HIST1H3C

Protein-coding gene in the species Homo sapiens

HIST1H3C

Available structures

PDB

Ortholog 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

Aliases

HIST1H3C, H3.1, H3/c, H3FC, histone cluster 1, H3c, histone cluster 1 H3 family member c, H3C3

External IDs

OMIM: 602812; MGI: 2448355; HomoloGene: 134495; GeneCards: HIST1H3C; OMA:HIST1H3C - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p22.2	Start	26,045,411 bp^[1]
Band	6p22.2	End	26,045,821 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3\|3 F2.1	Start	96,154,001 bp^[2]
Band	3\|3 F2.1	End	96,155,825 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

stomach

colon

lung

kidney

heart

vagina

ovary

testicle

Top expressed in

genital tubercle

secondary oocyte

primary oocyte

embryo

zygote

embryo

morula

tail of embryo

bone marrow

epiblast

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

Species

Human

Mouse

Entrez


8352


15077

Ensembl


ENSG00000278272


ENSMUSG00000093769

UniProt


P68431


P84228

RefSeq (mRNA)


NM_003531


NM_178216

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: 26.05 – 26.05 Mb

Chr 3: 96.15 – 96.16 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Histone H3.1 is a protein that in humans is encoded by the HIST1H3C gene.^[5]^[6]^[7]^[8]

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 H3 family. Transcripts from this gene lack polyA tails, instead containing a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000278272 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000093769 – 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.
^ Kardalinou E, Eick S, Albig W, Doenecke D (Dec 1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones". Journal of Cellular Biochemistry. 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173. S2CID 42454232.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: HIST1H3C histone cluster 1, H3c".

Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Human Genetics. 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". Molecular and Cellular Biology. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
Munakata T, Adachi N, Yokoyama N, et al. (2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes to Cells. 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893. S2CID 20198031.
Hsu JY, Sun ZW, Li X, et al. (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, 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): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
Lachner M, O'Carroll D, Rea S, et al. (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, et al. (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, et al. (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.
Nielsen PR, Nietlispach D, Mott HR, et al. (2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9". Nature. 416 (6876): 103–7. Bibcode:2002Natur.416..103N. doi:10.1038/nature722. PMID 11882902. S2CID 4423019.
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". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Umehara T, Horikoshi M (2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis". Journal of Biological Chemistry. 278 (37): 35660–7. doi:10.1074/jbc.M303549200. PMID 12842904.
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". The EMBO Journal. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
Black BE, Foltz DR, Chakravarthy S, et al. (2004). "Structural determinants for generating centromeric chromatin". Nature. 430 (6999): 578–82. Bibcode:2004Natur.430..578B. doi:10.1038/nature02766. PMID 15282608. S2CID 4392941.

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
2hue: Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
2io5: Crystal structure of the CIA- histone H3-H4 complex
2nzd: Nucleosome core particle containing 145 bp of DNA