H2A Histone Family, Member Y (H2AFY)

H2A.y; H2A/y; H2AF12M; mH2A1; macroH2A1.2; Core histone macro-H2A.1; Medulloblastoma antigen MU-MB-50.205

SPN	O056
HGNC	4740
MGI	1349392
PubMed	22103616
RGD	621462
UniProt	O75367
Wiki	H2AFY

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.

H2AFY encodes a member of the histone H2A family. It replaces conventional H2A histones in a subset of nucleosomes where it represses transcription and participates in stable X chromosome inactivation. Alternative splicing results in multiple transcript variants encoding different isoforms.

Reference

"Isolation of cDNA clones encoding human histone macroH2A1 subtypes."
Biochim. Biophys. Acta 1399:73-77(1998) [PubMed] [Europe PMC] [Abstract]

"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [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 comparative analysis of human chromosome 5."
Nature 431:268-274(2004) [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]

"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries."
Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract]

"Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals."
Nature 393:599-601(1998) [PubMed] [Europe PMC] [Abstract]

"The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling."
Mol. Cell 11:1033-1041(2003) [PubMed] [Europe PMC] [Abstract]

"Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain."
Biochem. Biophys. Res. Commun. 336:204-209(2005) [PubMed] [Europe PMC] [Abstract]

"Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]

"The macro domain is an ADP-ribose binding module."
EMBO J. 24:1911-1920(2005) [PubMed] [Europe PMC] [Abstract]

"Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]

"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]

"Mechanism of polymerase II transcription repression by the histone variant macroH2A."
Mol. Cell. Biol. 26:1156-1164(2006) [PubMed] [Europe PMC] [Abstract]

"Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry."
Mol. Cell. Proteomics 5:194-203(2006) [PubMed] [Europe PMC] [Abstract]

"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"Structural characterization of the histone variant macroH2A."
Mol. Cell. Biol. 25:7616-7624(2005) [PubMed] [Europe PMC] [Abstract]

"Splicing regulates NAD metabolite binding to histone macroH2A."
Nat. Struct. Mol. Biol. 12:624-625(2005) [PubMed] [Europe PMC] [Abstract]

"Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases."
Mol. Cell 36:39-50(2009) [PubMed] [Europe PMC] [Abstract]