STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
DNAAF1Dynein assembly factor 1, axonemal; Cilium-specific protein required for the stability of the ciliary architecture. Plays a role in cytoplasmic preassembly of dynein arms. Involved in regulation of microtubule-based cilia and actin-based brush border microvilli (725 aa)    
Predicted Functional Partners:
Axonemal dynein light intermediate polypeptide 1; May play a dynamic role in flagellar motility; Belongs to the inner dynein arm light chain family
Dynein intermediate chain 2, axonemal; Part of the dynein complex of respiratory cilia; Belongs to the dynein intermediate chain family
Zinc finger MYND domain-containing protein 10; Required for motile ciliary function. Probably involved in axonemal assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility. May act by indirectly regulating transcription of dynein proteins; Belongs to the ZMYND10 family
Dynein heavy chain 5, axonemal; Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles; Dyneins, axonemal
Protein kintoun; Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment
Dynein assembly factor 3, axonemal; Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia; Belongs to the DNAAF3 family
X-prolyl aminopeptidase 3; Belongs to the peptidase M24B family
Dynein assembly factor 5, axonemal; Cytoplasmic protein involved in the delivery of the dynein machinery to the motile cilium. It is required for the assembly of the axonemal dynein inner and outer arms, two structures attached to the peripheral outer doublet A microtubule of the axoneme, that play a crucial role in cilium motility
Coiled-coil domain-containing protein 40; Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC39 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (By similarity). Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39; Belongs to the CCDC40 family
Radial spoke head protein 4 homolog A; Probable component of the axonemal radial spoke head. Radial spokes are regularly spaced along cilia, sperm and flagella axonemes. They consist of a thin stalk which is attached to a subfiber of the outer doublet microtubule, and a bulbous head which is attached to the stalk and appears to interact with the projections from the central pair of microtubules
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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