HIST1H1E

H1-4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3TZD, 5JJZ
Identifiers
Aliases	H1-4 , histone cluster 1, H1e, H1.4, H1E, H1F4, H1s-4, dJ221C16.5, histone cluster 1 H1 family member e, RMNS, HIST1H1E, H1.4 linker histone, cluster member
External IDs	OMIM: 142220; MGI: 1931527; HomoloGene: 130534; GeneCards: H1-4; OMA:H1-4 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6p22.2 Start 26,156,329 bp [1] End 26,157,115 bp [1]
Gene location (Mouse) Chr. Chromosome 13 (mouse) [2] Band 13|13 A3.1 Start 23,804,612 bp [2] End 23,806,541 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon tendon of biceps brachii sural nerve epithelium of colon testicle bone marrow cells gonad corpus callosum secondary oocyte muscle of thigh Top expressed in genital tubercle ascending aorta aortic valve tail of embryo embryo muscle of thigh embryo granulocyte zygote morula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding chromatin DNA binding protein binding RNA binding nucleotide binding double-stranded DNA binding calcium ion binding ATP binding GTP binding AMP binding dATP binding ADP binding nucleosomal DNA binding Cellular component nucleosome extracellular exosome nucleus chromosome Biological process regulation of transcription by RNA polymerase II histone H3-K4 trimethylation nucleosome assembly negative regulation of transcription by RNA polymerase II histone H3-K27 trimethylation regulation of transcription, DNA-templated chromosome condensation negative regulation of DNA recombination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3008 50709 Ensembl ENSG00000168298 ENSMUSG00000051627 UniProt P10412 P43274 RefSeq (mRNA) NM_005321 NM_015787 RefSeq (protein) NP_005312 NP_005312.1 NP_056602 Location (UCSC) Chr 6: 26.16 – 26.16 Mb Chr 13: 23.8 – 23.81 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H1.4 is a protein that in humans is encoded by the HIST1H1E gene. ^{[5] [6] [7]}

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 large histone gene cluster on chromosome 6. ^[7]

HIST1H1E syndrome

HIST1H1E syndrome is a rare autosomal dominant disorder caused by a heterozygous pathogenic variant in the HIST1H1E gene, which is characterized by a set of recognizable clinical features such as hypotonia, intellectual disability, behavioral issues, skeletal, testes (undescended) and thyroid, heart anomalies, and ectodermal issues. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000168298 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000051627 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D (Nov 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.
6. 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.
7. "Entrez Gene: HIST1H1E histone cluster 1, H1e".
8. Burkardt D, Tatton-Brown K (October 3, 1993). "HIST1H1E Syndrome". In Adam MP, Mirzaa GM, Pagon RA, Wallace SE, Bean LJ, Gripp KW, Amemiya A (eds.). GeneReviews. University of Washington, Seattle. PMID   33270410 – via PubMed.

Further reading

• 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. doi:10.1093/oxfordjournals.jbchem.a121722. PMID   3782055.
• Strom R, Santoro R, D'Erme M, Mastrantonio S, Reale A, Marenzi S, Zardo G, Caiafa P (1995). "Specific variants of H1 histone regulate CpG methylation in eukaryotic DNA". Gene. 157 (1–2): 253–6. doi:10.1016/0378-1119(95)91236-S. PMID   7607502.
• Albig W, Drabent B, Kunz J, Kalff-Suske M, Grzeschik KH, Doenecke D (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, Kioschis P, Poustka A, Meergans K, Doenecke D (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. doi:10.1007/s004390050630. PMID   9439656. S2CID   38539096.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Morrison H, Jeppesen P (2003). "Allele-specific underacetylation of histone H4 downstream from promoters is associated with X-inactivation in human cells". Chromosome Res. 10 (7): 579–95. doi:10.1023/A:1020966719605. PMID   12498347. S2CID   21076644.
• Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi: 10.1038/nature02055 . PMID   14574404.
• Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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. PMC   528928 . PMID   15489334.
• Garcia BA, Busby SA, Barber CM, Shabanowitz J, Allis CD, Hunt DF (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, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• Daujat S, Zeissler U, Waldmann T, Happel N, Schneider R (2006). "HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding". J. Biol. Chem. 280 (45): 38090–5. doi: 10.1074/jbc.C500229200 . PMID   16127177.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.
• Trojer P, Li G, Sims RJ, Vaquero A, Kalakonda N, Boccuni P, Lee D, Erdjument-Bromage H, Tempst P (2007). "L3MBTL1, a histone-methylation-dependent chromatin lock". Cell. 129 (5): 915–28. doi: 10.1016/j.cell.2007.03.048 . PMID   17540172. S2CID   16425537.