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O14933

- UB2L6_HUMAN

UniProt

O14933 - UB2L6_HUMAN

Protein

Ubiquitin/ISG15-conjugating enzyme E2 L6

Gene

UBE2L6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.3 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ISG15 ligase activity Source: Ensembl
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: ProtInc

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. cytokine-mediated signaling pathway Source: Reactome
    3. innate immune response Source: Reactome
    4. ISG15-protein conjugation Source: Ensembl
    5. modification-dependent protein catabolic process Source: Ensembl
    6. negative regulation of type I interferon production Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiO14933.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC:6.3.2.19)
    Alternative name(s):
    Retinoic acid-induced gene B protein
    Short name:
    RIG-B
    UbcH8
    Ubiquitin carrier protein L6
    Ubiquitin-protein ligase L6
    Gene namesi
    Name:UBE2L6
    Synonyms:UBCH8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:12490. UBE2L6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37139.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 153153Ubiquitin/ISG15-conjugating enzyme E2 L6PRO_0000082478Add
    BLAST

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiO14933.
    PaxDbiO14933.
    PRIDEiO14933.

    PTM databases

    PhosphoSiteiO14933.

    Expressioni

    Tissue specificityi

    Present in natural killer cells (at protein level).1 Publication

    Inductioni

    By IFNB1/IFN-beta.1 Publication

    Gene expression databases

    ArrayExpressiO14933.
    BgeeiO14933.
    CleanExiHS_UBE2L6.
    GenevestigatoriO14933.

    Organism-specific databases

    HPAiHPA003328.

    Interactioni

    Subunit structurei

    Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated).5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RNF144BQ7Z4194EBI-2129974,EBI-2129982
    RNF19BQ6ZMZ03EBI-2129974,EBI-2466594
    Rnf40Q8CJB92EBI-2129974,EBI-6110162From a different organism.

    Protein-protein interaction databases

    BioGridi114672. 41 interactions.
    DIPiDIP-41477N.
    IntActiO14933. 26 interactions.
    MINTiMINT-240858.
    STRINGi9606.ENSP00000287156.

    Structurei

    Secondary structure

    1
    153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1613
    Beta strandi22 – 276
    Beta strandi34 – 396
    Helixi46 – 483
    Beta strandi49 – 568
    Turni59 – 624
    Beta strandi67 – 726
    Beta strandi81 – 833
    Helixi88 – 903
    Turni92 – 943
    Helixi101 – 11313
    Beta strandi117 – 1193
    Helixi123 – 1319
    Helixi133 – 14715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WZVX-ray2.10A/B2-153[»]
    1WZWX-ray2.40A2-153[»]
    2KJHNMR-A2-153[»]
    ProteinModelPortaliO14933.
    SMRiO14933. Positions 3-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14933.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiO14933.
    KOiK04553.
    OMAiPEKPPYN.
    OrthoDBiEOG7GXPD8.
    PhylomeDBiO14933.
    TreeFamiTF313043.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14933-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA    50
    FNLRISFPPE YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK 100
    TCQVLEALNV LVNRPNIREP LRMDLADLLT QNPELFRKNA EEFTLRFGVD 150
    RPS 153
    Length:153
    Mass (Da):17,769
    Last modified:June 16, 2009 - v4
    Checksum:iD79768775344EFAE
    GO
    Isoform 2 (identifier: O14933-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-66: Missing.

    Show »
    Length:87
    Mass (Da):10,086
    Checksum:iCD4DEC38615607B1
    GO

    Sequence cautioni

    The sequence CAB64566.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_037344Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243268
    , AJ243269, AJ243270, AJ243271 Genomic DNA. Translation: CAB64566.1. Different initiation.
    AF061736 mRNA. Translation: AAD17525.1.
    AK315755 mRNA. Translation: BAG38109.1.
    CR457126 mRNA. Translation: CAG33407.1.
    AK226165 mRNA. No translation available.
    AP002893 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW73757.1.
    CH471076 Genomic DNA. Translation: EAW73759.1.
    BC032491 mRNA. Translation: AAH32491.1.
    AF031141 mRNA. Translation: AAB86433.1.
    CCDSiCCDS7960.1. [O14933-1]
    CCDS7961.1. [O14933-2]
    RefSeqiNP_004214.1. NM_004223.4. [O14933-1]
    NP_937826.1. NM_198183.2. [O14933-2]
    UniGeneiHs.425777.

