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HIST1H2BJ – Wikipedia – Enzyklopädie

HIST1H2BJ – Wikipedia

Posted on September 28, 2019 by lordneo

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

H2BC11

Protein HIST1H2BJ PDB 1aoi.png

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3A6N, 3AFA, 3AN2, 3AV1, 3AV2, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3W96, 3W97, 3W98, 3W99, 3WA9, 3WAA, 3WTP, 4CAY, 5CPJ, 5B0Z, 4YM5, 5AV9, 5AVB, 5AV5, 4YM6, 5CPI, 5AV6, 5AV8, 5CPK, 5AVC, 5B0Y, 4Z5T, 5FUG, 5B24, 2RVQ, 5AY8, 5B2I, 5B40, 5B2J

Identifiers

Aliases

H2BC11, H2B/r, H2BFR, H2BJ, histone cluster 1, H2bj, histone cluster 1 H2B family member j, H2B clustered histone 11, HIST1H2BJ

External IDs

OMIM: 615044 MGI: 2448415 HomoloGene: 128594 GeneCards: H2BC11

Wikidata

Histone H2B type 1-J is a protein that in humans is encoded by the HIST1H2BJ gene.^[5]^[6]^[7]

Histones are basic nuclear proteins that are responsible for the 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 H2B family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the histone microcluster on chromosome 6p21.33.^[7]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000124635 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000068854 – Ensembl, May 2017
^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Zhong R, Roeder RG, Heintz N (Jan 1984). “The primary structure and expression of four cloned human histone genes”. Nucleic Acids Res. 11 (21): 7409–7425. doi:10.1093/nar/11.21.7409. PMC 326492. PMID 6647026.
^ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). “The human and mouse replication-dependent histone genes”. Genomics. 80 (5): 487–498. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
^ ^a ^b “Entrez Gene: HIST1H2BJ histone cluster 1, H2bj”.

Further reading[edit]

Alnemri ES, Litwack G (1989). “Glucocorticoid-induced lymphocytolysis is not mediated by an induced endonuclease”. J. Biol. Chem. 264 (7): 4104–11. doi:10.1016/S0021-9258(19)84968-2. PMID 2917990.
Frohm M, Gunne H, Bergman AC, et al. (1996). “Biochemical and antibacterial analysis of human wound and blister fluid”. Eur. J. Biochem. 237 (1): 86–92. doi:10.1111/j.1432-1033.1996.0086n.x. PMID 8620898.
Albig W, Doenecke D (1998). “The human histone gene cluster at the D6S105 locus”. Hum. Genet. 101 (3): 284–294. 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.
Albig W, Trappe R, Kardalinou E, et al. (1999). “The human H2A and H2B histone gene complement”. Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID 10064132. S2CID 12807248.
Ahn J, Gruen JR (1999). “The genomic organization of the histone clusters on human 6p21.3”. Mamm. Genome. 10 (7): 768–770. doi:10.1007/s003359901089. PMID 10384058. S2CID 28275496.
Deng L, de la Fuente C, Fu P, et al. (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.
Deng L, Wang D, de la Fuente C, et al. (2001). “Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA”. Virology. 289 (2): 312–326. doi:10.1006/viro.2001.1129. PMID 11689053.
Galasinski SC, Louie DF, Gloor KK, et al. (2002). “Global regulation of post-translational modifications on core histones”. J. Biol. Chem. 277 (4): 2579–2588. doi:10.1074/jbc.M107894200. PMID 11709551.
Weinmann AS, Yan PS, Oberley MJ, et al. (2002). “Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis”. Genes Dev. 16 (2): 235–244. doi:10.1101/gad.943102. PMC 155318. PMID 11799066.
Kim HS, Cho JH, Park HW, et al. (2002). “Endotoxin-neutralizing antimicrobial proteins of the human placenta”. J. Immunol. 168 (5): 2356–64. doi:10.4049/jimmunol.168.5.2356. PMID 11859126.
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. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. doi:10.1016/s1570-9639(03)00059-1. PMID 12686141.
Cheung WL, Ajiro K, Samejima K, et al. (2003). “Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase”. Cell. 113 (4): 507–517. doi:10.1016/S0092-8674(03)00355-6. PMID 12757711. S2CID 21854.
Tollin M, Bergman P, Svenberg T, et al. (2004). “Antimicrobial peptides in the first line defence of human colon mucosa”. Peptides. 24 (4): 523–530. doi:10.1016/S0196-9781(03)00114-1. PMID 12860195. S2CID 7435936.
Mungall AJ, Palmer SA, Sims SK, et al. (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.
Lusic M, Marcello A, Cereseto A, Giacca M (2004). “Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter”. EMBO J. 22 (24): 6550–6561. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
Howell SJ, Wilk D, Yadav SP, Bevins CL (2004). “Antimicrobial polypeptides of the human colonic epithelium”. Peptides. 24 (11): 1763–1770. doi:10.1016/j.peptides.2003.07.028. PMID 15019208. S2CID 28953527.

PDB gallery

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
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
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
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
1m19: 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
1p3a: 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
1p3g: 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
1p3l: 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
1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone ‘Sin’ Mutants
1s32: Molecular Recognition of the Nucleosomal ‘Supergroove’
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
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
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
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
2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
2nzd: Nucleosome core particle containing 145 bp of DNA