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Protein

Histone H1.2

Gene

Hist1h1c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity2 Publications

GO - Molecular functioni

  • chromatin DNA binding Source: MGI
  • DNA binding Source: MGI
  • double-stranded DNA binding Source: GO_Central
  • nucleosomal DNA binding Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-211227 Activation of DNA fragmentation factor
R-MMU-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.2
Alternative name(s):
H1 VAR.1
H1c
Gene namesi
Name:Hist1h1c
Synonyms:H1f2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1931526 Hist1h1c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Triple-deficient mice (Hist1h1c, Hist1h1d and Hist1h1e) die by midgestation with a broad range of defects. These embryos have about 50% of the normal ratio of H1 to nucleosomes, demonstrating that critical levels of total H1 histones are essential for mouse embryogenesis.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54R → A: Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding. 1 Publication1
Mutagenesisi54R → K: Retains the positive charge, resulting in slightly decreased nucleosome-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001959152 – 212Histone H1.2Add BLAST211

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei17N6-acetyllysineCombined sources1
Modified residuei23N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei26N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei27N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei34N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei34N6-crotonyllysine; alternate1 Publication1
Modified residuei34N6-methyllysine; alternateBy similarity1
Modified residuei46N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei52N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei52N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei54Citrulline1 Publication1
Modified residuei63N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei64N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei64N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei64N6-crotonyllysine; alternate1 Publication1
Modified residuei75N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei81N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei85N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei85N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei85N6-crotonyllysine; alternate1 Publication1
Modified residuei90N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei90N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei90N6-crotonyllysine; alternateBy similarity1
Modified residuei97N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei97N6-crotonyllysine; alternateBy similarity1
Modified residuei97N6-succinyllysine; alternateCombined sources1
Modified residuei104Phosphoserine; by PKCBy similarity1
Modified residuei106N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei110N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei117N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei121N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei129N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei136N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei146PhosphothreonineBy similarity1
Modified residuei148N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei159N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei159N6-crotonyllysine; alternate1 Publication1
Modified residuei168N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei168N6-crotonyllysine; alternate1 Publication1
Modified residuei186N6-methyllysine; by EHMT1 and EHMT2By similarity1
Modified residuei187ADP-ribosylserineBy similarity1
Modified residuei212N6-(2-hydroxyisobutyryl)lysine1 Publication1

Post-translational modificationi

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
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.1 Publication
ADP-ribosylated on Ser-187 in response to DNA damage.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
Hydroxybutyrylation of histones is induced by starvation.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP15864
PaxDbiP15864
PeptideAtlasiP15864
PRIDEiP15864

PTM databases

iPTMnetiP15864
PhosphoSitePlusiP15864

Expressioni

Gene expression databases

BgeeiENSMUSG00000036181 Expressed in 288 organ(s), highest expression level in blood
CleanExiMM_HIST1H1C
ExpressionAtlasiP15864 baseline and differential
GenevisibleiP15864 MM

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NaspQ99MD93EBI-913436,EBI-913410

Protein-protein interaction databases

BioGridi206061, 10 interactors
DIPiDIP-35245N
IntActiP15864, 7 interactors
MINTiP15864
STRINGi10090.ENSMUSP00000045816

Structurei

3D structure databases

ProteinModelPortaliP15864
SMRiP15864
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 109H15PROSITE-ProRule annotationAdd BLAST74

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

Phylogenomic databases

eggNOGiKOG4012 Eukaryota
ENOG4112541 LUCA
GeneTreeiENSGT00670000097781
HOGENOMiHOG000251627
HOVERGENiHBG009035
InParanoidiP15864
KOiK11275
OMAiSWIDMIK
OrthoDBiEOG091G0XGD
TreeFamiTF313664

Family and domain databases

CDDicd00073 H15, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR005818 Histone_H1/H5_H15
IPR005819 Histone_H5
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00538 Linker_histone, 1 hit
PRINTSiPR00624 HISTONEH5
SMARTiView protein in SMART
SM00526 H15, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS51504 H15, 1 hit

Sequencei

Sequence statusi: Complete.

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

P15864-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEAAPAAPA AAPPAEKAPA KKKAAKKPAG VRRKASGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GILVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPQA KKAGAAKAKK PAGAAKKPKK ATGAATPKKA
160 170 180 190 200
AKKTPKKAKK PAAAAVTKKV AKSPKKAKVT KPKKVKSASK AVKPKAAKPK
210
VAKAKKVAAK KK
Length:212
Mass (Da):21,267
Last modified:January 23, 2007 - v2
Checksum:i2872A9BCD50C840D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25365 Genomic DNA Translation: AAA37808.1
J03482 Genomic DNA Translation: AAA37807.1
Y12291 Genomic DNA Translation: CAA72970.1
AY158905 Genomic DNA Translation: AAO06216.1
CCDSiCCDS26361.1
PIRiA28470
B35245
RefSeqiNP_056601.1, NM_015786.3
UniGeneiMm.193539

Genome annotation databases

EnsembliENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181
GeneIDi50708
KEGGimmu:50708
UCSCiuc007puq.3 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25365 Genomic DNA Translation: AAA37808.1
J03482 Genomic DNA Translation: AAA37807.1
Y12291 Genomic DNA Translation: CAA72970.1
AY158905 Genomic DNA Translation: AAO06216.1
CCDSiCCDS26361.1
PIRiA28470
B35245
RefSeqiNP_056601.1, NM_015786.3
UniGeneiMm.193539

3D structure databases

ProteinModelPortaliP15864
SMRiP15864
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206061, 10 interactors
DIPiDIP-35245N
IntActiP15864, 7 interactors
MINTiP15864
STRINGi10090.ENSMUSP00000045816

PTM databases

iPTMnetiP15864
PhosphoSitePlusiP15864

Proteomic databases

EPDiP15864
PaxDbiP15864
PeptideAtlasiP15864
PRIDEiP15864

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181
GeneIDi50708
KEGGimmu:50708
UCSCiuc007puq.3 mouse

Organism-specific databases

CTDi3006
MGIiMGI:1931526 Hist1h1c

Phylogenomic databases

eggNOGiKOG4012 Eukaryota
ENOG4112541 LUCA
GeneTreeiENSGT00670000097781
HOGENOMiHOG000251627
HOVERGENiHBG009035
InParanoidiP15864
KOiK11275
OMAiSWIDMIK
OrthoDBiEOG091G0XGD
TreeFamiTF313664

Enzyme and pathway databases

ReactomeiR-MMU-211227 Activation of DNA fragmentation factor
R-MMU-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)

Miscellaneous databases

PROiPR:P15864
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036181 Expressed in 288 organ(s), highest expression level in blood
CleanExiMM_HIST1H1C
ExpressionAtlasiP15864 baseline and differential
GenevisibleiP15864 MM

Family and domain databases

CDDicd00073 H15, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR005818 Histone_H1/H5_H15
IPR005819 Histone_H5
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00538 Linker_histone, 1 hit
PRINTSiPR00624 HISTONEH5
SMARTiView protein in SMART
SM00526 H15, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS51504 H15, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH12_MOUSE
AccessioniPrimary (citable) accession number: P15864
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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