Recombinant Human Core histone macro-H2A.1 (MACROH2A1)

1. This article points to a splicing-regulated, proto-oncogenic role for the macroH2A1.2 variant and suggests manipulation of macroH2A1.2 expression as a potential therapeutic means to interfere with tumorigenesis. PMID:29249653
2. The Skp2-mH2A1-CDK8 axis has a critical role in breast cancer development via dysregulation of the G2/M transition, polyploidy, cell growth dysregulation, and loss of tumor suppression. PMID:25818643
3. We show that composite nucleosomes containing mH2A and NRF-1 are stably positioned on gene regulatory regions and can buffer transcriptional noise associated with antiviral responses PMID:25959814
4. High MacroH2A1 expression is associated with epigenetic markers for activation of lipogenic genes in fat-induced steatosis. PMID:25526730
5. macroH2A1.1 expression correlates with poor survival of triple-negative breast cancer patients PMID:24911873
6. MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation. PMID:25306110
7. MacroH2A1 specifically recruits PELP1 to the promoters of macroH2A1 target genes, but macroH2A1 occupancy occurs independent of PELP1. This recruitment allows macroH2A1 and PELP1 to cooperatively regulate gene expression outcomes. PMID:24752897
8. The results demonstrate that macroH2A1 is a new factor involved in the regulation of rDNA transcription. PMID:24071584
9. macro histone variants (macroH2A) are expressed at low levels in stem cells and are up-regulated during differentiation PMID:23595991
10. Both macroH2A1 isoforms may play a role in hepatocellular carcinoma pathogenesis and may be considered as novel diagnostic markers for human hepatocellular carcinoma. PMID:23372727
11. MacroH2A1 splicing isoforms differentially regulate the transcription of a set of genes involved in redox metabolism. PMID:23022728
12. The histone variant macroH2A1.1 is recruited to DNA double-strand breaks through a mechanism involving PARP1. PMID:23031826
13. Within the macro domain of mH2A1.2, a trinucleotide insertion (-EIS-) sequence not found in mH2A1.1 was essential for the interaction between HER-2 and mH2A1.2 as well as mH2A1.2-induced HER-2 expression and cell proliferation. PMID:22589551
14. ATRX (alpha-thalassemia/MR, X-linked) is a novel macroH2A-interacting protein PMID:22391447
15. H2AFY is specifically overexpressed in the blood and frontal cortex of patients with Huntington disease compared with controls PMID:21969577
16. macroH2A can play either a positive or negative role in transcriptional regulation in a context-dependent manner. Additionally, macroH2A has been linked to the control of the cell cycle and cell proliferation. PMID:20543561
17. significant inverse correlation between mH2A and CDK8 expression levels exists in melanoma patient samples PMID:21179167
18. distributed during the maintainance phase of x inactivation throughout cell cycle PMID:12082075
19. MACROH2A1 deposition is regulated by the CULLIN3/SPOP ligase complex and is actively involved in stable X inactivation. PMID:15897469
20. A specific interaction between mH2A1.1 and PARP-1 was demonstrated and found to be associated with inactivation of PARP-1 enzymatic activity. PMID:17158748
21. multiple short sequences dispersed along the macroH2A1 histone domain individually supported enrichment on the inactive X chromosome when introduced into H2A PMID:17570398
22. A phosphorylation site, S137ph, was identified in mH2A1;S137ph is enriched in mitosis. PMID:18227505
23. expression of histone macroH2A1.1 and macroH2A2 predicts lung cancer recurrence. PMID:19648962
24. show that distinct macrodomains, including those of histone macroH2A1.1, are recruited to sites of PARP1 activation induced by laser-generated DNA damage. PMID:19680243
25. an unexpected role for macroH2A1 in the escape from heterochromatin-associated silencing and the enhancement of autosomal gene transcription PMID:20008927

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HGNC: 4740

UNIGENE: Hs.420272

KEGG: hsa:9555

STRING: 9606.ENSP00000423563

OMIM: 610054