| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BRD4 | H4C6 | ENSP00000263377 | ENSP00000244537 | Bromodomain-containing protein 4; Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal- inducible genes by associating with the P-TEFb complex and re [...] | Histone H4; 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. | 0.999 |
| BRD4 | SMYD2 | ENSP00000263377 | ENSP00000355924 | Bromodomain-containing protein 4; Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal- inducible genes by associating with the P-TEFb complex and re [...] | N-lysine methyltransferase SMYD2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.488 |
| BRD4 | SMYD5 | ENSP00000263377 | ENSP00000374152 | Bromodomain-containing protein 4; Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal- inducible genes by associating with the P-TEFb complex and re [...] | SET and MYND domain-containing protein 5; SMYD family member 5; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.519 |
| DCD | SMYD5 | ENSP00000406773 | ENSP00000374152 | Survival-promoting peptide; DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity, cleaving on the C- terminal side of Arg and, to a lesser extent, Lys residues. | SET and MYND domain-containing protein 5; SMYD family member 5; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.727 |
| DCD | WWOX | ENSP00000406773 | ENSP00000457230 | Survival-promoting peptide; DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity, cleaving on the C- terminal side of Arg and, to a lesser extent, Lys residues. | WW domain-containing oxidoreductase; Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm. | 0.520 |
| H4C6 | BRD4 | ENSP00000244537 | ENSP00000263377 | Histone H4; 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. | Bromodomain-containing protein 4; Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal- inducible genes by associating with the P-TEFb complex and re [...] | 0.999 |
| H4C6 | SMYD3 | ENSP00000244537 | ENSP00000419184 | Histone H4; 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. | Histone-lysine N-methyltransferase SMYD3; Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences ; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. | 0.724 |
| H4C6 | SMYD5 | ENSP00000244537 | ENSP00000374152 | Histone H4; 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. | SET and MYND domain-containing protein 5; SMYD family member 5; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.655 |
| SETD1B | SETD3 | ENSP00000474253 | ENSP00000327436 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | 0.639 |
| SETD1B | SMYD1 | ENSP00000474253 | ENSP00000393453 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | Histone-lysine N-methyltransferase SMYD1; Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.526 |
| SETD1B | SMYD2 | ENSP00000474253 | ENSP00000355924 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | N-lysine methyltransferase SMYD2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.607 |
| SETD1B | SMYD3 | ENSP00000474253 | ENSP00000419184 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | Histone-lysine N-methyltransferase SMYD3; Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences ; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. | 0.755 |
| SETD1B | SMYD4 | ENSP00000474253 | ENSP00000304360 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | SET and MYND domain containing 4; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.504 |
| SETD1B | SMYD5 | ENSP00000474253 | ENSP00000374152 | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | SET and MYND domain-containing protein 5; SMYD family member 5; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.553 |
| SETD3 | SETD1B | ENSP00000327436 | ENSP00000474253 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | Histone-lysine N-methyltransferase SETD1B; Histone methyltransferase that specifically methylates 'Lys- 4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro; Belongs t [...] | 0.639 |
| SETD3 | SMYD1 | ENSP00000327436 | ENSP00000393453 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | Histone-lysine N-methyltransferase SMYD1; Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.440 |
| SETD3 | SMYD2 | ENSP00000327436 | ENSP00000355924 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | N-lysine methyltransferase SMYD2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.680 |
| SETD3 | SMYD3 | ENSP00000327436 | ENSP00000419184 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | Histone-lysine N-methyltransferase SMYD3; Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences ; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. | 0.714 |
| SETD3 | SMYD4 | ENSP00000327436 | ENSP00000304360 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | SET and MYND domain containing 4; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.444 |
| SETD3 | SMYD5 | ENSP00000327436 | ENSP00000374152 | Actin-histidine N-methyltransferase; Protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N- methyltransferase activity and probably only catalyzes histidine methylation of actin. | SET and MYND domain-containing protein 5; SMYD family member 5; Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.556 |