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Protein

V(D)J recombination-activating protein 1

Gene

Rag1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 an 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

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Mg2+ or Mn2+.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi266Zinc 11 Publication1
Metal bindingi270Zinc 11 Publication1
Metal bindingi290Zinc 21 Publication1
Metal bindingi293Zinc 11 Publication1
Metal bindingi293Zinc 21 Publication1
Metal bindingi295Zinc 11 Publication1
Metal bindingi305Zinc 31 Publication1
Metal bindingi307Zinc 31 Publication1
Metal bindingi310Zinc 21 Publication1
Metal bindingi313Zinc 21 Publication1
Metal bindingi325Zinc 31 Publication1
Metal bindingi328Zinc 31 Publication1
Metal bindingi355Zinc 41 Publication1
Metal bindingi360Zinc 41 Publication1
Metal bindingi372Zinc 41 Publication1
Metal bindingi376Zinc 41 Publication1
Metal bindingi600Divalent metal cation; catalyticCurated1
Metal bindingi708Divalent metal cation; catalyticCurated1
Sitei893Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site1
Metal bindingi962Divalent metal cation; catalyticCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri290 – 329RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri351 – 380RAG1-typePROSITE-ProRule annotationAdd BLAST30
DNA bindingi389 – 456NBDPROSITE-ProRule annotationAdd BLAST68

GO - Molecular functioni

  • endonuclease activity Source: UniProtKB
  • histone binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: MGI
  • B cell differentiation Source: UniProtKB
  • DNA recombination Source: MGI
  • histone monoubiquitination Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • negative regulation of T cell apoptotic process Source: MGI
  • negative regulation of thymocyte apoptotic process Source: MGI
  • positive regulation of T cell differentiation Source: CACAO
  • pre-B cell allelic exclusion Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • regulation of T cell differentiation Source: MGI
  • T cell differentiation in thymus Source: UniProtKB
  • T cell homeostasis Source: MGI
  • thymus development Source: MGI
  • 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

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-1266695. Interleukin-7 signaling.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97848. Rag1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi233K → M: Abolishes autoubiquitination. 1 Publication1
Mutagenesisi307H → A: Displays lower E3 ligase activity and affects the joining step of V(D)J recombination. 1 Publication1
Mutagenesisi325C → G: Loss of E3 ligase activity and affects the joining step of V(D)J recombination. 2 Publications1
Mutagenesisi391R → A: Defects in converting nicked products to hairpins. 1 Publication1
Mutagenesisi391R → L: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication1
Mutagenesisi393R → A: Impairs DNA-binding and hairpin formation while maintaining some nicking activity. 1 Publication1
Mutagenesisi401R → A: Allows robust hairpin activity. 1 Publication1
Mutagenesisi402R → A: Defects in converting nicked products to hairpins. 1 Publication1
Mutagenesisi405K → A: Reduced hairpin activity. 1 Publication1
Mutagenesisi406H → A: Allows robust hairpin activity. 1 Publication1
Mutagenesisi407R → A: Impairs DNA-binding and reduces hairpin formation without affecting nicking activity. 1 Publication1
Mutagenesisi443N → A: Impairs DNA-binding; when associated with A-445. 1 Publication1
Mutagenesisi445H → A: Impairs DNA-binding; when associated with A-443. 1 Publication1
Mutagenesisi546D → A: Loss of DNA-binding. 1
Mutagenesisi560D → A: Loss of DNA-binding. 1
Mutagenesisi597E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi600D → A: Loss of cleavage and strand transfer activities. 3 Publications1
Mutagenesisi600D → N: Loss of cleavage (both nicking and hairpin formation). 3 Publications1
Mutagenesisi707Y → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi708D → A: Loss of cleavage and strand transfer activities without affecting allelic exclusion. 4 Publications1
Mutagenesisi708D → N: Loss of cleavage (both nicking and hairpin formation). 4 Publications1
Mutagenesisi709E → A: Impaired cleavage (defective in hairpin formation). 1 Publication1
Mutagenesisi709E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi713R → A or C: Impaired cleavage (both nicking and hairpin formation). 1
Mutagenesisi719E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi725Y → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi760W → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi792D → N: Impaired cleavage. 1 Publication1
Mutagenesisi811E → A: Impaired cleavage. 1 Publication1
Mutagenesisi811E → Q: Loss of DNA-binding. 1 Publication1
Mutagenesisi893W → A: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi893W → F: Capable of nicking and retains some hairpinning. 1 Publication1
Mutagenesisi935Y → A, L or F: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi935Y → S or T: Capable of both nicking and hairpinning. 1 Publication1
Mutagenesisi938K → A: Capable of nicking but defective for hairpinning. 1
Mutagenesisi956W → A: Deficient in both nicking and hairpin formation. 1 Publication1
Mutagenesisi959E → Q: Impaired cleavage. 1 Publication1
Mutagenesisi962E → A or Q: Loss of cleavage (both nicking and hairpin formation). 3 Publications1
Mutagenesisi971F → A or W: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi972R → A: Capable of nicking but defective for hairpinning. 1 Publication1
Mutagenesisi973K → A: Moderately defective with 56% of activity. 1 Publication1
Mutagenesisi986D → N: Impaired cleavage. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560051 – 1040V(D)J recombination-activating protein 1Add BLAST1040

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki233Glycyl 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

MaxQBiP15919.
PaxDbiP15919.
PRIDEiP15919.

PTM databases

iPTMnetiP15919.
PhosphoSitePlusiP15919.

