gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Histone cluster 3, H3

H3t, H3.4, HIST3H3
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is located separately from the other H3 genes that are in the histone gene cluster on chromosome 6p22-p21.3. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Histone, CAN, H2A, H4, fibrillin-1
Papers on H3t
Tissue-specific expression of histone H3 variants diversified after species separation.
Ohkawa et al., Fukuoka, Japan. In Epigenetics Chromatin, 2014
In the mouse genome, we identified 14 uncharacterized H3 genes, among which 13 are similar to H3.3 and do not have human or rat counterparts, and one is similar to human testis-specific H3 variant, H3T/H3.4,
Pathway analysis for a genome-wide association study of pneumoconiosis.
Ni et al., Nanjing, China. In Toxicol Lett, 2014
The second strongest mechanism was that rs2230656 modulates HIST3H3 to affect its role in chromatin assembly processes (p<0.001;
The Tudor domain of the PHD finger protein 1 is a dual reader of lysine trimethylation at lysine 36 of histone H3 and lysine 27 of histone variant H3t.
Jeltsch et al., Stuttgart, Germany. In J Mol Biol, 2014
We studied the interaction of the PHF1 Tudor domain with modified histone peptides and found that it recognizes H3K36me3 and H3tK27me3 (on the histone variant H3t) and that it uses the same trimethyllysine binding pocket for the interaction with both peptides.
Telomere length regulates TERRA levels through increased trimethylation of telomeric H3K9 and HP1α.
Decottignies et al., Brussels, Belgium. In Nat Struct Mol Biol, 2012
Elongated telomeres show increased trimethylated histone H3 Lys9 (H3K9me3)density.
Peptidylarginine deiminase 2-catalyzed histone H3 arginine 26 citrullination facilitates estrogen receptor α target gene activation.
Coonrod et al., Ithaca, United States. In Proc Natl Acad Sci U S A, 2012
17beta-estradiol stimulation induces the recruitment of PAD2 to target promoters by ERalpha, whereby PAD2 then citrullinates H3R26, which leads to local chromatin decondensation and transcriptional activation.
β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
Sifers et al., Houston, United States. In J Biol Chem, 2012
O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
Global histone modification pattern associated with recurrence and disease-free survival in non-small cell lung cancer patients.
Jang et al., Seoul, South Korea. In Pathol Int, 2012
our data suggest that global histone H3 and H4 modification patterns are potential markers of tumor recurrence and disease-free survival in non-small cell lung cancer
Human histone acetyltransferase 1 protein preferentially acetylates H4 histone molecules in H3.1-H4 over H3.3-H4.
Zhang et al., Rochester, United States. In J Biol Chem, 2012
HAT1 differentially impacts nucleosome assembly of H3.1-H4 and H3.3-H4.
Gene expression profiles in HPV-immortalized human cervical cells treated with the nicotine-derived carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone.
El-Bayoumy et al., State College, United States. In Chem Biol Interact, 2009
Genes identified are categorized as immune response (LTB4R), RNA surveillance pathway (SMG1), metabolism (ALDH7A1), genes frequently expressed in later stages of neoplastic development (MT1F), DNA binding (HIST3H3 and CHD1L), and protein biosynthesis (UBA52).
Expression of histone H3 tails with combinatorial lysine modifications under the reprogrammed genetic code for the investigation on epigenetic markers.
Suga et al., Tokyo, Japan. In Chem Biol, 2008
We report the ribosomal synthesis of N-terminal peptides of histone H3, so-called H3 tail (H3t), with combinatorial methyl and acetyl modifications of selected lysine residues, and the application of such peptides to studying the influence of lysine modification on H3t binding to chromodomain of heterochromatin protein 1 (chromoHP1).
Nucleosome formation with the testis-specific histone H3 variant, H3t, by human nucleosome assembly proteins in vitro.
Kurumizaka et al., Tokyo, Japan. In Nucleic Acids Res, 2008
Human Nap2 promotes nucleosome assembly with H3t/H4.
Deposition and function of histone H3 variants in Tetrahymena thermophila.
Gorovsky et al., Rochester, United States. In Mol Cell Biol, 2006
In Tetrahymena, HHT1 and HHT2 genes encode the same major histone H3; HHT3 and HHT4 encode similar minor H3 variants (H3s), H3.3 and H3.4.
Proteomic analysis of human O6-methylguanine-DNA methyltransferase by affinity chromatography and tandem mass spectrometry.
Srivenugopal et al., Amarillo, United States. In Biochem Biophys Res Commun, 2006
These procedures identified >60 MGMT-interacting proteins with diverse functions including those involved in DNA replication and repair (MCM2, PCNA, ORC1, DNA polymerase delta, MSH-2, and DNA-dependent protein kinase), cell cycle progression (CDK1, cyclin B, CDK2, CDC7, CDC10, 14-3-3 protein, and p21(waf1/cip1)), RNA processing and translation (poly(A)-binding protein, nucleolin, heterogeneous nuclear ribonucleoproteins, A2/B1, and elongation factor-1alpha), several histones (H4, H3.4, and H2A.1), and topoisomerase I.
share on facebooktweetadd +1mail to friends