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P15919

- RAG1_MOUSE

UniProt

P15919 - RAG1_MOUSE

Protein

V(D)J recombination-activating protein 1

Gene

Rag1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 KPNA1.14 Publications

    Cofactori

    Binds 1 divalent metal cation per subunit. Magnesium or manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi266 – 2661Zinc 11 Publication
    Metal bindingi270 – 2701Zinc 11 Publication
    Metal bindingi290 – 2901Zinc 21 Publication
    Metal bindingi293 – 2931Zinc 11 Publication
    Metal bindingi293 – 2931Zinc 21 Publication
    Metal bindingi295 – 2951Zinc 11 Publication
    Metal bindingi305 – 3051Zinc 31 Publication
    Metal bindingi307 – 3071Zinc 31 Publication
    Metal bindingi310 – 3101Zinc 21 Publication
    Metal bindingi313 – 3131Zinc 21 Publication
    Metal bindingi325 – 3251Zinc 31 Publication
    Metal bindingi328 – 3281Zinc 31 Publication
    Metal bindingi355 – 3551Zinc 41 Publication
    Metal bindingi360 – 3601Zinc 41 Publication
    Metal bindingi372 – 3721Zinc 41 Publication
    Metal bindingi376 – 3761Zinc 41 Publication
    Metal bindingi600 – 6001Divalent metal cation; catalyticCurated
    Metal bindingi708 – 7081Divalent metal cation; catalyticCurated
    Sitei893 – 8931Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site
    Metal bindingi962 – 9621Divalent metal cation; catalyticCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri290 – 32940RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 38030RAG1-typeAdd
    BLAST
    DNA bindingi389 – 45668NBDPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. endonuclease activity Source: UniProtKB
    3. histone binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. sequence-specific DNA binding Source: UniProtKB
    8. ubiquitin-protein transferase activity Source: UniProtKB
    9. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. adaptive immune response Source: MGI
    2. B cell differentiation Source: UniProtKB
    3. death Source: MGI
    4. DNA recombination Source: MGI
    5. histone monoubiquitination Source: UniProtKB
    6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    7. negative regulation of T cell apoptotic process Source: MGI
    8. negative regulation of thymocyte apoptotic process Source: MGI
    9. nucleic acid phosphodiester bond hydrolysis Source: GOC
    10. pre-B cell allelic exclusion Source: UniProtKB
    11. protein autoubiquitination Source: UniProtKB
    12. regulation of T cell differentiation Source: MGI
    13. T cell differentiation in thymus Source: UniProtKB
    14. T cell homeostasis Source: MGI
    15. thymus development Source: MGI
    16. V(D)J recombination Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Endonuclease, Hydrolase, Ligase, Nuclease

