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P43275 (H11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.1
Alternative name(s):
H1 VAR.3
Histone H1a
Short name=H1a
Gene names
Name:Hist1h1a
Synonyms:H1a, H1f1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Interacts with DFFB By similarity.

Subcellular location

Nucleus. Chromosome. Note: Mainly localizes in euchromatin By similarity.

Tissue specificity

Restricted to thymus, testis and spleen. Present also in lymphocytic and neuronal cells. Increases in testis starting with a low level at day 5 and reaching high concentrations in 20-day old and adult animals. Ref.2

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. Ref.7

Citrullination at Arg-56 (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.

Disruption phenotype

Deficient-mice developed normally until the adult stage. No anatomic abnormalities are detected, mice are fertile and they show normal spermatogenesis and testicular morphology. The lack of phenotype may be due to a compensatory function of other histone H1 subtypes. Ref.8

Sequence similarities

Belongs to the histone H1/H5 family.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 213212Histone H1.1
PRO_0000195914

Regions

Domain38 – 11174H15

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue171N6-acetyllysine Ref.10
Modified residue561Citrulline
Modified residue771N6-acetyllysine Ref.10
Modified residue921N6-acetyllysine Ref.10
Modified residue1061Phosphoserine By similarity
Modified residue1211N6-acetyllysine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P43275 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 03A46320A100B203

FASTA21321,785
        10         20         30         40         50         60 
MSETAPVAQA ASTATEKPAA AKKTKKPAKA AAPRKKPAGP SVSELIVQAV SSSKERSGVS 

        70         80         90        100        110        120 
LAALKKSLAA AGYDVEKNNS RIKLGLKSLV NKGTLVQTKG TGAAGSFKLN KKAESKAITT 

       130        140        150        160        170        180 
KVSVKAKASG AAKKPKKTAG AAAKKTVKTP KKPKKPAVSK KTSKSPKKPK VVKAKKVAKS 

       190        200        210 
PAKAKAVKPK ASKAKVTKPK TPAKPKKAAP KKK 

« Hide

References

« Hide 'large scale' references
[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/c.
[2]"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], TISSUE SPECIFICITY.
Strain: 129/Sv.
[3]"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].
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
[7]"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.
[8]"Spermatogenesis in mice is not affected by histone H1.1 deficiency."
Rabini S., Franke K., Saftig P., Bode C., Doenecke D., Drabent B.
Exp. Cell Res. 255:114-124(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-56.
[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; LYS-17; LYS-77; LYS-92 AND LYS-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26164 Genomic DNA. Translation: AAA37761.1.
Y12290 Genomic DNA. Translation: CAA72969.1.
AY158903 Genomic DNA. Translation: AAO06214.1.
AL590388 Genomic DNA. Translation: CAI25836.1.
CH466561 Genomic DNA. Translation: EDL32534.1.
BC116820 mRNA. Translation: AAI16821.1.
BC116850 mRNA. Translation: AAI16851.1.
PIRS43949.
RefSeqNP_085112.1. NM_030609.3.
UniGeneMm.377137.
Mm.480242.

3D structure databases

ProteinModelPortalP43275.
SMRP43275. Positions 38-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid219818. 9 interactions.
IntActP43275. 1 interaction.
MINTMINT-1868385.
STRING10090.ENSMUSP00000062030.

PTM databases

PhosphoSiteP43275.

Proteomic databases

PaxDbP43275.
PRIDEP43275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055770; ENSMUSP00000062030; ENSMUSG00000049539.
GeneID80838.
KEGGmmu:80838.
UCSCuc007puz.1. mouse.

Organism-specific databases

CTD3024.
MGIMGI:1931523. Hist1h1a.

Phylogenomic databases

eggNOGNOG258621.
GeneTreeENSGT00670000097781.
HOGENOMHOG000251627.
HOVERGENHBG009035.
InParanoidP43275.
KOK11275.
OMADKYIAGN.
OrthoDBEOG74TX2T.
TreeFamTF313664.

Gene expression databases

BgeeP43275.
CleanExMM_HIST1H1A.
GenevestigatorP43275.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350151.
PROP43275.
SOURCESearch...

Entry information

Entry nameH11_MOUSE
AccessionPrimary (citable) accession number: P43275
Secondary accession number(s): Q5SZ98
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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