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Q96SW2

- CRBN_HUMAN

UniProt

Q96SW2 - CRBN_HUMAN

Protein

Protein cereblon

Gene

CRBN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ATP-dependent peptidase activity Source: InterPro
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of ion transmembrane transport Source: Ensembl
    2. negative regulation of protein homooligomerization Source: Ensembl
    3. positive regulation of protein homodimerization activity Source: Ensembl
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein ubiquitination Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein cereblon
    Gene namesi
    Name:CRBN
    ORF Names:AD-006
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30185. CRBN.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. membrane Source: UniProtKB-SubCell
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal recessive 2A (MRT2A) [MIM:607417]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. MRT2A patients display mild mental retardation with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi384 – 3841Y → A: Abolishes thalidomide-binding without affecting DCX protein ligase complex activity; when associated with A-386. 1 Publication
    Mutagenesisi386 – 3861W → A: Abolishes thalidomide-binding without affecting DCX protein ligase complex activity; when associated with A-384. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi607417. phenotype.
    Orphaneti88616. Autosomal recessive nonsyndromic intellectual disability.
    1620. Distal monosomy 3p.
    PharmGKBiPA134926851.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 442442Protein cereblonPRO_0000076160Add
    BLAST

    Post-translational modificationi

    Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ96SW2.
    PaxDbiQ96SW2.
    PRIDEiQ96SW2.

    PTM databases

    PhosphoSiteiQ96SW2.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in brain.2 Publications

    Gene expression databases

    BgeeiQ96SW2.
    CleanExiHS_CRBN.
    GenevestigatoriQ96SW2.

    Organism-specific databases

    HPAiHPA045910.

    Interactioni

    Subunit structurei

    Interacts with KCNT1 By similarity. Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi119360. 16 interactions.
    IntActiQ96SW2. 8 interactions.
    MINTiMINT-4537481.
    STRINGi9606.ENSP00000231948.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M91X-ray1.10B229-240[»]
    ProteinModelPortaliQ96SW2.
    SMRiQ96SW2. Positions 80-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 317238LonAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni339 – 442104Thalidomide-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CRBN family.Curated
    Contains 1 Lon domain.Curated

    Phylogenomic databases

    eggNOGiNOG313031.
    HOGENOMiHOG000067866.
    HOVERGENiHBG054571.
    InParanoidiQ96SW2.
    KOiK11793.
    OMAiCQDTEIT.
    PhylomeDBiQ96SW2.
    TreeFamiTF106115.

    Family and domain databases

    InterProiIPR003111. Pept_S16_N.
    IPR015947. PUA-like_domain.
    [Graphical view]
    PfamiPF02190. LON. 1 hit.
    [Graphical view]
    SMARTiSM00464. LON. 1 hit.
    [Graphical view]
    SUPFAMiSSF88697. SSF88697. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96SW2-1) [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

    MAGEGDQQDA AHNMGNHLPL LPAESEEEDE MEVEDQDSKE AKKPNIINFD    50
    TSLPTSHTYL GADMEEFHGR TLHDDDSCQV IPVLPQVMMI LIPGQTLPLQ 100
    LFHPQEVSMV RNLIQKDRTF AVLAYSNVQE REAQFGTTAE IYAYREEQDF 150
    GIEIVKVKAI GRQRFKVLEL RTQSDGIQQA KVQILPECVL PSTMSAVQLE 200
    SLNKCQIFPS KPVSREDQCS YKWWQKYQKR KFHCANLTSW PRWLYSLYDA 250
    ETLMDRIKKQ LREWDENLKD DSLPSNPIDF SYRVAACLPI DDVLRIQLLK 300
    IGSAIQRLRC ELDIMNKCTS LCCKQCQETE ITTKNEIFSL SLCGPMAAYV 350
    NPHGYVHETL TVYKACNLNL IGRPSTEHSW FPGYAWTVAQ CKICASHIGW 400
    KFTATKKDMS PQKFWGLTRS ALLPTIPDTE DEISPDKVIL CL 442
    Length:442
    Mass (Da):50,546
    Last modified:December 1, 2001 - v1
    Checksum:i90DF77D98A8BEAA8
    GO
    Isoform 2 (identifier: Q96SW2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         23-23: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:441
    Mass (Da):50,475
    Checksum:i28B44733BBB461C1
    GO

    Sequence cautioni

    The sequence AAF17211.1 differs from that shown. Reason: Frameshift at positions 347, 397 and 401.
    The sequence BAG35471.1 differs from that shown. Reason: Frameshift at position 347.
    The sequence BAG35471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291K → R in AAH67811. (PubMed:16641997)Curated
    Sequence conflicti237 – 2371L → P in BAG35471. (PubMed:14702039)Curated
    Sequence conflicti292 – 2921D → G in BAG35471. (PubMed:14702039)Curated
    Sequence conflicti330 – 3301E → G in BAG35471. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei23 – 231Missing in isoform 2. 1 PublicationVSP_015209

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027507 mRNA. Translation: BAB55162.1.
    AK312577 mRNA. Translation: BAG35471.1. Sequence problems.
    AC024060 Genomic DNA. No translation available.
    BC017419 mRNA. Translation: AAH17419.1.
    BC067811 mRNA. Translation: AAH67811.1.
    AF117230 mRNA. Translation: AAF17211.1. Frameshift.
    CR627060 mRNA. Translation: CAH10361.1.
    CCDSiCCDS2562.1. [Q96SW2-1]
    CCDS54547.1. [Q96SW2-2]
    RefSeqiNP_001166953.1. NM_001173482.1. [Q96SW2-2]
    NP_057386.2. NM_016302.3. [Q96SW2-1]
    UniGeneiHs.18925.

