H2AFY

Core histone macro-H2A.1 is a protein that in humans is encoded by the H2AFY gene.[5][6][7]

MACROH2A1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1U35, 1ZR3, 1ZR5, 2F8N, 2FXK, 3HQH, 3HSV, 3IID, 3IIF, 3IVB, 5IIT
Identifiers
Aliases	MACROH2A1, H2A.y, H2A/y, H2AF12M, H2AFJ, MACROH2A1.1, mH2A1, macroH2A1.2, H2A histone family member Y, H2AFY, macroH2A.1 histone
External IDs	OMIM: 610054 MGI: 1349392 HomoloGene: 3598 GeneCards: MACROH2A1
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q31.1 Start 135,333,900 bp[1] End 135,399,914 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13|13 B1 Start 56,073,619 bp[2] End 56,136,361 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein kinase binding • rDNA binding • protein serine/threonine kinase inhibitor activity • RNA polymerase II regulatory region sequence-specific DNA binding • chromatin binding • double-stranded methylated DNA binding • protein heterodimerization activity • RNA polymerase II core promoter sequence-specific DNA binding • core promoter sequence-specific DNA binding • DNA binding • chromatin DNA binding • enzyme binding • GO:0001948 protein binding • nucleosomal DNA binding • promoter-specific chromatin binding Cellular component • extracellular exosome • ESC/E(Z) complex • nucleolus • condensed chromosome • nuclear chromosome, telomeric region • chromosome • pericentric heterochromatin • nucleosome • cell nucleus • nuclear chromosome • sex chromatin • Barr body • nuclear chromatin • chromatin Biological process • chromatin silencing • negative regulation of histone H3-K4 methylation • regulation of chromatin silencing at rDNA • dosage compensation • negative regulation of cell cycle G2/M phase transition • positive regulation of gene expression, epigenetic • regulation of cell growth • positive regulation of keratinocyte differentiation • negative regulation of histone phosphorylation • negative regulation of protein serine/threonine kinase activity • negative regulation of transcription from RNA polymerase II promoter • nucleosome assembly • negative regulation of protein localization to chromosome, telomeric region • negative regulation of gene expression, epigenetic • negative regulation of histone H3-K27 methylation • epigenetic regulation of gene expression • positive regulation of maintenance of mitotic sister chromatid cohesion • establishment of protein localization to chromatin • negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter • regulation of lipid metabolic process • covalent chromatin modification • regulation of response to oxidative stress • negative regulation of response to oxidative stress • positive regulation of response to oxidative stress • chromatin organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9555	26914
Ensembl	ENSG00000113648	ENSMUSG00000015937
UniProt	O75367	Q9QZQ8
RefSeq (mRNA)	NM_001040158 NM_004893 NM_138609 NM_138610	NM_001159513 NM_001159514 NM_001159515 NM_012015
RefSeq (protein)	NP_001035248 NP_004884 NP_613075 NP_613258	NP_001152985 NP_001152986 NP_001152987 NP_036145
Location (UCSC)	Chr 5: 135.33 – 135.4 Mb	Chr 13: 56.07 – 56.14 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7] Expression of these isoforms is associated to several cancers, such as hepatocellular carcinoma.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000113648 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000015937 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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 (Jul 1998). "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 95 (14): 8175–80. doi:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160.
6. Lee Y, Hong M, Kim JW, Hong YM, Choe YK, Chang SY, Lee KS, Choe IS (Jul 1998). "Isolation of cDNA clones encoding human histone macroH2A1 subtypes". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1399 (1): 73–7. doi:10.1016/s0167-4781(98)00098-0. PMID 9714746.
7. "Entrez Gene: H2AFY H2A histone family, member Y".
8. Rappa F, Greco A, Podrini C, Cappello F, Foti M, Bourgoin L, Peyrou M, Marino A, Scibetta N, Williams R, Mazzoccoli G, Federici M, Pazienza V, Vinciguerra M (2013). "Immunopositivity for histone macroH2A1 isoforms marks steatosis-associated hepatocellular carcinoma". PLOS ONE. 8 (1): e54458. doi:10.1371/journal.pone.0054458. PMC 3553099. PMID 23372727.

