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    H3-3B H3.3 histone B [ Homo sapiens (human) ]

    Gene ID: 3021, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Pediatric glioma histone H3.3 K27M/G34R mutations drive abnormalities in PML nuclear bodies.

    Pediatric glioma histone H3.3 K27M/G34R mutations drive abnormalities in PML nuclear bodies.
    Voon HPJ, Hii L, Garvie A, Udugama M, Krug B, Russo C, Chüeh AC, Daly RJ, Morey A, Bell TDM, Turner SJ, Rosenbluh J, Daniel P, Firestein R, Mann JR, Collas P, Jabado N, Wong LH., Free PMC Article

    04/2/2024
    Histone H3.3 beyond cancer: Germline mutations in Histone 3 Family 3A and 3B cause a previously unidentified neurodegenerative disorder in 46 patients.

    Histone H3.3 beyond cancer: Germline mutations in Histone 3 Family 3A and 3B cause a previously unidentified neurodegenerative disorder in 46 patients.
    Bryant L, Li D, Cox SG, Marchione D, Joiner EF, Wilson K, Janssen K, Lee P, March ME, Nair D, Sherr E, Fregeau B, Wierenga KJ, Wadley A, Mancini GMS, Powell-Hamilton N, van de Kamp J, Grebe T, Dean J, Ross A, Crawford HP, Powis Z, Cho MT, Willing MC, Manwaring L, Schot R, Nava C, Afenjar A, Lessel D, Wagner M, Klopstock T, Winkelmann J, Catarino CB, Retterer K, Schuette JL, Innis JW, Pizzino A, Lüttgen S, Denecke J, Strom TM, Monaghan KG, DDD Study, Yuan ZF, Dubbs H, Bend R, Lee JA, Lyons MJ, Hoefele J, Günthner R, Reutter H, Keren B, Radtke K, Sherbini O, Mrokse C, Helbig KL, Odent S, Cogne B, Mercier S, Bezieau S, Besnard T, Kury S, Redon R, Reinson K, Wojcik MH, Õunap K, Ilves P, Innes AM, Kernohan KD, Care4Rare Canada Consortium, Costain G, Meyn MS, Chitayat D, Zackai E, Lehman A, Kitson H, CAUSES Study, Martin MG, Martinez-Agosto JA, Undiagnosed Diseases Network, Nelson SF, Palmer CGS, Papp JC, Parker NH, Sinsheimer JS, Vilain E, Wan J, Yoon AJ, Zheng A, Brimble E, Ferrero GB, Radio FC, Carli D, Barresi S, Brusco A, Tartaglia M, Thomas JM, Umana L, Weiss MM, Gotway G, Stuurman KE, Thompson ML, McWalter K, Stumpel CTRM, Stevens SJC, Stegmann APA, Tveten K, Vøllo A, Prescott T, Fagerberg C, Laulund LW, Larsen MJ, Byler M, Lebel RR, Hurst AC, Dean J, Schrier Vergano SA, Norman J, Mercimek-Andrews S, Neira J, Van Allen MI, Longo N, Sellars E, Louie RJ, Cathey SS, Brokamp E, Heron D, Snyder M, Vanderver A, Simon C, de la Cruz X, Padilla N, Crump JG, Chung W, Garcia B, Hakonarson HH, Bhoj EJ., Free PMC Article

    04/30/2022
    Gene of the month: H3F3A and H3F3B.

    Gene of the month: H3F3A and H3F3B.
    Aldera AP, Govender D.

    01/22/2022
    The histone variant H3.3 regulates the transcription of the hepatitis B virus.

    The histone variant H3.3 regulates the transcription of the hepatitis B virus.
    Alvarez-Astudillo F, Garrido D, Varas-Godoy M, Gutiérrez JL, Villanueva RA, Loyola A.

    01/15/2022
    The interaction of histone modification related H3F3B and NSD2 genes increases the susceptibility to schizophrenia in a Chinese population.

    The interaction of histone modification related H3F3B and NSD2 genes increases the susceptibility to schizophrenia in a Chinese population.
    Liu W, Fang Y, Shi Y, Cheng Y, Sun C, Cui D.

    06/5/2021
    Histone H3.3 G34 mutations promote aberrant PRC2 activity and drive tumor progression.

    Histone H3.3 G34 mutations promote aberrant PRC2 activity and drive tumor progression.
    Jain SU, Khazaei S, Marchione DM, Lundgren SM, Wang X, Weinberg DN, Deshmukh S, Juretic N, Lu C, Allis CD, Garcia BA, Jabado N, Lewis PW., Free PMC Article

    03/28/2021
    SNPs in SLC22A3 and H3F3B may influence lipid levels through altering the expression of local genes. SNPs in H3F3B may influence CAD risk through altering the expression of local genes.

    Putative functional SNPs in SLC22A3 and H3F3B might influence the development of CAD by regulating the lipid levels.
    Mo X, Zhang H, Lei S, Xu T, Wang A, Guo Z, Zhang Y.

    11/3/2018
    evidence that a SNP in the gene H3F3B is associated with a broad schizophrenia spectrum phenotype and also alters the function of a miRNA target site within the 3' UTR of the gene.

    Validation of a microRNA target site polymorphism in H3F3B that is potentially associated with a broad schizophrenia phenotype.
    Manley W, Moreau MP, Azaro M, Siecinski SK, Davis G, Buyske S, Vieland V, Bassett AS, Brzustowicz L., Free PMC Article

    08/25/2018
    It has been suggested that H3.3K36M mutant proteins alter epigenomes of specific progenitor cells, which in turn lead to cellular transformation and tumorigenesis.

    Probe the function of histone lysine 36 methylation using histone H3 lysine 36 to methionine mutant transgene in mammalian cells.
    Fang D, Gan H, Wang H, Zhou H, Zhang Z., Free PMC Article

    06/9/2018
    Report H3F3A/B mutations in cell tumors of bone, chondroblastomas, and aneurysmal bone cysts.

    Diagnostic value of histone 3 mutations in osteoclast-rich bone tumors.
    Nohr E, Lee LH, Cates JM, Perizzolo M, Itani D.

    12/9/2017
    H3F3A and H3F3B mutation analysis appears to be a highly specific, although less sensitive, diagnostic tool for the distinction of GCTB and chondroblastoma from other giant cell-containing tumors.

    Mutation Analysis of H3F3A and H3F3B as a Diagnostic Tool for Giant Cell Tumor of Bone and Chondroblastoma.
    Cleven AH, Höcker S, Briaire-de Bruijn I, Szuhai K, Cleton-Jansen AM, Bovée JV.

    01/30/2016
    A remarkable picture of tumor type specificity for histone H3.3 driver alterations emerges, indicating that histone H3.3 residues, mutations and genes have distinct functions.

    Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone.
    Behjati S, Tarpey PS, Presneau N, Scheipl S, Pillay N, Van Loo P, Wedge DC, Cooke SL, Gundem G, Davies H, Nik-Zainal S, Martin S, McLaren S, Goodie V, Robinson B, Butler A, Teague JW, Halai D, Khatri B, Myklebost O, Baumhoer D, Jundt G, Hamoudi R, Tirabosco R, Amary MF, Futreal PA, Stratton MR, Campbell PJ, Flanagan AM., Free PMC Article

    02/15/2014
    DAXX functions as a bona fide histone chaperone involved in the replication-independent deposition of H3.3

    The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.
    Drané P, Ouararhni K, Depaux A, Shuaib M, Hamiche A., Free PMC Article

    07/5/2010
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