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P15864 (H12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.2
Alternative name(s):
H1 VAR.1
H1c
Gene names
Name:Hist1h1c
Synonyms:H1f2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length212 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. 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

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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NaspQ99MD93EBI-913436,EBI-913410

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 212211Histone H1.2
PRO_0000195915

Regions

Domain36 – 10974H15

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue21Phosphoserine By similarity
Modified residue171N6-acetyllysine; alternate Ref.10
Modified residue341N6-crotonyl-L-lysine; alternate Ref.8
Modified residue341N6-methyllysine; alternate By similarity
Modified residue541Citrulline
Modified residue641N6-crotonyl-L-lysine Ref.8
Modified residue851N6-crotonyl-L-lysine Ref.8
Modified residue901N6-crotonyl-L-lysine By similarity
Modified residue971N6-crotonyl-L-lysine; alternate By similarity
Modified residue971N6-succinyllysine; alternate Ref.10
Modified residue1041Phosphoserine; by PKC By similarity
Modified residue1461Phosphothreonine By similarity
Modified residue1591N6-crotonyl-L-lysine Ref.8
Modified residue1681N6-crotonyl-L-lysine Ref.8
Modified residue1861N6-methyllysine; by EHMT1 and EHMT2 By similarity
Cross-link17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis541R → A: Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding. Ref.9
Mutagenesis541R → K: Retains the positive charge, resulting in slightly decreased nucleosome-binding. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P15864 [UniParc].

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

FASTA21221,267
        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

« Hide 'large scale' 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.
[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-54, MUTAGENESIS OF ARG-54.
[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 AND LYS-17, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-97, 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
M25365 Genomic DNA. Translation: AAA37808.1.
J03482 Genomic DNA. Translation: AAA37807.1.
Y12291 Genomic DNA. Translation: CAA72970.1.
AY158905 Genomic DNA. Translation: AAO06216.1.
PIRA28470.
B35245.
RefSeqNP_056601.1. NM_015786.2.
UniGeneMm.193539.

3D structure databases

ProteinModelPortalP15864.
SMRP15864. Positions 36-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206061. 7 interactions.
DIPDIP-35245N.
IntActP15864. 3 interactions.
MINTMINT-1867285.

PTM databases

PhosphoSiteP15864.

Proteomic databases

PaxDbP15864.
PRIDEP15864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
GeneID50708.
KEGGmmu:50708.
UCSCuc007puq.2. mouse.

Organism-specific databases

CTD3006.
MGIMGI:1931526. Hist1h1c.

Phylogenomic databases

eggNOGNOG258621.
HOGENOMHOG000251627.
HOVERGENHBG009035.
InParanoidP15864.
KOK11275.
OrthoDBEOG74TX2T.
TreeFamTF313664.

Gene expression databases

ArrayExpressP15864.
BgeeP15864.
CleanExMM_HIST1H1C.
GenevestigatorP15864.

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

NextBio307561.
PROP15864.
SOURCESearch...

Entry information

Entry nameH12_MOUSE
AccessionPrimary (citable) accession number: P15864
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 118 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