    Genome annotation databases

    EnsembliENST00000231948; ENSP00000231948; ENSG00000113851. [Q96SW2-1]
    ENST00000432408; ENSP00000412499; ENSG00000113851. [Q96SW2-2]
    GeneIDi51185.
    KEGGihsa:51185.
    UCSCiuc003bpq.3. human. [Q96SW2-1]
    uc003bpr.3. human. [Q96SW2-2]

    Polymorphism databases

    DMDMi73918916.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    A short story - Issue 117 of May 2010

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027507 mRNA. Translation: BAB55162.1 .
    AK312577 mRNA. Translation: BAG35471.1 . Sequence problems.
    AC024060 Genomic DNA. No translation available.
    BC017419 mRNA. Translation: AAH17419.1 .
    BC067811 mRNA. Translation: AAH67811.1 .
    AF117230 mRNA. Translation: AAF17211.1 . Frameshift.
    CR627060 mRNA. Translation: CAH10361.1 .
    CCDSi CCDS2562.1. [Q96SW2-1 ]
    CCDS54547.1. [Q96SW2-2 ]
    RefSeqi NP_001166953.1. NM_001173482.1. [Q96SW2-2 ]
    NP_057386.2. NM_016302.3. [Q96SW2-1 ]
    UniGenei Hs.18925.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M91 X-ray 1.10 B 229-240 [» ]
    ProteinModelPortali Q96SW2.
    SMRi Q96SW2. Positions 80-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119360. 16 interactions.
    IntActi Q96SW2. 8 interactions.
    MINTi MINT-4537481.
    STRINGi 9606.ENSP00000231948.

    PTM databases

    PhosphoSitei Q96SW2.

    Polymorphism databases

    DMDMi 73918916.

    Proteomic databases

    MaxQBi Q96SW2.
    PaxDbi Q96SW2.
    PRIDEi Q96SW2.

    Protocols and materials databases

    DNASUi 51185.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231948 ; ENSP00000231948 ; ENSG00000113851 . [Q96SW2-1 ]
    ENST00000432408 ; ENSP00000412499 ; ENSG00000113851 . [Q96SW2-2 ]
    GeneIDi 51185.
    KEGGi hsa:51185.
    UCSCi uc003bpq.3. human. [Q96SW2-1 ]
    uc003bpr.3. human. [Q96SW2-2 ]

    Organism-specific databases

    CTDi 51185.
    GeneCardsi GC03M003166.
    HGNCi HGNC:30185. CRBN.
    HPAi HPA045910.
    MIMi 607417. phenotype.
    609262. gene.
    neXtProti NX_Q96SW2.
    Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
    1620. Distal monosomy 3p.
    PharmGKBi PA134926851.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313031.
    HOGENOMi HOG000067866.
    HOVERGENi HBG054571.
    InParanoidi Q96SW2.
    KOi K11793.
    OMAi CQDTEIT.
    PhylomeDBi Q96SW2.
    TreeFami TF106115.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GeneWikii Cereblon.
    GenomeRNAii 51185.
    NextBioi 54159.
    PROi Q96SW2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96SW2.
    CleanExi HS_CRBN.
    Genevestigatori Q96SW2.

    Family and domain databases

    InterProi IPR003111. Pept_S16_N.
    IPR015947. PUA-like_domain.
    [Graphical view ]
    Pfami PF02190. LON. 1 hit.
    [Graphical view ]
    SMARTi SM00464. LON. 1 hit.
    [Graphical view ]
    SUPFAMi SSF88697. SSF88697. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "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: Brain.
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-442.
      Tissue: Adrenal gland.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-250.
      Tissue: Fetal kidney.
    6. "A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation."
      Higgins J.J., Pucilowska J., Lombardi R.Q., Rooney J.P.
      Neurology 63:1927-1931(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRT2A, TISSUE SPECIFICITY.
    7. "Primary function analysis of human mental retardation related gene CRBN."
      Xin W., Xiaohua N., Peilin C., Xin C., Yaqiong S., Qihan W.
      Mol. Biol. Rep. 35:251-256(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Dysregulation of large-conductance Ca2+-activated K+ channel expression in nonsyndromal mental retardation due to a cereblon p.R419X mutation."
      Higgins J.J., Hao J., Kosofsky B.E., Rajadhyaksha A.M.
      Neurogenetics 9:219-223(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Identification of a primary target of thalidomide teratogenicity."
      Ito T., Ando H., Suzuki T., Ogura T., Hotta K., Imamura Y., Yamaguchi Y., Handa H.
      Science 327:1345-1350(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A DCX COMPLEX WITH DDB1; RBX1 AND CUL4A, THALIDOMIDE-BINDING, UBIQUITINATION, MUTAGENESIS OF TYR-384 AND TRP-386.

    Entry informationi

    Entry nameiCRBN_HUMAN
    AccessioniPrimary (citable) accession number: Q96SW2
    Secondary accession number(s): B2R6H4
    , C9IZA9, C9JAH6, Q6AI62, Q6NVZ0, Q9UHW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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

    Miscellaneous

    Specifically binds thalidomide, a drug widely prescribed to pregnant women in the late 1950s. Thalidomide was sold as a sedative but was found to be teratogenic, causing multiple birth defects. Recently, thalidomide use has increased for the treatment of multiple myeloma and erythema nodosum leprosum, a painful complication of leprosy. Thalidomide teratogenic activity may be a consequence of CRBN-binding, which inhibits the ubiquitin ligase activity of the DCX (DDB1-CUL4-X-box) protein ligase complex, possibly leading to abnormal regulation of the BMP and FGF8 signaling pathways (PubMed:20223979).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3