HIST1H1B: Difference between revisions

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{{Infobox_gene}}
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'''Histone H1.5''' is a [[protein]] that in humans is encoded by the ''HIST1H1B'' [[gene]].<ref name="pmid9031620">{{cite journal |vauthors=Albig W, Meergans T, Doenecke D | title = Characterization of the H1.5 gene completes the set of human H1 subtype genes | journal = Gene | volume = 184 | issue = 2 | pages = 141–8 |date=Mar 1997 | pmid = 9031620 | pmc = | doi =10.1016/S0378-1119(96)00582-3  }}</ref><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: HIST1H1B histone cluster 1, H1b| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3009| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HIST1H1B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ghc.
| PDB = {{PDB2|1ghc}}
| Name = Histone cluster 1, H1b
| HGNCid = 4719
| Symbol = HIST1H1B
| AltSymbols =; H1; H1.5; H1F5; MGC126630; MGC126632
| OMIM = 142711
| ECnumber =
| Homologene = 74548
| MGIid = 1861461
| GeneAtlas_image1 = PBB_GE_HIST1H1B_214534_at_tn.png
| 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 = 3009
    | Hs_Ensembl = ENSG00000184357
    | Hs_RefseqProtein = NP_005313
    | Hs_RefseqmRNA = NM_005322
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 27942606
    | Hs_GenLoc_end = 27943286
    | Hs_Uniprot = P16401
    | Mm_EntrezGene = 56702
    | Mm_Ensembl = ENSMUSG00000058773
    | Mm_RefseqmRNA = NM_020034
    | Mm_RefseqProtein = NP_064418
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 21787348
    | Mm_GenLoc_end = 21788019
    | Mm_Uniprot = Q1WWK3
  }}
}}
'''Histone cluster 1, H1b''', also known as '''HIST1H1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H1B histone cluster 1, H1b| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3009| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H1B histone cluster 1, H1b| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3009| accessdate = }}</ref>
| summary_text = Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.<ref name="entrez" />
}}
}}