    Keywords - Biological processi

    DNA recombination, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V(D)J recombination-activating protein 1
    Short name:
    RAG-1
    Including the following 2 domains:
    Endonuclease RAG1 (EC:3.1.-.-)
    E3 ubiquitin-protein ligase RAG1 (EC:6.3.2.-)
    Gene namesi
    Name:Rag1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:97848. Rag1.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice display a severe combined immunodeficiency phenotype. The have a small lymphoid organs that do not contain mature B and T-lymphocytes. The arrest of B- and T-cell differentiation occurs at an early stage and correlates with the inability to perform V(D)J recombination. The frequency of homologous immunoglobulin pairing is much lower. No obvious neuroanatomical or behavioral abnormalities have been observed.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi233 – 2331K → M: Abolishes autoubiquitination. 1 Publication
    Mutagenesisi307 – 3071H → A: Displays lower E3 ligase activity and affects the joining step of V(D)J recombination. 1 Publication
    Mutagenesisi325 – 3251C → G: Loss of E3 ligase activity and affects the joining step of V(D)J recombination. 2 Publications
    Mutagenesisi391 – 3911R → A: Defects in converting nicked products to hairpins. 1 Publication
    Mutagenesisi391 – 3911R → L: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication
    Mutagenesisi393 – 3931R → A: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication
    Mutagenesisi401 – 4011R → A: Allows robust hairpin activity. 1 Publication
    Mutagenesisi402 – 4021R → A: Defects in converting nicked products to hairpins. 1 Publication
    Mutagenesisi405 – 4051K → A: Reduced hairpin activity. 1 Publication
    Mutagenesisi406 – 4061H → A: Allows robust hairpin activity. 1 Publication
    Mutagenesisi407 – 4071R → A: Impairs DNA-binding and reduces hairpin formation without affecting nicking activity. 1 Publication
    Mutagenesisi443 – 4431N → A: Impairs DNA-binding; when associated with A-445. 1 Publication
    Mutagenesisi445 – 4451H → A: Impairs DNA-binding; when associated with A-443. 1 Publication
    Mutagenesisi546 – 5461D → A: Loss of DNA-binding.
    Mutagenesisi560 – 5601D → A: Loss of DNA-binding.
    Mutagenesisi597 – 5971E → Q: Impaired cleavage. 1 Publication
    Mutagenesisi600 – 6001D → A: Loss of cleavage and strand transfer activities. 3 Publications
    Mutagenesisi600 – 6001D → N: Loss of cleavage (both nicking and hairpin formation). 3 Publications
    Mutagenesisi707 – 7071Y → A: Deficient in both nicking and hairpin formation. 1 Publication
    Mutagenesisi708 – 7081D → A: Loss of cleavage and strand transfer activities without affecting allelic exclusion. 4 Publications
    Mutagenesisi708 – 7081D → N: Loss of cleavage (both nicking and hairpin formation). 4 Publications
    Mutagenesisi709 – 7091E → A: Impaired cleavage (defective in hairpin formation). 1 Publication
    Mutagenesisi709 – 7091E → Q: Impaired cleavage. 1 Publication
    Mutagenesisi713 – 7131R → A or C: Impaired cleavage (both nicking and hairpin formation).
    Mutagenesisi719 – 7191E → Q: Impaired cleavage. 1 Publication
    Mutagenesisi725 – 7251Y → A: Deficient in both nicking and hairpin formation. 1 Publication
    Mutagenesisi760 – 7601W → A: Deficient in both nicking and hairpin formation. 1 Publication
    Mutagenesisi792 – 7921D → N: Impaired cleavage. 1 Publication
    Mutagenesisi811 – 8111E → A: Impaired cleavage. 1 Publication
    Mutagenesisi811 – 8111E → Q: Loss of DNA-binding. 1 Publication
    Mutagenesisi893 – 8931W → A: Capable of nicking but defective for hairpinning. 1 Publication
    Mutagenesisi893 – 8931W → F: Capable of nicking and retains some hairpinning. 1 Publication
    Mutagenesisi935 – 9351Y → A, L or F: Capable of nicking but defective for hairpinning. 1 Publication
    Mutagenesisi935 – 9351Y → S or T: Capable of both nicking and hairpinning. 1 Publication
    Mutagenesisi938 – 9381K → A: Capable of nicking but defective for hairpinning.
    Mutagenesisi956 – 9561W → A: Deficient in both nicking and hairpin formation. 1 Publication
    Mutagenesisi959 – 9591E → Q: Impaired cleavage. 1 Publication
    Mutagenesisi962 – 9621E → A or Q: Loss of cleavage (both nicking and hairpin formation). 3 Publications
    Mutagenesisi971 – 9711F → A or W: Capable of nicking but defective for hairpinning. 1 Publication
    Mutagenesisi972 – 9721R → A: Capable of nicking but defective for hairpinning. 1 Publication
    Mutagenesisi973 – 9731K → A: Moderately defective with 56% of activity. 1 Publication
    Mutagenesisi986 – 9861D → N: Impaired cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10401040V(D)J recombination-activating protein 1PRO_0000056005Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki233 – 233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Autoubiquitinated in the presence of CDC34/UBCH3.2 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP15919.
    PRIDEiP15919.

    PTM databases

    PhosphoSiteiP15919.

    Expressioni

    Tissue specificityi

    Maturing lymphoid cells and central nervous system.

    Gene expression databases

    BgeeiP15919.
    CleanExiMM_RAG1.
    GenevestigatoriP15919.

    Interactioni

    Subunit structurei

    Homodimer. Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. Interacts with VPRBP, leading to recruitment of the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to ubiquitinate proteins and limit error-prone repair during V(D)J recombination.6 Publications

    Protein-protein interaction databases

    BioGridi202574. 12 interactions.
    DIPiDIP-48518N.
    IntActiP15919. 5 interactions.
    MINTiMINT-4131682.

