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Gene Ontology Classifications
recombination activating gene 1

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Rag1. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene is involved in activation of immunoglobulin V-D-J recombination. The encoded protein is involved in recognition of the DNA substrate, but stable binding and cleavage activity also requires RAG2. Defects in this gene can be the cause of several diseases. [provided by RefSeq, Jul 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
  1. Ahn S et al. (2008) TSCOT+ thymic epithelial cell-mediated sensitive CD4 tolerance by direct presentation. PLoS Biol, 6:e191. (PubMed:18684012)
  2. Bellon SF et al. (1997) Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Biol, 4:586-91. (PubMed:9228952)
  3. Grazini U et al. (2010) The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining. Mol Cell, 37:282-93. (PubMed:20122409)
  4. Hewitt SL et al. (2009) RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning of immunoglobulin loci. Nat Immunol, 10:655-64. (PubMed:19448632)
  5. Hotchkiss RS et al. (1999) Overexpression of Bcl-2 in transgenic mice decreases apoptosis and improves survival in sepsis. J Immunol, 162:4148-56. (PubMed:10201940)
  6. Jones JM et al. (2003) Autoubiquitylation of the V(D)J recombinase protein RAG1. Proc Natl Acad Sci U S A, 100:15446-51. (PubMed:14671314)
  7. Kim DR et al. (1999) Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase. Genes Dev, 13:3070-80. (PubMed:10601033)
  8. Maitra R et al. (2009) A WW-like module in the RAG1 N-terminal domain contributes to previously unidentified protein-protein interactions. Nucleic Acids Res, 37:3301-9. (PubMed:19324890)
  9. Mandal M et al. (2005) The BCL2A1 gene as a pre-T cell receptor-induced regulator of thymocyte survival. J Exp Med, 201:603-14. (PubMed:15728238)
  10. Maraskovsky E et al. (1997) Bcl-2 can rescue T lymphocyte development in interleukin-7 receptor-deficient mice but not in mutant rag-1-/- mice. Cell, 89:1011-9. (PubMed:9215624)
  11. Miyamoto A et al. (2002) Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cdelta. Nature, 416:865-9. (PubMed:11976687)
  12. Mombaerts P et al. (1992) RAG-1-deficient mice have no mature B and T lymphocytes. Cell, 68:869-77. (PubMed:1547488)
  13. Oettinger MA et al. (1990) RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science, 248:1517-23. (PubMed:2360047)
  14. Sadofsky MJ et al. (1993) Expression and V(D)J recombination activity of mutated RAG-1 proteins [published erratum appears in Nucleic Acids Res 1994 Feb 11;22(3):550] Nucleic Acids Res, 21:5644-50. (PubMed:8284210)
  15. Shui JW et al. (2012) HVEM signalling at mucosal barriers provides host defence against pathogenic bacteria. Nature, 488:222-5. (PubMed:22801499)
  16. Yin FF et al. (2009) Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat Struct Mol Biol, 16:499-508. (PubMed:19396172)
  17. Yurchenko V et al. (2003) The RAG1 N-terminal domain is an E3 ubiquitin ligase. Genes Dev, 17:581-5. (PubMed:12629039)

Go Annotations in Tabular Form (Text View) (GO Graph)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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