P68433 · H31_MOUSE

  • Protein
    Histone H3.1
  • Gene
    H3c1; H3c8; H3c10; H3c11
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

Miscellaneous

This histone is only present in mammals.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleoplasm
Cellular Componentnucleosome
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular Functionprotein heterodimerization activity
Molecular Functionstructural constituent of chromatin
Biological Processchromatin organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone H3.1

Gene names

    • Name
      H3c1
    • Synonyms
      H3a, Hist1h3a
    • Name
      H3c8
    • Synonyms
      H3.1-221, H3g, Hist1h3g
    • Name
      H3c10
    • Synonyms
      H3.1-291, H3h, Hist1h3h
    • Name
      H3c11
    • Synonyms
      H3.1-I, H3i, Hist1h3i

Organism names

  • Taxonomic identifier
  • Strains
    • CD-1
    • C57BL/CJ6
    • 129/Sv
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P68433
  • Secondary accessions
    • P02295
    • P02296
    • P16106
    • Q05A97
    • Q3B7Z8

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue, lipidation.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00002212492-136Histone H3.1
Modified residue3Asymmetric dimethylarginine; by PRMT6; alternate
Modified residue3Citrulline; alternate
Modified residue3Phosphoarginine; alternate
Modified residue4Phosphothreonine; by HASPIN and VRK1
Modified residue5Allysine; alternate
Modified residue5N6,N6,N6-trimethyllysine; alternate
Modified residue5N6,N6-dimethyllysine; alternate
Modified residue5N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue5N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue5N6-acetyllysine; alternate
Modified residue5N6-crotonyllysine; alternate
Modified residue5N6-methyllysine; alternate
Modified residue65-glutamyl dopamine; alternate
Modified residue65-glutamyl serotonin; alternate
Modified residue7Phosphothreonine; by PKC
Modified residue9Citrulline; alternate
Modified residue9Symmetric dimethylarginine; by PRMT5; alternate
Modified residue10N6,N6,N6-trimethyllysine; alternate
Modified residue10N6,N6-dimethyllysine; alternate
Modified residue10N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue10N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue10N6-acetyllysine; alternate
Modified residue10N6-crotonyllysine; alternate
Modified residue10N6-lactoyllysine; alternate
Modified residue10N6-methyllysine; alternate
Modified residue11ADP-ribosylserine; alternate
Modified residue11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5
Modified residue12Phosphothreonine; by PKC and CHEK1
Modified residue15N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue15N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue15N6-acetyllysine; alternate
Modified residue15N6-glutaryllysine; alternate
Modified residue15N6-lactoyllysine; alternate
Modified residue15N6-succinyllysine; alternate
Modified residue18Asymmetric dimethylarginine; by CARM1; alternate
Modified residue18Citrulline; alternate
Modified residue19N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue19N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue19N6-acetyllysine; alternate
Modified residue19N6-butyryllysine; alternate
Modified residue19N6-crotonyllysine; alternate
Modified residue19N6-glutaryllysine; alternate
Modified residue19N6-lactoyllysine; alternate
Modified residue19N6-methyllysine; alternate
Lipidation19N6-decanoyllysine
Modified residue24N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue24N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue24N6-acetyllysine; alternate
Modified residue24N6-butyryllysine; alternate
Modified residue24N6-crotonyllysine; alternate
Modified residue24N6-glutaryllysine; alternate
Modified residue24N6-lactoyllysine; alternate
Modified residue24N6-methyllysine; alternate
Modified residue27Citrulline
Modified residue28N6,N6,N6-trimethyllysine; alternate
Modified residue28N6,N6-dimethyllysine; alternate
Modified residue28N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue28N6-acetyllysine; alternate
Modified residue28N6-butyryllysine; alternate
Modified residue28N6-crotonyllysine; alternate
Modified residue28N6-glutaryllysine; alternate
Modified residue28N6-lactoyllysine; alternate
Modified residue28N6-methyllysine; alternate
Modified residue29ADP-ribosylserine; alternate
Modified residue29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5
Modified residue37N6,N6,N6-trimethyllysine; alternate
Modified residue37N6,N6-dimethyllysine; alternate
Modified residue37N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue37N6-acetyllysine; alternate
Modified residue37N6-butyryllysine; alternate
Modified residue37N6-methyllysine; alternate
Modified residue38N6-butyryllysine; alternate
Modified residue38N6-methyllysine; alternate
Modified residue42Phosphotyrosine
Modified residue57N6,N6,N6-trimethyllysine; alternate
Modified residue57N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue57N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue57N6-acetyllysine; alternate
Modified residue57N6-crotonyllysine; alternate
Modified residue57N6-glutaryllysine; alternate
Modified residue57N6-lactoyllysine; alternate
Modified residue57N6-methyllysine; by EHMT2; alternate
Modified residue57N6-succinyllysine; alternate
Modified residue58Phosphoserine
Modified residue65N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue65N6-methyllysine; alternate
Modified residue80N6,N6,N6-trimethyllysine; alternate
Modified residue80N6,N6-dimethyllysine; alternate
Modified residue80N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue80N6-acetyllysine; alternate
Modified residue80N6-butyryllysine; alternate
Modified residue80N6-glutaryllysine; alternate
Modified residue80N6-lactoyllysine; alternate
Modified residue80N6-methyllysine; alternate
Modified residue80N6-succinyllysine; alternate
Modified residue81Phosphothreonine
Modified residue87Phosphoserine
Modified residue108Phosphothreonine
Modified residue116N6-acetyllysine; alternate
Modified residue116N6-glutaryllysine; alternate
Modified residue123N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue123N6-acetyllysine; alternate
Modified residue123N6-butyryllysine; alternate
Modified residue123N6-glutaryllysine; alternate
Modified residue123N6-methyllysine; alternate
Modified residue123N6-succinyllysine; alternate
Modified residue129Phosphoarginine
Modified residue130Phosphoarginine
Modified residue132Phosphoarginine

