:0005547--F:phosphatidylinositol-3,4,5-trisphosphate binding GO:0043325--F:phosphatidylinositol-3,4-bisphosphate binding GO:0080025--F:phosphatidylinositol-3,5-bisphosphate binding GO:0005546--F:phosphatidylinositol-4,5-bisphosphate binding GO:0061630--F:ubiquitin protein ligase activity GO:0008270--F:zinc ion binding GO:0030183--P:B cell differentiation GO:0002358--P:B cell homeostatic proliferation GO:0002326--P:B cell lineage commitment GO:0016568--P:chromatin modification GO:0006310--P:DNA recombination GO:0046622--P:positive regulation of organ growth GO:0002331--P:pre-B cell allelic exclusion GO:0016567--P:protein ubiquitination GO:0030217--P:T cell differentiation GO:0033077--P:T cell differentiation in thymus GO:0002360--P:T cell lineage commitment GO:0033151--P:V(D)J recombination
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Orthology |
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Created Date |
25-Jun-2016 |