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P43276

- H15_MOUSE

UniProt

P43276 - H15_MOUSE

Protein

Histone H1.5

Gene

Hist1h1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (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. muscle organ development Source: MGI
    2. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H1.5
    Alternative name(s):
    H1 VAR.5
    H1b
    Gene namesi
    Name:Hist1h1b
    Synonyms:H1f5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1861461. Hist1h1b.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 223222Histone H1.5PRO_0000195918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei17 – 171N6-acetyllysine1 Publication
    Modified residuei18 – 181Phosphoserine1 Publication
    Modified residuei27 – 271N6-methyllysineBy similarity
    Modified residuei34 – 341N6-succinyllysine1 Publication
    Modified residuei36 – 361PhosphothreonineBy similarity
    Modified residuei46 – 461N6-acetyllysine1 Publication
    Modified residuei54 – 541Citrulline1 Publication
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei135 – 1351PhosphothreonineBy similarity
    Modified residuei152 – 1521PhosphothreonineBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei170 – 1701PhosphoserineBy similarity
    Modified residuei186 – 1861PhosphoserineBy 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
    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, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP43276.
    PRIDEiP43276.

    PTM databases

    PhosphoSiteiP43276.

    Expressioni

    Gene expression databases

    ArrayExpressiP43276.
    BgeeiP43276.
    CleanExiMM_HIST1H1B.
    GenevestigatoriP43276.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Msx1P132973EBI-903960,EBI-903969

    Protein-protein interaction databases

    BioGridi208131. 1 interaction.
    IntActiP43276. 3 interactions.
    MINTiMINT-1868570.

    Structurei

    3D structure databases

    ProteinModelPortaliP43276.
    SMRiP43276. Positions 37-109.
    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

    GeneTreeiENSGT00670000097781.
    HOGENOMiHOG000251627.
    HOVERGENiHBG009035.
    InParanoidiP43276.
    KOiK11275.
    OMAiFIRKGMD.
    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.

    P43276-1 [UniParc]FASTAAdd to Basket

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    MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA    50
    SKERGGVSLP ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG 100
    ASGSFKLNKK AASGEAKPKA KKTGAAKAKK PAGATPKKPK KTAGAKKTVK 150
    KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP KKAAKSPAKP KAVKSKASKP 200
    KVTKPKTAKP KAAKAKKAVS KKK 223
    Length:223
    Mass (Da):22,576
    Last modified:January 23, 2007 - v2
    Checksum:iB9C26AC31C2716B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611A → T in BAB32001. (PubMed:12408966)Curated
    Sequence conflicti120 – 1201A → V in BAB32001. (PubMed:12408966)Curated
    Sequence conflicti137 – 1371K → N in BAB32001. (PubMed:12408966)Curated
    Sequence conflicti195 – 1951S → F in BAB32001. (PubMed:12408966)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46227 Genomic DNA. Translation: CAA86299.1.
    U62922 Genomic DNA. Translation: AAB05798.1.
    AY158904 Genomic DNA. Translation: AAO06215.1.
    AK020117 mRNA. Translation: BAB32001.1.
    CCDSiCCDS26295.1.
    PIRiA35245.
    S49492.
    RefSeqiNP_064418.1. NM_020034.2.
    UniGeneiMm.221314.

    Genome annotation databases

    EnsembliENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
    GeneIDi56702.
    KEGGimmu:56702.
    UCSCiuc007pri.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46227 Genomic DNA. Translation: CAA86299.1 .
    U62922 Genomic DNA. Translation: AAB05798.1 .
    AY158904 Genomic DNA. Translation: AAO06215.1 .
    AK020117 mRNA. Translation: BAB32001.1 .
    CCDSi CCDS26295.1.
    PIRi A35245.
    S49492.
    RefSeqi NP_064418.1. NM_020034.2.
    UniGenei Mm.221314.

    3D structure databases

    ProteinModelPortali P43276.
    SMRi P43276. Positions 37-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208131. 1 interaction.
    IntActi P43276. 3 interactions.
    MINTi MINT-1868570.

    PTM databases

    PhosphoSitei P43276.

    Proteomic databases

    MaxQBi P43276.
    PRIDEi P43276.

    Protocols and materials databases

    DNASUi 56702.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080511 ; ENSMUSP00000079356 ; ENSMUSG00000058773 .
    GeneIDi 56702.
    KEGGi mmu:56702.
    UCSCi uc007pri.1. mouse.

    Organism-specific databases

    CTDi 3009.
    MGIi MGI:1861461. Hist1h1b.

    Phylogenomic databases

    GeneTreei ENSGT00670000097781.
    HOGENOMi HOG000251627.
    HOVERGENi HBG009035.
    InParanoidi P43276.
    KOi K11275.
    OMAi FIRKGMD.
    OrthoDBi EOG74TX2T.
    TreeFami TF313664.

    Miscellaneous databases

    NextBioi 313147.
    PROi P43276.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43276.
    Bgeei P43276.
    CleanExi MM_HIST1H1B.
    Genevestigatori P43276.

    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. "Isolation of two murine H1 histone genes and chromosomal mapping of the H1 gene complement."
      Drabent B., Franke K., Bode C., Kosciessa U., Bouterfa H., Hameister H., Doenecke D.
      Mamm. Genome 6:505-511(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Blood.
    2. "Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb."
      Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.
      Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-220.
      Strain: C57BL/6J.
      Tissue: Embryonic kidney.
    5. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. Cited for: CITRULLINATION AT ARG-54.
    7. "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-46 AND LYS-75, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiH15_MOUSE
    AccessioniPrimary (citable) accession number: P43276
    Secondary accession number(s): Q9CRM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 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