==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, Hayashi H, Iwai K |title=Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d. |journal=J. Biochem. |volume=106 |issue= 5 |pages= 844-57 |year= 1990 |pmid= 2613692 |doi=  }}
*{{cite journal  |vauthors=Ohe Y, Hayashi H, Iwai K |title=Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d |journal=J. Biochem. |volume=106 |issue= 5 |pages= 844–57 |year= 1990 |pmid= 2613692 |doi=  }}
*{{cite journal  | author=van Wijnen AJ, Wright KL, Massung RF, ''et al.'' |title=Two target sites for protein binding in the promoter region of a cell cycle regulated human H1 histone gene. |journal=Nucleic Acids Res. |volume=16 |issue= 2 |pages= 571-92 |year= 1988 |pmid= 2829131 |doi=  }}
*{{cite journal  | author=van Wijnen AJ |title=Two target sites for protein binding in the promoter region of a cell cycle regulated human H1 histone gene |journal=Nucleic Acids Res. |volume=16 |issue= 2 |pages= 571–92 |year= 1988 |pmid= 2829131 |doi=10.1093/nar/16.2.571 | pmc=334679 |name-list-format=vanc| author2=Wright KL | author3=Massung RF  | display-authors=3  | last4=Gerretsen  | first4=Martijn  | last5=Stein  | first5=Janet L.  | last6=Stein  | first6=Gary S. }}
*{{cite journal | author=Collar DG, Wright KL, van Wijnen AJ, ''et al.'' |title=The human H1 histone gene FNC16 is functionally expressed in proliferating HeLa S3 cells and is down-regulated during terminal differentiation in HL60 cells. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 15860-3 |year= 1988 |pmid= 3182772 |doi=  }}
*{{cite journal  | author=Collar DG |title=The human H1 histone gene FNC16 is functionally expressed in proliferating HeLa S3 cells and is down-regulated during terminal differentiation in HL60 cells |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 15860–3 |year= 1988 |pmid= 3182772 |doi=  |name-list-format=vanc| author2=Wright KL | author3=van Wijnen AJ  | display-authors=3  | last4=Ramsey  | first4=AL  | last5=Lian  | first5=J  | last6=Stein  | first6=JL  | last7=Stein  | first7=GS }}
*{{cite journal  | author=Ohe Y, Hayashi H, Iwai K |title=Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b. |journal=J. Biochem. |volume=100 |issue= 2 |pages= 359-68 |year= 1986 |pmid= 3782055 |doi=  }}
*{{cite journal  |vauthors=Ohe Y, Hayashi H, Iwai K |title=Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b |journal=J. Biochem. |volume=100 |issue= 2 |pages= 359–68 |year= 1986 |pmid= 3782055 |doi=  }}
*{{cite journal | author=Carozzi N, Marashi F, Plumb M, ''et al.'' |title=Clustering of human H1 and core histone genes. |journal=Science |volume=224 |issue= 4653 |pages= 1115-7 |year= 1984 |pmid= 6719136 |doi=  }}
*{{cite journal  | author=Carozzi N |title=Clustering of human H1 and core histone genes |journal=Science |volume=224 |issue= 4653 |pages= 1115–7 |year= 1984 |pmid= 6719136 |doi=10.1126/science.6719136 |name-list-format=vanc| author2=Marashi F  | author3=Plumb M  | display-authors=3  | last4=Zimmerman  | first4=S  | last5=Zimmerman  | first5=A  | last6=Coles | first6=L. | last7=Wells  | last8=Stein  | first8=G  | last9=Stein  | first9=J  | first7=JR  }}
*{{cite journal  | author=Aprelikova O, Xiong Y, Liu ET |title=Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18195-7 |year= 1995 |pmid= 7629134 |doi=  }}
*{{cite journal  |vauthors=Aprelikova O, Xiong Y, Liu ET |title=Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18195–7 |year= 1995 |pmid= 7629134 |doi=10.1074/jbc.270.31.18195  }}
*{{cite journal  | author=Albig W, Drabent B, Kunz J, ''et al.'' |title=All known human H1 histone genes except the H1(0) gene are clustered on chromosome 6. |journal=Genomics |volume=16 |issue= 3 |pages= 649-54 |year= 1993 |pmid= 8325638 |doi= 10.1006/geno.1993.1243 }}
*{{cite journal  | author=Albig W |title=All known human H1 histone genes except the H1(0) gene are clustered on chromosome 6 |journal=Genomics |volume=16 |issue= 3 |pages= 649–54 |year= 1993 |pmid= 8325638 |doi= 10.1006/geno.1993.1243 |name-list-format=vanc| author2=Drabent B | author3=Kunz J  | display-authors=3  | last4=Kalff-Suske  | first4=Martha  | last5=Grzeschik  | first5=Karl-Heinz  | last6=Doenecke  | first6=Detlef }}
*{{cite journal | author=Albig W, Meergans T, Doenecke D |title=Characterization of the H1.5 gene completes the set of human H1 subtype genes. |journal=Gene |volume=184 |issue= 2 |pages= 141-8 |year= 1997 |pmid= 9031620 |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= 284–94 |year= 1998 |pmid= 9439656 |doi=10.1007/s004390050630 }}
*{{cite journal | author=Albig W, Kioschis P, Poustka A, ''et al.'' |title=Human histone gene organization: nonregular arrangement within a large cluster. |journal=Genomics |volume=40 |issue= 2 |pages= 314-22 |year= 1997 |pmid= 9119399 |doi= 10.1006/geno.1996.4592 }}
