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Protein

Histone H1.2

Gene

Hist1h1c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • chromatin DNA binding Source: MGI
  • DNA binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • nucleosome assembly Source: InterPro
  • nucleosome positioning Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.2
Alternative name(s):
H1 VAR.1
H1c
Gene namesi
Name:Hist1h1c
Synonyms:H1f2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1931526. Hist1h1c.

Subcellular locationi

GO - Cellular componenti

  • nuclear euchromatin Source: MGI
  • nucleosome Source: InterPro
  • nucleus Source: MGI
  • transcriptionally active chromatin Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541R → A: Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding. 1 Publication
Mutagenesisi54 – 541R → K: Retains the positive charge, resulting in slightly decreased nucleosome-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 212211Histone H1.2PRO_0000195915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei26 – 261N6-acetyllysine; alternateBy similarity
Modified residuei26 – 261N6-methyllysine; alternateBy similarity
Modified residuei27 – 271N6-methyllysineBy similarity
Modified residuei34 – 341N6-crotonyllysine; alternate1 Publication
Modified residuei34 – 341N6-methyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysine; alternateBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei46 – 461N6-acetyllysineBy similarity
Modified residuei54 – 541Citrulline1 Publication
Modified residuei64 – 641N6-crotonyllysine1 Publication
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei85 – 851N6-crotonyllysine1 Publication
Modified residuei90 – 901N6-acetyllysine; alternateBy similarity
Modified residuei90 – 901N6-crotonyllysine; alternateBy similarity
Modified residuei97 – 971N6-crotonyllysine; alternateBy similarity
Modified residuei97 – 971N6-succinyllysine; alternate1 Publication
Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
Modified residuei146 – 1461PhosphothreonineBy similarity
Modified residuei154 – 1541PhosphothreonineBy similarity
Modified residuei159 – 1591N6-crotonyllysine1 Publication
Modified residuei168 – 1681N6-acetyllysine; alternateBy similarity
Modified residuei168 – 1681N6-crotonyllysine; alternate1 Publication
Modified residuei173 – 1731PhosphoserineBy similarity
Modified residuei186 – 1861N6-methyllysine; by EHMT1 and EHMT2By similarity
Modified residuei187 – 1871PhosphoserineBy similarity
Cross-linki205 – 205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

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
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

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15864.
PaxDbiP15864.
PRIDEiP15864.

PTM databases

PhosphoSiteiP15864.

Expressioni

Gene expression databases

BgeeiP15864.
CleanExiMM_HIST1H1C.
ExpressionAtlasiP15864. baseline and differential.
GenevisibleiP15864. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NaspQ99MD93EBI-913436,EBI-913410

Protein-protein interaction databases

BioGridi206061. 8 interactions.
DIPiDIP-35245N.
IntActiP15864. 3 interactions.
MINTiMINT-1867285.
STRINGi10090.ENSMUSP00000045816.

Structurei

3D structure databases

ProteinModelPortaliP15864.
SMRiP15864. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15PROSITE-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.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP15864.
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.

P15864-1 [UniParc]FASTAAdd 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.
CCDSiCCDS26361.1.
PIRiA28470.
B35245.
RefSeqiNP_056601.1. NM_015786.3.
UniGeneiMm.193539.

Genome annotation databases

EnsembliENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
GeneIDi50708.
KEGGimmu:50708.
UCSCiuc007puq.2. mouse.

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.
CCDSiCCDS26361.1.
PIRiA28470.
B35245.
RefSeqiNP_056601.1. NM_015786.3.
UniGeneiMm.193539.

3D structure databases

ProteinModelPortaliP15864.
SMRiP15864. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206061. 8 interactions.
DIPiDIP-35245N.
IntActiP15864. 3 interactions.
MINTiMINT-1867285.
STRINGi10090.ENSMUSP00000045816.

PTM databases

PhosphoSiteiP15864.

Proteomic databases

MaxQBiP15864.
PaxDbiP15864.
PRIDEiP15864.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
GeneIDi50708.
KEGGimmu:50708.
UCSCiuc007puq.2. mouse.

Organism-specific databases

CTDi3006.
MGIiMGI:1931526. Hist1h1c.

Phylogenomic databases

eggNOGiNOG258621.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP15864.
KOiK11275.
OrthoDBiEOG74TX2T.
TreeFamiTF313664.

Miscellaneous databases

NextBioi307561.
PROiP15864.
SOURCEiSearch...

Gene expression databases

BgeeiP15864.
CleanExiMM_HIST1H1C.
ExpressionAtlasiP15864. baseline and differential.
GenevisibleiP15864. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  10. Cited for: CITRULLINATION AT ARG-54, MUTAGENESIS OF ARG-54.

Entry informationi

Entry nameiH12_MOUSE
AccessioniPrimary (citable) accession number: P15864
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 127 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.