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P15918 (RAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V(D)J recombination-activating protein 1

Short name=RAG-1
Alternative name(s):
RING finger protein 74

Including the following 2 domains:

  1. Endonuclease RAG1
    EC=3.1.-.-
  2. E3 ubiquitin-protein ligase RAG1
    EC=6.3.2.-
Gene names
Name:RAG1
Synonyms:RNF74
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1043 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Cofactor

Binds 1 divalent metal cation per subunit. Magnesium or manganese By similarity.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Maturing lymphoid cells.

Domain

The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity By similarity. Ref.4

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 By similarity. Ref.4

Post-translational modification

Autoubiquitinated in the presence of CDC34/UBCH3 By similarity.

Involvement in disease

Combined cellular and humoral immune defects with granulomas (CHIDG) [MIM:233650]: Immunodeficiency disease with granulomas in the skin, mucous membranes, and internal organs. Other characteristics include hypogammaglobulinemia, a diminished number of T and B cells, and sparse thymic tissue on ultrasonography.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive (T(-)B(-)NK(+) SCID) [MIM:601457]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15

Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 Ref.15

Alpha/beta T-cell lymphopenia, with gamma/delta T-cell expansion, severe cytomegalovirus infection and autoimmunity (T-CMVA) [MIM:609889]: An immunological disorder characterized by oligoclonal expansion of TCR gamma/delta T-cells, TCR alpha/beta T-cell lymphopenia, severe, disseminated cytomegalovirus infection and autoimmune cytopenia.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the RAG1 family.

Contains 1 NBD (nonamer binding) DNA-binding domain.

Contains 1 RAG1-type zinc finger.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAM77798.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA recombination
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
SCID
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Endonuclease
Hydrolase
Ligase
Nuclease
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from sequence or structural similarity. Source: UniProtKB

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

V(D)J recombination

Inferred from sequence or structural similarity. Source: UniProtKB

adaptive immune response

Inferred from electronic annotation. Source: Ensembl

histone monoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

immune response

Traceable author statement Ref.7. Source: ProtInc

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of thymocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

pre-B cell allelic exclusion

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of T cell differentiation

Inferred from electronic annotation. Source: Ensembl

thymus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-1755109,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10431043V(D)J recombination-activating protein 1
PRO_0000056004

Regions

Zinc finger293 – 33240RING-type
Zinc finger354 – 38330RAG1-type
DNA binding392 – 45968NBD
Region1 – 288288Interaction with importin alpha-1

Sites

Metal binding2691Zinc 1 By similarity
Metal binding2731Zinc 1 By similarity
Metal binding2931Zinc 2 By similarity
Metal binding2961Zinc 1 By similarity
Metal binding2961Zinc 2 By similarity
Metal binding2981Zinc 1 By similarity
Metal binding3081Zinc 3 By similarity
Metal binding3101Zinc 3 By similarity
Metal binding3131Zinc 2 By similarity
Metal binding3161Zinc 2 By similarity
Metal binding3281Zinc 3 By similarity
Metal binding3311Zinc 3 By similarity
Metal binding3581Zinc 4 By similarity
Metal binding3631Zinc 4 By similarity
Metal binding3751Zinc 4 By similarity
Metal binding3791Zinc 4 By similarity
Metal binding6031Divalent metal cation; catalytic By similarity
Metal binding7111Divalent metal cation; catalytic By similarity
Metal binding9651Divalent metal cation; catalytic By similarity
Site8961Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site By similarity

