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Protein Page:
RAG1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RAG1 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 a 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. Homodimer. Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. Maturing lymphoid cells. Belongs to the RAG1 family. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.-; Ubiquitin conjugating system; EC 3.1.-.-; Ubiquitin ligase; EC 6.3.2.19; Ligase; DNA binding protein
Cellular Component: nucleus
Molecular Function: protein binding; acid-amino acid ligase activity; protein homodimerization activity; DNA binding; zinc ion binding; histone binding; sequence-specific DNA binding; endonuclease activity; metal ion binding; ubiquitin-protein ligase activity
Biological Process: adaptive immune response; protein autoubiquitination; V(D)J recombination; thymus development; pre-B cell allelic exclusion; T cell differentiation in the thymus; negative regulation of caspase activity; DNA recombination; histone monoubiquitination; B cell differentiation; immune response; regulation of T cell differentiation; T cell homeostasis
Reference #:  P15918 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase RAG1; Endonuclease RAG1; MGC43321; RAG-1; RAG1; recombination activating gene 1; recombination activating protein 1; RING finger protein 74; RNF74; V(D)J recombination-activating protein 1
Gene Symbols: RAG1
Molecular weight: 119,097 Da
Basal Isoelectric point: 8.94  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RAG1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
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Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K73-ub LDKADGQkPVPTQPL
0 1 K96 KKFHDNEKARGKAIH
0 1 Y127-p ADEHNRRyPVHGPVD
0 1 Y195-p SSAPCEVyFPRNVTM
0 1 T238-p QLSKKLKtVLDQARQ
0 2 K322-ub VCILRCLkVMGSYCP
0 1 S530-p QPPLKNVsSsTDVGI
1 0 S531 PPLKNVsSsTDVGII
0 1 S532-p PLKNVsSsTDVGIID
0 1 T633 SFTIMKITIAHSSQN
0 1 K903-ub WRSSCPAkECPESLC
0 1 K983-ac KMNARQSkCYEMEDV
  mouse

 
N72 PEKPGGQNSILTQRA
K95-ac KKFHADGkSSDKAVH
Y126 SDGHSRRYPVHGPVD
Y194 SSSHSQVYFPRKVTV
T237 QLSKKLKTVLNHARR
K319 ICILRCLKVMGSYCP
S527 QPPLKNVSsRTDVGI
S528-p PPLKNVSsRTDVGII
R529 PLKNVSsRTDVGIID
T630-p SFTVMRItIEHGSQN
K900 WRSSCPAKECPESLC
K980 KMNARQSKCYEMEDV
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