    Structurei

    Secondary structure

    1
    1040
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi266 – 2683
    Helixi273 – 2753
    Beta strandi276 – 2783
    Helixi282 – 2876
    Turni291 – 2933
    Beta strandi298 – 3025
    Beta strandi308 – 3103
    Helixi311 – 32010
    Turni326 – 3283
    Helixi334 – 3363
    Helixi342 – 3509
    Beta strandi352 – 3543
    Beta strandi363 – 3653
    Helixi366 – 3749
    Helixi396 – 3983
    Helixi401 – 42222
    Helixi427 – 44115
    Helixi445 – 45410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RMDX-ray2.10A265-380[»]
    3GNAX-ray2.40A389-464[»]
    3GNBX-ray3.00A389-464[»]
    ProteinModelPortaliP15919.
    SMRiP15919. Positions 265-380, 389-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15919.

    Family & Domainsi

    Domaini

    The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity.1 Publication
    The NBD (nonamer binding) DNA-binding domain mediates the specific binding to the nonamer RSS motif by forming a tightly interwoven homodimer that binds and synapses 2 nonamer elements, with each NBD making contact with both DNA molecules. Each RSS is composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either 12 bp or 23 bp.1 PublicationPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the RAG1 family.PROSITE-ProRule annotation
    Contains 1 NBD (nonamer binding) DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 RAG1-type zinc finger.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri290 – 32940RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 38030RAG1-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG45367.
    GeneTreeiENSGT00390000008679.
    HOGENOMiHOG000232009.
    HOVERGENiHBG003861.
    InParanoidiA2AVN8.
    KOiK10628.
    OMAiIAKRFRY.
    OrthoDBiEOG76MK7J.
    TreeFamiTF331926.

    Family and domain databases

    Gene3Di3.30.160.60. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR024627. RAG1.
    IPR023336. RAG_nonamer-bd_dom.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR019485. Znf_VDJ_recomb-activ_1.
    [Graphical view]
    PANTHERiPTHR11539. PTHR11539. 1 hit.
    PfamiPF12940. RAG1. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    PF10426. zf-RAG1. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00355. ZnF_C2H2. 2 hits.
    [Graphical view]
    PROSITEiPS51487. NBD. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15919-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASLPSTLS FSSAPDEIQH PQIKFSEWKF KLFRVRSFEK APEEAQKEKD     50
    SSEGKPYLEQ SPVVPEKPGG QNSILTQRAL KLHPKFSKKF HADGKSSDKA 100
    VHQARLRHFC RICGNRFKSD GHSRRYPVHG PVDAKTQSLF RKKEKRVTSW 150
    PDLIARIFRI DVKADVDSIH PTEFCHDCWS IMHRKFSSSH SQVYFPRKVT 200
    VEWHPHTPSC DICFTAHRGL KRKRHQPNVQ LSKKLKTVLN HARRDRRKRT 250
    QARVSSKEVL KKISNCSKIH LSTKLLAVDF PAHFVKSISC QICEHILADP 300
    VETSCKHLFC RICILRCLKV MGSYCPSCRY PCFPTDLESP VKSFLNILNS 350
    LMVKCPAQDC NEEVSLEKYN HHVSSHKESK ETLVHINKGG RPRQHLLSLT 400
    RRAQKHRLRE LKIQVKEFAD KEEGGDVKAV CLTLFLLALR ARNEHRQADE 450
    LEAIMQGRGS GLQPAVCLAI RVNTFLSCSQ YHKMYRTVKA ITGRQIFQPL 500
    HALRNAEKVL LPGYHPFEWQ PPLKNVSSRT DVGIIDGLSG LASSVDEYPV 550
    DTIAKRFRYD SALVSALMDM EEDILEGMRS QDLDDYLNGP FTVVVKESCD 600
    GMGDVSEKHG SGPAVPEKAV RFSFTVMRIT IEHGSQNVKV FEEPKPNSEL 650
    CCKPLCLMLA DESDHETLTA ILSPLIAERE AMKSSELTLE MGGIPRTFKF 700
    IFRGTGYDEK LVREVEGLEA SGSVYICTLC DTTRLEASQN LVFHSITRSH 750
    AENLQRYEVW RSNPYHESVE ELRDRVKGVS AKPFIETVPS IDALHCDIGN 800
    AAEFYKIFQL EIGEVYKHPN ASKEERKRWQ ATLDKHLRKR MNLKPIMRMN 850
    GNFARKLMTQ ETVDAVCELI PSEERHEALR ELMDLYLKMK PVWRSSCPAK 900
    ECPESLCQYS FNSQRFAELL STKFKYRYEG KITNYFHKTL AHVPEIIERD 950
    GSIGAWASEG NESGNKLFRR FRKMNARQSK CYEMEDVLKH HWLYTSKYLQ 1000
    KFMNAHNALK SSGFTMNSKE TLGDPLGIED SLESQDSMEF 1040
    Length:1,040
    Mass (Da):119,185
    Last modified:July 27, 2011 - v2
    Checksum:i7C2E6AD68DCBA081
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti609 – 6091H → L in AAA40028. (PubMed:2598259)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29475 mRNA. Translation: AAA40028.1.
    AL929569 Genomic DNA. Translation: CAM20888.1.
    CH466519 Genomic DNA. Translation: EDL27655.1.
    BC138342 mRNA. Translation: AAI38343.1.
    CCDSiCCDS16463.1.
    PIRiB33754.
    RefSeqiNP_033045.2. NM_009019.2.
    XP_006499075.1. XM_006499012.1.
    UniGeneiMm.828.

