STRINGSTRING
Wscd1 protein (mouse) - STRING interaction network
"Wscd1" - WSC domain containing 1 in Mus musculus
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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[Homology]
Score
Wscd1WSC domain containing 1; Belongs to the WSCD family (572 aa)    
Predicted Functional Partners:
Cfap161
Cilia- and flagella-associated protein 161; May play a role in motile cilia function, possibly by acting on dynein arm assembly (303 aa)
           
  0.629
Lysmd3
LysM, putative peptidoglycan-binding, domain containing 3 (305 aa)
     
   
  0.604
Mycbpap
MYCBP-associated protein; May play a role in spermatogenesis. May be involved in synaptic processes (By similarity) (932 aa)
           
  0.601
Tsen54
tRNA-splicing endonuclease subunit Sen54; Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5’ and 3’ splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2’,3’ cyclic phosphate and 5’-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA bo [...] (525 aa)
           
  0.577
Sgsm1
Small G protein signaling modulator 1; Interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. Promotes GTP hydrolysis by RAB34 and RAB36. Probably functions as GTPase effector with RAB9A and RAB9B; does not stimulate GTP hydrolysis with RAB9A and RAB9B; Belongs to the RUTBC family (1093 aa)
     
   
  0.575
Ankrd52
Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C; Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates (1076 aa)
       
 
  0.573
ENSMUSG00000044117
Uncharacterized protein C16orf45 homolog; RIKEN cDNA 2900011O08 gene (203 aa)
     
   
  0.570
Nkain2
Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 2; Na+/K+ transporting ATPase interacting 2; Belongs to the NKAIN family (208 aa)
     
   
  0.547
Dennd1b
DENN domain-containing protein 1B; Guanine nucleotide exchange factor (GEF) for RAB35 that acts as a regulator of T-cell receptor (TCR) internalization in TH2 cells. Acts by promoting the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Plays a role in clathrin-mediated endocytosis. Controls cytokine production in TH2 lymphocytes by controlling the rate of TCR internalization and routing to endosomes- acts by mediating clathrin-mediated endocytosis of TCR via its interaction with the adapter protein complex 2 (AP-2) and GEF activity. Dysregula [...] (691 aa)
           
  0.530
Syt10
Synaptotagmin-10; Ca(2+) sensor specifically required for the Ca(2+)- dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis. Acts through Ca(2+) and phospholipid binding to the C2 domain- Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE- complexes; both actions contribute to triggering exocytosis (By similarity) (523 aa)
     
   
  0.527
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus muscaris, Mus musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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