STRINGSTRING
his-26 his-26 his-46 his-46 hsp-90 hsp-90 his-37 his-37 his-50 his-50 his-31 his-31 his-64 his-64 his-5 his-5 his-56 his-56 his-60 his-60 chd-1 chd-1 his-38 his-38 his-18 his-18 his-28 his-28 smo-1 smo-1 his-1 his-1 his-67 his-67 his-10 his-10 his-14 his-14
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:
his-26Histone H4. (103 aa)
his-46Histone 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)
hsp-90Heat shock protein 90; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. By stabilizing the receptor-type guanylate cyclase daf-11 or another sig [...] (702 aa)
his-37Histone H4. (103 aa)
his-50Histone H4. (103 aa)
his-31Histone H4. (103 aa)
his-64Histone H4. (103 aa)
his-5Histone H4. (103 aa)
his-56Histone H4. (103 aa)
his-60Histone H4. (103 aa)
chd-1Chromodomain and Helicase Domain protein. (1461 aa)
his-38Histone H4. (103 aa)
his-18Histone H4. (103 aa)
his-28Histone H4. (103 aa)
smo-1Small ubiquitin-related modifier; Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic dev [...] (91 aa)
his-1Histone H4. (103 aa)
his-67Histone H4. (103 aa)
his-10Histone H4. (103 aa)
his-14Histone H4. (103 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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