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{{Infobox_gene}} | |||
'''Histone cluster 2, H3, pseudogene 2''', also known as '''HIST2H3PS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3PS2 histone cluster 2, H3, pseudogene 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=440686| accessdate = }}</ref> | |||
}} | |||
'''Histone cluster 2, H3, pseudogene 2''', also known as '''HIST2H3PS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3PS2 histone cluster 2, H3, pseudogene 2| url = | |||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=Ohe Y, Iwai K |title=Human spleen histone H3. Isolation and amino acid sequence. |journal=J. Biochem. |volume=90 |issue= 4 |pages= 1205–11 |year= 1982 |pmid= 7309716 |doi= }} | ||
*{{cite journal | *{{cite journal |vauthors=Goto H, Tomono Y, Ajiro K, etal |title=Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25543–9 |year= 1999 |pmid= 10464286 |doi=10.1074/jbc.274.36.25543 }} | ||
*{{cite journal | *{{cite journal |vauthors=Lachner M, O'Carroll D, Rea S, etal |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116–20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Goto H, Yasui Y, Nigg EA, Inagaki M |title=Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. |journal=Genes Cells |volume=7 |issue= 1 |pages= 11–7 |year= 2002 |pmid= 11856369 |doi=10.1046/j.1356-9597.2001.00498.x }} | ||
*{{cite journal | *{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, etal |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487–98 |year= 2003 |pmid= 12408966 |doi=10.1016/S0888-7543(02)96850-3 }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Preuss U, Landsberg G, Scheidtmann KH |title=Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. |journal=Nucleic Acids Res. |volume=31 |issue= 3 |pages= 878–85 |year= 2003 |pmid= 12560483 |doi=10.1093/nar/gkg176 | pmc=149197 }} | ||
*{{cite journal | *{{cite journal |vauthors=Wang Y, Wysocka J, Sayegh J, etal |title=Human PAD4 regulates histone arginine methylation levels via demethylimination. |journal=Science |volume=306 |issue= 5694 |pages= 279–83 |year= 2004 |pmid= 15345777 |doi= 10.1126/science.1101400 }} | ||
*{{cite journal | *{{cite journal |vauthors=Ananthanarayanan M, Li S, Balasubramaniyan N, etal |title=Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1. |journal=J. Biol. Chem. |volume=279 |issue= 52 |pages= 54348–57 |year= 2005 |pmid= 15471871 |doi= 10.1074/jbc.M410021200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }} | ||
*{{cite journal | *{{cite journal |vauthors=Huyen Y, Zgheib O, Ditullio RA, etal |title=Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. |journal=Nature |volume=432 |issue= 7015 |pages= 406–11 |year= 2004 |pmid= 15525939 |doi= 10.1038/nature03114 }} | ||
*{{cite journal | *{{cite journal |vauthors=Braastad CD, Hovhannisyan H, van Wijnen AJ, etal |title=Functional characterization of a human histone gene cluster duplication. |journal=Gene |volume=342 |issue= 1 |pages= 35–40 |year= 2005 |pmid= 15527963 |doi= 10.1016/j.gene.2004.07.036 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Dai J, Sultan S, Taylor SS, Higgins JM |title=The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. |journal=Genes Dev. |volume=19 |issue= 4 |pages= 472–88 |year= 2005 |pmid= 15681610 |doi= 10.1101/gad.1267105 | pmc=548948 }} | ||
*{{cite journal | *{{cite journal |vauthors=Choi HS, Choi BY, Cho YY, etal |title=Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha. |journal=J. Biol. Chem. |volume=280 |issue= 14 |pages= 13545–53 |year= 2005 |pmid= 15684425 |doi= 10.1074/jbc.M410521200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Garcia BA, Barber CM, Hake SB, etal |title=Modifications of human histone H3 variants during mitosis. |journal=Biochemistry |volume=44 |issue= 39 |pages= 13202–13 |year= 2005 |pmid= 16185088 |doi= 10.1021/bi050906n }} | ||
*{{cite journal | *{{cite journal |vauthors=Hake SB, Garcia BA, Duncan EM, etal |title=Expression patterns and post-translational modifications associated with mammalian histone H3 variants. |journal=J. Biol. Chem. |volume=281 |issue= 1 |pages= 559–68 |year= 2006 |pmid= 16267050 |doi= 10.1074/jbc.M509266200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Miao F, Li S, Chavez V, etal |title=Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. |journal=Mol. Endocrinol. |volume=20 |issue= 7 |pages= 1562–73 |year= 2006 |pmid= 16497732 |doi= 10.1210/me.2005-0365 }} | ||
