HIST2H3PS2: Difference between revisions

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{{Underlinked|date=March 2014}}
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{{Infobox_gene}}
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'''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>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Histone cluster 2, H3, pseudogene 2
| HGNCid = 32060
| Symbol = HIST2H3PS2
| AltSymbols =; MGC126031
| OMIM = 
| ECnumber = 
| Homologene = 
| MGIid = 
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}  
| Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 440686
    | Hs_Ensembl = ENSG00000203818
    | Hs_RefseqProtein = NP_001020474
    | Hs_RefseqmRNA = NM_001025303
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 147666756
    | Hs_GenLoc_end = 147667166
    | Hs_Uniprot = 
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''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 = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=440686| accessdate = }}</ref>


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=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  |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 | author=Goto H, Tomono Y, Ajiro K, ''et al.'' |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=  }}
*{{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 | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |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   |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  | author=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=  }}
*{{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 | author=Marzluff WF, Gongidi P, Woods KR, ''et al.'' |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487-98 |year= 2003 |pmid= 12408966 |doi=  }}
*{{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 | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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  | author=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=  }}
*{{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 | author=Wang Y, Wysocka J, Sayegh J, ''et al.'' |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   |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 | author=Ananthanarayanan M, Li S, Balasubramaniyan N, ''et al.'' |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   |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 | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{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 | author=Huyen Y, Zgheib O, Ditullio RA, ''et al.'' |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   |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 | author=Braastad CD, Hovhannisyan H, van Wijnen AJ, ''et al.'' |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   |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  | author=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 }}
*{{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 | author=Choi HS, Choi BY, Cho YY, ''et al.'' |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   |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 | author=Garcia BA, Barber CM, Hake SB, ''et al.'' |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   |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 | author=Hake SB, Garcia BA, Duncan EM, ''et al.'' |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   |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 | author=Miao F, Li S, Chavez V, ''et al.'' |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   |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 | author=Beck HC, Nielsen EC, Matthiesen R, ''et al.'' |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   |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 | author=Wang H, Zhai L, Xu J, ''et al.'' |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   |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 | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |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 }}
*{{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]]
 
 
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Latest revision as of 02:53, 15 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Histone cluster 2, H3, pseudogene 2, also known as HIST2H3PS2, is a human gene.[1]


References

  1. ↑ "Entrez Gene: HIST2H3PS2 histone cluster 2, H3, pseudogene 2".

Further reading


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