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Histone H3.3

 H33_BOVIN               Reviewed;         136 AA.
Q5E9F8; A4IFS1; Q862G6; Q862V0; Q862W6;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 114.
RecName: Full=Histone H3.3;
Name=H3F3A;
and
Name=H3F3B;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal cerebellum, and Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
"Identification of a novel phosphorylation site on histone H3 coupled
with mitotic chromosome condensation.";
J. Biol. Chem. 274:25543-25549(1999).
-!- FUNCTION: Variant histone H3 which replaces conventional H3 in a
wide range of nucleosomes in active genes. Constitutes the
predominant form of histone H3 in non-dividing cells and is
incorporated into chromatin independently of DNA synthesis.
Deposited at sites of nucleosomal displacement throughout
transcribed genes, suggesting that it represents an epigenetic
imprint of transcriptionally active chromatin. 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. {ECO:0000250|UniProtKB:P84243}.
-!- SUBUNIT: 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. Interacts with HIRA, a chaperone
required for its incorporation into nucleosomes. Interacts with
ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).
{ECO:0000250|UniProtKB:P84243}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle
independently of DNA synthesis.
-!- DOMAIN: Specific interaction of trimethylated form at 'Lys-36'
(H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-
32 residue with a composite pocket formed by the tandem bromo-PWWP
domains. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
PADI4 impairs methylation and represses transcription.
{ECO:0000250|UniProtKB:P84243}.
-!- PTM: 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.
{ECO:0000250|UniProtKB:P84243}.
-!- PTM: Specifically enriched in modifications associated with active
chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-
80. 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), which are linked to gene repression, are
underrepresented. 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.
{ECO:0000250|UniProtKB:P84243}.
-!- PTM: 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 MAP3K20 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 Tyr-42 (H3Y41ph) by JAK2 promotes
exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on
Ser-32 (H3S31ph) is specific to regions bordering centromeres in
metaphase chromosomes. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells,
monoubiquitination is required for V(D)J recombination (By
similarity). {ECO:0000250|UniProtKB:P84245}.
-!- PTM: 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.
{ECO:0000250|UniProtKB:P84243}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P84243}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC56518.1; Type=Frameshift; Positions=90, 133; Evidence={ECO:0000305};
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EMBL; AB099028; BAC56518.1; ALT_FRAME; mRNA.
EMBL; BT020962; AAX08979.1; -; mRNA.
EMBL; BT025472; ABF57428.1; -; mRNA.
EMBL; BC103071; AAI03072.1; -; mRNA.
EMBL; BC134734; AAI34735.1; -; mRNA.
RefSeq; NP_001014411.1; NM_001014389.2.
RefSeq; NP_001229500.1; NM_001242571.2.
UniGene; Bt.15474; -.
UniGene; Bt.60099; -.
UniGene; Bt.65132; -.
ProteinModelPortal; Q5E9F8; -.
SMR; Q5E9F8; -.
BioGrid; 160074; 16.
IntAct; Q5E9F8; 3.
STRING; 9913.ENSBTAP00000034581; -.
iPTMnet; Q5E9F8; -.
PaxDb; Q5E9F8; -.
PRIDE; Q5E9F8; -.
Ensembl; ENSBTAT00000034186; ENSBTAP00000034086; ENSBTAG00000024561.
Ensembl; ENSBTAT00000034695; ENSBTAP00000034581; ENSBTAG00000024909.
GeneID; 326601; -.
GeneID; 617051; -.
KEGG; bta:326601; -.
KEGG; bta:617051; -.
CTD; 3020; -.
CTD; 3021; -.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
HOGENOM; HOG000155290; -.
HOVERGEN; HBG001172; -.
InParanoid; Q5E9F8; -.
KO; K11253; -.
OMA; KRIEPEY; -.
OrthoDB; EOG091G0XGD; -.
TreeFam; TF314241; -.
Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-BTA-427359; SIRT1 negatively regulates rRNA Expression.
Reactome; R-BTA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-BTA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-BTA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-BTA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-BTA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
Proteomes; UP000009136; Chromosome 16.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000024561; -.
GO; GO:0001740; C:Barr body; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0000788; C:nuclear nucleosome; IEA:Ensembl.
GO; GO:0000786; C:nucleosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0042393; F:histone binding; IEA:Ensembl.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
GO; GO:1902340; P:negative regulation of chromosome condensation; IEA:Ensembl.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0031508; P:pericentric heterochromatin assembly; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0090230; P:regulation of centromere complex assembly; IEA:Ensembl.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0031509; P:telomeric heterochromatin assembly; IEA:Ensembl.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Chromosome; Citrullination;
Complete proteome; DNA-binding; Methylation; Nucleosome core; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 136 Histone H3.3.
/FTId=PRO_0000253954.
SITE 32 32 Interaction with ZMYND11.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 3 3 Citrulline; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 4 4 Phosphothreonine; by GSG2.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 Allysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 7 7 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 9 9 Citrulline; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
alternate.
{ECO:0000250|UniProtKB:P84244}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 10 10 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 10 10 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 11 11 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 11 11 Phosphoserine; alternate; by AURKB,
AURKC, RPS6KA3, RPS6KA4 and RPS6KA5.
{ECO:0000269|PubMed:10464286}.
MOD_RES 12 12 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 15 15 N6-acetyllysine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 18 18 Citrulline; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 19 19 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 19 19 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 24 24 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 24 24 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 27 27 Citrulline.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 28 28 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 29 29 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 29 29 Phosphoserine; alternate; by AURKB, AURKC
and RPS6KA5.
{ECO:0000269|PubMed:10464286}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 38 38 N6-methyllysine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 57 57 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 65 65 N6-methyllysine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84244}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 80 80 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 123 123 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P84243}.
SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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