    Genome annotation databases

    EnsembliENSMUST00000078494; ENSMUSP00000077584; ENSMUSG00000061311.
    GeneIDi19373.
    KEGGimmu:19373.
    UCSCiuc008lhk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29475 mRNA. Translation: AAA40028.1 .
    AL929569 Genomic DNA. Translation: CAM20888.1 .
    CH466519 Genomic DNA. Translation: EDL27655.1 .
    BC138342 mRNA. Translation: AAI38343.1 .
    CCDSi CCDS16463.1.
    PIRi B33754.
    RefSeqi NP_033045.2. NM_009019.2.
    XP_006499075.1. XM_006499012.1.
    UniGenei Mm.828.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RMD X-ray 2.10 A 265-380 [» ]
    3GNA X-ray 2.40 A 389-464 [» ]
    3GNB X-ray 3.00 A 389-464 [» ]
    ProteinModelPortali P15919.
    SMRi P15919. Positions 265-380, 389-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202574. 12 interactions.
    DIPi DIP-48518N.
    IntActi P15919. 5 interactions.
    MINTi MINT-4131682.

    PTM databases

    PhosphoSitei P15919.

    Proteomic databases

    PaxDbi P15919.
    PRIDEi P15919.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000078494 ; ENSMUSP00000077584 ; ENSMUSG00000061311 .
    GeneIDi 19373.
    KEGGi mmu:19373.
    UCSCi uc008lhk.2. mouse.

    Organism-specific databases

    CTDi 5896.
    MGIi MGI:97848. Rag1.

    Phylogenomic databases

    eggNOGi NOG45367.
    GeneTreei ENSGT00390000008679.
    HOGENOMi HOG000232009.
    HOVERGENi HBG003861.
    InParanoidi A2AVN8.
    KOi K10628.
    OMAi IAKRFRY.
    OrthoDBi EOG76MK7J.
    TreeFami TF331926.

    Miscellaneous databases

    EvolutionaryTracei P15919.
    NextBioi 296463.
    PROi P15919.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15919.
    CleanExi MM_RAG1.
    Genevestigatori P15919.

