Product: Histone H3 Antibody
Catalog: BF9211
Description: Mouse monoclonal antibody to Histone H3
Application: WB IHC IF/ICC IP ELISA
Reactivity: Human, Mouse, Rat
Mol.Wt.: 15KD; 15kD(Calculated).
Uniprot: P68431 | Q71DI3 | P84243
RRID: AB_2839427

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 1ml $1200 In stock

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Product Info

Source:
Mouse
Application:
WB 1:1000-1:5000, IF/ICC 1:200, IP 1:200, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Monoclonal [AFfirm07(AFB7534)]
Specificity:
The Histone H3 mouse monoclonal antibody can detect endogenous Histone H3 proteins.
RRID:
AB_2839427
Cite Format: Affinity Biosciences Cat# BF9211, RRID:AB_2839427.
Conjugate:
Unconjugated.
Purification:
affinity purification.
Storage:
1mg/ml in PBS, pH 7.4. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

H3 histone antibody, HIST1H3A antibody, Histone cluster 1, H3a antibody

Immunogens

Immunogen:

Mouse monoclonal antibody is prepared by immunizing recombinant protein.

Uniprot:
Gene(ID):
Description:
Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Core component of nucleosome.
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

PTMs - P68431/Q71DI3/P84243 As Substrate

Site PTM Type Enzyme
M1 Acetylation
R3 Methylation
T4 Phosphorylation Q99986 (VRK1)
K5 Acetylation
K5 Methylation
T7 Phosphorylation
K10 Acetylation
K10 Methylation
S11 Phosphorylation P31751 (AKT2) , Q99986 (VRK1) , Q96KB5 (PBK) , Q13153 (PAK1) , Q96GD4 (AURKB) , O14965 (AURKA) , Q16539 (MAPK14) , P51812 (RPS6KA3) , P11309 (PIM1) , P21980 (TGM2) , Q9UQB9 (AURKC) , O75582 (RPS6KA5)
T12 Phosphorylation O14757 (CHEK1) , O43293 (DAPK3)
K15 Acetylation
R18 Methylation
K19 Acetylation
K19 Methylation
K24 Acetylation
K24 Methylation
K28 Acetylation
K28 Methylation
S29 Phosphorylation P27361 (MAPK3) , P31751 (AKT2) , Q96GD4 (AURKB) , P45984 (MAPK9) , O75582 (RPS6KA5) , P28482 (MAPK1) , Q16539 (MAPK14) , P45983 (MAPK8)
K37 Acetylation
K37 Methylation
K37 Ubiquitination
K38 Methylation
Y42 Phosphorylation
T46 Phosphorylation Q05655 (PRKCD) , P31751 (AKT2)
K57 Acetylation
K57 Methylation
S58 Phosphorylation
K65 Methylation
K80 Acetylation
K80 Methylation
T81 Phosphorylation
S87 Phosphorylation
C97 S-Nitrosylation
K116 Acetylation
K123 Acetylation
K123 Methylation
Site PTM Type Enzyme
M1 Acetylation
R3 Methylation
T4 Phosphorylation
K5 Acetylation
K5 Methylation
T7 Phosphorylation
R9 Methylation
K10 Acetylation
K10 Methylation
S11 Phosphorylation
T12 Phosphorylation
K15 Acetylation
K15 Sumoylation
K15 Ubiquitination
R18 Methylation
K19 Acetylation
K19 Methylation
K19 Sumoylation
K19 Ubiquitination
K24 Acetylation
K24 Methylation
K24 Sumoylation
K24 Ubiquitination
K28 Acetylation
K28 Methylation
K28 Ubiquitination
S29 Phosphorylation
K37 Acetylation
K37 Methylation
K37 Ubiquitination
K38 Methylation
R41 Methylation
Y42 Phosphorylation
R43 Methylation
T46 Phosphorylation
R50 Methylation
K57 Acetylation
K57 Methylation
K57 Sumoylation
K57 Ubiquitination
S58 Phosphorylation
T59 Phosphorylation
R64 Methylation
K65 Methylation
K80 Acetylation
K80 Methylation
K80 Sumoylation
K80 Ubiquitination
T81 Phosphorylation
R84 Methylation
S97 Phosphorylation
Y100 Phosphorylation
T108 Phosphorylation
K116 Acetylation
K116 Ubiquitination
T119 Phosphorylation
K123 Acetylation
K123 Methylation
K123 Sumoylation
K123 Ubiquitination
R129 Methylation
Site PTM Type Enzyme
M1 Acetylation
R3 Methylation
T4 Phosphorylation
K5 Acetylation
K5 Methylation
T7 Phosphorylation
K10 Acetylation
K10 Methylation
S11 Phosphorylation P51812 (RPS6KA3) , O75582 (RPS6KA5) , O15111 (CHUK) , P06241 (FYN) , P31749 (AKT1) , Q15418 (RPS6KA1) , Q96GD4 (AURKB) , P17612 (PRKACA)
T12 Phosphorylation O14757 (CHEK1)
K15 Acetylation
R18 Methylation
K19 Acetylation
K19 Methylation
K24 Acetylation
K24 Methylation
K28 Acetylation
K28 Methylation
S29 Phosphorylation P17612 (PRKACA) , P28482 (MAPK1) , P27361 (MAPK3) , O75582 (RPS6KA5) , P45983 (MAPK8) , P45984 (MAPK9)
S32 Phosphorylation
K37 Acetylation
K37 Methylation
K37 Ubiquitination
Y42 Phosphorylation O60674 (JAK2)
T46 Phosphorylation
K57 Acetylation
K57 Methylation
S58 Phosphorylation
K65 Methylation
K80 Acetylation
K80 Methylation
T81 Phosphorylation
S87 Phosphorylation
C111 S-Nitrosylation
K116 Acetylation
K123 Acetylation
K123 Methylation

Research Backgrounds

Function:

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.

PTMs:

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.

Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.

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.

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.

Phosphorylated at Thr-4 (H3T3ph) by 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 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.

Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (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.

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.

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.

Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.

Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.

Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).

Subcellular Location:

Nucleus. Chromosome.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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.

Family&Domains:

Belongs to the histone H3 family.

Function:

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.

PTMs:

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.

Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.

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.

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.

Phosphorylated at Thr-4 (H3T3ph) by 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.

Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. 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.

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.

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.

Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.

Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.

Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).

Subcellular Location:

Nucleus. Chromosome.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer.

Family&Domains:

Belongs to the histone H3 family.

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.

PTMs:

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.

Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.

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.

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.

Phosphorylated at Thr-4 (H3T3ph) by 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.

Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (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.

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.

Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.

Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.

Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).

Subcellular Location:

Nucleus. Chromosome.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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).

Family&Domains:

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.

Belongs to the histone H3 family.

Research Fields

· Human Diseases > Substance dependence > Alcoholism.

· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.

· Human Diseases > Immune diseases > Systemic lupus erythematosus.

References

1). Cardiac SIRT1 ameliorates doxorubicin-induced cardiotoxicity by targeting sestrin 2. Redox Biology (PubMed: 35452917) [IF=11.4]

Application: WB    Species: Mouse    Sample: hearts and H9c2 cells

Fig. 2 The activation of SIRT1 by RES improved DOX-induced inflammation in mice hearts and H9c2 cells. (A) Cardiac inflammatory response was detected by IHC staining for tumor necrosis factor-α (TNF-α, brown considered positive staining) followed by a quantitative analysis of the positive stains (n = 6). (B) Relative myocardial interleukin-1β (Il1b) mRNA level was measured by RT-qPCR (n = 5–6). (C, D) H9c2 cells were transfected with NC-shRNA or Sirt1-shRNA for 24 h, and then treated with RES (20 μM) or DOX (1 μM) or both for 24 h. Relative Tnfa and Il1b mRNA levels were measured by RT-qPCR. Three independent experiments were performed. (E) Western blot analysis and densitometric quantification of nuclear nuclear factor κB p65 (NF-κB p65) expression in cardiac tissues of each group (n = 6). Histone H3 as an internal control. (F) Nuclear accumulation of NF-κB p65 (indicated by white arrows) determined by immunofluorescent staining with anti-NF-κB p65 antibody (red) in cardiac tissues. (G) Western blot analysis and densitometric quantification of nuclear NF-κB p65 expression in H9c2 cells of different groups. Three independent experiments were performed. Histone H3 as an internal control. Data were presented as mean ± SD. *P < 0.05, ns indicates no significance. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

2). Resveratrol and FGF1 Synergistically Ameliorates Doxorubicin-Induced Cardiotoxicity via Activation of SIRT1-NRF2 Pathway. Nutrients (PubMed: 36235670) [IF=5.9]

Application: WB    Species: Mouse    Sample:

Figure 4 The activation of NRF2 was elevated after RES and FGF1 co-treating in DOX-treated mice. (A–C) The expression of NRF2, HO-1 and NQO1 was detected by immunofluorescent staining in cardiac tissues, respectively. (D–G) The levels of relative protein expression were examined by Western blot assay with densitometric quantification (Ctrl: n = 4; other groups: n = 6). (H–J) Representative images of DHE (red) and DCFH-DA (green) staining and quantification of fluorescence intensity in H9c2 cells (n = 3). GAPDH or Histone H3 was used as loading controls for all Western blot assays. Data are expressed as means ± SD.

3). Gastrodin induces lysosomal biogenesis and autophagy to prevent the formation of foam cells via AMPK‐FoxO1‐TFEB signalling axis. Journal of Cellular and Molecular Medicine (PubMed: 33973365) [IF=5.3]

Application: WB    Species: Mouse    Sample: RAW264.7 cell

FIGURE 1 Foam cells are characterized by autophagy deficiency and lysosomal dysfunction. A-C, Protein levels of LC3I/II and p62 were determined by Western blotting. Representative Western blotting A, and quantitative analysis B and C, displayed a reduced protein level of LC3II and increased protein level of p62. D, The mRNA expression levels of autophagic genes were determined by RT-PCR. E, Foam cells displayed reduced autolysosomes as shown by the reduced red puncta of mRFP-GFP-LC3. F-H, Measurement of lysosomal biogenesis and function. F, LysoTracker staining for lysosomal biogenesis. G, Protein level of CTSD for lysosomal degradation capability. H, LysoSensor staining for pH. *P < .05; **P < .01. Results are means ± SD of three independent experiments. The value represents fold of vehicle

4). Piperlongumin Improves Survival in the Mouse Model of Sepsis: Effect on Coagulation Factors and Lung Inflammation. INFLAMMATION (PubMed: 35831643) [IF=5.1]

Application: WB    Species: Mouse    Sample: RAW264.7 cells

Fig. 7 PL inhibits the translocation of p-STAT3 into the nucleus after LPS stimulation in RAW264.7 cells. A The western blot results showed p-STAT3 protein levels in the nucleus of RAW264.7 cells and the relative expression levels of p-STAT3 normalized to histone. B The staining of p-STAT3 (green) and nuclei (blue) in RAW264.7 cells was observed by laser confocal microscopy (scale: 5 µm). Values are shown as mean ± SD.

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