Amino acid modifications

Cross-link234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant1561A → V. Ref.6
Corresponds to variant rs1801203 [ dbSNP | Ensembl ].
VAR_007800
Natural variant1691S → L.
Corresponds to variant rs4151027 [ dbSNP | Ensembl ].
VAR_029260
Natural variant2441R → G. Ref.5
Corresponds to variant rs199474683 [ dbSNP | Ensembl ].
VAR_007801
Natural variant2471R → H.
Corresponds to variant rs4151029 [ dbSNP | Ensembl ].
VAR_029261
Natural variant2491H → R. Ref.1 Ref.5
Corresponds to variant rs3740955 [ dbSNP | Ensembl ].
VAR_007802
Natural variant3021D → E.
Corresponds to variant rs4151030 [ dbSNP | Ensembl ].
VAR_020113
Natural variant3141R → W in CHIDG; reduced recombination activity. Ref.11
Corresponds to variant rs121918568 [ dbSNP | Ensembl ].
VAR_045957
Natural variant3281C → Y in OS. Ref.9
Corresponds to variant rs121918571 [ dbSNP | Ensembl ].
VAR_025971
Natural variant3961R → C in OS. Ref.7 Ref.8
Corresponds to variant rs104894289 [ dbSNP | Ensembl ].
VAR_008886
Natural variant3961R → H in OS. Ref.7 Ref.12
Corresponds to variant rs104894291 [ dbSNP | Ensembl ].
VAR_008887
Natural variant3961R → L in OS. Ref.9
Corresponds to variant rs104894291 [ dbSNP | Ensembl ].
VAR_025972
Natural variant4011S → P in OS. Ref.9 Ref.12
Corresponds to variant rs199474682 [ dbSNP | Ensembl ].
VAR_025973
Natural variant4101R → Q in OS/T(-)B(-)NK(+) SCID; atypical. Ref.9
Corresponds to variant rs199474684 [ dbSNP | Ensembl ].
VAR_025974
Natural variant4291D → G in OS. Ref.7
Corresponds to variant rs104894292 [ dbSNP | Ensembl ].
VAR_008888
Natural variant4331V → M in T(-)B(-)NK(+) SCID and OS/T(-)B(-)NK(+) SCID; atypical. Ref.9 Ref.12
Corresponds to variant rs199474679 [ dbSNP | Ensembl ].
VAR_025975
Natural variant4351M → V in OS. Ref.9
Corresponds to variant rs141524540 [ dbSNP | Ensembl ].
VAR_025976
Natural variant4441A → V in OS/T(-)B(-)NK(+) SCID; atypical. Ref.9
Corresponds to variant rs199474685 [ dbSNP | Ensembl ].
VAR_025977
Natural variant4491R → K.
Corresponds to variant rs4151031 [ dbSNP | Ensembl ].
VAR_029262
Natural variant4541L → Q in OS. Ref.14
Corresponds to variant rs199474677 [ dbSNP | Ensembl ].
VAR_067274
Natural variant4741R → C Probable disease-associated mutation found in a patient with relatively late onset of infections and isolated T-cell lymphopenia. Ref.13
Corresponds to variant rs199474678 [ dbSNP | Ensembl ].
VAR_067275
Natural variant4741R → H in OS/T(-)B(-)NK(+) SCID; atypical. Ref.9
Corresponds to variant rs199474686 [ dbSNP | Ensembl ].
VAR_025978
Natural variant5071R → W in OS/T(-)B(-)NK(+) SCID and CHIDG; atypical; reduced recombination activity when associated with H-737. Ref.9 Ref.11
Corresponds to variant rs104894298 [ dbSNP | Ensembl ].
VAR_025979
Natural variant5221W → C in OS/T(-)B(-)NK(+) SCID; atypical. Ref.9
Corresponds to variant rs193922461 [ dbSNP | Ensembl ].
VAR_025980
Natural variant5251P → S.
Corresponds to variant rs4151032 [ dbSNP | Ensembl ].
VAR_029263
Natural variant5591R → S in T(-)B(-)NK(+) SCID and OS. Ref.9 Ref.12
Corresponds to variant rs199474681 [ dbSNP | Ensembl ].
VAR_025981
Natural variant5611R → C in OS. Ref.7
Corresponds to variant rs104894285 [ dbSNP | Ensembl ].
VAR_008890
Natural variant5611R → H in OS. Ref.7
Corresponds to variant rs104894284 [ dbSNP | Ensembl ].
VAR_008889
Natural variant6241R → C in OS. Ref.9
Corresponds to variant rs199474688 [ dbSNP | Ensembl ].
VAR_025982
Natural variant6241R → H in T(-)B(-)NK(+) SCID. Ref.6 Ref.12
Corresponds to variant rs199474680 [ dbSNP | Ensembl ].
VAR_007803
Natural variant6691E → G in OS. Ref.9
Corresponds to variant rs199474689 [ dbSNP | Ensembl ].
VAR_025983
Natural variant6991R → W in OS; also in a patient with multiple autoimmune disorders. Ref.15
Corresponds to variant rs199474676 [ dbSNP | Ensembl ].
VAR_067276
Natural variant7221E → K in T(-)B(-)NK(+) SCID. Ref.6
Corresponds to variant rs28933392 [ dbSNP | Ensembl ].
VAR_007804
Natural variant7371R → H in OS and CHIDG; reduced recombination activity when associated with T-507. Ref.7 Ref.11
Corresponds to variant rs104894286 [ dbSNP | Ensembl ].
VAR_008891
Natural variant7531H → L in OS/T(-)B(-)NK(+) SCID; atypical. Ref.9
Corresponds to variant rs199474687 [ dbSNP | Ensembl ].
VAR_025984
Natural variant7781R → Q in CHIDG; reduced recombination activity. Ref.11
Corresponds to variant rs121918569 [ dbSNP | Ensembl ].
VAR_045958
Natural variant8201K → R.
Corresponds to variant rs2227973 [ dbSNP | Ensembl ].
VAR_008892
Natural variant8411R → W in T-CMVA; also found in a patient with an atypical form of severe combined immunodeficiency /Omenn syndrome. Ref.10
Corresponds to variant rs104894287 [ dbSNP | Ensembl ].
VAR_025985
Natural variant8551N → I in immunodeficiency; severe combined. Ref.9
Corresponds to variant rs199474690 [ dbSNP | Ensembl ].
VAR_025986
Natural variant8801E → K.
Corresponds to variant rs4151033 [ dbSNP | Ensembl ].
VAR_020114
Natural variant8851L → R in OS. Ref.8
Corresponds to variant rs199474691 [ dbSNP | Ensembl ].
VAR_008893
Natural variant8871D → N.
Corresponds to variant rs4151034 [ dbSNP | Ensembl ].
VAR_029264
Natural variant9121Y → C in OS. Ref.7
Corresponds to variant rs104894290 [ dbSNP | Ensembl ].
VAR_008894
Natural variant9751R → Q in OS. Ref.9
Corresponds to variant rs150739647 [ dbSNP | Ensembl ].
VAR_025987
Natural variant9751R → W in CHIDG; reduced recombination activity. Ref.11
Corresponds to variant rs121918570 [ dbSNP | Ensembl ].
VAR_045959
Natural variant9811Q → P in T-CMVA. Ref.10
Corresponds to variant rs104894288 [ dbSNP | Ensembl ].
VAR_025988

