H1-2 H1.2 linker histone, cluster member [Homo sapiens (human)] - Gene

Summary

Official Symbol: H1-2provided by HGNC
Official Full Name: H1.2 linker histone, cluster memberprovided by HGNC
Primary source: HGNC:HGNC:4716
See related: Ensembl:ENSG00000187837 MIM:142710; AllianceGenome:HGNC:4716
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: H1C; H1.2; H1F2; H1s-1; HIST1H1C
Summary: 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 replication-dependent histone that is 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. [provided by RefSeq, Aug 2015]
Orthologs: mouse all
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Genomic context

Location:: 6p22.2

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	6	NC_000006.12 (26055740..26056470, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	6	NC_060930.1 (25923905..25924635, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	6	NC_000006.11 (26055968..26056698, complement)

Chromosome 6 - NC_000006.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Histone H1.2 Inhibited EMCV Replication through Enhancing MDA5-Mediated IFN-beta Signaling Pathway.
Title: Histone H1.2 Inhibited EMCV Replication through Enhancing MDA5-Mediated IFN-β Signaling Pathway.
Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2.
Title: Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2.
Site-specific ubiquitylation acts as a regulator of linker histone H1.
Title: Site-specific ubiquitylation acts as a regulator of linker histone H1.
these findings suggest that linker histone H1.2 functions as a physiological barrier for ATM to target the chromatin, and PARylation-mediated active H1.2 turnover is required for robust ATM activation and DNA damage repair.
Title: Destabilization of linker histone H1.2 is essential for ATM activation and DNA damage repair.
Taken together, these data provide important insights into a surprisingly complex hTR-RNA interaction network and define an unexpected non-coding RNA role for HIST1H1C in regulating telomere length homeostasis.
Title: The RNA interactome of human telomerase RNA reveals a coding-independent role for a histone mRNA in telomere homeostasis.
The linker histone H1.2 is a novel component of nucleolar organizer regions.
Title: The linker histone H1.2 is a novel component of the nucleolar organizer regions.
results define a network of E2F target genes as susceptible to the regulatory influence of H1.2, where H1.2 augments global association of pRb with chromatin, enhances transcriptional repression by pRb, and facilitates pRb-dependent cell-cycle arrest
Title: Linker Histone H1.2 Directs Genome-wide Chromatin Association of the Retinoblastoma Tumor Suppressor Protein and Facilitates Its Function.
BRG1 participates in gene repression by interacting with H1.2, facilitating its deposition and stabilizing nucleosome positioning around the transcription start site.
Title: Hormone-induced repression of genes requires BRG1-mediated H1.2 deposition at target promoters.
Results show that histones H1.2 and H1.4 were observed in MDA-MB-231 metastatic breast cancer cells. The phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during M phase suggesting that these events are cell cycle-dependent. Also, the study reports the observation of the H1.2 SNP variant A18V in MCF-10A cells.
Title: Quantitative Mass Spectrometry Reveals that Intact Histone H1 Phosphorylations are Variant Specific and Exhibit Single Molecule Hierarchical Dependence.
Integration with apoptotic intermediates (via C-terminal tail interactions) may constitute a more generalized function of linker histone isoforms in apoptotic cascades.
Title: The C-terminal domain (CTD) in linker histones antagonizes anti-apoptotic proteins to modulate apoptotic outcomes at the mitochondrion.

Submit: New GeneRIF Correction See all GeneRIFs (21)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Pr55(Gag)	gag	Cellular biotinylated histone cluster 1, H1c (HIST1H1C) protein is incorporated into HIV-1 Gag virus-like particles	PubMed
Tat	tat	Overexpression of NPM1 enhances HIV-1 Tat-mediated transactivation by reducing the histone H1 occupancy on the chromatinized template of HIV-1 LTR	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

WI-11794 (e-PCR)
- UniSTS:41031

RH67930 (e-PCR)
- UniSTS:4961

Hist1h1e (e-PCR), detects polymorphism
- UniSTS:526010

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables chromatin DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables double-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables nucleosomal DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of chromatin	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chromosome condensation	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of DNA recombination	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of transcription by RNA polymerase II	IEA Inferred from Electronic Annotation more info
involved_in nucleosome assembly	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of euchromatin	IBA Inferred from Biological aspect of Ancestor more info
part_of euchromatin	IDA Inferred from Direct Assay more info	PubMed
part_of nucleosome	IEA Inferred from Electronic Annotation more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: histone H1.2

Names: H1 histone family, member 2; histone 1, H1c; histone H1c; histone H1d; histone H1s-1; histone cluster 1 H1 family member c; histone cluster 1, H1c

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.