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P68433

- H31_MOUSE

UniProt

P68433 - H31_MOUSE

Protein

Histone H3.1

Gene

Hist1h3a

more
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. nucleosome assembly Source: InterPro
    2. regulation of gene silencing Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_196580. Condensation of Prophase Chromosomes.
    REACT_198563. Amyloids.
    REACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_222475. PRC2 methylates histones and DNA.
    REACT_224328. SIRT1 negatively regulates rRNA Expression.
    REACT_226125. Packaging Of Telomere Ends.
    REACT_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3.1
    Gene namesi
    Name:Hist1h3a
    Synonyms:H3a
    AND
    Name:Hist1h3g
    Synonyms:H3.1-221, H3g
    AND
    Name:Hist1h3h
    Synonyms:H3.1-291, H3h
    AND
    Name:Hist1h3i
    Synonyms:H3.1-I, H3i
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:2668828. Hist1h3a.
    MGI:2145541. Hist1h3g.
    MGI:2448349. Hist1h3h.
    MGI:2448350. Hist1h3i.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 136135Histone H3.1PRO_0000221249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
    Modified residuei3 – 31Citrulline; alternateBy similarity
    Modified residuei3 – 31Phosphoarginine; alternateCurated
    Modified residuei4 – 41Phosphothreonine; by GSG21 Publication
    Modified residuei5 – 51Allysine; alternateBy similarity
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
    Modified residuei5 – 51N6-crotonyllysine; alternate1 Publication
    Modified residuei5 – 51N6-methyllysine; alternate2 Publications
    Modified residuei7 – 71Phosphothreonine; by PKCBy similarity
    Modified residuei9 – 91Citrulline; alternate1 Publication
    Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternate1 Publication
    Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei10 – 101N6-acetyllysine; alternate2 Publications
    Modified residuei10 – 101N6-crotonyllysine; alternate1 Publication
    Modified residuei10 – 101N6-methyllysine; alternate2 Publications
    Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications
    Modified residuei12 – 121Phosphothreonine; by PKC and CHEK1By similarity
    Modified residuei15 – 151N6-acetyllysine3 Publications
    Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate4 Publications
    Modified residuei18 – 181Citrulline; alternate1 Publication
    Modified residuei19 – 191N6-acetyllysine; alternate3 Publications
    Modified residuei19 – 191N6-crotonyllysine; alternate1 Publication
    Modified residuei19 – 191N6-methyllysine; alternate1 Publication
    Modified residuei24 – 241N6-acetyllysine; alternate3 Publications
    Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
    Modified residuei24 – 241N6-methyllysine; alternate1 Publication
    Modified residuei27 – 271CitrullineBy similarity
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei28 – 281N6-acetyllysine; alternate1 Publication
    Modified residuei28 – 281N6-crotonyllysine; alternate1 Publication
    Modified residuei28 – 281N6-methyllysine; alternate2 Publications
    Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications
    Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei37 – 371N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei37 – 371N6-acetyllysine; alternate1 Publication
    Modified residuei37 – 371N6-methyllysine; alternate2 Publications
    Modified residuei38 – 381N6-methyllysineBy similarity
    Modified residuei42 – 421PhosphotyrosineBy similarity
    Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei57 – 571N6-acetyllysine; alternateBy similarity
    Modified residuei57 – 571N6-crotonyllysine; alternate1 Publication
    Modified residuei57 – 571N6-methyllysine; by EHMT2; alternateBy similarity
    Modified residuei58 – 581PhosphoserineBy similarity
    Modified residuei65 – 651N6-methyllysineBy similarity
    Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei80 – 801N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
    Modified residuei80 – 801N6-methyllysine; alternate2 Publications
    Modified residuei81 – 811PhosphothreonineBy similarity
    Modified residuei108 – 1081PhosphothreonineBy similarity
    Modified residuei116 – 1161N6-acetyllysineBy similarity
    Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
    Modified residuei123 – 1231N6-methyllysine; alternate1 Publication
    Modified residuei129 – 1291PhosphoarginineCurated
    Modified residuei130 – 1301PhosphoarginineCurated
    Modified residuei132 – 1321PhosphoarginineSequence Analysis

    Post-translational modificationi

    Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.7 Publications
    Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.6 Publications
    Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters By similarity.By similarity
    Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.10 Publications
    Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.12 Publications
    Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins By similarity. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.By similarity1 Publication
    Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression By similarity.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

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP68433.
    PaxDbiP68433.
    PRIDEiP68433.