Sequences

Sequence LengthMass (Da)Tools
P15918 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 5417A7413DA8CB65

FASTA1,043119,097
        10         20         30         40         50         60 
MAASFPPTLG LSSAPDEIQH PHIKFSEWKF KLFRVRSFEK TPEEAQKEKK DSFEGKPSLE 

        70         80         90        100        110        120 
QSPAVLDKAD GQKPVPTQPL LKAHPKFSKK FHDNEKARGK AIHQANLRHL CRICGNSFRA 

       130        140        150        160        170        180 
DEHNRRYPVH GPVDGKTLGL LRKKEKRATS WPDLIAKVFR IDVKADVDSI HPTEFCHNCW 

       190        200        210        220        230        240 
SIMHRKFSSA PCEVYFPRNV TMEWHPHTPS CDICNTARRG LKRKSLQPNL QLSKKLKTVL 

       250        260        270        280        290        300 
DQARQARQHK RRAQARISSK DVMKKIANCS KIHLSTKLLA VDFPEHFVKS ISCQICEHIL 

       310        320        330        340        350        360 
ADPVETNCKH VFCRVCILRC LKVMGSYCPS CRYPCFPTDL ESPVKSFLSV LNSLMVKCPA 

       370        380        390        400        410        420 
KECNEEVSLE KYNHHISSHK ESKEIFVHIN KGGRPRQHLL SLTRRAQKHR LRELKLQVKA 

       430        440        450        460        470        480 
FADKEEGGDV KSVCMTLFLL ALRARNEHRQ ADELEAIMQG KGSGLQPAVC LAIRVNTFLS 

       490        500        510        520        530        540 
CSQYHKMYRT VKAITGRQIF QPLHALRNAE KVLLPGYHHF EWQPPLKNVS SSTDVGIIDG 

       550        560        570        580        590        600 
LSGLSSSVDD YPVDTIAKRF RYDSALVSAL MDMEEDILEG MRSQDLDDYL NGPFTVVVKE 

       610        620        630        640        650        660 
SCDGMGDVSE KHGSGPVVPE KAVRFSFTIM KITIAHSSQN VKVFEEAKPN SELCCKPLCL 

       670        680        690        700        710        720 
MLADESDHET LTAILSPLIA EREAMKSSEL MLELGGILRT FKFIFRGTGY DEKLVREVEG 

       730        740        750        760        770        780 
LEASGSVYIC TLCDATRLEA SQNLVFHSIT RSHAENLERY EVWRSNPYHE SVEELRDRVK 

