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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 | ZCCHC13 | zinc finger, CCHC domain containing 13 (166 aa) | ||||||||||||
Predicted Functional Partners:
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 | LRRC3DN | LRRC3 downstream neighbor (non-protein coding) (244 aa) |
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0.754 | ||||||||||
 | PAPD7 | PAP associated domain containing 7; DNA polymerase, probably involved in DNA repair. May play a role in sister chromatid cohesion. Does not play a role in replication-dependent histone mRNA degradation (542 aa) |
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0.674 | |||||||||
 | PAPD5 | PAP associated domain containing 5; Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. DNA polymerase, probably involved in DNA repair. May play a role in sister chromatid cohesion (698 aa) |
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0.666 | |||||||||
 | PRMT1 | protein arginine methyltransferase 1 (371 aa) |
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0.653 | ||||||||
 | PRMT8 | protein arginine methyltransferase 8; Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (394 aa) |
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0.653 | ||||||||
 | PRMT6 | protein arginine methyltransferase 6; Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 ’Arg-2’ to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on hi [...] (375 aa) |
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0.653 | ||||||||
 | PRMT2 | protein arginine methyltransferase 2; Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1- dependent manner). May be involved in growth regulation (433 aa) |
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0.653 | ||||||||
 | PRMT3 | protein arginine methyltransferase 3; Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins (531 aa) |
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0.653 | ||||||||
 | CHIC1 | cysteine-rich hydrophobic domain 1 (224 aa) |
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0.641 | ||||||||||
 | PDZRN3 | PDZ domain containing ring finger 3; E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation (By similarity) (1066 aa) |
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0.591 | ||||||||||
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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