    PTM databases

    PhosphoSiteiP68433.

    Expressioni

    Developmental stagei

    Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.1 Publication

    Gene expression databases

    BgeeiP68433.
    CleanExiMM_HIST1H3A.
    MM_HIST1H3G.
    MM_HIST1H3H.
    MM_HIST1H3I.
    GenevestigatoriP68433.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A612LO410942EBI-1179609,EBI-1179574From a different organism.
    Carm1Q9WVG64EBI-1179609,EBI-4414343
    Cbx1P839176EBI-79743,EBI-78119
    SETD7Q8WTS62EBI-79743,EBI-1268586From a different organism.
    YwhaeP6225911EBI-1179609,EBI-356480
    YwhazP6310117EBI-1179609,EBI-354751

    Protein-protein interaction databases

    IntActiP68433. 31 interactions.
    MINTiMINT-191105.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi46 – 5510
    Helixi65 – 7713
    Beta strandi80 – 823
    Helixi87 – 11428
    Beta strandi118 – 1203
    Helixi122 – 13211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GUWNMR-B2-17[»]
    1U35X-ray3.00A/E1-136[»]
    2V83X-ray2.40D/E2-10[»]
    2W5ZX-ray2.20C2-9[»]
    2WP1X-ray2.10P/Q15-24[»]
    2XL3X-ray2.70D/F2-9[»]
    4EZHX-ray2.52C/D25-35[»]
    ProteinModelPortaliP68433.
    SMRiP68433. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68433.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00740000114849.
    HOVERGENiHBG001172.
    InParanoidiP68433.
    KOiK11253.
    OMAiRISKMAR.
    OrthoDBiEOG7HB5C2.
    PhylomeDBiP68433.
    TreeFamiTF314241.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view]
    PANTHERiPTHR11426. PTHR11426. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00622. HISTONEH3.
    SMARTiSM00428. H3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P68433-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR    50
    EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY 100
    LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
    Length:136
    Mass (Da):15,404
    Last modified:January 23, 2007 - v2
    Checksum:i9B89008EA50A0EF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01684 Genomic DNA. Translation: CAA25839.1.
    M32460 Genomic DNA. Translation: AAA37811.1.
    M32462 Genomic DNA. Translation: AAA37813.1.
    X16496 Genomic DNA. Translation: CAA34512.1.
    U62670 Genomic DNA. Translation: AAB04763.1.
    U62672 Genomic DNA. Translation: AAB04765.1.
    AY158944 Genomic DNA. Translation: AAO06254.1.
    AY158945 Genomic DNA. Translation: AAO06255.1.
    AY158946 Genomic DNA. Translation: AAO06256.1.
    AY158952 Genomic DNA. Translation: AAO06262.1.
    Y12290 Genomic DNA. Translation: CAA72968.1.
    AK006742 mRNA. Translation: BAB24722.1.
    AK018952 mRNA. Translation: BAB31493.1.
    AK155722 mRNA. Translation: BAE33402.1.
    AL590388 Genomic DNA. Translation: CAI25837.1.
    AL589651 Genomic DNA. Translation: CAI24113.1.
    AL589651 Genomic DNA. Translation: CAI24105.1.
    BC107285 mRNA. Translation: AAI07286.1.
    BC107287 mRNA. Translation: AAI07288.1.
    BC115816 mRNA. Translation: AAI15817.1.
    BC116383 mRNA. Translation: AAI16384.1.
    BC125355 mRNA. Translation: AAI25356.1.
    BC125357 mRNA. Translation: AAI25358.1.
    CCDSiCCDS26289.1.
    CCDS26296.1.
    CCDS26342.1.
    CCDS26368.1.
    PIRiA39525.
    S06755.
    RefSeqiNP_038578.2. NM_013550.5.
    NP_659539.1. NM_145073.2.
    NP_835513.1. NM_178206.2.
    NP_835514.1. NM_178207.2.
    UniGeneiMm.221301.
    Mm.261657.
    Mm.377874.
    Mm.390558.
    Mm.397328.

