node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BANP | PRPF19 | ENSP00000376902 | ENSP00000227524 | Protein BANP; Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest (By similarity); Belongs to the BANP/SMAR1 family. | Pre-mRNA-processing factor 19; Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and [...] | 0.811 |
BANP | SETMAR | ENSP00000376902 | ENSP00000373354 | Protein BANP; Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest (By similarity); Belongs to the BANP/SMAR1 family. | Histone-lysine N-methyltransferase SETMAR; Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double- strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. In parallel, has a histone methyltransf [...] | 0.896 |
CAMKMT | H3-2 | ENSP00000367755 | ENSP00000499501 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | H3.2 histone. | 0.571 |
CAMKMT | H3-3B | ENSP00000367755 | ENSP00000254810 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 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 [...] | 0.573 |
CAMKMT | H3-4 | ENSP00000367755 | ENSP00000355657 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 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. | 0.571 |
CAMKMT | H3-5 | ENSP00000367755 | ENSP00000339835 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 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. | 0.571 |
CAMKMT | H3C12 | ENSP00000367755 | ENSP00000352252 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 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. | 0.571 |
CAMKMT | H3C13 | ENSP00000367755 | ENSP00000333277 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 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. | 0.571 |
CAMKMT | SETMAR | ENSP00000367755 | ENSP00000373354 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone-lysine N-methyltransferase SETMAR; Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double- strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. In parallel, has a histone methyltransf [...] | 0.747 |
H3-2 | CAMKMT | ENSP00000499501 | ENSP00000367755 | H3.2 histone. | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 0.571 |
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 | 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 | SETMAR | ENSP00000499501 | ENSP00000373354 | H3.2 histone. | Histone-lysine N-methyltransferase SETMAR; Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double- strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. In parallel, has a histone methyltransf [...] | 0.728 |
H3-3B | CAMKMT | ENSP00000254810 | ENSP00000367755 | 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 [...] | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 0.573 |
H3-3B | H3-2 | ENSP00000254810 | ENSP00000499501 | 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 [...] | H3.2 histone. | 0.882 |
H3-3B | H3-4 | ENSP00000254810 | ENSP00000355657 | 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 [...] | 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. | 0.909 |
H3-3B | H3-5 | ENSP00000254810 | ENSP00000339835 | 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 [...] | 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. | 0.810 |