       790        800        810        820        830        840 
GVSAKPFIET VPSIDALHCD IGNAAEFYKI FQLEIGEVYK NPNASKEERK RWQATLDKHL 

       850        860        870        880        890        900 
RKKMNLKPIM RMNGNFARKL MTKETVDAVC ELIPSEERHE ALRELMDLYL KMKPVWRSSC 

       910        920        930        940        950        960 
PAKECPESLC QYSFNSQRFA ELLSTKFKYR YEGKITNYFH KTLAHVPEII ERDGSIGAWA 

       970        980        990       1000       1010       1020 
SEGNESGNKL FRRFRKMNAR QSKCYEMEDV LKHHWLYTSK YLQKFMNAHN ALKTSGFTMN 

      1030       1040 
PQASLGDPLG IEDSLESQDS MEF 

« Hide

References

« Hide 'large scale' references
[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], VARIANT ARG-249.
[2]NIEHS SNPs program
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1."
Cortes P., Ye Z.-S., Baltimore D.
Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF IMPORTIN ALPHA-1 BINDING DOMAIN.
[5]"Two new variants of RAG-1 protein predicted by SSCP."
Nomdedeu J.F., Lasa A., Seminago R., Rubiol E., Baiget M., Soler J.
Hum. Mutat. 8:191-192(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-244 AND ARG-249.
[6]"RAG mutations in human B cell-negative SCID."
Schwarz K., Gauss G.H., Ludwig L., Pannicke U., Li Z., Linder D., Friedrich W., Seger R.A., Hansen-Hagge T.E., Desiderio S., Lieber M.R., Bartram C.R.
Science 274:97-99(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS T(-)B(-)NK(+) SCID HIS-624 AND LYS-722, VARIANT VAL-156.
[7]"Partial V(D)J recombination activity leads to Omenn syndrome."
Villa A., Santagata S., Bozzi F., Giliani S., Frattini A., Imberti L., Gatta L.B., Ochs H.D., Schwarz K., Notarangelo L.D., Vezzoni P., Spanopoulou E.
Cell 93:885-896(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OS CYS-396; HIS-396; GLY-429; HIS-561; CYS-561; HIS-737 AND CYS-912.
[8]"Characterization of immune function and analysis of RAG gene mutations in Omenn syndrome and related disorders."
Wada T., Takei K., Kudo M., Shimura S., Kasahara Y., Koizumi S., Kawa-Ha K., Ishida Y., Imashuku S., Seki H., Yachie A.
Clin. Exp. Immunol. 119:148-155(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OS CYS-396 AND ARG-885.
[9]"V(D)J recombination defects in lymphocytes due to RAG mutations: severe immunodeficiency with a spectrum of clinical presentations."
Villa A., Sobacchi C., Notarangelo L.D., Bozzi F., Abinun M., Abrahamsen T.G., Arkwright P.D., Baniyash M., Brooks E.G., Conley M.E., Cortes P., Duse M., Fasth A., Filipovich A.M., Infante A.J., Jones A., Mazzolari E., Muller S.M. expand/collapse author list , Pasic S., Rechavi G., Sacco M.G., Santagata S., Schroeder M.L., Seger R., Strina D., Ugazio A., Vaeliaho J., Vihinen M., Vogler L.B., Ochs H., Vezzoni P., Friedrich W., Schwarz K.
Blood 97:81-88(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OS TYR-328; LEU-396; PRO-401; VAL-435; SER-559; CYS-624; GLY-669 AND GLN-975, VARIANTS OS/T(-)B(-)NK(+) SCID GLN-410; MET-433; VAL-444; HIS-474; TRP-507; CYS-522 AND LEU-753, VARIANT IMMUNODEFICIENCY ILE-855.
[10]"A novel immunodeficiency associated with hypomorphic RAG1 mutations and CMV infection."
de Villartay J.-P., Lim A., Al-Mousa H., Dupont S., Dechanet-Merville J., Coumau-Gatbois E., Gougeon M.-L., Lemainque A., Eidenschenk C., Jouanguy E., Abel L., Casanova J.-L., Fischer A., Le Deist F.
J. Clin. Invest. 115:3291-3299(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS T-CMVA TRP-841 AND PRO-981.
[11]"An immunodeficiency disease with RAG mutations and granulomas."
Schuetz C., Huck K., Gudowius S., Megahed M., Feyen O., Hubner B., Schneider D.T., Manfras B., Pannicke U., Willemze R., Knuechel R., Goebel U., Schulz A., Borkhardt A., Friedrich W., Schwarz K., Niehues T.
N. Engl. J. Med. 358:2030-2038(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHIDG TRP-314; TRP-507; HIS-737; GLN-778 AND TRP-975, CHARACTERIZATION OF VARIANTS CHIDG TRP-314; TRP-507; HIS-737; GLN-778 AND TRP-975.
[12]"Molecular analysis of T-B-NK+ severe combined immunodeficiency and Omenn syndrome cases in Saudi Arabia."
Alsmadi O., Al-Ghonaium A., Al-Muhsen S., Arnaout R., Al-Dhekri H., Al-Saud B., Al-Kayal F., Al-Saud H., Al-Mousa H.
BMC Med. Genet. 10:116-116(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS T(-)B(-)NK(+) SCID MET-433; SER-559 AND HIS-624, VARIANTS OS HIS-396 AND PRO-401.
[13]"Highly variable clinical phenotypes of hypomorphic RAG1 mutations."
Avila E.M., Uzel G., Hsu A., Milner J.D., Turner M.L., Pittaluga S., Freeman A.F., Holland S.M.
Pediatrics 126:E1248-E1252(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-474.
[14]"Novel mutations in RAG1/2 and ADA genes in Israeli patients presenting with T-B-SCID or Omenn syndrome."
Dalal I., Tasher D., Somech R., Etzioni A., Garti B.Z., Lev D., Cohen S., Somekh E., Leshinsky-Silver E.
Clin. Immunol. 140:284-290(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OS GLN-454.
[15]"Clinical characteristics and molecular analysis of three Chinese children with Omenn syndrome."
Zhang Z.Y., Zhao X.D., Jiang L.P., Liu E.M., Cui Y.X., Wang M., Wei H., Yu J., An Y.F., Yang X.Q.
Pediatr. Allergy Immunol. 22:482-487(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OS TRP-699.
+Additional computationally mapped references.