    Genome annotation databases

    EnsembliENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000062417.
    ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
    ENSMUST00000091754; ENSMUSP00000089348; ENSMUSG00000069312.
    ENSMUST00000099704; ENSMUSP00000097295; ENSMUSG00000075032.
    GeneIDi319152.
    319153.
    360198.
    97908.
    KEGGimmu:319152.
    mmu:319153.
    mmu:360198.
    mmu:97908.
    UCSCiuc007prc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01684 Genomic DNA. Translation: CAA25839.1 .
    M32460 Genomic DNA. Translation: AAA37811.1 .
    M32462 Genomic DNA. Translation: AAA37813.1 .
    X16496 Genomic DNA. Translation: CAA34512.1 .
    U62670 Genomic DNA. Translation: AAB04763.1 .
    U62672 Genomic DNA. Translation: AAB04765.1 .
    AY158944 Genomic DNA. Translation: AAO06254.1 .
    AY158945 Genomic DNA. Translation: AAO06255.1 .
    AY158946 Genomic DNA. Translation: AAO06256.1 .
    AY158952 Genomic DNA. Translation: AAO06262.1 .
    Y12290 Genomic DNA. Translation: CAA72968.1 .
    AK006742 mRNA. Translation: BAB24722.1 .
    AK018952 mRNA. Translation: BAB31493.1 .
    AK155722 mRNA. Translation: BAE33402.1 .
    AL590388 Genomic DNA. Translation: CAI25837.1 .
    AL589651 Genomic DNA. Translation: CAI24113.1 .
    AL589651 Genomic DNA. Translation: CAI24105.1 .
    BC107285 mRNA. Translation: AAI07286.1 .
    BC107287 mRNA. Translation: AAI07288.1 .
    BC115816 mRNA. Translation: AAI15817.1 .
    BC116383 mRNA. Translation: AAI16384.1 .
    BC125355 mRNA. Translation: AAI25356.1 .
    BC125357 mRNA. Translation: AAI25358.1 .
    CCDSi CCDS26289.1.
    CCDS26296.1.
    CCDS26342.1.
    CCDS26368.1.
    PIRi A39525.
    S06755.
    RefSeqi NP_038578.2. NM_013550.5.
    NP_659539.1. NM_145073.2.
    NP_835513.1. NM_178206.2.
    NP_835514.1. NM_178207.2.
    UniGenei Mm.221301.
    Mm.261657.
    Mm.377874.
    Mm.390558.
    Mm.397328.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GUW NMR - B 2-17 [» ]
    1U35 X-ray 3.00 A/E 1-136 [» ]
    2V83 X-ray 2.40 D/E 2-10 [» ]
    2W5Z X-ray 2.20 C 2-9 [» ]
    2WP1 X-ray 2.10 P/Q 15-24 [» ]
    2XL3 X-ray 2.70 D/F 2-9 [» ]
    4EZH X-ray 2.52 C/D 25-35 [» ]
    ProteinModelPortali P68433.
    SMRi P68433. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P68433. 31 interactions.
    MINTi MINT-191105.

    PTM databases

    PhosphoSitei P68433.

    Proteomic databases

    MaxQBi P68433.
    PaxDbi P68433.
    PRIDEi P68433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080859 ; ENSMUSP00000079670 ; ENSMUSG00000062417 .
    ENSMUST00000091701 ; ENSMUSP00000089293 ; ENSMUSG00000069265 .
    ENSMUST00000091754 ; ENSMUSP00000089348 ; ENSMUSG00000069312 .
    ENSMUST00000099704 ; ENSMUSP00000097295 ; ENSMUSG00000075032 .
    GeneIDi 319152.
    319153.
    360198.
    97908.
    KEGGi mmu:319152.
    mmu:319153.
    mmu:360198.
    mmu:97908.
    UCSCi uc007prc.1. mouse.

