H1f1 H1.1 linker histone, cluster member [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: H1f1provided by MGI
Official Full Name: H1.1 linker histone, cluster memberprovided by MGI
Primary source: MGI:MGI:1931523
See related: Ensembl:ENSMUSG00000049539 AllianceGenome:MGI:1931523
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: H1a; H1-1; H1.1; H1var3; Hist1h1a
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. [provided by RefSeq, Aug 2015]
Orthologs: human all
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Genomic context

Location:: 13 A3.1; 13 9.91 cM

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	13	NC_000079.7 (23947651..23948395)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	13	NC_000079.6 (23763668..23764412)

Chromosome 13 - NC_000079.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

histone H2A.X phosphorylation by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding
Title: Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.
the C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
Title: The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo.
H1 isoforms H1.0, H1.1, and H1.2 are non-responsive to hormone whereas prolonged dexamethasone treatment effectively dephosphorylated the H1.3, H1.4, and H1.5 isoforms
Title: Hormone-mediated dephosphorylation of specific histone H1 isoforms.

Submit: New GeneRIF Correction

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (1) 1 citation
Endonuclease-mediated (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:488651

NoName (e-PCR)
- UniSTS:491516

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables chromatin DNA binding	ISO Inferred from Sequence Orthology more info
enables double-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables heparin binding	IDA Inferred from Direct Assay more info	PubMed
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 nucleosome assembly	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of receptor-mediated endocytosis	IDA Inferred from Direct Assay more info	PubMed
involved_in spermatogenesis	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within spermatogenesis	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cell surface	IDA Inferred from Direct Assay more info	PubMed
part_of chromatin	ISO Inferred from Sequence Orthology more info
located_in chromosome	IEA Inferred from Electronic Annotation more info
part_of euchromatin	ISO Inferred from Sequence Orthology more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
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
located_in vesicle	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: histone H1.1

Names: H1 VAR.3; H1 histone family, member 1; histone 1, H1a; histone H1a; histone cluster 1, H1a

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.

mRNA and Protein(s)

NM_030609.3 → NP_085112.1 histone H1.1

See identical proteins and their annotated locations for NP_085112.1

Status: REVIEWED

Source sequence(s)

AL590388

Consensus CDS

CCDS26369.1

UniProtKB/Swiss-Prot

P43275, Q5SZ98

Related

ENSMUSP00000062030.2, ENSMUST00000055770.4

Conserved Domains (1) summary

cd00073
Location:40 → 121

H15; linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated ...