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STRINGSTRING
DLG5 DLG5 SEC24C SEC24C P4HB P4HB NDUFB10 NDUFB10 DTNA DTNA SYNC SYNC UTRN UTRN SNTA1 SNTA1 DMD DMD SNTB1 SNTB1 SNTB2 SNTB2
"DTNA" - dystrobrevin, alpha in Homo sapiens
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 protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DTNAdystrobrevin, alpha (743 aa)    
Predicted Functional Partners:
DMD
dystrophin (3685 aa)
        score_image   score_image score_image 0.978
SNTA1
syntrophin, alpha 1; Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5- bisphosphate (By similarity) (505 aa)
        score_image   score_image   0.964
UTRN
utrophin; May play a role in anchoring the cytoskeleton to the plasma membrane (By similarity) (3433 aa)
        score_image   score_image score_image 0.946
SNTB1
syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1); Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (538 aa)
        score_image   score_image   0.919
SEC24C
SEC24 family, member C (S. cerevisiae); Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex (1094 aa)
        score_image       0.899
SYNC
syncoilin, intermediate filament protein (482 aa)
        score_image   score_image   0.891
SNTB2
syntrophin, beta 2 (dystrophin-associated protein A1, 59kDa, basic component 2); Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN (540 aa)
        score_image   score_image   0.885
DLG5
discs, large homolog 5 (Drosophila) (1919 aa)
        score_image       0.858
NDUFB10
NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 10, 22kDa; Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (172 aa)
        score_image       0.858
P4HB
prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] (508 aa)
        score_image   score_image   0.796
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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