Histone H1.2 - Mus musculus (Mouse)

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P15864 (H12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone H1.2

Alternative name(s):
H1 VAR.1
H1c

Gene names

Name:	Hist1h1c
Synonyms:	H1f2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.7
Subcellular location	Nucleus. Chromosome. Note: Mainly localizes in euchromatin By similarity.
Domain	The C-terminal domain is required for high-affinity binding to chromatin By similarity.
Post-translational modification	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. Ref.5 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. Ref.8
Disruption phenotype	No visible phenotype. 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, demonstrating that critical levels of total H1 histones are essential for mouse embryogenesis. Ref.6 Ref.7
Sequence similarities	Belongs to the histone H1/H5 family. Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro nucleosome positioning Inferred from mutant phenotype Ref.6. Source: MGI
Cellular_component	nucleosome Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from direct assay PubMed 15562002. Source: MGI
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 212

211

Histone H1.2

PRO_0000195915

Regions

Domain

36 – 109

H15

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-crotonyl-L-lysine; alternate Ref.8

Modified residue

N6-methyllysine; alternate By similarity

Modified residue

N6-crotonyl-L-lysine Ref.8

Modified residue

N6-crotonyl-L-lysine Ref.8

Modified residue

N6-crotonyl-L-lysine By similarity

Modified residue

N6-crotonyl-L-lysine By similarity

Modified residue

104

Phosphoserine; by PKC By similarity

Modified residue

146

Phosphothreonine By similarity

Modified residue

159

N6-crotonyl-L-lysine Ref.8

Modified residue

168

N6-crotonyl-L-lysine Ref.8

Modified residue

186

N6-methyllysine; by EHMT1 and EHMT2 By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

205

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P15864 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2872A9BCD50C840D
Show »

FASTA

212

21,267

        10         20         30         40         50         60 
MSEAAPAAPA AAPPAEKAPA KKKAAKKPAG VRRKASGPPV SELITKAVAA SKERSGVSLA 

        70         80         90        100        110        120 
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GILVQTKGTG ASGSFKLNKK AASGEAKPQA 

       130        140        150        160        170        180 
KKAGAAKAKK PAGAAKKPKK ATGAATPKKA AKKTPKKAKK PAAAAVTKKV AKSPKKAKVT 

       190        200        210 
KPKKVKSASK AVKPKAAKPK VAKAKKVAAK KK

« Hide

References

[1]	"Different 3'-end processing produces two independently regulated mRNAs from a single H1 histone gene." Cheng G., Nandi A., Clerk S., Skoultchi A.I. Proc. Natl. Acad. Sci. U.S.A. 86:7002-7006(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and characterization of a mouse fully replication-dependent H1 gene within a genomic cluster of core histone genes." Yang Y.-S., Brown D.T., Wellman S.E., Sittman D.B. J. Biol. Chem. 262:17118-17125(1987) [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/c.
[4]	"The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"In vivo phosphorylation of histone H1 variants during the cell cycle." Talasz H., Helliger W., Puschendorf B., Lindner H. Biochemistry 35:1761-1767(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[6]	"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.
[7]	"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.
[8]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-159 AND LYS-168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M25365 Genomic DNA. Translation: AAA37808.1. J03482 Genomic DNA. Translation: AAA37807.1. Y12291 Genomic DNA. Translation: CAA72970.1. AY158905 Genomic DNA. Translation: AAO06216.1.
IPI	IPI00223713.
PIR	A28470. B35245.
RefSeq	NP_056601.1. NM_015786.2.
UniGene	Mm.193539.
3D structure databases
ProteinModelPortal	P15864.
SMR	P15864. Positions 36-109.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35245N.
IntAct	P15864. 1 interaction.
PTM databases
PhosphoSite	P15864.
Proteomic databases
PaxDb	P15864.
PRIDE	P15864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
GeneID	50708.
KEGG	mmu:50708.
Organism-specific databases
CTD	3006.
MGI	MGI:1931526. Hist1h1c.
Phylogenomic databases
eggNOG	NOG258621.
HOGENOM	HOG000251627.
HOVERGEN	HBG009035.
InParanoid	P15864.
KO	K11275.
OMA	PGAKATT.
Gene expression databases
ArrayExpress	P15864.
Bgee	P15864.
CleanEx	MM_HIST1H1C.
Genevestigator	P15864.
GermOnline	ENSMUSG00000036181. Mus musculus.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00538. Linker_histone. 1 hit. [Graphical view]
PRINTS	PR00624. HISTONEH5.
SMART	SM00526. H15. 1 hit. [Graphical view]
PROSITE	PS51504. H15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	307561.
SOURCE	Search...

Entry information

Entry name

H12_MOUSE

Accession

Primary (citable) accession number: P15864

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents