STRINGSTRING
DSM5745_10087 DSM5745_10087 DSM5745_10061 DSM5745_10061 DSM5745_08433 DSM5745_08433 DSM5745_07029 DSM5745_07029 DSM5745_06701 DSM5745_06701 DSM5745_05860 DSM5745_05860 DSM5745_04281 DSM5745_04281 DSM5745_02775 DSM5745_02775 DSM5745_02806 DSM5745_02806 DSM5745_03855 DSM5745_03855 DSM5745_03854 DSM5745_03854 DSM5745_01738 DSM5745_01738 DSM5745_01739 DSM5745_01739 DSM5745_00148 DSM5745_00148 DSM5745_00169 DSM5745_00169
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
DSM5745_10087Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. 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 histones. (504 aa)
DSM5745_10061Uncharacterized protein; 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. (113 aa)
DSM5745_08433DUF2236 domain-containing protein. (400 aa)
DSM5745_07029Uncharacterized protein. (161 aa)
DSM5745_06701Uncharacterized protein. (285 aa)
DSM5745_05860Histone 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. (103 aa)
DSM5745_04281Histone domain-containing protein. (194 aa)
DSM5745_02775Histone H1. (197 aa)
DSM5745_02806CENP-T_C domain-containing protein. (481 aa)
DSM5745_03855Histone H2B; Belongs to the histone H2B family. (140 aa)
DSM5745_03854Histone H2A; Belongs to the histone H2A family. (132 aa)
DSM5745_01738Histone H3; Belongs to the histone H3 family. (136 aa)
DSM5745_01739Histone 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. (103 aa)
DSM5745_00148DUF2236 domain-containing protein. (433 aa)
DSM5745_00169Histone H2A; Belongs to the histone H2A family. (136 aa)
Your Current Organism:
Aspergillus mulundensis
NCBI taxonomy Id: 1810919
Other names: A. mulundensis, Aspergillus mulundensis Bills and Frisvad, 2015, Aspergillus sp. AJC-2016d, Aspergillus sp. QY-2015, Aspergillus sydowii var. GB-2015, Aspergillus sydowii var. mulundensis, CBS 140610, DSM 5745, DSMZ 5745, DTO 316-C9, IBT 33104
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