STRINGSTRING
his-28 his-28 his-46 his-46 hsp-3 hsp-3 nex-3 nex-3 his-37 his-37 his-50 his-50 his-31 his-31 his-64 his-64 hsp-4 hsp-4 his-5 his-5 his-56 his-56 his-60 his-60 his-38 his-38 his-18 his-18 hsp-75 hsp-75 act-3 act-3 act-1 act-1 nex-2 nex-2 his-1 his-1 his-67 his-67 taf-6.1 taf-6.1 nex-1 nex-1 ubq-2 ubq-2 his-26 his-26 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-28Histone 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-3Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. (661 aa)
nex-3Annexin. (317 aa)
his-37Histone H4. (103 aa)
his-50Histone H4. (103 aa)
his-31Histone H4. (103 aa)
his-64Histone H4. (103 aa)
hsp-4Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. (657 aa)
his-5Histone H4. (103 aa)
his-56Histone H4. (103 aa)
his-60Histone H4. (103 aa)
his-38Histone H4. (103 aa)
his-18Histone H4. (103 aa)
hsp-75HATPase_c domain-containing protein. (672 aa)
act-3Actin-1; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. (376 aa)
act-1Actin-1. (376 aa)
nex-2Annexin. (497 aa)
his-1Histone H4. (103 aa)
his-67Histone H4. (103 aa)
taf-6.1TAF domain-containing protein. (470 aa)
nex-1Annexin. (322 aa)
ubq-2Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] (128 aa)
his-26Histone 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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