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P68432

- H31_BOVIN

UniProt

P68432 - H31_BOVIN

Protein

Histone H3.1

Gene
N/A
Organism
Bos taurus (Bovine)
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_203215. Senescence-Associated Secretory Phenotype (SASP).
    REACT_206540. Amyloids.
    REACT_207393. PRC2 methylates histones and DNA.
    REACT_207666. Condensation of Prophase Chromosomes.
    REACT_209769. Meiotic recombination.
    REACT_211838. RNA Polymerase I Promoter Opening.
    REACT_214253. NoRC negatively regulates rRNA expression.
    REACT_215067. Factors involved in megakaryocyte development and platelet production.
    REACT_217942. SIRT1 negatively regulates rRNA Expression.
    REACT_219482. HATs acetylate histones.
    REACT_222355. formation of the beta-catenin:TCF transactivating complex.
    REACT_225163. RNA Polymerase I Chain Elongation.
    REACT_225657. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3.1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 23

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 136135Histone H3.1PRO_0000221256Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
    Modified residuei3 – 31Citrulline; alternateBy similarity
    Modified residuei4 – 41PhosphothreonineBy similarity
    Modified residuei5 – 51Allysine; alternateBy similarity
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei5 – 51N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei5 – 51N6-acetyllysine; alternateBy similarity
    Modified residuei5 – 51N6-crotonyllysine; alternateBy similarity
    Modified residuei5 – 51N6-methyllysine; alternateBy similarity
    Modified residuei7 – 71Phosphothreonine; by PKCBy similarity
    Modified residuei9 – 91Citrulline; alternateBy similarity
    Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternateBy similarity
    Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei10 – 101N6-acetyllysine; alternateBy similarity
    Modified residuei10 – 101N6-crotonyllysine; alternateBy similarity
    Modified residuei10 – 101N6-methyllysine; alternate1 Publication
    Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA51 Publication
    Modified residuei12 – 121Phosphothreonine; by PKC and CHEK1By similarity
    Modified residuei15 – 151N6-acetyllysine1 Publication
    Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternateBy similarity
    Modified residuei18 – 181Citrulline; alternateBy similarity
    Modified residuei19 – 191N6-acetyllysine; alternateBy similarity
    Modified residuei19 – 191N6-crotonyllysine; alternateBy similarity
    Modified residuei19 – 191N6-methyllysine; alternateBy similarity
    Modified residuei24 – 241N6-acetyllysine; alternate1 Publication
    Modified residuei24 – 241N6-crotonyllysine; alternateBy similarity
    Modified residuei24 – 241N6-methyllysine; alternateBy similarity
    Modified residuei27 – 271CitrullineBy similarity
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
    Modified residuei28 – 281N6-crotonyllysine; alternateBy similarity
    Modified residuei28 – 281N6-methyllysine; alternate1 Publication
    Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA51 Publication
    Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei37 – 371N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei37 – 371N6-acetyllysine; alternateBy similarity
    Modified residuei37 – 371N6-methyllysine; alternateBy similarity
    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; alternateBy similarity
    Modified residuei57 – 571N6-methyllysine; by EHMT2; alternateBy similarity
    Modified residuei58 – 581PhosphoserineBy similarity
    Modified residuei65 – 651N6-methyllysineBy similarity
    Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei80 – 801N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
    Modified residuei80 – 801N6-methyllysine; alternateBy similarity
    Modified residuei81 – 811PhosphothreonineBy similarity
    Modified residuei108 – 1081PhosphothreonineBy similarity
    Modified residuei116 – 1161N6-acetyllysineBy similarity
    Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
    Modified residuei123 – 1231N6-methyllysine; alternateBy similarity

    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 By similarity.By similarity
    Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    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. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity.By similarity
    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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP68432.
    PRIDEiP68432.

    Expressioni

    Developmental stagei

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

    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
    SUV39H1O434632EBI-79764,EBI-349968From a different organism.

    Protein-protein interaction databases

    BioGridi619877. 1 interaction.
    IntActiP68432. 9 interactions.
    STRINGi9913.ENSBTAP00000050291.

    Structurei

    3D structure databases

    ProteinModelPortaliP68432.
    SMRiP68432. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00740000114849.
    HOGENOMiHOG000155290.
    HOVERGENiHBG001172.
    InParanoidiP68432.
    KOiK11253.
    OMAiQKEMART.
    OrthoDBiEOG7HB5C2.
    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.

    P68432-1 [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

    PIRiA02624. HSBO3.
    RefSeqiXP_002697506.1. XM_002697460.2.
    XP_002697557.1. XM_002697511.2.
    XP_002697575.1. XM_002697529.2.
    XP_005196701.1. XM_005196644.1.
    XP_005196705.1. XM_005196648.1.
    XP_005196706.1. XM_005196649.1.
    XP_005223855.1. XM_005223798.1.
    XP_005223856.1. XM_005223799.1.
    XP_595303.1. XM_595303.2.
    XP_874006.1. XM_868913.2.

