Histone Cluster 1, H2ad (HIST1H2AD)

H2AFG; H2A/g; H2A.3; H2A Histone Family Member G

SPN	K062
HGNC	4729
MGI	2448289
PubMed	9119399
UniProt	P20671
Wiki	HIST1H2AD

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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.

HIST1H2AD is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.

Reference

"Nucleotide sequences of mouse histone genes H2A and H3.1."
Nucleic Acids Res. 17:8861-8861(1989) [PubMed] [Europe PMC] [Abstract]

"Human histone gene organization: nonregular arrangement within a large cluster."
Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]

"The human and mouse replication-dependent histone genes."
Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo."
Genes Dev. 18:877-888(2004) [PubMed] [Europe PMC] [Abstract]

"Phosphorylation of histone H2A inhibits transcription on chromatin templates."
J. Biol. Chem. 279:21866-21872(2004) [PubMed] [Europe PMC] [Abstract]

"Role of histone H2A ubiquitination in Polycomb silencing."
Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]

"Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes."
Biochemistry 44:5827-5834(2005) [PubMed] [Europe PMC] [Abstract]

"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]

"DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A."
Genes Dev. 20:1343-1352(2006) [PubMed] [Europe PMC] [Abstract]

"Precise characterization of human histones in the H2A gene family by top down mass spectrometry."
J. Proteome Res. 5:248-253(2006) [PubMed] [Europe PMC] [Abstract]

"RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins."
Cell 131:887-900(2007) [PubMed] [Europe PMC] [Abstract]

"RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly."
Cell 131:901-914(2007) [PubMed] [Europe PMC] [Abstract]

"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage."
Cell 136:420-434(2009) [PubMed] [Europe PMC] [Abstract]

"RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins."
Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract]

"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]

"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling."
Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract]

"A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase."
Cell Cycle 11:2538-2544(2012) [PubMed] [Europe PMC] [Abstract]

"VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription."
Mol. Cell 52:459-467(2013) [PubMed] [Europe PMC] [Abstract]

"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]

"TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein."
Nature 516:116-120(2014) [PubMed] [Europe PMC] [Abstract]