Web resources

GeneReviews
NIEHS-SNPs
RAG1base

RAG1 deficiency database

Mendelian genes recombination activating gene 1 (RAG1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29474 mRNA. Translation: AAA60248.1.
AY130302 Genomic DNA. Translation: AAM77798.1. Sequence problems.
AC139427 Genomic DNA. No translation available.
PIRA33754.
RefSeqNP_000439.1. NM_000448.2.
XP_005253098.1. XM_005253041.1.
UniGeneHs.677010.
Hs.73958.

3D structure databases

ProteinModelPortalP15918.
SMRP15918. Positions 268-383, 392-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111832. 18 interactions.
IntActP15918. 5 interactions.
MINTMINT-1511469.
STRING9606.ENSP00000299440.

PTM databases

PhosphoSiteP15918.

Proteomic databases

PaxDbP15918.
PRIDEP15918.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299440; ENSP00000299440; ENSG00000166349.
GeneID5896.
KEGGhsa:5896.
UCSCuc001mwu.4. human.

Organism-specific databases

CTD5896.
GeneCardsGC11P036546.
HGNCHGNC:9831. RAG1.
MIM179615. gene.
233650. phenotype.
601457. phenotype.
603554. phenotype.
609889. phenotype.
neXtProtNX_P15918.
Orphanet231154. Combined immunodeficiency T+ B+ due to partial RAG1 deficiency.
157949. Combined immunodeficiency with skin granulomas.
39041. Omenn syndrome.
331206. Severe combined immunodeficiency due to complete RAG1/2 deficiency.
PharmGKBPA34185.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45367.
HOGENOMHOG000232009.
HOVERGENHBG003861.
InParanoidP15918.
KOK10628.
OMATIAKRFR.
PhylomeDBP15918.
TreeFamTF331926.

Gene expression databases

ArrayExpressP15918.
BgeeP15918.
CleanExHS_RAG1.
GenevestigatorP15918.

Family and domain databases

Gene3D3.30.160.60. 1 hit.
3.30.40.10. 1 hit.
InterProIPR024627. 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]
PANTHERPTHR11539. PTHR11539. 1 hit.
PfamPF12940. RAG1. 1 hit.
PF00097. zf-C3HC4. 1 hit.
PF10426. zf-RAG1. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEPS51487. NBD. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5896.
NextBio22934.
PROP15918.
SOURCESearch...

Entry information

Entry nameRAG1_HUMAN
AccessionPrimary (citable) accession number: P15918
Secondary accession number(s): Q8NER2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 30, 2010
Last modified: March 19, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM