HIST1H3B

Protein-coding gene in the species Homo sapiens
HIST1H3B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3WKJ, 3B95, 2C1J, 3AYW, 3WA9, 3U4S, 5AVB, 2CV5, 5AV5, 3U31, 2UXN, 3AZK, 2C1N, 5C11, 3QO2, 3X1V, 5C13, 4A0J, 4U68, 5AV8, 4LLB, 3U5O, 1O9S, 4FT2, 4HON, 3W99, 3ZVY, 4Z0R, 5AVC, 1CT6, 1Q3L, 3O37, 3W97, 3SOW, 3KMT, 4YM6, 4A7J, 3UEE, 2KWK, 4F4U, 3UEF, 3UIG, 4BD3, 3AZL, 4QBR, 4F56, 3AFA, 4LKA, 5CPK, 5FFV, 3V43, 5CH1, 3U5P, 3AZI, 3U5N, 3AZH, 3UIK, 4QBQ, 1U35, 4UY4, 2OT7, 5AV9, 2B2W, 3U3D, 3AZF, 3W98, 4I51, 4X3K, 4FWF, 2B2T, 2B2V, 4A0N, 2KWJ, 3WAA, 3QJ6, 5DAH, 3AZG, 3AZE, 3X1T, 3RIY, 2L75, 3A1B, 2VPG, 4QBS, 3O35, 5CPJ, 3ZG6, 4YM5, 3AZJ, 2RI7, 3AZN, 3AVR, 5CPI, 2LBM, 3W96, 3O34, 2M0O, 4L7X, 5CH2, 5AV6, 3AZM, 4UP0, 3X1S, 2OX0, 3UII, 3SOU, 4N4H, 4TN7, 1CS9, 3X1U, 4LXL, 2B2U, 2OQ6, 3RIG, 5C3I, 4YHP, 5B24, 5D6Y, 4YHZ, 4Z2M, 5HJD, 5HJC, 5HJB, 5B2I, 5HYN, 5FB0, 5FB1, 5IQL, 5B2J, 5JIN

Identifiers
AliasesH3C2, H3/l, H3FL, histone cluster 1, H3b, histone cluster 1 H3 family member b
External IDsOMIM: 602819; MGI: 2448351; HomoloGene: 136775; GeneCards: H3C2; OMA:H3C2 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for HIST1H3B
Genomic location for HIST1H3B
Band6p22.2Start26,031,650 bp[1]
End26,032,060 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for HIST1H3B
Genomic location for HIST1H3B
Band3|3 F2.1Start96,175,970 bp[2]
End96,176,457 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • stomach

  • lung

  • colon

  • kidney

  • heart

  • Achilles tendon

  • bone marrow
Top expressed in
  • uterus

  • zygote

  • secondary oocyte

  • primary oocyte

  • embryo

  • bone marrow

  • mesencephalon

  • tail of embryo

  • genital tubercle

  • neural tube
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA binding
  • histone binding
  • protein binding
  • protein heterodimerization activity
  • cadherin binding
  • nucleosomal DNA binding
Cellular component
  • membrane
  • nucleoplasm
  • chromosome
  • extracellular region
  • nuclear chromosome
  • extracellular exosome
  • nucleosome
  • nucleus
  • protein-containing complex
Biological process
  • telomere organization
  • epigenetic maintenance of chromatin in transcription-competent conformation
  • protein heterotetramerization
  • blood coagulation
  • DNA replication-dependent chromatin assembly
  • rDNA heterochromatin assembly
  • negative regulation of gene expression, epigenetic
  • chromatin organization
  • regulation of gene silencing by miRNA
  • nucleosome assembly
  • interleukin-7-mediated signaling pathway
  • regulation of megakaryocyte differentiation
  • regulation of hematopoietic stem cell differentiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8358

319154

Ensembl

ENSG00000274267

ENSMUSG00000074403

UniProt

P68431

P84228

RefSeq (mRNA)

NM_003537

NM_178215

RefSeq (protein)

NP_066298
NP_003520
NP_003525
NP_003527

NP_473386
NP_835734
NP_783584
NP_835510
NP_835587

NP_038576
NP_835511
NP_835512

Location (UCSC)Chr 6: 26.03 – 26.03 MbChr 3: 96.18 – 96.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Histone H3.1 is a protein that in humans is encoded by the H3C2 gene.[5][6][7]

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.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000274267 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074403 – 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. ^ Zhong R, Roeder RG, Heintz N (Jan 1984). "The primary structure and expression of four cloned human histone genes". Nucleic Acids Res. 11 (21): 7409–25. doi:10.1093/nar/11.21.7409. PMC 326492. PMID 6647026.
  6. ^ 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.
  7. ^ 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.
  8. ^ "Entrez Gene: HIST1H3B histone cluster 1, H3b".

Further reading

  • Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D (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.
  • Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G, Stein J (1986). "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences". Biochem. Cell Biol. 64 (4): 277–89. doi:10.1139/o86-039. PMID 3013246.
  • Ohe Y, Iwai K (1982). "Human spleen histone H3. Isolation and amino acid sequence". J. Biochem. 90 (4): 1205–11. doi:10.1093/oxfordjournals.jbchem.a133573. PMID 7309716.
  • Kardalinou E, Eick S, Albig W, Doenecke D (1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones". J. Cell. Biochem. 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173. S2CID 42454232.
  • 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. doi:10.1016/S0378-1119(96)00582-3. PMID 9031620.
  • 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.
  • 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.
  • Goto H, Tomono Y, Ajiro K, Kosako H, Fujita M, Sakurai M, Okawa K, Iwamatsu A, Okigaki T (1999). "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation". J. Biol. Chem. 274 (36): 25543–25549. doi:10.1074/jbc.274.36.25543. PMID 10464286.
  • Hsu JY, Sun ZW, Li X, Reuben M, Tatchell K, Bishop DK, Grushcow JM, Brame CJ, Caldwell JA (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. S2CID 16057773.
  • Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG (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): 278–295. doi:10.1006/viro.2000.0593. PMID 11080476. S2CID 20145752.
  • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. Bibcode:2001Natur.410..116L. doi:10.1038/35065132. PMID 11242053. S2CID 4331863.
  • Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P (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, Wang H, Chansky HA, Schubach WH, Hickstein DD, Zhang Y (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. S2CID 10912876.
  • Goto H, Yasui Y, Nigg EA, Inagaki M (2002). "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation". Genes Cells. 7 (1): 11–7. doi:10.1046/j.1356-9597.2001.00498.x. PMID 11856369. S2CID 23717416.
  • 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.
  • Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase". Nucleic Acids Res. 31 (3): 878–85. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483.
  • 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): 805–811. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.

External links

  • Overview of all the structural information available in the PDB for UniProt: P68431 (Histone H3.1) at the PDBe-KB.
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  • 1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
    1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
  • 1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
    1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
  • 1f66: 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
    1f66: 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
  • 1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
    1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
  • 1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
    1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
  • 1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
    1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
  • 1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
    1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
  • 1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1s32: Molecular Recognition of the Nucleosomal 'Supergroove'
    1s32: Molecular Recognition of the Nucleosomal 'Supergroove'
  • 1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
    1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
  • 1u35: Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
    1u35: Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
  • 1zbb: Structure of the 4_601_167 Tetranucleosome
    1zbb: Structure of the 4_601_167 Tetranucleosome
  • 1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
    1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
  • 2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
    2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
  • 2cv5: Crystal structure of human nucleosome core particle
    2cv5: Crystal structure of human nucleosome core particle
  • 2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
    2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
  • 2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
    2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
  • 2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
    2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
  • 2hue: Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
    2hue: Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
  • 2io5: Crystal structure of the CIA- histone H3-H4 complex
    2io5: Crystal structure of the CIA- histone H3-H4 complex
  • 2nzd: Nucleosome core particle containing 145 bp of DNA
    2nzd: Nucleosome core particle containing 145 bp of DNA
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