    Genome annotation databases

    EnsembliENST00000287156; ENSP00000287156; ENSG00000156587. [O14933-1]
    ENST00000340573; ENSP00000341980; ENSG00000156587. [O14933-2]
    GeneIDi9246.
    KEGGihsa:9246.
    UCSCiuc001nkn.2. human. [O14933-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243268
    , AJ243269 , AJ243270 , AJ243271 Genomic DNA. Translation: CAB64566.1 . Different initiation.
    AF061736 mRNA. Translation: AAD17525.1 .
    AK315755 mRNA. Translation: BAG38109.1 .
    CR457126 mRNA. Translation: CAG33407.1 .
    AK226165 mRNA. No translation available.
    AP002893 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW73757.1 .
    CH471076 Genomic DNA. Translation: EAW73759.1 .
    BC032491 mRNA. Translation: AAH32491.1 .
    AF031141 mRNA. Translation: AAB86433.1 .
    CCDSi CCDS7960.1. [O14933-1 ]
    CCDS7961.1. [O14933-2 ]
    RefSeqi NP_004214.1. NM_004223.4. [O14933-1 ]
    NP_937826.1. NM_198183.2. [O14933-2 ]
    UniGenei Hs.425777.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WZV X-ray 2.10 A/B 2-153 [» ]
    1WZW X-ray 2.40 A 2-153 [» ]
    2KJH NMR - A 2-153 [» ]
    ProteinModelPortali O14933.
    SMRi O14933. Positions 3-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114672. 41 interactions.
    DIPi DIP-41477N.
    IntActi O14933. 26 interactions.
    MINTi MINT-240858.
    STRINGi 9606.ENSP00000287156.

    PTM databases

    PhosphoSitei O14933.

    Proteomic databases

    MaxQBi O14933.
    PaxDbi O14933.
    PRIDEi O14933.

    Protocols and materials databases

    DNASUi 9246.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287156 ; ENSP00000287156 ; ENSG00000156587 . [O14933-1 ]
    ENST00000340573 ; ENSP00000341980 ; ENSG00000156587 . [O14933-2 ]
    GeneIDi 9246.
    KEGGi hsa:9246.
    UCSCi uc001nkn.2. human. [O14933-1 ]

    Organism-specific databases

    CTDi 9246.
    GeneCardsi GC11M057319.
    HGNCi HGNC:12490. UBE2L6.
    HPAi HPA003328.
    MIMi 603890. gene.
    neXtProti NX_O14933.
    PharmGKBi PA37139.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi O14933.
    KOi K04553.
    OMAi PEKPPYN.
    OrthoDBi EOG7GXPD8.
    PhylomeDBi O14933.
    TreeFami TF313043.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki O14933.

    Miscellaneous databases

    ChiTaRSi UBE2L6. human.
    EvolutionaryTracei O14933.
    GeneWikii UBE2L6.
    GenomeRNAii 9246.
    NextBioi 34661.
    PROi O14933.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14933.
    Bgeei O14933.
    CleanExi HS_UBE2L6.
    Genevestigatori O14933.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12."
      Ardley H.C., Rose S.A., Tan N., Leek J.P., Markham A.F., Robinson P.A.
      Cytogenet. Cell Genet. 89:137-140(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. "Human retinoic acid induced gene B (RIG-B) mRNA."
      Liu T., Mao M., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y., Wang Z., Chen S., Chen Z.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Thymus.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Brain.
    9. "Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity."
      Kumar S., Kao W.H., Howley P.M.
      J. Biol. Chem. 272:13548-13554(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-153 (ISOFORM 1).
    10. "The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein."
      Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A., Huibregtse J.M., Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 140-146, FUNCTION IN ISG15 ATTACHMENT, INDUCTION BY IFNB1.
    11. "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."
      Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.
      Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF19A.
    12. "Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme."
      Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.
      J. Biochem. 138:711-719(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ISGYLATION.
    13. "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."
      Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.
      FEBS Lett. 580:940-947(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF144B.
    14. "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase."
      Fortier J.M., Kornbluth J.
      J. Immunol. 176:6454-6463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF19B, TISSUE SPECIFICITY.
    15. "Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation."
      Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T., Kramer O.H.
      Leukemia 24:1412-1421(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF FLT3, INTERACTION WITH FLT3.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of Ubch8."
      Mizushima T., Suzuki M., Teshima N., Yamane T., Murata S., Tanaka K.
      Submitted (MAR-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-153.
    18. "The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site."
      Serniwka S.A., Shaw G.S.
      Biochemistry 48:12169-12179(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.

    Entry informationi

    Entry nameiUB2L6_HUMAN
    AccessioniPrimary (citable) accession number: O14933
    Secondary accession number(s): A6NDM6
    , A8MY53, Q8N5D8, Q9UEZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 145 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3