P68433 · H31_MOUSE
- ProteinHistone H3.1
- GeneH3c1; H3c8; H3c10; H3c11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids136 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Miscellaneous
This histone is only present in mammals.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | chromatin organization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H3.1
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP68433
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000221249 | 2-136 | Histone H3.1 | |||
Sequence: ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | ||||||
Modified residue | 3 | Asymmetric dimethylarginine; by PRMT6; alternate | ||||
Sequence: R | ||||||
Modified residue | 3 | Citrulline; alternate | ||||
Sequence: R | ||||||
Modified residue | 3 | Phosphoarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 4 | Phosphothreonine; by HASPIN and VRK1 | ||||
Sequence: T | ||||||
Modified residue | 5 | Allysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 5 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 6 | 5-glutamyl dopamine; alternate | ||||
Sequence: Q | ||||||
Modified residue | 6 | 5-glutamyl serotonin; alternate | ||||
Sequence: Q | ||||||
Modified residue | 7 | Phosphothreonine; by PKC | ||||
Sequence: T | ||||||
Modified residue | 9 | Citrulline; alternate | ||||
Sequence: R | ||||||
Modified residue | 9 | Symmetric dimethylarginine; by PRMT5; alternate | ||||
Sequence: R | ||||||
Modified residue | 10 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 10 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 11 | ADP-ribosylserine; alternate | ||||
Sequence: S | ||||||
Modified residue | 11 | Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 | ||||
Sequence: S | ||||||
Modified residue | 12 | Phosphothreonine; by PKC and CHEK1 | ||||
Sequence: T | ||||||
Modified residue | 15 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 18 | Asymmetric dimethylarginine; by CARM1; alternate | ||||
Sequence: R | ||||||
Modified residue | 18 | Citrulline; alternate | ||||
Sequence: R | ||||||
Modified residue | 19 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 19 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Lipidation | 19 | N6-decanoyllysine | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 27 | Citrulline | ||||
Sequence: R | ||||||
Modified residue | 28 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 28 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 29 | ADP-ribosylserine; alternate | ||||
Sequence: S | ||||||
Modified residue | 29 | Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 | ||||
Sequence: S | ||||||
Modified residue | 37 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 37 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 37 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 37 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 37 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 37 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 38 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 38 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 42 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 57 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-methyllysine; by EHMT2; alternate | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 65 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 65 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 81 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 87 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 108 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 116 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 116 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-butyryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-glutaryllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 123 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 129 | Phosphoarginine | ||||
Sequence: R | ||||||
Modified residue | 130 | Phosphoarginine | ||||
Sequence: R | ||||||
Modified residue | 132 | Phosphoarginine | ||||
Sequence: R |
Post-translational modification
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 (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.
Phosphorylated at Thr-4 (H3T3ph) by VRK1 (By similarity).
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 or isoform M2 of PKM (PKM2) 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.
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 or isoform M2 of PKM (PKM2) 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.
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
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination
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).
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.
Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting.
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 by PARP1 or PARP2 constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).
Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic neuron differentiation (PubMed:30867594).
H3Q5ser is associated with trimethylation of Lys-5 (H3K4me3) and enhances general transcription factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating transcription (PubMed:30867594).
H3Q5ser is associated with trimethylation of Lys-5 (H3K4me3) and enhances general transcription factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating transcription (PubMed:30867594).
Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area (VTA) neurons (By similarity).
H3Q5dop mediates neurotransmission-independent role of nuclear dopamine by regulating relapse-related transcriptional plasticity in the reward system (By similarity).
H3Q5dop mediates neurotransmission-independent role of nuclear dopamine by regulating relapse-related transcriptional plasticity in the reward system (By similarity).
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.
Gene expression databases
Interaction
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 TONSL; CHAF1A; CHAF1B; MCM2 and DNAJC9 (By similarity).
Interacts with NASP; NASP is a histone chaperone that stabilizes and maintains a soluble pool of Histone H3-H4 dimers (By similarity).
Interacts with NASP; NASP is a histone chaperone that stabilizes and maintains a soluble pool of Histone H3-H4 dimers (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P68433 | Cbx1 P83917 | 6 | EBI-79743, EBI-78119 | |
XENO | P68433 | SETD7 Q8WTS6 | 2 | EBI-79743, EBI-1268586 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYR |
Sequence similarities
Belongs to the histone H3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length136
- Mass (Da)15,404
- Last updated2007-01-23 v2
- Checksum9B89008EA50A0EF6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X01684 EMBL· GenBank· DDBJ | CAA25839.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32460 EMBL· GenBank· DDBJ | AAA37811.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32462 EMBL· GenBank· DDBJ | AAA37813.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X16496 EMBL· GenBank· DDBJ | CAA34512.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U62670 EMBL· GenBank· DDBJ | AAB04763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U62672 EMBL· GenBank· DDBJ | AAB04765.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY158944 EMBL· GenBank· DDBJ | AAO06254.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY158945 EMBL· GenBank· DDBJ | AAO06255.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY158946 EMBL· GenBank· DDBJ | AAO06256.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY158952 EMBL· GenBank· DDBJ | AAO06262.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y12290 EMBL· GenBank· DDBJ | CAA72968.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK006742 EMBL· GenBank· DDBJ | BAB24722.1 EMBL· GenBank· DDBJ | mRNA | ||
AK018952 EMBL· GenBank· DDBJ | BAB31493.1 EMBL· GenBank· DDBJ | mRNA | ||
AK155722 EMBL· GenBank· DDBJ | BAE33402.1 EMBL· GenBank· DDBJ | mRNA | ||
AL589651 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590388 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC107285 EMBL· GenBank· DDBJ | AAI07286.1 EMBL· GenBank· DDBJ | mRNA | ||
BC107287 EMBL· GenBank· DDBJ | AAI07288.1 EMBL· GenBank· DDBJ | mRNA | ||
BC115816 EMBL· GenBank· DDBJ | AAI15817.1 EMBL· GenBank· DDBJ | mRNA | ||
BC116383 EMBL· GenBank· DDBJ | AAI16384.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125355 EMBL· GenBank· DDBJ | AAI25356.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125357 EMBL· GenBank· DDBJ | AAI25358.1 EMBL· GenBank· DDBJ | mRNA |