    Family and domain databases

    Gene3Di 3.30.160.60. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR024627. RAG1.
    IPR023336. RAG_nonamer-bd_dom.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR019485. Znf_VDJ_recomb-activ_1.
    [Graphical view ]
    PANTHERi PTHR11539. PTHR11539. 1 hit.
    Pfami PF12940. RAG1. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    PF10426. zf-RAG1. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00355. ZnF_C2H2. 2 hits.
    [Graphical view ]
    PROSITEi PS51487. NBD. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The V(D)J recombination activating gene, RAG-1."
      Schatz D.G., Oettinger M.A., Baltimore D.
      Cell 59:1035-1048(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: DISRUPTION PHENOTYPE.
    6. "Expression and V(D)J recombination activity of mutated RAG-1 proteins."
      Sadofsky M.J., Hesse J.E., McBlane J.F., Gellert M.
      Nucleic Acids Res. 21:5644-5650(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps."
      McBlane J.F., van Gent D.C., Ramsden D.A., Romeo C., Cuomo C.A., Gellert M., Oettinger M.A.
      Cell 83:387-395(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAG2.
    8. "RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination."
      Agrawal A., Schatz D.G.
      Cell 89:43-53(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE RAG COMPLEX.
    9. "Stimulation of V(D)J cleavage by high mobility group proteins."
      van Gent D.C., Hiom K., Paull T.T., Gellert M.
      EMBO J. 16:2665-2670(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RAG COMPLEX.
    10. "Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination."
      Landree M.A., Wibbenmeyer J.A., Roth D.B.
      Genes Dev. 13:3059-3069(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ENDONUCLEASE, DNA-BINDING, COFACTOR, MUTAGENESIS OF GLU-597; ASP-600; ASP-708; GLU-709; GLU-719; ASP-792; GLU-811; GLU-959; GLU-962 AND ASP-986.
    11. "Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase."
      Kim D.R., Dai Y., Mundy C.L., Yang W., Oettinger M.A.
      Genes Dev. 13:3070-3080(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-600; ASP-708 AND GLU-962.
    12. "Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex."
      Fugmann S.D., Villey I.J., Ptaszek L.M., Schatz D.G.
      Mol. Cell 5:97-107(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-600 AND ASP-708.
    13. "The RAG1 N-terminal domain is an E3 ubiquitin ligase."
      Yurchenko V., Xue Z., Sadofsky M.
      Genes Dev. 17:581-585(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE.
    14. "Autoubiquitylation of the V(D)J recombinase protein RAG1."
      Jones J.M., Gellert M.
      Proc. Natl. Acad. Sci. U.S.A. 100:15446-15451(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, UBIQUITINATION AT LYS-233, RING-TYPE ZINC-FINGER, MUTAGENESIS OF LYS-233 AND CYS-325.
    15. "Amino acid residues in Rag1 crucial for DNA hairpin formation."
      Lu C.P., Sandoval H., Brandt V.L., Rice P.A., Roth D.B.
      Nat. Struct. Mol. Biol. 13:1010-1015(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-707; TYR-725; TRP-760; TRP-893; TYR-935; TRP-956; GLU-962; PHE-971; ARG-972 AND LYS-973.
    16. "H3K4me3 stimulates the V(D)J RAG complex for both nicking and hairpinning in trans in addition to tethering in cis: implications for translocations."
      Shimazaki N., Tsai A.G., Lieber M.R.
      Mol. Cell 34:535-544(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase."
      Simkus C., Makiya M., Jones J.M.
      Mol. Immunol. 46:1319-1325(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION.
    18. Cited for: FUNCTION, MUTAGENESIS OF ASP-708.
    19. "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining."
      Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F.
      Mol. Cell 37:282-293(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE, MUTAGENESIS OF HIS-307 AND CYS-325.
    20. "VprBP binds full-length RAG1 and is required for B-cell development and V(D)J recombination fidelity."
      Kassmeier M.D., Mondal K., Palmer V.L., Raval P., Kumar S., Perry G.A., Anderson D.K., Ciborowski P., Jackson S., Xiong Y., Swanson P.C.
      EMBO J. 31:945-958(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VPRBP.
    21. "Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster."
      Bellon S.F., Rodgers K.K., Schatz D.G., Coleman J.E., Steitz T.A.
      Nat. Struct. Biol. 4:586-591(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 265-380 IN COMPLEX WITH ZINC, SUBUNIT.
    22. "Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis."
      Yin F.F., Bailey S., Innis C.A., Ciubotaru M., Kamtekar S., Steitz T.A., Schatz D.G.
      Nat. Struct. Mol. Biol. 16:499-508(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 389-464 IN COMPLEX WITH DNA NONAMER, FUNCTION AS ENDONUCLEASE, DNA-BINDING, DOMAIN NBD, INTERACTION WITH RAG2, MUTAGENESIS OF ARG-391; ARG-393; ARG-401; ARG-402; LYS-405; HIS-406; ARG-407; ASN-443 AND HIS-445.

    Entry informationi

    Entry nameiRAG1_MOUSE
    AccessioniPrimary (citable) accession number: P15919
    Secondary accession number(s): A2AVN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3