*{{cite journal | *{{cite journal |vauthors=Beck HC, Nielsen EC, Matthiesen R, etal |title=Quantitative proteomic analysis of post-translational modifications of human histones. |journal=Mol. Cell. Proteomics |volume=5 |issue= 7 |pages= 1314–25 |year= 2006 |pmid= 16627869 |doi= 10.1074/mcp.M600007-MCP200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Wang H, Zhai L, Xu J, etal |title=Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. |journal=Mol. Cell |volume=22 |issue= 3 |pages= 383–94 |year= 2006 |pmid= 16678110 |doi= 10.1016/j.molcel.2006.03.035 }} | ||
*{{cite journal | *{{cite journal |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
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[[Category:Pseudogenes]] | |||
{{gene-1-stub}} |
Latest revision as of 02:53, 15 October 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Histone cluster 2, H3, pseudogene 2, also known as HIST2H3PS2, is a human gene.[1]
References
Further reading
- Ohe Y, Iwai K (1982). "Human spleen histone H3. Isolation and amino acid sequence". J. Biochem. 90 (4): 1205–11. PMID 7309716.
- Goto H, Tomono Y, Ajiro K, et al. (1999). "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation". J. Biol. Chem. 274 (36): 25543–9. doi:10.1074/jbc.274.36.25543. PMID 10464286.
- Lachner M, O'Carroll D, Rea S, et al. (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.
- Goto H, Yasui Y, Nigg EA, Inagaki M (2002). "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation". Genes Cells. 7 (1): 11–7. doi:10.1046/j.1356-9597.2001.00498.x. PMID 11856369.
- Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- 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.
- Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase". Nucleic Acids Res. 31 (3): 878–85. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483.
- Wang Y, Wysocka J, Sayegh J, et al. (2004). "Human PAD4 regulates histone arginine methylation levels via demethylimination". Science. 306 (5694): 279–83. doi:10.1126/science.1101400. PMID 15345777.
- Ananthanarayanan M, Li S, Balasubramaniyan N, et al. (2005). "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1". J. Biol. Chem. 279 (52): 54348–57. doi:10.1074/jbc.M410021200. PMID 15471871.
- 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.
- Huyen Y, Zgheib O, Ditullio RA, et al. (2004). "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks". Nature. 432 (7015): 406–11. doi:10.1038/nature03114. PMID 15525939.
- Braastad CD, Hovhannisyan H, van Wijnen AJ, et al. (2005). "Functional characterization of a human histone gene cluster duplication". Gene. 342 (1): 35–40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.
- Dai J, Sultan S, Taylor SS, Higgins JM (2005). "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment". Genes Dev. 19 (4): 472–88. doi:10.1101/gad.1267105. PMC 548948. PMID 15681610.
- Choi HS, Choi BY, Cho YY, et al. (2005). "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha". J. Biol. Chem. 280 (14): 13545–53. doi:10.1074/jbc.M410521200. PMID 15684425.
- Garcia BA, Barber CM, Hake SB, et al. (2005). "Modifications of human histone H3 variants during mitosis". Biochemistry. 44 (39): 13202–13. doi:10.1021/bi050906n. PMID 16185088.
- Hake SB, Garcia BA, Duncan EM, et al. (2006). "Expression patterns and post-translational modifications associated with mammalian histone H3 variants". J. Biol. Chem. 281 (1): 559–68. doi:10.1074/jbc.M509266200. PMID 16267050.
- Miao F, Li S, Chavez V, et al. (2006). "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17". Mol. Endocrinol. 20 (7): 1562–73. doi:10.1210/me.2005-0365. PMID 16497732.
- Beck HC, Nielsen EC, Matthiesen R, et al. (2006). "Quantitative proteomic analysis of post-translational modifications of human histones". Mol. Cell. Proteomics. 5 (7): 1314–25. doi:10.1074/mcp.M600007-MCP200. PMID 16627869.
- Wang H, Zhai L, Xu J, et al. (2006). "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage". Mol. Cell. 22 (3): 383–94. doi:10.1016/j.molcel.2006.03.035. PMID 16678110.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
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