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P62803

- H4_BOVIN

UniProt

P62803 - H4_BOVIN

Protein

Histone H4

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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi17 – 215

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. negative regulation of megakaryocyte differentiation Source: Ensembl
    2. nucleosome assembly Source: InterPro

    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_211829. Meiotic synapsis.
    REACT_211838. RNA Polymerase I Promoter Opening.
    REACT_214253. NoRC negatively regulates rRNA expression.
    REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
    REACT_217942. SIRT1 negatively regulates rRNA Expression.
    REACT_217981. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_219482. HATs acetylate histones.
    REACT_220535. Packaging Of Telomere Ends.
    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 H4
    Alternative name(s):
    H4.1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 23, UP000009136: Chromosome 5

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. nucleolus Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. nucleosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 103102Histone H4PRO_0000158289Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternateBy similarity
    Modified residuei4 – 41Citrulline; alternateBy similarity
    Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternateBy similarity
    Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity
    Modified residuei6 – 61N6-acetyllysine; alternateBy similarity
    Modified residuei6 – 61N6-crotonyllysine; alternateBy similarity
    Modified residuei9 – 91N6-acetyllysine; alternateBy similarity
    Modified residuei9 – 91N6-crotonyllysine; alternateBy similarity
    Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
    Modified residuei13 – 131N6-crotonyllysine; alternateBy similarity
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-crotonyllysine; alternateBy similarity
    Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei21 – 211N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei21 – 211N6-methyllysine; alternate1 Publication
    Modified residuei32 – 321N6-acetyllysineBy similarity
    Modified residuei48 – 481Phosphoserine; by PAK2By similarity
    Modified residuei52 – 521PhosphotyrosineBy similarity
    Modified residuei89 – 891PhosphotyrosineBy similarity
    Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
    Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
    Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

    Post-translational modificationi

    Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.By similarity
    Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.By similarity
    Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6 By similarity. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity.By similarity
    Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing By similarity.By similarity
    Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 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 at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) By similarity.By similarity
    Sumoylated, which is associated with transcriptional repression.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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP62803.
    PRIDEiP62803.

    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.

    Protein-protein interaction databases

    BioGridi158101. 4 interactions.
    DIPiDIP-44668N.
    IntActiP62803. 1 interaction.
    STRINGi9913.ENSBTAP00000047761.

    Structurei

    3D structure databases

    ProteinModelPortaliP62803.
    SMRiP62803. Positions 21-102.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H4 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00750000117310.
    ENSGT00750000117311.
    HOGENOMiHOG000234654.
    HOVERGENiHBG051878.
    InParanoidiP62803.
    KOiK11254.
    OMAiYEEVRVV.
    OrthoDBiEOG77T174.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR001951. Histone_H4.
    IPR019809. Histone_H4_CS.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00623. HISTONEH4.
    SMARTiSM00417. H4. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00047. HISTONE_H4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL    50
    IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG 100
    FGG 103
    Length:103
    Mass (Da):11,367
    Last modified:January 23, 2007 - v2
    Checksum:iA9E5DFD3F8B97598
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551T → A in AAI42000. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001288 mRNA. Translation: AAC39176.1.
    BC114196 mRNA. Translation: AAI14197.1.
    BC141999 mRNA. Translation: AAI42000.1.
    BC142359 mRNA. Translation: AAI42360.1.
    PIRiA92050. HSBO4.
    RefSeqiNP_001093194.1. NM_001099724.2.
    NP_001139343.1. NM_001145871.2.
    NP_776305.1. NM_173880.2.
    XP_002684676.1. XM_002684630.2.
    XP_002686104.1. XM_002686058.2.
    XP_002697516.1. XM_002697470.2.
    XP_002697555.1. XM_002697509.2.
    XP_002697556.1. XM_002697510.2.
    XP_003581994.1. XM_003581946.2.
    XP_005196696.1. XM_005196639.1.
    XP_005196707.1. XM_005196650.1.
    XP_005223784.1. XM_005223727.1.
    XP_005223853.1. XM_005223796.1.
    XP_005223857.1. XM_005223800.1.
    XP_597168.2. XM_597168.3.
    XP_605163.2. XM_605163.3.
    XP_605779.2. XM_605779.3.
    XP_874074.1. XM_868981.4.
    UniGeneiBt.104550.
    Bt.113.
    Bt.58502.
    Bt.61355.

