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    H1-4 H1.4 linker histone, cluster member [ Homo sapiens (human) ]

    Gene ID: 3008, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Frameshift mutations at the C-terminus of HIST1H1E result in a specific DNA hypomethylation signature.

    Frameshift mutations at the C-terminus of HIST1H1E result in a specific DNA hypomethylation signature.
    Ciolfi A, Aref-Eshghi E, Pizzi S, Pedace L, Miele E, Kerkhof J, Flex E, Martinelli S, Radio FC, Ruivenkamp CAL, Santen GWE, Bijlsma E, Barge-Schaapveld D, Ounap K, Siu VM, Kooy RF, Dallapiccola B, Sadikovic B, Tartaglia M., Free PMC Article

    08/21/2021
    The identification of 30 patients with HIST1H1E variants has allowed the clarification of the HIST1H1E syndrome phenotype.

    HIST1H1E heterozygous protein-truncating variants cause a recognizable syndrome with intellectual disability and distinctive facial gestalt: A study to clarify the HIST1H1E syndrome phenotype in 30 individuals.
    Burkardt DD, Zachariou A, Loveday C, Allen CL, Amor DJ, Ardissone A, Banka S, Bourgois A, Coubes C, Cytrynbaum C, Faivre L, Marion G, Horton R, Kotzot D, Lay-Son G, Lees M, Low K, Luk HM, Mark P, McConkie-Rosell A, McDonald M, Pappas J, Phillipe C, Shears D, Skotko B, Stewart F, Stewart H, Temple IK, Mau-Them FT, Verdugo RA, Weksberg R, Zarate YA, Graham JM, Tatton-Brown K.

    08/12/2020
    Crystallographic studies of an histone H1.4K26me3:lysine demethylase 4A (KDM4A) complex iidicate a conserved binding geometry to that of H3K9me3.

    Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26.
    Walport LJ, Hopkinson RJ, Chowdhury R, Zhang Y, Bonnici J, Schiller R, Kawamura A, Schofield CJ., Free PMC Article

    06/29/2019
    Results show that histones H1.2 and H1.4 were observed in MDA-MB-231 metastatic breast cancer cells. The phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during M phase suggesting that these events are cell cycle-dependent.

    Quantitative Mass Spectrometry Reveals that Intact Histone H1 Phosphorylations are Variant Specific and Exhibit Single Molecule Hierarchical Dependence.
    Chen Y, Hoover ME, Dang X, Shomo AA, Guan X, Marshall AG, Freitas MA, Young NL., Free PMC Article

    12/17/2016
    This study identified and confirmed HIST1H1E protein changes within the postsynaptic density in schizophrenia.

    Proteomic and genomic evidence implicates the postsynaptic density in schizophrenia.
    Föcking M, Lopez LM, English JA, Dicker P, Wolff A, Brindley E, Wynne K, Cagney G, Cotter DR.

    12/12/2015
    Histone H1.2-T165 post translational modifications are dispensable for chromatin binding and cell proliferation while the H1.4-K26 modifications are essential for proper cell cycle progression.

    Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications.
    Terme JM, Millán-Ariño L, Mayor R, Luque N, Izquierdo-Bouldstridge A, Bustillos A, Sampaio C, Canes J, Font I, Sima N, Sancho M, Torrente L, Forcales S, Roque A, Suau P, Jordan A.

    08/16/2014
    Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma.

    Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma.
    Li H, Kaminski MS, Li Y, Yildiz M, Ouillette P, Jones S, Fox H, Jacobi K, Saiya-Cork K, Bixby D, Lebovic D, Roulston D, Shedden K, Sabel M, Marentette L, Cimmino V, Chang AE, Malek SN., Free PMC Article

    05/10/2014
    H1.4K34 acetylation is mediated by GCN5 and is preferentially enriched at promoters of active genes, where it stimulates transcription by increasing H1 mobility and recruiting a general transcription factor.

    A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation.
    Kamieniarz K, Izzo A, Dundr M, Tropberger P, Ozretic L, Kirfel J, Scheer E, Tropel P, Wisniewski JR, Tora L, Viville S, Buettner R, Schneider R., Free PMC Article

    06/16/2012
    the N-terminal domain of H1 is an important determinant of affinity and specificity of H1-chromatin interactions.

    The N-terminal domain determines the affinity and specificity of H1 binding to chromatin.
    Öberg C, Belikov S.

    05/26/2012
    PKA-mediated H1.4S35 phosphorylation dissociates H1.4 from mitotic chromatin but also suggest that this phosphorylation is necessary for specific mitotic functions.

    Protein kinase A-mediated serine 35 phosphorylation dissociates histone H1.4 from mitotic chromosome.
    Chu CS, Hsu PH, Lo PW, Scheer E, Tora L, Tsai HJ, Tsai MD, Juan LJ., Free PMC Article

    12/17/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Investigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study.
    Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A.

    12/5/2010
    Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins

    Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins.
    Trojer P, Zhang J, Yonezawa M, Schmidt A, Zheng H, Jenuwein T, Reinberg D., Free PMC Article

    01/21/2010
    Allele-specific underacetylation of histone H4 downstream from promoter is associated with X-inactivation in human cells.

    Allele-specific underacetylation of histone H4 downstream from promoters is associated with X-inactivation in human cells.
    Morrison H, Jeppesen P.

    01/21/2010
    the lysine residue adjacent to the phosphorylation site found on the serine residue on the H1.4 peptide KARKSAGAAKR was also shown to be methylated, raising the question of whether the hypothesized "methyl/phos" switch could be extended to linker histones

    Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry.
    Garcia BA, Busby SA, Barber CM, Shabanowitz J, Allis CD, Hunt DF.

    01/21/2010
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