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P43275

- H11_MOUSE

UniProt

P43275 - H11_MOUSE

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Protein

Histone H1.1

Gene

Hist1h1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- 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 similarity

GO - Molecular functioni

  1. chromatin DNA binding Source: Ensembl
  2. DNA binding Source: MGI

GO - Biological processi

  1. nucleosome assembly Source: InterPro
  2. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.1
Alternative name(s):
H1 VAR.3
Histone H1a
Short name:
H1a
Gene namesi
Name:Hist1h1a
Synonyms:H1a, H1f1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1931523. Hist1h1a.

Subcellular locationi

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

GO - Cellular componenti

  1. nuclear euchromatin Source: Ensembl
  2. nucleosome Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 213212Histone H1.1PRO_0000195914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei17 – 171N6-acetyllysine1 Publication
Modified residuei56 – 561Citrulline1 Publication
Modified residuei77 – 771N6-acetyllysine1 Publication
Modified residuei92 – 921N6-acetyllysine1 Publication
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei121 – 1211N6-acetyllysine1 Publication

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.1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiP43275.
PaxDbiP43275.
PRIDEiP43275.

PTM databases

PhosphoSiteiP43275.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP43275.
CleanExiMM_HIST1H1A.
GenevestigatoriP43275.

Interactioni

Subunit structurei

Interacts with DFFB.By similarity

Protein-protein interaction databases

BioGridi219818. 9 interactions.
IntActiP43275. 1 interaction.
MINTiMINT-1868385.
STRINGi10090.ENSMUSP00000062030.

Structurei

3D structure databases

ProteinModelPortaliP43275.
SMRiP43275. Positions 38-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 11174H15PROSITE-ProRule annotationAdd
BLAST

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
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258621.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP43275.
KOiK11275.
OrthoDBiEOG74TX2T.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43275-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSETAPVAQA ASTATEKPAA AKKTKKPAKA AAPRKKPAGP SVSELIVQAV
60 70 80 90 100
SSSKERSGVS LAALKKSLAA AGYDVEKNNS RIKLGLKSLV NKGTLVQTKG
110 120 130 140 150
TGAAGSFKLN KKAESKAITT KVSVKAKASG AAKKPKKTAG AAAKKTVKTP
160 170 180 190 200
KKPKKPAVSK KTSKSPKKPK VVKAKKVAKS PAKAKAVKPK ASKAKVTKPK
210
TPAKPKKAAP KKK
Length:213
Mass (Da):21,785
Last modified:January 23, 2007 - v2
Checksum:i03A46320A100B203
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26369.1.
PIRiS43949.
RefSeqiNP_085112.1. NM_030609.3.
UniGeneiMm.480242.

Genome annotation databases

EnsembliENSMUST00000055770; ENSMUSP00000062030; ENSMUSG00000049539.
GeneIDi80838.
KEGGimmu:80838.
UCSCiuc007puz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26369.1.
PIRi S43949.
RefSeqi NP_085112.1. NM_030609.3.
UniGenei Mm.480242.

3D structure databases

ProteinModelPortali P43275.
SMRi P43275. Positions 38-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 219818. 9 interactions.
IntActi P43275. 1 interaction.
MINTi MINT-1868385.
STRINGi 10090.ENSMUSP00000062030.

PTM databases

PhosphoSitei P43275.

Proteomic databases

MaxQBi P43275.
PaxDbi P43275.
PRIDEi P43275.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055770 ; ENSMUSP00000062030 ; ENSMUSG00000049539 .
GeneIDi 80838.
KEGGi mmu:80838.
UCSCi uc007puz.1. mouse.

Organism-specific databases

CTDi 3024.
MGIi MGI:1931523. Hist1h1a.

Phylogenomic databases

eggNOGi NOG258621.
GeneTreei ENSGT00670000097781.
HOGENOMi HOG000251627.
HOVERGENi HBG009035.
InParanoidi P43275.
KOi K11275.
OrthoDBi EOG74TX2T.
TreeFami TF313664.

Miscellaneous databases

NextBioi 350151.
PROi P43275.
SOURCEi Search...

Gene expression databases

Bgeei P43275.
CleanExi MM_HIST1H1A.
Genevestigatori P43275.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00538. Linker_histone. 1 hit.
[Graphical view ]
PRINTSi PR00624. HISTONEH5.
SMARTi SM00526. H15. 1 hit.
[Graphical view ]
PROSITEi PS51504. H15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiH11_MOUSE
AccessioniPrimary (citable) accession number: P43275
Secondary accession number(s): Q5SZ98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3