*{{cite journal  | author=New L |title=Cloning and characterization of RLPK, a novel RSK-related protein kinase |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 1026–32 |year= 1999 |pmid= 9873047 |doi=10.1074/jbc.274.2.1026 |name-list-format=vanc| author2=Zhao M | author3=Li Y  | display-authors=3  | last4=Bassett  | first4=WW  | last5=Feng  | first5=Y  | last6=Ludwig  | first6=S  | last7=Padova  | first7=FD  | last8=Gram  | first8=H  | last9=Han  | first9=J }}
*{{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=Chadwick BP, Willard HF |title=A Novel Chromatin Protein, Distantly Related to Histone H2a, Is Largely Excluded from the Inactive X Chromosome |journal=J. Cell Biol. |volume=152 |issue= 2 |pages= 375–84 |year= 2001 |pmid= 11266453 |doi=10.1083/jcb.152.2.375  | pmc=2199617  }}
*{{cite journal  | author=New L, Zhao M, Li Y, ''et al.'' |title=Cloning and characterization of RLPK, a novel RSK-related protein kinase. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 1026-32 |year= 1999 |pmid= 9873047 |doi=  }}
*{{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= 16899–903 |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=Chadwick BP, Willard HF |title=A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. |journal=J. Cell Biol. |volume=152 |issue= 2 |pages= 375-84 |year= 2001 |pmid= 11266453 |doi=  }}
*{{cite journal  |vauthors=Giampuzzi M, Oleggini R, Di Donato A |title=Demonstration of in vitro interaction between tumor suppressor lysyl oxidase and histones H1 and H2: definition of the regions involved |journal=Biochim. Biophys. Acta |volume=1647 |issue= 1–2 |pages= 245–51 |year= 2003 |pmid= 12686141 |doi= 10.1016/s1570-9639(03)00059-1}}
*{{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  | author=Mungall AJ |title=The DNA sequence and analysis of human chromosome 6 |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055  |name-list-format=vanc| author2=Palmer SA  | author3=Sims SK  | display-authors=3  | last4=Edwards  | first4=C. A.  | last5=Ashurst  | first5=J. L.  | last6=Wilming  | first6=L.  | last7=Jones  | first7=M. C.  | last8=Horton  | first8=R.  | last9=Hunt  | first9=S. E. }}
*{{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=Vaquero A |title=Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin |journal=Mol. Cell |volume=16 |issue= 1 |pages= 93–105 |year= 2004 |pmid= 15469825 |doi= 10.1016/j.molcel.2004.08.031  |name-list-format=vanc| author2=Scher M  | author3=Lee D  | display-authors=3  | last4=Erdjument-Bromage  | first4=Hediye  | last5=Tempst  | first5=Paul  | last6=Reinberg  | first6=Danny }}
*{{cite journal | author=Giampuzzi M, Oleggini R, Di Donato A |title=Demonstration of in vitro interaction between tumor suppressor lysyl oxidase and histones H1 and H2: definition of the regions involved. |journal=Biochim. Biophys. Acta |volume=1647 |issue= 1-2 |pages= 245-51 |year= 2003 |pmid= 12686141 |doi=  }}
*{{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= 2121–7 |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=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{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= 1219–27 |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=Vaquero A, Scher M, Lee D, ''et al.'' |title=Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. |journal=Mol. Cell |volume=16 |issue= 1 |pages= 93-105 |year= 2004 |pmid= 15469825 |doi= 10.1016/j.molcel.2004.08.031 }}
*{{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=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  | author=Garcia BA, Busby SA, Barber CM, ''et al.'' |title=Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry. |journal=J. Proteome Res. |volume=3 |issue= 6 |pages= 1219-27 |year= 2005 |pmid= 15595731 |doi= 10.1021/pr0498887 }}
*{{cite journal  | author=Andersen JS, Lam YW, Leung AK, ''et al.'' |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77-83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3009}}
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Latest revision as of 13:37, 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 H1.5 is a protein that in humans is encoded by the HIST1H1B gene.[1][2][3][4]

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.[4]

References

  1. ↑ Albig W, Meergans T, Doenecke D (Mar 1997). "Characterization of the H1.5 gene completes the set of human H1 subtype genes". Gene. 184 (2): 141–8. doi:10.1016/S0378-1119(96)00582-3. PMID 9031620.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 4.0 4.1 "Entrez Gene: HIST1H1B histone cluster 1, H1b".

Further reading



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