Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15919

- RAG1_MOUSE

UniProt

P15919 - RAG1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 homodimerization activity Source: UniProtKB
  6. sequence-specific DNA binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: UniProtKB
  8. 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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP15919. baseline and differential.
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.
InParanoidiP15919.
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

        10         20         30         40         50
MAASLPSTLS FSSAPDEIQH PQIKFSEWKF KLFRVRSFEK APEEAQKEKD
60 70 80 90 100
SSEGKPYLEQ SPVVPEKPGG QNSILTQRAL KLHPKFSKKF HADGKSSDKA
110 120 130 140 150
VHQARLRHFC RICGNRFKSD GHSRRYPVHG PVDAKTQSLF RKKEKRVTSW
160 170 180 190 200
PDLIARIFRI DVKADVDSIH PTEFCHDCWS IMHRKFSSSH SQVYFPRKVT
210 220 230 240 250
VEWHPHTPSC DICFTAHRGL KRKRHQPNVQ LSKKLKTVLN HARRDRRKRT
260 270 280 290 300
QARVSSKEVL KKISNCSKIH LSTKLLAVDF PAHFVKSISC QICEHILADP
310 320 330 340 350
VETSCKHLFC RICILRCLKV MGSYCPSCRY PCFPTDLESP VKSFLNILNS
360 370 380 390 400
LMVKCPAQDC NEEVSLEKYN HHVSSHKESK ETLVHINKGG RPRQHLLSLT
410 420 430 440 450
RRAQKHRLRE LKIQVKEFAD KEEGGDVKAV CLTLFLLALR ARNEHRQADE
460 470 480 490 500
LEAIMQGRGS GLQPAVCLAI RVNTFLSCSQ YHKMYRTVKA ITGRQIFQPL
510 520 530 540 550
HALRNAEKVL LPGYHPFEWQ PPLKNVSSRT DVGIIDGLSG LASSVDEYPV
560 570 580 590 600
DTIAKRFRYD SALVSALMDM EEDILEGMRS QDLDDYLNGP FTVVVKESCD
610 620 630 640 650
GMGDVSEKHG SGPAVPEKAV RFSFTVMRIT IEHGSQNVKV FEEPKPNSEL
660 670 680 690 700
CCKPLCLMLA DESDHETLTA ILSPLIAERE AMKSSELTLE MGGIPRTFKF
710 720 730 740 750
IFRGTGYDEK LVREVEGLEA SGSVYICTLC DTTRLEASQN LVFHSITRSH
760 770 780 790 800
AENLQRYEVW RSNPYHESVE ELRDRVKGVS AKPFIETVPS IDALHCDIGN
810 820 830 840 850
AAEFYKIFQL EIGEVYKHPN ASKEERKRWQ ATLDKHLRKR MNLKPIMRMN
860 870 880 890 900
GNFARKLMTQ ETVDAVCELI PSEERHEALR ELMDLYLKMK PVWRSSCPAK
910 920 930 940 950
ECPESLCQYS FNSQRFAELL STKFKYRYEG KITNYFHKTL AHVPEIIERD
960 970 980 990 1000
GSIGAWASEG NESGNKLFRR FRKMNARQSK CYEMEDVLKH HWLYTSKYLQ
1010 1020 1030 1040
KFMNAHNALK SSGFTMNSKE TLGDPLGIED SLESQDSMEF
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 P15919.
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.
ExpressionAtlasi P15919. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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