Histone Cluster 2, H2aa3 (HIST2H2AA3)

H2AFO; HIST2H2AA; H2A.2; H2A/q; HIST2H2AA4; H2A Histone Family Member O

SPN	K065
HGNC	4736
MGI	96097
PubMed	22402960
RGD	1307165
UniProt	Q6FI13
Wiki	HIST2H2AA3

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. HIST2H2AA3 is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.

Reference

"The relative expression of human histone H2A genes is similar in different types of proliferating cells."
DNA Cell Biol. 13:161-170(1994) [PubMed] [Europe PMC] [Abstract]

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

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and biological annotation of human chromosome 1."
Nature 441:315-321(2006) [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]