node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
H3-2 | H3-3A | ENSP00000499501 | ENSP00000355780 | H3.2 histone. | H3.3 histone A. | 0.871 |
H3-2 | H3-3B | ENSP00000499501 | ENSP00000254810 | H3.2 histone. | Histone H3.3; 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 [...] | 0.882 |
H3-2 | H3-4 | ENSP00000499501 | ENSP00000355657 | H3.2 histone. | Histone H3.1t; 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. | 0.865 |
H3-2 | H3-5 | ENSP00000499501 | ENSP00000339835 | H3.2 histone. | Histone H3.3C; 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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes. | 0.871 |
H3-2 | H3C1 | ENSP00000499501 | ENSP00000480826 | H3.2 histone. | H3 clustered histone 1. | 0.946 |
H3-2 | H3C10 | ENSP00000499501 | ENSP00000358160 | H3.2 histone. | H3 clustered histone 10. | 0.932 |
H3-2 | H3C12 | ENSP00000499501 | ENSP00000352252 | H3.2 histone. | Histone H3.1; 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. | 0.944 |
H3-2 | H3C13 | ENSP00000499501 | ENSP00000333277 | H3.2 histone. | Histone H3.2; 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. | 0.903 |
H3-2 | MORC3 | ENSP00000499501 | ENSP00000383333 | H3.2 histone. | MORC family CW-type zinc finger protein 3; Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism. Sumoylated MORC3-NBs can also associate with PML-NBs. Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity. Binds RNA in vitro. May be required for influenza A transcription during viral infection. | 0.918 |
H3-2 | TRIM33 | ENSP00000499501 | ENSP00000351250 | H3.2 histone. | E3 ubiquitin-protein ligase TRIM33; Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor o [...] | 0.972 |
H3-3A | H3-2 | ENSP00000355780 | ENSP00000499501 | H3.3 histone A. | H3.2 histone. | 0.871 |
H3-3A | H3-3B | ENSP00000355780 | ENSP00000254810 | H3.3 histone A. | Histone H3.3; 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 [...] | 0.937 |
H3-3A | H3-4 | ENSP00000355780 | ENSP00000355657 | H3.3 histone A. | Histone H3.1t; 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. | 0.855 |
H3-3A | H3-5 | ENSP00000355780 | ENSP00000339835 | H3.3 histone A. | Histone H3.3C; 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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes. | 0.801 |
H3-3A | H3C1 | ENSP00000355780 | ENSP00000480826 | H3.3 histone A. | H3 clustered histone 1. | 0.868 |
H3-3A | H3C10 | ENSP00000355780 | ENSP00000358160 | H3.3 histone A. | H3 clustered histone 10. | 0.856 |
H3-3A | H3C12 | ENSP00000355780 | ENSP00000352252 | H3.3 histone A. | Histone H3.1; 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. | 0.860 |
H3-3A | H3C13 | ENSP00000355780 | ENSP00000333277 | H3.3 histone A. | Histone H3.2; 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. | 0.871 |
H3-3A | MORC3 | ENSP00000355780 | ENSP00000383333 | H3.3 histone A. | MORC family CW-type zinc finger protein 3; Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism. Sumoylated MORC3-NBs can also associate with PML-NBs. Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity. Binds RNA in vitro. May be required for influenza A transcription during viral infection. | 0.908 |
H3-3A | TRIM33 | ENSP00000355780 | ENSP00000351250 | H3.3 histone A. | E3 ubiquitin-protein ligase TRIM33; Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor o [...] | 0.912 |