STRINGSTRING
Rps26 Rps26 Rps5 Rps5 Rps19 Rps19 Xpo1 Xpo1 Rrp8 Rrp8 Rps2 Rps2 Rps7 Rps7 Rpl7 Rpl7 Rps15 Rps15 Rps3 Rps3 Rps18 Rps18
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:
Rps2640S ribosomal protein S26; Belongs to the eukaryotic ribosomal protein eS26 family. (115 aa)
Rps540S ribosomal protein S5, N-terminally processed; Belongs to the universal ribosomal protein uS7 family. (204 aa)
Rps1940S ribosomal protein S19; Required for pre-rRNA processing and maturation of 40S ribosomal subunits; Belongs to the eukaryotic ribosomal protein eS19 family. (145 aa)
Xpo1Exportin-1; Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from t [...] (1071 aa)
Rrp8Ribosomal RNA-processing protein 8; Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and pr [...] (503 aa)
Rps240S ribosomal protein S2; Belongs to the universal ribosomal protein uS5 family. (293 aa)
Rps740S ribosomal protein S7; Required for rRNA maturation. (194 aa)
Rpl760S ribosomal protein L7; Component of the large ribosomal subunit (By similarity). Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (By similarity); Belongs to the universal ribosomal protein uL30 family. (270 aa)
Rps1540S ribosomal protein S15; Belongs to the universal ribosomal protein uS19 family. (145 aa)
Rps340S ribosomal protein S3; Involved in translation as a component of the 40S small ribosomal subunit (By similarity). Has endonuclease activity and plays a role in repair of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity). Displays high binding affinity for 7,8-dihydro-8- oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity). Has also been shown to bind with similar affinity to intact and damaged DNA (By similarity). S [...] (243 aa)
Rps1840S ribosomal protein S18; Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA. (152 aa)
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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