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Protein

Histone H1.4

Gene

Hist1h1e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation.2 Publications

GO - Molecular functioni

  • chromatin DNA binding Source: Ensembl
  • DNA binding Source: MGI
  • poly(A) RNA binding Source: Ensembl

GO - Biological processi

  • histone H3-K27 trimethylation Source: MGI
  • histone H3-K4 trimethylation Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • nucleosome assembly Source: InterPro
  • nucleosome positioning Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.4
Alternative name(s):
H1 VAR.2
H1e
Gene namesi
Name:Hist1h1e
Synonyms:H1f4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1931527. Hist1h1e.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.By similarity

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • nuclear heterochromatin Source: Ensembl
  • nucleosome Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Triple-deficient mice (HIST1H1C/HIST1H1D/HIST1H1E) die by midgestation with a broad range of defects. These embryos have about 50% of the normal ratio of H1 to nucleosomes. This proves at least that a correct stoichiometry of linker histone deposition on chromatin is essential.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 219218Histone H1.4PRO_0000195917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei17 – 171N6-acetyllysineCombined sources
Modified residuei18 – 181PhosphothreonineCombined sources
Modified residuei26 – 261N6-acetyllysine; alternateBy similarity
Modified residuei26 – 261N6-methyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei54 – 541Citrulline1 Publication
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei146 – 1461PhosphothreonineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity

Post-translational modificationi

Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1 (By similarity).By similarity
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.By similarity
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

EPDiP43274.
MaxQBiP43274.
PaxDbiP43274.
PRIDEiP43274.

PTM databases

iPTMnetiP43274.
PhosphoSiteiP43274.

Expressioni

Gene expression databases

BgeeiP43274.
CleanExiMM_HIST1H1E.
GenevisibleiP43274. MM.

Interactioni

Protein-protein interaction databases

BioGridi206062. 5 interactions.
IntActiP43274. 6 interactions.
MINTiMINT-1868492.
STRINGi10090.ENSMUSP00000057308.

Structurei

3D structure databases

ProteinModelPortaliP43274.
SMRiP43274. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15PROSITE-ProRule annotationAdd
BLAST

Domaini

The C-terminal domain is required for high-affinity binding to chromatin.By similarity

Sequence similaritiesi

Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP43274.
KOiK11275.
OMAiCLSSICF.
OrthoDBiEOG74TX2T.
PhylomeDBiP43274.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPAAPA APAPAEKTPV KKKARKAAGG AKRKTSGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPKA KRAGAAKAKK PAGAAKKPKK AAGTATAKKS
160 170 180 190 200
TKKTPKKAKK PAAAAGAKKA KSPKKAKATK AKKAPKSPAK AKTVKPKAAK
210
PKTSKPKAAK PKKTAAKKK
Length:219
Mass (Da):21,977
Last modified:January 23, 2007 - v2
Checksum:i9463467F699F3625
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26163 Genomic DNA. Translation: AAA37760.1.
L04141 Genomic DNA. Translation: AAA37814.1.
Y12292 Genomic DNA. Translation: CAA72971.1.
BC089600 mRNA. Translation: AAH89600.1.
CCDSiCCDS26355.1.
PIRiI49742.
RefSeqiNP_056602.1. NM_015787.4.
UniGeneiMm.170587.

Genome annotation databases

EnsembliENSMUST00000062045; ENSMUSP00000057308; ENSMUSG00000051627.
GeneIDi50709.
KEGGimmu:50709.
UCSCiuc007puj.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26163 Genomic DNA. Translation: AAA37760.1.
L04141 Genomic DNA. Translation: AAA37814.1.
Y12292 Genomic DNA. Translation: CAA72971.1.
BC089600 mRNA. Translation: AAH89600.1.
CCDSiCCDS26355.1.
PIRiI49742.
RefSeqiNP_056602.1. NM_015787.4.
UniGeneiMm.170587.

3D structure databases

ProteinModelPortaliP43274.
SMRiP43274. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206062. 5 interactions.
IntActiP43274. 6 interactions.
MINTiMINT-1868492.
STRINGi10090.ENSMUSP00000057308.

PTM databases

iPTMnetiP43274.
PhosphoSiteiP43274.

Proteomic databases

EPDiP43274.
MaxQBiP43274.
PaxDbiP43274.
PRIDEiP43274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062045; ENSMUSP00000057308; ENSMUSG00000051627.
GeneIDi50709.
KEGGimmu:50709.
UCSCiuc007puj.3. mouse.

Organism-specific databases

CTDi3008.
MGIiMGI:1931527. Hist1h1e.

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP43274.
KOiK11275.
OMAiCLSSICF.
OrthoDBiEOG74TX2T.
PhylomeDBiP43274.
TreeFamiTF313664.

Miscellaneous databases

NextBioi307565.
PROiP43274.
SOURCEiSearch...

Gene expression databases

BgeeiP43274.
CleanExiMM_HIST1H1E.
GenevisibleiP43274. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two replication-dependent mouse H1 histone genes."
    Dong Y., Sirotkin A.M., Yang Y.-S., Brown D.T., Sittman D.B., Skoultchi A.I.
    Nucleic Acids Res. 22:1421-1428(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
    Tissue: Spleen.
  2. "Identification through overexpression and tagging of the variant type of the mouse H1e and H1c genes."
    Brown D.T., Sittman D.B.
    J. Biol. Chem. 268:713-718(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Expression of murine H1 histone genes during postnatal development."
    Franke K., Drabent B., Doenecke D.
    Biochim. Biophys. Acta 1398:232-242(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  5. "H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo."
    Fan Y., Nikitina T., Morin-Kensicki E.M., Zhao J., Magnuson T.R., Woodcock C.L., Skoultchi A.I.
    Mol. Cell. Biol. 23:4559-4572(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation."
    Fan Y., Nikitina T., Zhao J., Fleury T.J., Bhattacharyya R., Bouhassira E.E., Stein A., Woodcock C.L., Skoultchi A.I.
    Cell 123:1199-1212(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN GENE REGULATION.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Spleen.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-17, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: CITRULLINATION AT ARG-54.

Entry informationi

Entry nameiH14_MOUSE
AccessioniPrimary (citable) accession number: P43274
Secondary accession number(s): Q5EBH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.