Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DOT1 | SET1 | Q6C4Y5 | Q6CEK8 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.973 |
| DOT1 | SET9 | Q6C4Y5 | Q6C519 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | Histone-lysine N-methyltransferase SET9; Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3. | 0.943 |
| DOT1 | YALI0_A06215g | Q6C4Y5 | W0TYQ1 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | 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. | 0.796 |
| DOT1 | YALI0_C11385g | Q6C4Y5 | Q6C0C5 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | 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. | 0.891 |
| DOT1 | YALI0_D21684g | Q6C4Y5 | W0TYN1 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | YALI0D21684p. | 0.936 |
| DOT1 | YALI0_E13552g | Q6C4Y5 | Q6C606 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | YALI0E13552p. | 0.929 |
| DOT1 | YALI0_E32725g | Q6C4Y5 | Q6C3R4 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | YALI0E32725p. | 0.929 |
| DOT1 | YALI0_F00374g | Q6C4Y5 | Q6C3E6 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | 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. | 0.810 |
| DOT1 | set-2 | Q6C4Y5 | Q6C5G5 | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | Histone-lysine N-methyltransferase, H3 lysine-36 specific; Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.966 |
| SET1 | DOT1 | Q6CEK8 | Q6C4Y5 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | 0.973 |
| SET1 | SET9 | Q6CEK8 | Q6C519 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | Histone-lysine N-methyltransferase SET9; Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3. | 0.954 |
| SET1 | YALI0_A06215g | Q6CEK8 | W0TYQ1 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 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. | 0.766 |
| SET1 | YALI0_C11385g | Q6CEK8 | Q6C0C5 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 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. | 0.921 |
| SET1 | YALI0_D21684g | Q6CEK8 | W0TYN1 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | YALI0D21684p. | 0.932 |
| SET1 | YALI0_E13552g | Q6CEK8 | Q6C606 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | YALI0E13552p. | 0.949 |
| SET1 | YALI0_E32725g | Q6CEK8 | Q6C3R4 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | YALI0E32725p. | 0.949 |
| SET1 | YALI0_F00374g | Q6CEK8 | Q6C3E6 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 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. | 0.838 |
| SET1 | set-2 | Q6CEK8 | Q6C5G5 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | Histone-lysine N-methyltransferase, H3 lysine-36 specific; Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.985 |
| SET9 | DOT1 | Q6C519 | Q6C4Y5 | Histone-lysine N-methyltransferase SET9; Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3. | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. | 0.943 |
| SET9 | SET1 | Q6C519 | Q6CEK8 | Histone-lysine N-methyltransferase SET9; Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3. | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily. | 0.954 |
page 1 of 5