HIST2H3C: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Histone H3.2''' is a [[protein]] that in humans is encoded by the ''HIST2H3C'' [[gene]].<ref name="pmid12408966">{{cite journal | vauthors = Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ | title = The human and mouse replication-dependent histone genes | journal = Genomics | volume = 80 | issue = 5 | pages = 487–498 | date = Oct 2002 | pmid = 12408966 | pmc =  | doi = 10.1016/S0888-7543(02)96850-3 }}</ref><ref name="pmid3013246">{{cite journal | vauthors = Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G, Stein J | title = Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences | journal = Biochem Cell Biol | volume = 64 | issue = 4 | pages = 277–289 | date = Jul 1986 | pmid = 3013246 | pmc = | doi = 10.1139/o86-039 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3C histone cluster 2, H3c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_HIST2H3C_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
| PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1f66}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1m18}}, {{PDB2|1m19}}, {{PDB2|1m1a}}, {{PDB2|1p34}}, {{PDB2|1p3a}}, {{PDB2|1p3b}}, {{PDB2|1p3f}}, {{PDB2|1p3g}}, {{PDB2|1p3i}}, {{PDB2|1p3k}}, {{PDB2|1p3l}}, {{PDB2|1p3m}}, {{PDB2|1p3o}}, {{PDB2|1p3p}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|1u35}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2hue}}, {{PDB2|2io5}}, {{PDB2|2nzd}}
| Name = Histone cluster 2, H3c
| HGNCid = 20503
| Symbol = HIST2H3C
| AltSymbols =; H3; H3.2; H3/M; H3F2; H3FM; MGC9629; H3/n; H3/o
| OMIM = 142780
| ECnumber = 
| Homologene = 79492
| MGIid = 2448355
| 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 = 126961
    | Hs_Ensembl = 
    | Hs_RefseqProtein = XP_001124743
    | Hs_RefseqmRNA = XM_001124743
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 15077
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_886396
    | Mm_RefseqProtein = XP_891489
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Histone cluster 2, H3c''', also known as '''HIST2H3C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3C histone cluster 2, H3c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H3C histone cluster 2, H3c| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
HIST2H3C has been shown to [[Protein-protein interaction|interact]] with [[NCOA6]].<ref name=pmid12482968>{{cite journal | vauthors = Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW | title = Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins | journal = Mol. Cell. Biol. | volume = 23 | issue = 1 | pages = 140–149 | date = Jan 2003 | pmid = 12482968 | pmc = 140670 | doi = 10.1128/MCB.23.1.140-149.2003 }}</ref>
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Green L, Van Antwerpen R, Stein J, Stein G, Tripputi P, Emanuel B, Selden J, Croce C | title = A major human histone gene cluster on the long arm of chromosome 1 | journal = Science | volume = 226 | issue = 4676 | pages = 838–840 | year = 1984 | pmid = 6494913 | doi = 10.1126/science.6494913 }}
| citations =
* {{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=Marashi F, Helms S, Shiels A, ''et al.'' |title=Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences. |journal=Biochem. Cell Biol. |volume=64 |issue= 4 |pages= 277-89 |year= 1986 |pmid= 3013246 |doi=  }}
* {{cite journal | vauthors = Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M | title = Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay | journal = Biochim. Biophys. Acta | volume = 1296 | issue = 2 | pages = 219–27 | year = 1996 | pmid = 8814229 | doi = 10.1016/0167-4838(96)00072-6 }}
*{{cite journal | author=Green L, Van Antwerpen R, Stein J, ''et al.'' |title=A major human histone gene cluster on the long arm of chromosome 1. |journal=Science |volume=226 |issue= 4676 |pages= 838-40 |year= 1984 |pmid= 6494913 |doi= }}
* {{cite journal | vauthors = Albig W, Doenecke D | title = The human histone gene cluster at the D6S105 locus | journal = Hum. Genet. | volume = 101 | issue = 3 | pages = 284–294 | year = 1998 | pmid = 9439656 | doi = 10.1007/s004390050630 }}
*{{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 = El Kharroubi A, Piras G, Zensen R, Martin MA | title = Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter | journal = Mol. Cell. Biol. | volume = 18 | issue = 5 | pages = 2535–44 | year = 1998 | pmid = 9566873 | pmc = 110633 | doi =  10.1128/mcb.18.5.2535}}
*{{cite journal | author=Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M |title=Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay. |journal=Biochim. Biophys. Acta |volume=1296 |issue= 2 |pages= 219-27 |year= 1996 |pmid= 8814229 |doi= }}
* {{cite journal | vauthors = Ahn J, Gruen JR | title = The genomic organization of the histone clusters on human 6p21.3 | journal = Mamm. Genome | volume = 10 | issue = 7 | pages = 768–770 | year = 1999 | pmid = 10384058 | doi = 10.1007/s003359901089 }}
*{{cite journal | author=Albig W, Doenecke D |title=The human histone gene cluster at the D6S105 locus. |journal=Hum. Genet. |volume=101 |issue= 3 |pages= 284-94 |year= 1998 |pmid= 9439656 |doi= }}
* {{cite journal | vauthors = Goto H, Tomono Y, Ajiro K, Kosako H, Fujita M, Sakurai M, Okawa K, Iwamatsu A, Okigaki T, Takahashi T, Inagaki M | title = Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation | journal = J. Biol. Chem. | volume = 274 | issue = 36 | pages = 25543–25549 | year = 1999 | pmid = 10464286 | doi = 10.1074/jbc.274.36.25543 }}
