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    DPF2 double PHD fingers 2 [ Homo sapiens (human) ]

    Gene ID: 5977, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    DPF2-related Coffin-Siris syndrome type 7 in two generations.

    DPF2-related Coffin-Siris syndrome type 7 in two generations.
    Kolokotronis K, Suter AA, Ivanovski I, Frey T, Bahr A, Rauch A, Steindl K.

    07/1/2024
    BAF45D knockdown decreases cell viability, inhibits colony formation, induces cell apoptosis and S-phase arrest in human pancreatic cancer cells.

    BAF45D knockdown decreases cell viability, inhibits colony formation, induces cell apoptosis and S-phase arrest in human pancreatic cancer cells.
    Liu Z, Liu L, Sun R, Liu C.

    02/2/2021
    de novo variants in DPF2 cause Coffin-Siris syndrome and propose a dominant-negative mechanism of pathogenicity.

    Mutations in the BAF-Complex Subunit DPF2 Are Associated with Coffin-Siris Syndrome.
    Vasileiou G, Vergarajauregui S, Endele S, Popp B, Büttner C, Ekici AB, Gerard M, Bramswig NC, Albrecht B, Clayton-Smith J, Morton J, Tomkins S, Low K, Weber A, Wenzel M, Altmüller J, Li Y, Wollnik B, Hoganson G, Plona MR, Cho MT, Deciphering Developmental Disorders Study, Thiel CT, Lüdecke HJ, Strom TM, Calpena E, Wilkie AOM, Wieczorek D, Engel FB, Reis A., Free PMC Article

    12/22/2018
    Authors show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via bipartite binding pockets on the DPF2 surface. Blocking these interactions through targeted mutagenesis of DPF2 abolishes its recruitment to target chromatin regions as well as its ability to prevent myeloid differentiation in vivo.

    Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.
    Huber FM, Greenblatt SM, Davenport AM, Martinez C, Xu Y, Vu LP, Nimer SD, Hoelz A., Free PMC Article

    05/26/2018
    Upon influenza virus infection, DPF2 dysregulated IFN-beta induction and expression of cytokines/chemokines and antiviral proteins. This study provides evidence that influenza virus utilizes DPF2 to escape host innate immunity.

    Double Plant Homeodomain Fingers 2 (DPF2) Promotes the Immune Escape of Influenza Virus by Suppressing Beta Interferon Production.
    Shin D, Lee J, Park JH, Min JY., Free PMC Article

    07/29/2017
    The demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylation with the strongest preference for propionylation (Kcr).

    Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.
    Xiong X, Panchenko T, Yang S, Zhao S, Yan P, Zhang W, Xie W, Li Y, Zhao Y, Allis CD, Li H., Free PMC Article

    05/13/2017
    the role of SMARCA4 and the two SWI/SNF subunits SMARCD2/BAF60B and DPF2/BAF45D in leukaemia, was investigated.

    SWI/SNF Subunits SMARCA4, SMARCD2 and DPF2 Collaborate in MLL-Rearranged Leukaemia Maintenance.
    Cruickshank VA, Sroczynska P, Sankar A, Miyagi S, Rundsten CF, Johansen JV, Helin K., Free PMC Article

    06/28/2016
    DPF2 decreases monomeric and mono-ubiquitinated OCT4, assembles poly-ubiquitin chains on OCT4 mainly through Ub-K48 linkage

    DPF2 regulates OCT4 protein level and nuclear distribution.
    Liu C, Zhang D, Shen Y, Tao X, Liu L, Zhong Y, Fang S.

    01/2/2016
    crystal structure of the C2H2-type zinc finger domain of human DPF2 with a canonical C2H2 fold, which contains two beta strands and one alpha helix, was reported.

    Crystal structure of the Cys2His2-type zinc finger domain of human DPF2.
    Zhang W, Xu C, Bian C, Tempel W, Crombet L, MacKenzie F, Min J, Liu Z, Qi C.

    11/19/2011
    found that targeting Requiem and Alg-2 did not result in extended culture viability, but resulted in an increase in maximum viable cell numbers and cumulative IVCD under fed-batch conditions

    Simultaneous targeting of Requiem & Alg-2 in Chinese hamster ovary cells for improved recombinant protein production.
    Lim Y, Mantalaris A, Yap MG, Wong DC.

    02/5/2011
    REQ functions as an efficient adaptor protein between the SWI/SNF complex and RelB/p52 and plays important roles in noncanonical NF-kappaB transcriptional activation and its associated oncogenic activity.

    Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a noncanonical NF-kappaB pathway.
    Tando T, Ishizaka A, Watanabe H, Ito T, Iida S, Haraguchi T, Mizutani T, Izumi T, Isobe T, Akiyama T, Inoue J, Iba H., Free PMC Article

    08/9/2010
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