    Genome annotation databases

    EnsembliENSBTAT00000029245; ENSBTAP00000029245; ENSBTAG00000030504.
    ENSBTAT00000033367; ENSBTAP00000033280; ENSBTAG00000024178.
    ENSBTAT00000033368; ENSBTAP00000033281; ENSBTAG00000024179.
    ENSBTAT00000033375; ENSBTAP00000033288; ENSBTAG00000024185.
    ENSBTAT00000044974; ENSBTAP00000042409; ENSBTAG00000031719.
    ENSBTAT00000044998; ENSBTAP00000042428; ENSBTAG00000039812.
    ENSBTAT00000045033; ENSBTAP00000042460; ENSBTAG00000031756.
    ENSBTAT00000045043; ENSBTAP00000042466; ENSBTAG00000031762.
    ENSBTAT00000045044; ENSBTAP00000042467; ENSBTAG00000031763.
    ENSBTAT00000052402; ENSBTAP00000047761; ENSBTAG00000040277.
    ENSBTAT00000054510; ENSBTAP00000052235; ENSBTAG00000025391.
    ENSBTAT00000056505; ENSBTAP00000053034; ENSBTAG00000040155.
    ENSBTAT00000063932; ENSBTAP00000054635; ENSBTAG00000032453.
    GeneIDi280691.
    516742.
    517138.
    518961.
    526789.
    527388.
    527645.
    528329.
    529647.
    530773.
    617875.
    KEGGibta:280691.
    bta:516742.
    bta:517138.
    bta:518961.
    bta:526789.
    bta:527388.
    bta:527645.
    bta:528329.
    bta:529647.
    bta:530773.
    bta:617875.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001288 mRNA. Translation: AAC39176.1 .
    BC114196 mRNA. Translation: AAI14197.1 .
    BC141999 mRNA. Translation: AAI42000.1 .
    BC142359 mRNA. Translation: AAI42360.1 .
    PIRi A92050. HSBO4.
    RefSeqi NP_001093194.1. NM_001099724.2.
    NP_001139343.1. NM_001145871.2.
    NP_776305.1. NM_173880.2.
    XP_002684676.1. XM_002684630.2.
    XP_002686104.1. XM_002686058.2.
    XP_002697516.1. XM_002697470.2.
    XP_002697555.1. XM_002697509.2.
    XP_002697556.1. XM_002697510.2.
    XP_003581994.1. XM_003581946.2.
    XP_005196696.1. XM_005196639.1.
    XP_005196707.1. XM_005196650.1.
    XP_005223784.1. XM_005223727.1.
    XP_005223853.1. XM_005223796.1.
    XP_005223857.1. XM_005223800.1.
    XP_597168.2. XM_597168.3.
    XP_605163.2. XM_605163.3.
    XP_605779.2. XM_605779.3.
    XP_874074.1. XM_868981.4.
    UniGenei Bt.104550.
    Bt.113.
    Bt.58502.
    Bt.61355.

    3D structure databases

    ProteinModelPortali P62803.
    SMRi P62803. Positions 21-102.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 158101. 4 interactions.
    DIPi DIP-44668N.
    IntActi P62803. 1 interaction.
    STRINGi 9913.ENSBTAP00000047761.

