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    CENPS centromere protein S [ Homo sapiens (human) ]

    Gene ID: 378708, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    MHF prefers branched DNA over dsDNA because it engages two duplex arms. MHF engages DNA forks or various four-way junctions independent of the junction-site structure. The DNA-binding interface of MHF is important for cellular resistance to DNA damage.

    The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes.
    Zhao Q, Saro D, Sachpatzidis A, Singh TR, Schlingman D, Zheng XF, Mack A, Tsai MS, Mochrie S, Regan L, Meetei AR, Sung P, Xiong Y., Free PMC Article

    10/31/2015
    The MHF complex, which is a heterotetramer that comprises two MHF1-MHF2 heterodimers, is remodeled by FANCM to favor recognition of branched DNA over dsDNA.

    The histone-fold complex MHF is remodeled by FANCM to recognize branched DNA and protect genome stability.
    Fox D 3rd, Yan Z, Ling C, Zhao Y, Lee DY, Fukagawa T, Yang W, Wang W., Free PMC Article

    12/27/2014
    CENP-S is not found in a soluble complex with its binding partner CENP-T but it interacts strongly and specifically with immobilized CENP-T in an in vivo binding assay.

    A CENP-S/X complex assembles at the centromere in S and G2 phases of the human cell cycle.
    Dornblut C, Quinn N, Monajambashi S, Prendergast L, van Vuuren C, Münch S, Deng W, Leonhardt H, Cardoso MC, Hoischen C, Diekmann S, Sullivan KF., Free PMC Article

    09/13/2014
    It discusses current knowledge of the biological roles of CENP-S and CENP-X and how their dual existence may be a common feature of CCAN (constitutive centromere-associated network) proteins.

    Emerging roles for centromere-associated proteins in DNA repair and genetic recombination.
    Osman F, Whitby MC.

    08/30/2014
    A long, positively charged patch exposed on the surface of the (MHF1-MHF2) complex plays a critical role in double-stranded DNA binding to chromatin.

    Structural peculiarities of the (MHF1-MHF2)4 octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: a solution SAXS study.
    Wang W, Guo Q, Shtykova EV, Liu G, Xu J, Teng M, Liu P, Dong Y.

    11/16/2013
    MHF1 and MHF2 form a compact tetramer to which FANCM-F binds through a 'dual-V' shaped structure.

    The structure of the FANCM-MHF complex reveals physical features for functional assembly.
    Tao Y, Jin C, Li X, Qi S, Chu L, Niu L, Yao X, Teng M., Free PMC Article

    07/28/2012
    provide biochemical evidence that MHF1 and MHF2 assemble into a heterodimer that binds DNA and enhances the DNA branch migration activity of FANCM.

    MHF1-MHF2, a histone-fold-containing protein complex, participates in the Fanconi anemia pathway via FANCM.
    Singh TR, Saro D, Ali AM, Zheng XF, Du CH, Killen MW, Sachpatzidis A, Wahengbam K, Pierce AJ, Xiong Y, Sung P, Meetei AR., Free PMC Article

    10/14/2010
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article

    09/15/2010
    Results identified a centromere protein S (CENP-S)-containing subcomplex that includes the new constitutive kinetochore protein CENP-X.

    The CENP-S complex is essential for the stable assembly of outer kinetochore structure.
    Amano M, Suzuki A, Hori T, Backer C, Okawa K, Cheeseman IM, Fukagawa T., Free PMC Article

    01/21/2010
    These results indicate that APITD1 is not the tumor suppressor gene on 1p36 responsible for the negative prognostic effect in uveal melanoma with concurrent loss of chromosome arm 1p, region 36, and chromosome 3.

    Expression of APITD1 is not related to copy number changes of chromosomal region 1p36 or the prognosis of uveal melanoma.
    van Gils W, Mensink HW, Kilic E, Vaarwater J, Verbiest MM, Paridaens D, Luyten GP, de Klein A, Brüggenwirth HT.

    01/21/2010
    Mutations in APITD1 is not a common abnormality of neuroblastoma tumours.

    A novel 1p36.2 located gene, APITD1, with tumour-suppressive properties and a putative p53-binding domain, shows low expression in neuroblastoma tumours.
    Krona C, Ejeskär K, Carén H, Abel F, Sjöberg RM, Martinsson T., Free PMC Article

    01/21/2010
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