HIST1H3A: Difference between revisions
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}) |
m Bot: HTTP→HTTPS |
||
Line 1: | Line 1: | ||
{{Infobox_gene}} | |||
{{ | '''Histone H3.1''' is a [[protein]] that in humans is encoded by the ''HIST1H3A'' [[gene]].<ref name="pmid9119399">{{cite journal |vauthors=Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D | title = Human histone gene organization: nonregular arrangement within a large cluster | journal = Genomics | volume = 40 | issue = 2 | pages = 314–22 |date=Apr 1997 | pmid = 9119399 | pmc = | doi = 10.1006/geno.1996.4592 }}</ref><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 = 487–98 |date=Oct 2002 | pmid = 12408966 | pmc = | doi =10.1016/S0888-7543(02)96850-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIST1H3A histone cluster 1, H3a| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8350| accessdate = }}</ref> | ||
}} | |||
| | |||
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | ||
{{PBB_Summary | {{PBB_Summary | ||
| section_title = | | 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 the large histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez" | | 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 the large histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez" /> | ||
}} | }} | ||
==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=Albig W, Kardalinou E, Drabent B, etal |title=Isolation and characterization of two human H1 histone genes within clusters of core histone genes |journal=Genomics |volume=10 |issue= 4 |pages= 940–8 |year= 1991 |pmid= 1916825 |doi=10.1016/0888-7543(91)90183-F }} | ||
*{{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= 284–94 |year= 1998 |pmid= 9439656 |doi=10.1007/s004390050630 }} | |||
*{{cite journal | | *{{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 |doi= 10.1128/mcb.18.5.2535| pmc=110633 }} | ||
*{{cite journal | | *{{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= 768–70 |year= 1999 |pmid= 10384058 |doi=10.1007/s003359901089 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Rea S, Eisenhaber F, O'Carroll D, etal |title=Regulation of chromatin structure by site-specific histone H3 methyltransferases |journal=Nature |volume=406 |issue= 6796 |pages= 593–9 |year= 2000 |pmid= 10949293 |doi= 10.1038/35020506 }} | ||
*{{cite journal | *{{cite journal |vauthors=Hsu JY, Sun ZW, Li X, etal |title=Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes |journal=Cell |volume=102 |issue= 3 |pages= 279–91 |year= 2000 |pmid= 10975519 |doi=10.1016/S0092-8674(00)00034-9 }} | ||
*{{cite journal | *{{cite journal |vauthors=Deng L, de la Fuente C, Fu P, etal |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 | *{{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=Deng L, Wang D, de la Fuente C, etal |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 | *{{cite journal |vauthors=Yang L, Xia L, Wu DY, etal |title=Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor |journal=Oncogene |volume=21 |issue= 1 |pages= 148–52 |year= 2002 |pmid= 11791185 |doi= 10.1038/sj.onc.1204998 }} | ||
*{{cite journal | *{{cite journal |vauthors=Nielsen PR, Nietlispach D, Mott HR, etal |title=Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 |journal=Nature |volume=416 |issue= 6876 |pages= 103–7 |year= 2002 |pmid= 11882902 |doi= 10.1038/nature722 }} | ||
*{{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=Koessler H, Doenecke D, Albig W |title=Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines |journal=DNA Cell Biol. |volume=22 |issue= 4 |pages= 233–41 |year= 2003 |pmid= 12823900 |doi= 10.1089/104454903321908629 }} | ||
*{{cite journal |vauthors=Coleman MA, Miller KA, Beernink PT, etal |title=Identification of chromatin-related protein interactions using protein microarrays |journal=Proteomics |volume=3 |issue= 11 |pages= 2101–7 |year= 2004 |pmid= 14595808 |doi= 10.1002/pmic.200300593 }} | |||
*{{cite journal | | *{{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= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631 | pmc=291826 }} | ||
*{{cite journal | *{{cite journal |vauthors=Citterio E, Papait R, Nicassio F, etal |title=Np95 is a histone-binding protein endowed with ubiquitin ligase activity |journal=Mol. Cell. Biol. |volume=24 |issue= 6 |pages= 2526–35 |year= 2004 |pmid= 14993289 |doi=10.1128/MCB.24.6.2526-2535.2004 | pmc=355858 }} | ||
*{{cite journal | | |||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=8350}} | |||
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> | |||
{{PBB_Controls | |||
| update_page = yes | |||
| require_manual_inspection = no | |||
| update_protein_box = yes | |||
| update_summary = yes | |||
| update_citations = yes | |||
}} | |||
{{protein-stub}} | {{protein-stub}} | ||
Latest revision as of 13:40, 31 August 2017
VALUE_ERROR (nil) | |||||||
---|---|---|---|---|---|---|---|
Identifiers | |||||||
Aliases | |||||||
External IDs | GeneCards: [1] | ||||||
Orthologs | |||||||
Species | Human | Mouse | |||||
Entrez |
|
| |||||
Ensembl |
|
| |||||
UniProt |
|
| |||||
RefSeq (mRNA) |
|
| |||||
RefSeq (protein) |
|
| |||||
Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
|
Histone H3.1 is a protein that in humans is encoded by the HIST1H3A gene.[1][2][3]
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 the large histone gene cluster on chromosome 6p22-p21.3.[3]
References
- ↑ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
- ↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ↑ 3.0 3.1 "Entrez Gene: HIST1H3A histone cluster 1, H3a".
Further reading
- Albig W, Kardalinou E, Drabent B, et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
- Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
- El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
- Ahn J, Gruen JR (1999). "The genomic organization of the histone clusters on human 6p21.3". Mamm. Genome. 10 (7): 768–70. doi:10.1007/s003359901089. PMID 10384058.
- Rea S, Eisenhaber F, O'Carroll D, et al. (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases". Nature. 406 (6796): 593–9. doi:10.1038/35020506. PMID 10949293.
- Hsu JY, Sun ZW, Li X, et al. (2000). "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes". Cell. 102 (3): 279–91. doi:10.1016/S0092-8674(00)00034-9. PMID 10975519.
- Deng L, de la Fuente C, Fu P, et al. (2001). "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.
- 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.
- Deng L, Wang D, de la Fuente C, et al. (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.
- Yang L, Xia L, Wu DY, et al. (2002). "Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor". Oncogene. 21 (1): 148–52. doi:10.1038/sj.onc.1204998. PMID 11791185.
- Nielsen PR, Nietlispach D, Mott HR, et al. (2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9". Nature. 416 (6876): 103–7. doi:10.1038/nature722. PMID 11882902.
- 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.
- Koessler H, Doenecke D, Albig W (2003). "Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines". DNA Cell Biol. 22 (4): 233–41. doi:10.1089/104454903321908629. PMID 12823900.
- Coleman MA, Miller KA, Beernink PT, et al. (2004). "Identification of chromatin-related protein interactions using protein microarrays". Proteomics. 3 (11): 2101–7. doi:10.1002/pmic.200300593. PMID 14595808.
- Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
- Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity". Mol. Cell. Biol. 24 (6): 2526–35. doi:10.1128/MCB.24.6.2526-2535.2004. PMC 355858. PMID 14993289.
This protein-related article is a stub. You can help Wikipedia by expanding it. |