    Organism-specific databases

    CTDi 8350.
    8354.
    8355.
    8357.
    MGIi MGI:2668828. Hist1h3a.
    MGI:2145541. Hist1h3g.
    MGI:2448349. Hist1h3h.
    MGI:2448350. Hist1h3i.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00740000114849.
    HOVERGENi HBG001172.
    InParanoidi P68433.
    KOi K11253.
    OMAi RISKMAR.
    OrthoDBi EOG7HB5C2.
    PhylomeDBi P68433.
    TreeFami TF314241.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_196580. Condensation of Prophase Chromosomes.
    REACT_198563. Amyloids.
    REACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_222475. PRC2 methylates histones and DNA.
    REACT_224328. SIRT1 negatively regulates rRNA Expression.
    REACT_226125. Packaging Of Telomere Ends.
    REACT_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    EvolutionaryTracei P68433.
    NextBioi 353176.
    SOURCEi Search...

    Gene expression databases

    Bgeei P68433.
    CleanExi MM_HIST1H3A.
    MM_HIST1H3G.
    MM_HIST1H3H.
    MM_HIST1H3I.
    Genevestigatori P68433.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view ]
    PANTHERi PTHR11426. PTHR11426. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00622. HISTONEH3.
    SMARTi SM00428. H3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequences of four mouse histone H3 genes: implications for evolution of mouse histone genes."
      Taylor J.D., Wellman S.E., Marzluff W.F.
      J. Mol. Evol. 23:242-249(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3G AND HIST1H3H).
    3. "Nucleotide sequences of mouse histone genes H2A and H3.1."
      Kosciessa U., Doenecke D.
      Nucleic Acids Res. 17:8861-8861(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CD-1.
      Tissue: Testis.
    4. "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] (HIST1H3I).
      Strain: C57BL/CJ6.
    5. "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] (HIST1H3A; HIST1H3G; HIST1H3H AND HIST1H3I).
    6. Franke K., Drabent B., Doenecke D.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    7. "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].
      Strain: C57BL/6J.
      Tissue: Testis.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    9. "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].
    10. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 58-64, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    11. "Changes in the levels of three different classes of histone mRNA during murine erythroleukemia cell differentiation."
      Brown D.T., Wellman S.E., Sittman D.B.
      Mol. Cell. Biol. 5:2879-2886(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    12. "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation."
      Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.
      J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    13. "Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter."
      Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.
      Curr. Biol. 11:1981-1985(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5 AND ARG-18.
    14. "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
      Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
      J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-29.
    15. "Crosstalk between CARM1 methylation and CBP acetylation on histone H3."
      Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.
      Curr. Biol. 12:2090-2097(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT ARG-18.
    16. "Methylation at arginine 17 of histone H3 is linked to gene activation."
      Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.
      EMBO Rep. 3:39-44(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-18.
    17. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
      Goto H., Yasui Y., Nigg E.A., Inagaki M.
      Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    18. "Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry."
      Cocklin R.R., Wang M.
      J. Protein Chem. 22:327-334(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10; LYS-28; LYS-37; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
    19. Cited for: CITRULLINATION.
    20. "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
      Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
      Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-9, ACETYLATION AT LYS-10.
    21. "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
      Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
      EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-18.
    22. "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment."
      Dai J., Sultan S., Taylor S.S., Higgins J.M.G.
      Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-4 AND SER-11.
    23. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
      Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
      J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-29.
    24. "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
      Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
      J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    25. "Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28."
      Dunn K.L., Davie J.R.
      Oncogene 24:3492-3502(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    26. "Organismal differences in post-translational modifications in histones H3 and H4."
      Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
      J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
    27. "Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
      Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
      J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-37.
    28. "Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression."
      Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., Nakanishi M.
      Cell 132:221-232(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
    29. "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining."
      Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F.
      Mol. Cell 37:282-293(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    30. "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-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.

    Entry informationi

    Entry nameiH31_MOUSE
    AccessioniPrimary (citable) accession number: P68433
    Secondary accession number(s): P02295
    , P02296, P16106, Q05A97, Q3B7Z8, Q3B7Z9, Q5T009
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This histone is only present in mammals.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3