H1FX: Difference between revisions
Jump to navigation
Jump to search
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 H1x''' is a [[protein]] that in humans is encoded by the ''H1FX'' [[gene]].<ref name="pmid8964515">{{cite journal |vauthors=Yamamoto T, Horikoshi M | title = Cloning of the cDNA encoding a novel subtype of histone H1 | journal = Gene | volume = 173 | issue = 2 | pages = 281–285 |date=Dec 1996 | pmid = 8964515 | pmc = | doi =10.1016/0378-1119(96)00020-0 }}</ref><ref name="pmid9439656">{{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 |date=Feb 1998 | pmid = 9439656 | pmc = | doi =10.1007/s004390050630 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: H1FX H1 histone family, member X| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8971| 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. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 encodes a member of the histone H1 family.<ref name="entrez" | | summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 encodes a member of the histone H1 family.<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=Ohsumi K, Katagiri C |title=Occurrence of H1 subtypes specific to pronuclei and cleavage-stage cell nuclei of anuran amphibians |journal=Dev. Biol. |volume=147 |issue= 1 |pages= 110–120 |year= 1991 |pmid= 1879604 |doi=10.1016/S0012-1606(05)80011-9 }} | ||
*{{cite journal | author=Strausberg RL |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= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }} | |||
*{{cite journal | author=Sulimova GE |title=Human chromosome 3: integration of 60 NotI clones into a physical and gene map |journal=Cytogenet. Genome Res. |volume=98 |issue= 2–3 |pages= 177–183 |year= 2003 |pmid= 12698000 |doi= 10.1159/000069814 |name-list-format=vanc| author2=Kutsenko AS | author3=Rakhmanaliev ER | display-authors=3 | last4=Udina | first4=I.G. | last5=Kompaniytsev | first5=A.A. | last6=Protopopov | first6=A.I. | last7=Moisjak | first7=E.V. | last8=Klimov | first8=E.A. | last9=Muravenko | first9=O.V. }} | |||
*{{cite journal | author=Strausberg RL | *{{cite journal | author=Beausoleil SA |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–12135 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 |name-list-format=vanc| author2=Jedrychowski M | author3=Schwartz D | display-authors=3 | last4=Elias | first4=JE | last5=Villén | first5=J | last6=Li | first6=J | last7=Cohn | first7=MA | last8=Cantley | first8=LC | last9=Gygi | first9=SP }} | ||
*{{cite journal | author=Sulimova GE | *{{cite journal | author=Gerhard DS |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= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }} | ||
*{{cite journal | author=Beausoleil SA | *{{cite journal | author=Garcia BA |title=Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry |journal=J. Proteome Res. |volume=3 |issue= 6 |pages= 1219–1227 |year= 2005 |pmid= 15595731 |doi= 10.1021/pr0498887 |name-list-format=vanc| author2=Busby SA | author3=Barber CM | display-authors=3 | last4=Shabanowitz | first4=Jeffrey | last5=Allis | first5=C. David | last6=Hunt | first6=Donald F. }} | ||
*{{cite journal | author=Gerhard DS | *{{cite journal | author=Andersen JS |title=Nucleolar proteome dynamics |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 |name-list-format=vanc| author2=Lam YW | author3=Leung AK | display-authors=3 | last4=Ong | first4=Shao-En | last5=Lyon | first5=Carol E. | last6=Lamond | first6=Angus I. | last7=Mann | first7=Matthias }} | ||
*{{cite journal | author=Garcia BA | *{{cite journal |vauthors=Happel N, Schulze E, Doenecke D |title=Characterisation of human histone H1x |journal=Biol. Chem. |volume=386 |issue= 6 |pages= 541–551 |year= 2005 |pmid= 16006241 |doi= 10.1515/BC.2005.064 }} | ||
*{{cite journal | author=Andersen JS | *{{cite journal | author=Olsen JV |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–648 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |name-list-format=vanc| author2=Blagoev B | author3=Gnad F | display-authors=3 | last4=Macek | first4=Boris | last5=Kumar | first5=Chanchal | last6=Mortensen | first6=Peter | last7=Mann | first7=Matthias }} | ||
*{{cite journal | | *{{cite journal | author=Takata H |title=H1.X with different properties from other linker histones is required for mitotic progression |journal=FEBS Lett. |volume=581 |issue= 20 |pages= 3783–3788 |year= 2007 |pmid= 17632103 |doi= 10.1016/j.febslet.2007.06.076 |name-list-format=vanc| author2=Matsunaga S | author3=Morimoto A | display-authors=3 | last4=Onomaniwa | first4=R | last5=Uchiyama | first5=S | last6=Fukui | first6=K }} | ||
*{{cite journal | author=Olsen JV | |||
*{{cite journal | author=Takata H | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> | <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> | ||
| Line 43: | Line 37: | ||
}} | }} | ||
{{ | {{gene-3-stub}} | ||
Latest revision as of 13:24, 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 H1x is a protein that in humans is encoded by the H1FX gene.[1][2][3]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 encodes a member of the histone H1 family.[3]
References
- ↑ Yamamoto T, Horikoshi M (Dec 1996). "Cloning of the cDNA encoding a novel subtype of histone H1". Gene. 173 (2): 281–285. doi:10.1016/0378-1119(96)00020-0. PMID 8964515.
- ↑ Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–294. doi:10.1007/s004390050630. PMID 9439656.
- ↑ 3.0 3.1 "Entrez Gene: H1FX H1 histone family, member X".
Further reading
- Ohsumi K, Katagiri C (1991). "Occurrence of H1 subtypes specific to pronuclei and cleavage-stage cell nuclei of anuran amphibians". Dev. Biol. 147 (1): 110–120. doi:10.1016/S0012-1606(05)80011-9. PMID 1879604.
- 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Sulimova GE, Kutsenko AS, Rakhmanaliev ER, et al. (2003). "Human chromosome 3: integration of 60 NotI clones into a physical and gene map". Cytogenet. Genome Res. 98 (2–3): 177–183. doi:10.1159/000069814. PMID 12698000.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- 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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Garcia BA, Busby SA, Barber CM, et al. (2005). "Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry". J. Proteome Res. 3 (6): 1219–1227. doi:10.1021/pr0498887. PMID 15595731.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Happel N, Schulze E, Doenecke D (2005). "Characterisation of human histone H1x". Biol. Chem. 386 (6): 541–551. doi:10.1515/BC.2005.064. PMID 16006241.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Takata H, Matsunaga S, Morimoto A, et al. (2007). "H1.X with different properties from other linker histones is required for mitotic progression". FEBS Lett. 581 (20): 3783–3788. doi:10.1016/j.febslet.2007.06.076. PMID 17632103.
 | This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it. |