Expressioni

Tissue specificityi

Maturing lymphoid cells and central nervous system.

Gene expression databases

BgeeiENSMUSG00000061311.
CleanExiMM_RAG1.
GenevisibleiP15919. MM.

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

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi202574. 12 interactors.
DIPiDIP-48518N.
IntActiP15919. 5 interactors.
MINTiMINT-4131682.
STRINGi10090.ENSMUSP00000077584.

Structurei

Secondary structure

11040
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi266 – 268Combined sources3
Helixi273 – 275Combined sources3
Beta strandi276 – 278Combined sources3
Helixi282 – 287Combined sources6
Turni291 – 293Combined sources3
Beta strandi298 – 302Combined sources5
Beta strandi308 – 310Combined sources3
Helixi311 – 320Combined sources10
Turni326 – 328Combined sources3
Helixi334 – 336Combined sources3
Helixi342 – 350Combined sources9
Beta strandi352 – 354Combined sources3
Beta strandi363 – 365Combined sources3
Helixi366 – 374Combined sources9
Helixi396 – 398Combined sources3
Helixi401 – 422Combined sources22
Helixi427 – 441Combined sources15
Helixi445 – 454Combined sources10
Helixi464 – 473Combined sources10
Helixi478 – 492Combined sources15
Helixi500 – 510Combined sources11
Beta strandi517 – 521Combined sources5
Beta strandi534 – 536Combined sources3
Turni537 – 540Combined sources4
Beta strandi554 – 557Combined sources4
Helixi559 – 569Combined sources11
Helixi571 – 580Combined sources10
Beta strandi591 – 604Combined sources14
Beta strandi618 – 633Combined sources16
Beta strandi636 – 642Combined sources7
Beta strandi653 – 658Combined sources6
Helixi665 – 683Combined sources19
Beta strandi686 – 690Combined sources5
Beta strandi692 – 707Combined sources16
Helixi709 – 716Combined sources8
Beta strandi721 – 724Combined sources4
Beta strandi728 – 730Combined sources3
Helixi736 – 739Combined sources4
Helixi750 – 762Combined sources13
Helixi769 – 776Combined sources8
Helixi793 – 812Combined sources20
Turni813 – 817Combined sources5
Helixi823 – 840Combined sources18
Helixi851 – 857Combined sources7
Helixi860 – 866Combined sources7
Helixi867 – 869Combined sources3
Helixi874 – 894Combined sources21
Helixi898 – 901Combined sources4
Helixi903 – 907Combined sources5
Helixi909 – 921Combined sources13
Turni922 – 927Combined sources6
Beta strandi928 – 930Combined sources3
Helixi934 – 950Combined sources17
Helixi954 – 956Combined sources3
Helixi964 – 973Combined sources10
Helixi980 – 994Combined sources15
Helixi997 – 1003Combined sources7
Helixi1005 – 1007Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RMDX-ray2.10A265-380[»]
3GNAX-ray2.40A389-464[»]
3GNBX-ray3.00A389-464[»]
4WWXX-ray3.20B/E392-1008[»]
ProteinModelPortaliP15919.
SMRiP15919.
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.PROSITE-ProRule annotation1 Publication

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.PROSITE-ProRule annotationCurated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri290 – 329RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri351 – 380RAG1-typePROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IKNG. Eukaryota.
ENOG4110KH0. LUCA.
GeneTreeiENSGT00390000008679.
HOGENOMiHOG000232009.
HOVERGENiHBG003861.
InParanoidiP15919.
KOiK10628.
OMAiIAKRFRY.
OrthoDBiEOG091G00XO.
TreeFamiTF331926.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR024627. RAG1.
IPR019485. RAG1_Znf.
IPR023336. RAG_nonamer-bd_dom.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[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.
[Graphical view]
PROSITEiPS51487. NBD. 1 hit.
PS51765. ZF_RAG1. 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)DescriptionActionsGraphical viewLength
Sequence conflicti609H → L in AAA40028 (PubMed:2598259).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RMDX-ray2.10A265-380[»]
3GNAX-ray2.40A389-464[»]
3GNBX-ray3.00A389-464[»]
4WWXX-ray3.20B/E392-1008[»]
ProteinModelPortaliP15919.
SMRiP15919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202574. 12 interactors.
DIPiDIP-48518N.
IntActiP15919. 5 interactors.
MINTiMINT-4131682.
STRINGi10090.ENSMUSP00000077584.

PTM databases

iPTMnetiP15919.
PhosphoSitePlusiP15919.

Proteomic databases

MaxQBiP15919.
PaxDbiP15919.
PRIDEiP15919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5896.
MGIiMGI:97848. Rag1.

Phylogenomic databases

eggNOGiENOG410IKNG. Eukaryota.
ENOG4110KH0. LUCA.
GeneTreeiENSGT00390000008679.
HOGENOMiHOG000232009.
HOVERGENiHBG003861.
InParanoidiP15919.
KOiK10628.
OMAiIAKRFRY.
OrthoDBiEOG091G00XO.
TreeFamiTF331926.

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-1266695. Interleukin-7 signaling.

Miscellaneous databases

EvolutionaryTraceiP15919.
PROiP15919.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061311.
CleanExiMM_RAG1.
GenevisibleiP15919. MM.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR024627. RAG1.
IPR019485. RAG1_Znf.
IPR023336. RAG_nonamer-bd_dom.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[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.
[Graphical view]
PROSITEiPS51487. NBD. 1 hit.
PS51765. ZF_RAG1. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.