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P15864

- H12_MOUSE

UniProt

P15864 - H12_MOUSE

Protein

Histone H1.2

Gene

Hist1h1c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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. DNA binding Source: MGI
    2. protein binding Source: IntAct

    GO - Biological processi

    1. nucleosome assembly Source: InterPro
    2. nucleosome positioning Source: MGI

    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: Chromosome 13

    Organism-specific databases

    MGIiMGI:1931526. Hist1h1c.

    Subcellular locationi

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

    GO - Cellular componenti

    1. nucleosome Source: InterPro
    2. nucleus Source: UniProtKB-SubCell

    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 – 11RemovedBy similarity
    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 residuei34 – 341N6-crotonyllysine; alternate1 Publication
    Modified residuei34 – 341N6-methyllysine; alternateBy similarity
    Modified residuei54 – 541Citrulline1 Publication
    Modified residuei64 – 641N6-crotonyllysine1 Publication
    Modified residuei85 – 851N6-crotonyllysine1 Publication
    Modified residuei90 – 901N6-crotonyllysineBy similarity
    Modified residuei97 – 971N6-crotonyllysine; alternateBy similarity
    Modified residuei97 – 971N6-succinyllysine; alternate1 Publication
    Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
    Modified residuei146 – 1461PhosphothreonineBy similarity
    Modified residuei159 – 1591N6-crotonyllysine1 Publication
    Modified residuei168 – 1681N6-crotonyllysine1 Publication
    Modified residuei186 – 1861N6-methyllysine; by EHMT1 and EHMT2By 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

    PaxDbiP15864.
    PRIDEiP15864.

    PTM databases

    PhosphoSiteiP15864.

    Expressioni

    Gene expression databases

    ArrayExpressiP15864.
    BgeeiP15864.
    CleanExiMM_HIST1H1C.
    GenevestigatoriP15864.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

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

    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.
    OMAiIRRVIKN.
    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

    MSEAAPAAPA AAPPAEKAPA KKKAAKKPAG VRRKASGPPV SELITKAVAA    50
    SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GILVQTKGTG 100
    ASGSFKLNKK AASGEAKPQA KKAGAAKAKK PAGAAKKPKK ATGAATPKKA 150
    AKKTPKKAKK PAAAAVTKKV AKSPKKAKVT KPKKVKSASK AVKPKAAKPK 200
    VAKAKKVAAK KK 212
    Length:212
    Mass (Da):21,267
    Last modified:January 23, 2007 - v2
    Checksum:i2872A9BCD50C840D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS26361.1.
    PIRi A28470.
    B35245.
    RefSeqi NP_056601.1. NM_015786.3.
    UniGenei Mm.193539.

    3D structure databases

    ProteinModelPortali P15864.
    SMRi P15864. Positions 36-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206061. 8 interactions.
    DIPi DIP-35245N.
    IntActi P15864. 3 interactions.
    MINTi MINT-1867285.

    PTM databases

    PhosphoSitei P15864.

    Proteomic databases

    PaxDbi P15864.
    PRIDEi P15864.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040914 ; ENSMUSP00000045816 ; ENSMUSG00000036181 .
    GeneIDi 50708.
    KEGGi mmu:50708.
    UCSCi uc007puq.2. mouse.

    Organism-specific databases

    CTDi 3006.
    MGIi MGI:1931526. Hist1h1c.

    Phylogenomic databases

    eggNOGi NOG258621.
    HOGENOMi HOG000251627.
    HOVERGENi HBG009035.
    InParanoidi P15864.
    KOi K11275.
    OMAi IRRVIKN.
    OrthoDBi EOG74TX2T.
    TreeFami TF313664.

    Miscellaneous databases

    NextBioi 307561.
    PROi P15864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15864.
    Bgeei P15864.
    CleanExi MM_HIST1H1C.
    Genevestigatori P15864.

    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

    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. 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.

    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: October 1, 2014
    This is version 122 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