*{{cite journal | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535-44 |year= 1998 |pmid= 9566873 |doi=  }}
* {{cite journal | vauthors = Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F | title = Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones | journal = Virology | volume = 277 | issue = 2 | pages = 278–295 | year = 2001 | pmid = 11080476 | doi = 10.1006/viro.2000.0593 }}
*{{cite journal | author=Ahn J, Gruen JR |title=The genomic organization of the histone clusters on human 6p21.3. |journal=Mamm. Genome |volume=10 |issue= 7 |pages= 768-70 |year= 1999 |pmid= 10384058 |doi= }}
* {{cite journal | vauthors = Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T | title = Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins | journal = Nature | volume = 410 | issue = 6824 | pages = 116–120 | year = 2001 | pmid = 11242053 | doi = 10.1038/35065132 }}
*{{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 = Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S | title = Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene | journal = J. Biol. Chem. | volume = 276 | issue = 46 | pages = 42753–42760 | year = 2001 | pmid = 11509556 | doi = 10.1074/jbc.M102626200 }}
*{{cite journal | author=Deng L, de la Fuente C, Fu P, ''et al.'' |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278-95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }}
* {{cite journal | vauthors = Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F | title = Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA | journal = Virology | volume = 289 | issue = 2 | pages = 312–326 | year = 2001 | pmid = 11689053 | doi = 10.1006/viro.2001.1129 }}
*{{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 = 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 = 11–17 | year = 2002 | pmid = 11856369 | doi = 10.1046/j.1356-9597.2001.00498.x }}
*{{cite journal | author=Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S |title=Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene. |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 42753-60 |year= 2001 |pmid= 11509556 |doi= 10.1074/jbc.M102626200 }}
* {{cite journal | vauthors = 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 | title = BRCA1 supports XIST RNA concentration on the inactive X chromosome | journal = Cell | volume = 111 | issue = 3 | pages = 393–405 | year = 2002 | pmid = 12419249 | doi = 10.1016/S0092-8674(02)01052-8 }}
*{{cite journal | author=Deng L, Wang D, de la Fuente C, ''et al.'' |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312-26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 }}
* {{cite journal | vauthors = Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW | title = Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins | journal = Mol. Cell. Biol. | volume = 23 | issue = 1 | pages = 140–149 | year = 2003 | pmid = 12482968 | pmc = 140670 | doi = 10.1128/MCB.23.1.140-149.2003 }}
*{{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 = 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 = 878–885 | year = 2003 | pmid = 12560483 | pmc = 149197 | doi = 10.1093/nar/gkg176 }}
*{{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 = Yoon HG, Chan DW, Huang ZQ, Li J, Fondell JD, Qin J, Wong J | title = Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1 | journal = EMBO J. | volume = 22 | issue = 6 | pages = 1336–1346 | year = 2003 | pmid = 12628926 | pmc = 151047 | doi = 10.1093/emboj/cdg120 }}
*{{cite journal | author=Ganesan S, Silver DP, Greenberg RA, ''et al.'' |title=BRCA1 supports XIST RNA concentration on the inactive X chromosome. |journal=Cell |volume=111 |issue= 3 |pages= 393-405 |year= 2002 |pmid= 12419249 |doi= }}
* {{cite journal | vauthors = Lusic M, Marcello A, Cereseto A, Giacca M | title = Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter | journal = EMBO J. | volume = 22 | issue = 24 | pages = 6550–6561 | year = 2004 | pmid = 14657027 | pmc = 291826 | doi = 10.1093/emboj/cdg631 }}
*{{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 | author=Goo YH, Sohn YC, Kim DH, ''et al.'' |title=Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 1 |pages= 140-9 |year= 2003 |pmid= 12482968 |doi= }}
*{{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 | author=Yoon HG, Chan DW, Huang ZQ, ''et al.'' |title=Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. |journal=EMBO J. |volume=22 |issue= 6 |pages= 1336-46 |year= 2003 |pmid= 12628926 |doi= 10.1093/emboj/cdg120 }}
*{{cite journal | author=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550-61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=126961}}


{{protein-stub}}
{{protein-stub}}
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Latest revision as of 13:43, 31 August 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 H3.2 is a protein that in humans is encoded by the HIST2H3C gene.[1][2][3]

Function

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.[3]

Interactions

HIST2H3C has been shown to interact with NCOA6.[4]

References

  1. ↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–498. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
  2. ↑ Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G, Stein J (Jul 1986). "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences". Biochem Cell Biol. 64 (4): 277–289. doi:10.1139/o86-039. PMID 3013246.
  3. ↑ 3.0 3.1 "Entrez Gene: HIST2H3C histone cluster 2, H3c".
  4. ↑ Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.

Further reading


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