Post-translational modification

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.
Phosphorylated at Thr-4 (H3T3ph) by VRK1 (By similarity).
Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2) is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity).
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.
Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting.
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.
Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).
Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic neuron differentiation (PubMed:30867594).
H3Q5ser is associated with trimethylation of Lys-5 (H3K4me3) and enhances general transcription factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating transcription (PubMed:30867594).
Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area (VTA) neurons (By similarity).
H3Q5dop mediates neurotransmission-independent role of nuclear dopamine by regulating relapse-related transcriptional plasticity in the reward system (By similarity).
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Gene expression databases

Interaction

Subunit

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with TONSL; CHAF1A; CHAF1B; MCM2 and DNAJC9 (By similarity).
Interacts with NASP; NASP is a histone chaperone that stabilizes and maintains a soluble pool of Histone H3-H4 dimers (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P68433Cbx1 P839176EBI-79743, EBI-78119
XENO P68433SETD7 Q8WTS62EBI-79743, EBI-1268586
View interactors in UniProtKB
View CPX-5712 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-43Disordered

Sequence similarities

Belongs to the histone H3 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    136
  • Mass (Da)
    15,404
  • Last updated
    2007-01-23 v2
  • Checksum
    9B89008EA50A0EF6
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X01684
EMBL· GenBank· DDBJ
CAA25839.1
EMBL· GenBank· DDBJ
Genomic DNA
M32460
EMBL· GenBank· DDBJ
AAA37811.1
EMBL· GenBank· DDBJ
Genomic DNA
M32462
EMBL· GenBank· DDBJ
AAA37813.1
EMBL· GenBank· DDBJ
Genomic DNA
X16496
EMBL· GenBank· DDBJ
CAA34512.1
EMBL· GenBank· DDBJ
Genomic DNA
U62670
EMBL· GenBank· DDBJ
AAB04763.1
EMBL· GenBank· DDBJ
Genomic DNA
U62672
EMBL· GenBank· DDBJ
AAB04765.1
EMBL· GenBank· DDBJ
Genomic DNA
AY158944
EMBL· GenBank· DDBJ
AAO06254.1
EMBL· GenBank· DDBJ
Genomic DNA
AY158945
EMBL· GenBank· DDBJ
AAO06255.1
EMBL· GenBank· DDBJ
Genomic DNA
AY158946
EMBL· GenBank· DDBJ
AAO06256.1
EMBL· GenBank· DDBJ
Genomic DNA
AY158952
EMBL· GenBank· DDBJ
AAO06262.1
EMBL· GenBank· DDBJ
Genomic DNA
Y12290
EMBL· GenBank· DDBJ
CAA72968.1
EMBL· GenBank· DDBJ
Genomic DNA
AK006742
EMBL· GenBank· DDBJ
BAB24722.1
EMBL· GenBank· DDBJ
mRNA
AK018952
EMBL· GenBank· DDBJ
BAB31493.1
EMBL· GenBank· DDBJ
mRNA
AK155722
EMBL· GenBank· DDBJ
BAE33402.1
EMBL· GenBank· DDBJ
mRNA
AL589651
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL590388
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC107285
EMBL· GenBank· DDBJ
AAI07286.1
EMBL· GenBank· DDBJ
mRNA
BC107287
EMBL· GenBank· DDBJ
AAI07288.1
EMBL· GenBank· DDBJ
mRNA
BC115816
EMBL· GenBank· DDBJ
AAI15817.1
EMBL· GenBank· DDBJ
mRNA
BC116383
EMBL· GenBank· DDBJ
AAI16384.1
EMBL· GenBank· DDBJ
mRNA
BC125355
EMBL· GenBank· DDBJ
AAI25356.1
EMBL· GenBank· DDBJ
mRNA
BC125357
EMBL· GenBank· DDBJ
AAI25358.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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