P68432 (H31_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
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Clusters with 
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone H3.1 |
| Organism | Bos taurus (Bovine) [Reference proteome] |
| Taxonomic identifier | 9913 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 136 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. |
| 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. |
| Subcellular location | |
| Developmental stage | Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation. |
| 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) 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. 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. Ref.1 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. Ref.5 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. 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 By similarity. |
| Miscellaneous | This histone is only present in mammals. |
| Sequence similarities | Belongs to the histone H3 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosome Nucleosome core Nucleus |
| Ligand | DNA-binding |
| PTM | Acetylation Citrullination Disulfide bond Methylation Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | nucleosome assembly Inferred from electronic annotation. Source: InterPro regulation of gene silencingInferred from electronic annotation. Source: Compara |
| Cellular_component | nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| SUV39H1 | O43463 | 2 | EBI-79764,EBI-349968 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 Ref.2 | ||||||||
| Chain | 2 – 136 | 135 | Histone H3.1 | PRO_0000221256 | |||||||
Amino acid modifications | |||||||||||
| Modified residue | 3 | 1 | Asymmetric dimethylarginine; by PRMT6 By similarity | ||||||||
| Modified residue | 4 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 5 | 1 | Allysine; alternate By similarity | ||||||||
| Modified residue | 5 | 1 | N6,N6,N6-trimethyllysine; alternate By similarity | ||||||||
| Modified residue | 5 | 1 | N6,N6-dimethyllysine; alternate By similarity | ||||||||
| Modified residue | 5 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 5 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 5 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Modified residue | 7 | 1 | Phosphothreonine; by PKC By similarity | ||||||||
| Modified residue | 9 | 1 | Citrulline; alternate By similarity | ||||||||
| Modified residue | 9 | 1 | Symmetric dimethylarginine; by PRMT5; alternate By similarity | ||||||||
| Modified residue | 10 | 1 | N6,N6,N6-trimethyllysine; alternate Ref.1 | ||||||||
| Modified residue | 10 | 1 | N6,N6-dimethyllysine; alternate Ref.1 | ||||||||
| Modified residue | 10 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 10 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 10 | 1 | N6-methyllysine; alternate Ref.1 | ||||||||
| Modified residue | 11 | 1 | Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.5 | ||||||||
| Modified residue | 12 | 1 | Phosphothreonine; by PKC and CHEK1 By similarity | ||||||||
| Modified residue | 15 | 1 | N6-acetyllysine Ref.1 | ||||||||
| Modified residue | 18 | 1 | Asymmetric dimethylarginine; by CARM1; alternate By similarity | ||||||||
| Modified residue | 18 | 1 | Citrulline; alternate By similarity | ||||||||
| Modified residue | 19 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 19 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 19 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Modified residue | 24 | 1 | N6-acetyllysine; alternate Ref.1 | ||||||||
| Modified residue | 24 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 24 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Modified residue | 28 | 1 | N6,N6,N6-trimethyllysine; alternate Ref.1 | ||||||||
| Modified residue | 28 | 1 | N6,N6-dimethyllysine; alternate Ref.1 | ||||||||
| Modified residue | 28 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 28 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 28 | 1 | N6-methylated lysine; alternate By similarity | ||||||||
| Modified residue | 28 | 1 | N6-methyllysine; alternate Ref.1 | ||||||||
| Modified residue | 29 | 1 | Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.5 | ||||||||
| Modified residue | 37 | 1 | N6,N6,N6-trimethyllysine; alternate By similarity | ||||||||
| Modified residue | 37 | 1 | N6,N6-dimethyllysine; alternate By similarity | ||||||||
| Modified residue | 37 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 37 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Modified residue | 38 | 1 | N6-methyllysine By similarity | ||||||||
| Modified residue | 42 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 57 | 1 | N6,N6,N6-trimethyllysine; alternate By similarity | ||||||||
| Modified residue | 57 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 57 | 1 | N6-crotonyl-L-lysine; alternate By similarity | ||||||||
| Modified residue | 57 | 1 | N6-methyllysine; by EHMT2; alternate By similarity | ||||||||
| Modified residue | 58 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 65 | 1 | N6-methyllysine By similarity | ||||||||
| Modified residue | 80 | 1 | N6,N6,N6-trimethyllysine; alternate By similarity | ||||||||
| Modified residue | 80 | 1 | N6,N6-dimethyllysine; alternate By similarity | ||||||||
| Modified residue | 80 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 80 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Modified residue | 81 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 108 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 123 | 1 | N6-acetyllysine; alternate By similarity | ||||||||
| Modified residue | 123 | 1 | N6-methyllysine; alternate By similarity | ||||||||
| Disulfide bond | 97 ↔ 111 | In monomeric form; alternate Ref.1 | |||||||||
| Disulfide bond | 97 | Interchain; in polymeric form; alternate Ref.1 | |||||||||
| Disulfide bond | 111 | Interchain; in polymeric form; alternate Ref.1 | |||||||||
Sequences
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References
| [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, DISULFIDE BONDS, 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. |
Cross-references
Entry information
| Entry name | H31_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P68432 Secondary accession number(s): P02295, P02296, P16106 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |