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 Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Your Input:
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Neighborhood |
Gene Fusion |
Cooccurence |
Coexpression |
Experiments |
Databases |
Textmining |
[Homology] |
Score |
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 | RIOK1 | RIO kinase 1 (yeast) (568 aa) | ||||||||||||
Predicted Functional Partners:
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 | MAGOH | mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] (146 aa) |
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0.996 | |||||||||
 | PRMT5 | protein arginine methyltransferase 5; Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of [...] (637 aa) |
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0.884 | |||||||||
 | SBNO1 | strawberry notch homolog 1 (Drosophila) (1393 aa) |
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0.813 | ||||||||||
 | RASGEF1A | RasGEF domain family, member 1A; Guanine nucleotide exchange factor (GEF) with specificity for RAP2A, KRAS, HRAS, and NRAS (in vitro). Plays a role in cell migration (481 aa) |
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0.813 | ||||||||||
 | PNO1 | partner of NOB1 homolog (S. cerevisiae) (252 aa) |
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0.784 | ||||||||
 | RRP12 | ribosomal RNA processing 12 homolog (S. cerevisiae) (1297 aa) |
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0.775 | ||||||||
 | KRR1 | KRR1, small subunit (SSU) processome component, homolog (yeast); Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity) (381 aa) |
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0.774 | ||||||||
 | TGFBRAP1 | transforming growth factor, beta receptor associated protein 1; Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2 (860 aa) |
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0.763 | |||||||||
 | BYSL | bystin-like; Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos (437 aa) |
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0.761 | ||||||||
 | NMD3 | NMD3 homolog (S. cerevisiae); Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit (503 aa) |
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0.757 | ||||||||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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