Hist1h1c

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
Inferred from direct assayⁱ
- 15562002
double-stranded DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
nucleosomal DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chromosome condensation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
histone H3-K27 trimethylation
Source: MGI
Inferred from genetic interactionⁱ
- 22701719
histone H3-K4 trimethylation
Source: MGI
Inferred from genetic interactionⁱ
- 22701719
negative regulation of chromatin silencing
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of DNA recombination
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of transcription by RNA polymerase II
Source: MGI
Inferred from genetic interactionⁱ
- 22083958
nucleosome assembly Source: InterPro
nucleosome positioning
Source: MGI
Inferred from mutant phenotypeⁱ
- 12808097
regulation of transcription, DNA-templated
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of transcription by RNA polymerase II
Source: MGI
Inferred from mutant phenotypeⁱ
- 22701719

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Enzyme and pathway databases

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

Reactomeⁱ

R-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
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 13

Organism-specific databases

MGIⁱ	MGI:1931526 Hist1h1c

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 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	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, Phosphoprotein

Proteomic databases

EPDⁱ	P15864
PaxDbⁱ	P15864
PeptideAtlas More...PeptideAtlasⁱ	P15864
PRIDEⁱ	P15864

PTM databases

iPTMnetⁱ	P15864
PhosphoSitePlusⁱ	P15864

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000036181 Expressed in 288 organ(s), highest expression level in blood
CleanExⁱ	MM_HIST1H1C
ExpressionAtlasⁱ	P15864 baseline and differential
Genevisibleⁱ	P15864 MM

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Nasp	Q99MD9	3	EBI-913436,EBI-913410

With

Entry

#Exp.

IntAct

Notes

Nasp

Q99MD9

3

EBI-913436,EBI-913410

Protein-protein interaction databases

BioGridⁱ	206061, 10 interactors
Database of interacting proteins More...DIPⁱ	DIP-35245N
IntActⁱ	P15864, 7 interactors
Molecular INTeraction database More...MINTⁱ	P15864
STRINGⁱ	10090.ENSMUSP00000045816

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P15864
SMRⁱ	P15864
ModBaseⁱ	Search...
MobiDBⁱ	Search...

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 ENOG4112541 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00670000097781
HOGENOMⁱ	HOG000251627
HOVERGENⁱ	HBG009035
InParanoidⁱ	P15864
KEGG Orthology (KO) More...KOⁱ	K11275
OMAⁱ	SWIDMIK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0XGD
TreeFamⁱ	TF313664

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00073 H15, 1 hit
Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR005818 Histone_H1/H5_H15 IPR005819 Histone_H5 IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P15864-1 [UniParc]FASTA Add 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS26361.1
PIRⁱ	A28470 B35245
NCBI Reference Sequences More...RefSeqⁱ	NP_056601.1, NM_015786.3
UniGeneⁱ	Mm.193539

Genome annotation databases

Ensemblⁱ	ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181
GeneIDⁱ	50708
KEGGⁱ	mmu:50708
UCSC genome browser More...UCSCⁱ	uc007puq.3 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P15864	Histone cluster 1, H1c		MOUSE		212	UniRef100_P15864
Uncharacterized protein (Fragment)		MOUSE		136

Protein	Similar proteins		Species	Score	Length	Source
P15864	Histone H1.2		HUMAN		213	UniRef90_P15864
Histone cluster 1, H1c		MOUSE		212
Histone cluster 1 H1 family member c		GORGO		213
HIST1H1C isoform 1		PANTR		213
Uncharacterized protein		PANPA		213
+46

Protein	Similar proteins		Species	Score	Length	Source
P15864	Histone H1.2		HUMAN		213	UniRef50_P15864
Histone H1A		XENLA		210
Histone H1.2		BOVIN		213
Histone cluster 1, H1c		MOUSE		212
Uncharacterized protein		OTOGA		213
+393

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
UniGeneⁱ	Mm.193539

3D structure databases

ProteinModelPortalⁱ	P15864
SMRⁱ	P15864
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	206061, 10 interactors
DIPⁱ	DIP-35245N
IntActⁱ	P15864, 7 interactors
MINTⁱ	P15864
STRINGⁱ	10090.ENSMUSP00000045816

PTM databases

iPTMnetⁱ	P15864
PhosphoSitePlusⁱ	P15864

Proteomic databases

EPDⁱ	P15864
PaxDbⁱ	P15864
PeptideAtlasⁱ	P15864
PRIDEⁱ	P15864

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181
GeneIDⁱ	50708
KEGGⁱ	mmu:50708
UCSCⁱ	uc007puq.3 mouse

Organism-specific databases

CTDⁱ	3006
MGIⁱ	MGI:1931526 Hist1h1c

Phylogenomic databases

eggNOGⁱ	KOG4012 Eukaryota ENOG4112541 LUCA
GeneTreeⁱ	ENSGT00670000097781
HOGENOMⁱ	HOG000251627
HOVERGENⁱ	HBG009035
InParanoidⁱ	P15864
KOⁱ	K11275
OMAⁱ	SWIDMIK
OrthoDBⁱ	EOG091G0XGD
TreeFamⁱ	TF313664

Enzyme and pathway databases

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

Reactomeⁱ

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

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P15864
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000036181 Expressed in 288 organ(s), highest expression level in blood
CleanExⁱ	MM_HIST1H1C
ExpressionAtlasⁱ	P15864 baseline and differential
Genevisibleⁱ	P15864 MM

Family and domain databases

CDDⁱ	cd00073 H15, 1 hit
Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR005818 Histone_H1/H5_H15 IPR005819 Histone_H5 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...

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:	November 7, 2018
	This is version 155 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

Complete proteome, Reference proteome

Documents

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

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UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P15864 (H12_MOUSE)

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Histone H1.2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