HIST1H1B

From Wikipedia, the free encyclopedia

Histone cluster 1, H1b

PDB rendering based on 1ghc.

Available structures: 1ghc

Identifiers

Symbol(s)

HIST1H1B; H1; H1.5; H1F5; MGC126630; MGC126632

External IDs

OMIM: 142711 MGI: 1861461 HomoloGene: 74548

Gene ontology
Molecular Function:	• DNA binding
Cellular Component:	• nucleosome • nucleus • chromosome
Biological Process:	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005322 (mRNA)
NP_005313 (protein)

NM_020034 (mRNA)
NP_064418 (protein)

Location

Chr 6: 27.94 - 27.94 Mb

Chr 13: 21.79 - 21.79 Mb

Pubmed search

[1]

[2]

Histone cluster 1, H1b, also known as HIST1H1B, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: HIST1H1B histone cluster 1, H1b.

[edit] Further reading

Ohe Y, Hayashi H, Iwai K (1990). "Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d.". J. Biochem. 106 (5): 844–57. PMID 2613692.
van Wijnen AJ, Wright KL, Massung RF, et al. (1988). "Two target sites for protein binding in the promoter region of a cell cycle regulated human H1 histone gene.". Nucleic Acids Res. 16 (2): 571–92. PMID 2829131.
Collar DG, Wright KL, van Wijnen AJ, et al. (1988). "The human H1 histone gene FNC16 is functionally expressed in proliferating HeLa S3 cells and is down-regulated during terminal differentiation in HL60 cells.". J. Biol. Chem. 263 (31): 15860–3. PMID 3182772.
Ohe Y, Hayashi H, Iwai K (1986). "Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b.". J. Biochem. 100 (2): 359–68. PMID 3782055.
Carozzi N, Marashi F, Plumb M, et al. (1984). "Clustering of human H1 and core histone genes.". Science 224 (4653): 1115–7. PMID 6719136.
Aprelikova O, Xiong Y, Liu ET (1995). "Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase.". J. Biol. Chem. 270 (31): 18195–7. PMID 7629134.
Albig W, Drabent B, Kunz J, et al. (1993). "All known human H1 histone genes except the H1(0) gene are clustered on chromosome 6.". Genomics 16 (3): 649–54. doi:10.1006/geno.1993.1243. PMID 8325638.
Albig W, Meergans T, Doenecke D (1997). "Characterization of the H1.5 gene completes the set of human H1 subtype genes.". Gene 184 (2): 141–8. PMID 9031620.
Albig W, Kioschis P, Poustka A, et al. (1997). "Human histone gene organization: nonregular arrangement within a large cluster.". Genomics 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus.". Hum. Genet. 101 (3): 284–94. PMID 9439656.
New L, Zhao M, Li Y, et al. (1999). "Cloning and characterization of RLPK, a novel RSK-related protein kinase.". J. Biol. Chem. 274 (2): 1026–32. PMID 9873047.
Chadwick BP, Willard HF (2001). "A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome.". J. Cell Biol. 152 (2): 375–84. PMID 11266453.
Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes.". Genomics 80 (5): 487–98. PMID 12408966.
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. PMID 12477932.
Giampuzzi M, Oleggini R, Di Donato A (2003). "Demonstration of in vitro interaction between tumor suppressor lysyl oxidase and histones H1 and H2: definition of the regions involved.". Biochim. Biophys. Acta 1647 (1-2): 245–51. PMID 12686141.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Vaquero A, Scher M, Lee D, et al. (2004). "Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.". Mol. Cell 16 (1): 93–105. doi:10.1016/j.molcel.2004.08.031. PMID 15469825.
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): 2121–7. doi:10.1101/gr.2596504. 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): 1219–27. 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.