H2AFY

H2A histone family, member Y

PDB rendering based on 1u35.

Available structures
PDB	1U35, 1ZR3, 1ZR5, 2F8N, 2FXK, 3HSV, 3IID, 3IIF, 3IVB

Identifiers

Symbols

H2AFY; H2A.y; H2A/y; H2AF12M; H2AFJ; MACROH2A1.1; mH2A1; macroH2A1.2

External IDs

OMIM: 610054 MGI: 1349392 HomoloGene: 3598 GeneCards: H2AFY Gene

Gene Ontology
Molecular function	• DNA binding • chromatin binding
Cellular component	• nucleosome • condensed chromosome • Barr body • nucleus
Biological process	• nucleosome assembly • dosage compensation • chromatin modification
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
134.67 – 134.74 Mb

Chr 13:
56.17 – 56.24 Mb

PubMed search

[1]

[2]

Core histone macro-H2A.1 is a protein that in humans is encoded by the H2AFY gene.^[1]^[2]^[3]

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 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.^[3]

References

^ Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z (Aug 1998). "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 (14): 8175–80. doi:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=20949.
^ Lee Y, Hong M, Kim JW, Hong YM, Choe YK, Chang SY, Lee KS, Choe IS (Sep 1998). "Isolation of cDNA clones encoding human histone macroH2A1 subtypes". Biochim Biophys Acta 1399 (1): 73–7. PMID 9714746.
^ ^a ^b "Entrez Gene: H2AFY H2A histone family, member Y". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9555.

El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter". Mol. Cell. Biol. 18 (5): 2535–44. PMC 110633. PMID 9566873. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110633.
Costanzi C, Pehrson JR (1998). "Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals". Nature 393 (6685): 599–601. doi:10.1038/31275. PMID 9634239.
Zhang QH, Ye M, Wu XY et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310934.
Deng L, de la Fuente C, Fu P et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones". Virology 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
Chadwick BP, Willard HF (2001). "Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant". Hum. Mol. Genet. 10 (10): 1101–13. doi:10.1093/hmg/10.10.1101. PMID 11331621.
Deng L, Wang D, de la Fuente C et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
Chadwick BP, Willard HF (2002). "Cell cycle–dependent localization of macroH2A in chromatin of the inactive X chromosome". J. Cell Biol. 157 (7): 1113–23. doi:10.1083/jcb.200112074. PMC 2173542. PMID 12082075. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173542.
Takahashi I, Kameoka Y, Hashimoto K (2002). "MacroH2A1.2 binds the nuclear protein Spop". Biochim. Biophys. Acta 1591 (1–3): 63–8. doi:10.1016/S0167-4889(02)00249-5. PMID 12183056.
Ganesan S, Silver DP, Greenberg RA et al. (2002). "BRCA1 supports XIST RNA concentration on the inactive X chromosome". Cell 111 (3): 393–405. doi:10.1016/S0092-8674(02)01052-8. PMID 12419249.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Angelov D, Molla A, Perche PY et al. (2003). "The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling". Mol. Cell 11 (4): 1033–41. doi:10.1016/S1097-2765(03)00100-X. PMID 12718888.
Behrends U, Schneider I, Rössler S et al. (2003). "Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries". Int. J. Cancer 106 (2): 244–51. doi:10.1002/ijc.11208. PMID 12800201.
Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=291826.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Acín-Pérez R, Bayona-Bafaluy MP, Fernández-Silva P et al. (2004). "Respiratory Complex III Is Required to Maintain Complex I in Mammalian Mitochondria". Mol. Cell 13 (6): 805–15. doi:10.1016/S1097-2765(04)00124-8. PMC 3164363. PMID 15053874. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3164363.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Zhang R, Poustovoitov MV, Ye X et al. (2005). "Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA". Dev. Cell 8 (1): 19–30. doi:10.1016/j.devcel.2004.10.019. PMID 15621527.
Hernández-Muñoz I, Lund AH, van der Stoop P et al. (2005). "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 (21): 7635–40. doi:10.1073/pnas.0408918102. PMC 1140410. PMID 15897469. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1140410.

PDB gallery

1u35: Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

1yd9: 1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.

1zr3: Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B)

1zr5: Crystal structure of the macro-domain of human core histone variant macroH2A1.2

2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes

2fxk: Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)

H2AFY

References

Further reading