Further reading

• El Kharroubi A, Piras G, Zensen R, Martin MA (May 1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Molecular and Cellular Biology. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Costanzi C, Pehrson JR (Jun 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, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F (Nov 2000). "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 (May 2001). "Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant". Human Molecular Genetics. 10 (10): 1101–13. doi:10.1093/hmg/10.10.1101. PMID 11331621.
• Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F (Oct 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 (Jun 2002). "Cell cycle-dependent localization of macroH2A in chromatin of the inactive X chromosome". The Journal of Cell Biology. 157 (7): 1113–23. doi:10.1083/jcb.200112074. PMC 2173542. PMID 12082075.
• Takahashi I, Kameoka Y, Hashimoto K (Aug 2002). "MacroH2A1.2 binds the nuclear protein Spop". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1591 (1–3): 63–8. doi:10.1016/S0167-4889(02)00249-5. PMID 12183056.
• Ganesan S, Silver DP, Greenberg RA, Avni D, Drapkin R, Miron A, Mok SC, Randrianarison V, Brodie S, Salstrom J, Rasmussen TP, Klimke A, Marrese C, Marahrens Y, Deng CX, Feunteun J, Livingston DM (Nov 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.
• Angelov D, Molla A, Perche PY, Hans F, Côté J, Khochbin S, Bouvet P, Dimitrov S (Apr 2003). "The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling". Molecular Cell. 11 (4): 1033–41. doi:10.1016/S1097-2765(03)00100-X. PMID 12718888.
• Behrends U, Schneider I, Rössler S, Frauenknecht H, Golbeck A, Lechner B, Eigenstetter G, Zobywalski C, Müller-Weihrich S, Graubner U, Schmid I, Sackerer D, Späth M, Goetz C, Prantl F, Asmuss HP, Bise K, Mautner J (Aug 2003). "Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries". International Journal of Cancer. 106 (2): 244–51. doi:10.1002/ijc.11208. PMID 12800201.
• Lusic M, Marcello A, Cereseto A, Giacca M (Dec 2003). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". The EMBO Journal. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
• Acín-Pérez R, Bayona-Bafaluy MP, Fernández-Silva P, Moreno-Loshuertos R, Pérez-Martos A, Bruno C, Moraes CT, Enríquez JA (Mar 2004). "Respiratory complex III is required to maintain complex I in mammalian mitochondria". Molecular Cell. 13 (6): 805–15. doi:10.1016/S1097-2765(04)00124-8. PMC 3164363. PMID 15053874.
• Zhang R, Poustovoitov MV, Ye X, Santos HA, Chen W, Daganzo SM, Erzberger JP, Serebriiskii IG, Canutescu AA, Dunbrack RL, Pehrson JR, Berger JM, Kaufman PD, Adams PD (Jan 2005). "Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA". Developmental Cell. 8 (1): 19–30. doi:10.1016/j.devcel.2004.10.019. PMID 15621527.
• Hernández-Muñoz I, Lund AH, van der Stoop P, Boutsma E, Muijrers I, Verhoeven E, Nusinow DA, Panning B, Marahrens Y, van Lohuizen M (May 2005). "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase". Proceedings of the National Academy of Sciences of the United States of America. 102 (21): 7635–40. doi:10.1073/pnas.0408918102. PMC 1140410. PMID 15897469.
• Ioudinkova ES, Barat A, Pichugin A, Markova E, Sklyar I, Pirozhkova I, Robin C, Lipinski M, Ogryzko V, Vassetzky YS, Razin SV (2012). "Distinct distribution of ectopically expressed histone variants H2A.Bbd and MacroH2A in open and closed chromatin domains". PLOS ONE. 7 (10): e47157. doi:10.1371/journal.pone.0047157. PMC 3484066. PMID 23118866.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Core histone macro-H2A.1