    Genome annotation databases

    EnsembliENSBTAT00000033364; ENSBTAP00000051709; ENSBTAG00000024175.
    ENSBTAT00000033374; ENSBTAP00000047915; ENSBTAG00000024184.
    ENSBTAT00000033376; ENSBTAP00000053020; ENSBTAG00000024186.
    ENSBTAT00000044972; ENSBTAP00000048362; ENSBTAG00000031717.
    ENSBTAT00000044975; ENSBTAP00000052244; ENSBTAG00000031721.
    ENSBTAT00000045036; ENSBTAP00000051924; ENSBTAG00000031759.
    ENSBTAT00000045041; ENSBTAP00000048719; ENSBTAG00000031761.
    ENSBTAT00000045045; ENSBTAP00000049208; ENSBTAG00000031766.
    ENSBTAT00000045050; ENSBTAP00000051492; ENSBTAG00000031773.
    ENSBTAT00000047042; ENSBTAP00000044281; ENSBTAG00000033117.
    GeneIDi101908845.
    517139.
    523214.
    525511.
    616800.
    788250.
    KEGGibta:101908845.
    bta:517139.
    bta:523214.
    bta:525511.
    bta:616800.
    bta:788250.

    Cross-referencesi

    Sequence databases

    PIRi A02624. HSBO3.
    RefSeqi XP_002697506.1. XM_002697460.2.
    XP_002697557.1. XM_002697511.2.
    XP_002697575.1. XM_002697529.2.
    XP_005196701.1. XM_005196644.1.
    XP_005196705.1. XM_005196648.1.
    XP_005196706.1. XM_005196649.1.
    XP_005223855.1. XM_005223798.1.
    XP_005223856.1. XM_005223799.1.
    XP_595303.1. XM_595303.2.
    XP_874006.1. XM_868913.2.

    3D structure databases

    ProteinModelPortali P68432.
    SMRi P68432. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 619877. 1 interaction.
    IntActi P68432. 9 interactions.
    STRINGi 9913.ENSBTAP00000050291.

    Proteomic databases

    PaxDbi P68432.
    PRIDEi P68432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000033364 ; ENSBTAP00000051709 ; ENSBTAG00000024175 .
    ENSBTAT00000033374 ; ENSBTAP00000047915 ; ENSBTAG00000024184 .
    ENSBTAT00000033376 ; ENSBTAP00000053020 ; ENSBTAG00000024186 .
    ENSBTAT00000044972 ; ENSBTAP00000048362 ; ENSBTAG00000031717 .
    ENSBTAT00000044975 ; ENSBTAP00000052244 ; ENSBTAG00000031721 .
    ENSBTAT00000045036 ; ENSBTAP00000051924 ; ENSBTAG00000031759 .
    ENSBTAT00000045041 ; ENSBTAP00000048719 ; ENSBTAG00000031761 .
    ENSBTAT00000045045 ; ENSBTAP00000049208 ; ENSBTAG00000031766 .
    ENSBTAT00000045050 ; ENSBTAP00000051492 ; ENSBTAG00000031773 .
    ENSBTAT00000047042 ; ENSBTAP00000044281 ; ENSBTAG00000033117 .
    GeneIDi 101908845.
    517139.
    523214.
    525511.
    616800.
    788250.
    KEGGi bta:101908845.
    bta:517139.
    bta:523214.
    bta:525511.
    bta:616800.
    bta:788250.

    Organism-specific databases

    CTDi 8351.
    8352.
    8353.
    8354.
    8355.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00740000114849.
    HOGENOMi HOG000155290.
    HOVERGENi HBG001172.
    InParanoidi P68432.
    KOi K11253.
    OMAi QKEMART.
    OrthoDBi EOG7HB5C2.
    TreeFami TF314241.

    Enzyme and pathway databases

    Reactomei REACT_203215. Senescence-Associated Secretory Phenotype (SASP).
    REACT_206540. Amyloids.
    REACT_207393. PRC2 methylates histones and DNA.
    REACT_207666. Condensation of Prophase Chromosomes.
    REACT_209769. Meiotic recombination.
    REACT_211838. RNA Polymerase I Promoter Opening.
    REACT_214253. NoRC negatively regulates rRNA expression.
    REACT_215067. Factors involved in megakaryocyte development and platelet production.
    REACT_217942. SIRT1 negatively regulates rRNA Expression.
    REACT_219482. HATs acetylate histones.
    REACT_222355. formation of the beta-catenin:TCF transactivating complex.
    REACT_225163. RNA Polymerase I Chain Elongation.
    REACT_225657. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    NextBioi 20872386.

    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. "Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3."
      Delange R.J., Hooper J.A., Smith E.L.
      J. Biol. Chem. 248:3261-3274(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-136, ACETYLATION AT LYS-15 AND LYS-24, METHYLATION AT LYS-10 AND LYS-28.
      Tissue: Thymus.
    2. "Histone III. VI. Two forms of calf thymus histone III."
      Patthy L., Smith E.L.
      J. Biol. Chem. 250:1919-1920(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-136.
      Tissue: Thymus.
    3. "Histone 3. I. Isolation and sequences of the tryptic peptides from the maleylated calf thymus protein."
      Delange R.J., Smith E.L.
      J. Biol. Chem. 248:3248-3254(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Thymus.
    4. "Histone 3. II. Isolation and sequences of chymotryptic peptides from calf thymus histone 3."
      Hooper J.A., Smith E.L.
      J. Biol. Chem. 248:3255-3260(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Thymus.
    5. "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.

    Entry informationi

    Entry nameiH31_BOVIN
    AccessioniPrimary (citable) accession number: P68432
    Secondary accession number(s): P02295, P02296, P16106
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 92 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.

    Caution

    Disulfide bonds have been reported but this may not be physiologically relevant.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3