UniProtKB - P15864 (H12_MOUSE)
Protein
Histone H1.2
Gene
H1-2
Organism
Mus musculus (Mouse)
Status
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
- chromosome condensation Source: GO_Central
- histone H3-K27 trimethylation Source: MGI
- histone H3-K4 trimethylation Source: MGI
- negative regulation of chromatin silencing Source: GO_Central
- negative regulation of DNA recombination Source: GO_Central
- negative regulation of transcription by RNA polymerase II Source: MGI
- nucleosome assembly Source: InterPro
- nucleosome positioning Source: MGI
- regulation of transcription by RNA polymerase II Source: MGI
Keywordsi
Molecular function | DNA-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H1.2Alternative name(s): H1 VAR.1 H1c |
Gene namesi | Name:H1-2By similarity Synonyms:H1f2Imported, Hist1h1cImported |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1931526, H1f2 |
Subcellular locationi
Nucleus
Other locations
Note: Mainly localizes in euchromatin.By similarity
Nucleus
- nucleus Source: MGI
Other locations
- euchromatin Source: MGI
- nucleosome Source: InterPro
- transcriptionally active chromatin Source: MGI
Keywords - Cellular componenti
Chromosome, NucleusPathology & Biotechi
Disruption phenotypei
No visible phenotype. Triple-deficient mice (H1-2, H1-3 and H1-4) 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 54 | R → A: Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding. 1 Publication | 1 | |
Mutagenesisi | 54 | R → K: Retains the positive charge, resulting in slightly decreased nucleosome-binding. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000195915 | 2 – 212 | Histone H1.2Add BLAST | 211 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 17 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 23 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 26 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 27 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 34 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 34 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 34 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 46 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 52 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 52 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 54 | Citrulline1 Publication | 1 | |
Modified residuei | 63 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 64 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 64 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 64 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 75 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 81 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 85 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 85 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 85 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 90 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 90 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 90 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 97 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 97 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 97 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 104 | Phosphoserine; by PKCBy similarity | 1 | |
Modified residuei | 106 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 110 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 117 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 121 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 129 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 136 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 146 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 148 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 159 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 159 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 168 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 168 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 186 | N6-methyllysine; by EHMT1 and EHMT2By similarity | 1 | |
Modified residuei | 187 | ADP-ribosylserineBy similarity | 1 | |
Modified residuei | 212 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 |
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, PhosphoproteinProteomic databases
EPDi | P15864 |
jPOSTi | P15864 |
PaxDbi | P15864 |
PeptideAtlasi | P15864 |
PRIDEi | P15864 |
ProteomicsDBi | 271491 |
PTM databases
iPTMneti | P15864 |
PhosphoSitePlusi | P15864 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000036181, Expressed in blood and 305 other tissues |
Genevisiblei | P15864, MM |
Interactioni
Binary interactionsi
P15864
With | #Exp. | IntAct |
---|---|---|
Nasp [Q99MD9] | 3 | EBI-913436,EBI-913410 |
Protein-protein interaction databases
BioGRIDi | 206061, 22 interactors |
DIPi | DIP-35245N |
IntActi | P15864, 7 interactors |
MINTi | P15864 |
STRINGi | 10090.ENSMUSP00000045816 |
Miscellaneous databases
RNActi | P15864, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 36 – 109 | H15PROSITE-ProRule annotationAdd BLAST | 74 |
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
eggNOGi | KOG4012, Eukaryota |
GeneTreei | ENSGT00940000163082 |
HOGENOMi | CLU_052897_7_0_1 |
InParanoidi | P15864 |
OMAi | NSAITHG |
OrthoDBi | 1565299at2759 |
TreeFami | TF313664 |
Family and domain databases
CDDi | cd00073, H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005819, H1/H5 IPR005818, Histone_H1/H5_H15 IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538, Linker_histone, 1 hit |
PRINTSi | PR00624, HISTONEH5 |
SMARTi | View protein in SMART SM00526, H15, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504, H15, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P15864-1 [UniParc]FASTAAdd to basket
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
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 |
CCDSi | CCDS26361.1 |
PIRi | A28470 B35245 |
RefSeqi | NP_056601.1, NM_015786.3 |
Genome annotation databases
Ensembli | ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181 |
GeneIDi | 50708 |
KEGGi | mmu:50708 |
UCSCi | uc007puq.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 |
CCDSi | CCDS26361.1 |
PIRi | A28470 B35245 |
RefSeqi | NP_056601.1, NM_015786.3 |
3D structure databases
SMRi | P15864 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 206061, 22 interactors |
DIPi | DIP-35245N |
IntActi | P15864, 7 interactors |
MINTi | P15864 |
STRINGi | 10090.ENSMUSP00000045816 |
PTM databases
iPTMneti | P15864 |
PhosphoSitePlusi | P15864 |
Proteomic databases
EPDi | P15864 |
jPOSTi | P15864 |
PaxDbi | P15864 |
PeptideAtlasi | P15864 |
PRIDEi | P15864 |
ProteomicsDBi | 271491 |
Protocols and materials databases
Antibodypediai | 25499, 416 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181 |
GeneIDi | 50708 |
KEGGi | mmu:50708 |
UCSCi | uc007puq.3, mouse |
Organism-specific databases
CTDi | 50708 |
MGIi | MGI:1931526, H1f2 |
Phylogenomic databases
eggNOGi | KOG4012, Eukaryota |
GeneTreei | ENSGT00940000163082 |
HOGENOMi | CLU_052897_7_0_1 |
InParanoidi | P15864 |
OMAi | NSAITHG |
OrthoDBi | 1565299at2759 |
TreeFami | TF313664 |
Miscellaneous databases
BioGRID-ORCSi | 50708, 2 hits in 52 CRISPR screens |
ChiTaRSi | Hist1h1c, mouse |
PROi | PR:P15864 |
RNActi | P15864, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000036181, Expressed in blood and 305 other tissues |
Genevisiblei | P15864, MM |
Family and domain databases
CDDi | cd00073, H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005819, H1/H5 IPR005818, Histone_H1/H5_H15 IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538, Linker_histone, 1 hit |
PRINTSi | PR00624, HISTONEH5 |
SMARTi | View protein in SMART SM00526, H15, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504, H15, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H12_MOUSE | |
Accessioni | P15864Primary (citable) accession number: P15864 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 172 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families