    Proteomic databases

    PaxDbi P62803.
    PRIDEi P62803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000029245 ; ENSBTAP00000029245 ; ENSBTAG00000030504 .
    ENSBTAT00000033367 ; ENSBTAP00000033280 ; ENSBTAG00000024178 .
    ENSBTAT00000033368 ; ENSBTAP00000033281 ; ENSBTAG00000024179 .
    ENSBTAT00000033375 ; ENSBTAP00000033288 ; ENSBTAG00000024185 .
    ENSBTAT00000044974 ; ENSBTAP00000042409 ; ENSBTAG00000031719 .
    ENSBTAT00000044998 ; ENSBTAP00000042428 ; ENSBTAG00000039812 .
    ENSBTAT00000045033 ; ENSBTAP00000042460 ; ENSBTAG00000031756 .
    ENSBTAT00000045043 ; ENSBTAP00000042466 ; ENSBTAG00000031762 .
    ENSBTAT00000045044 ; ENSBTAP00000042467 ; ENSBTAG00000031763 .
    ENSBTAT00000052402 ; ENSBTAP00000047761 ; ENSBTAG00000040277 .
    ENSBTAT00000054510 ; ENSBTAP00000052235 ; ENSBTAG00000025391 .
    ENSBTAT00000056505 ; ENSBTAP00000053034 ; ENSBTAG00000040155 .
    ENSBTAT00000063932 ; ENSBTAP00000054635 ; ENSBTAG00000032453 .
    GeneIDi 280691.
    516742.
    517138.
    518961.
    526789.
    527388.
    527645.
    528329.
    529647.
    530773.
    617875.
    KEGGi bta:280691.
    bta:516742.
    bta:517138.
    bta:518961.
    bta:526789.
    bta:527388.
    bta:527645.
    bta:528329.
    bta:529647.
    bta:530773.
    bta:617875.

    Organism-specific databases

    CTDi 373325.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00750000117310.
    ENSGT00750000117311.
    HOGENOMi HOG000234654.
    HOVERGENi HBG051878.
    InParanoidi P62803.
    KOi K11254.
    OMAi YEEVRVV.
    OrthoDBi EOG77T174.

    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_211829. Meiotic synapsis.
    REACT_211838. RNA Polymerase I Promoter Opening.
    REACT_214253. NoRC negatively regulates rRNA expression.
    REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
    REACT_217942. SIRT1 negatively regulates rRNA Expression.
    REACT_217981. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_219482. HATs acetylate histones.
    REACT_220535. Packaging Of Telomere Ends.
    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 20804878.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR001951. Histone_H4.
    IPR019809. Histone_H4_CS.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00623. HISTONEH4.
    SMARTi SM00417. H4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00047. HISTONE_H4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Poly A-containing histone H4 mRNA variant (H4-v.1): isolation and sequence determination from bovine adrenal medulla."
      Gendron N., Dumont M., Gagne M.-F., Lemaire S.
      Biochim. Biophys. Acta 1396:32-38(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H4-V.1).
      Tissue: Adrenal medulla.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus and Hereford.
      Tissue: Hypothalamus, Ileum and Thymus.
    3. "Structure of the glycine-rich, arginine-rich histone of the Novikoff hepatoma."
      Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.
      Cancer Res. 30:2942-2951(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, METHYLATION AT LYS-21.
    4. "Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence."
      Ogawa Y., Quagliarotti G., Jordan J.J., Taylor C.W., Starbuck W.C., Busch H.
      J. Biol. Chem. 244:4387-4392(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-50.
      Tissue: Thymus.
    5. "Structural analysis of the glycine-rich, arginine-rich histone. II. Sequence of the half of the molecule containing the aromatic amino acids."
      Quagliarotti G., Ogawa Y., Taylor C.W., Sautiere P., Jordan J., Starbuck W.C., Busch H.
      J. Biol. Chem. 244:1796-1802(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-103.
      Tissue: Thymus.

    Entry informationi

    Entry nameiH4_BOVIN
    AccessioniPrimary (citable) accession number: P62803
    Secondary accession number(s): A5PJ80
    , A5PK53, A8QFF4, P02304, P02305
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 102 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3