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  • 11.0 [archived version]
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SIPA1L2 SIPA1L2 DNAJC13 DNAJC13 RALGAPA2 RALGAPA2 ZC3H11A ZC3H11A C1orf168 C1orf168 CDH24 CDH24 DNAH1 DNAH1 LIMCH1 LIMCH1 DNAH7 DNAH7 MYO7B MYO7B FRAS1 FRAS1
"C1orf168" - FYN-binding protein 2 in Homo sapiens
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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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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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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C1orf168FYN-binding protein 2; Adapter protein that plays a role in T-cell receptor (TCR)-mediated activation of signaling pathways. Required for T- cell activation and integrin-mediated T-cell adhesion in response to TCR stimulation (728 aa)    
Predicted Functional Partners:
ZC3H11A
Zinc finger CCCH domain-containing protein 11A; Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex; Zinc fingers CCCH-type (810 aa)
           
  0.663
SIPA1L2
Signal-induced proliferation-associated 1-like protein 2; Signal induced proliferation associated 1 like 2; PDZ domain containing (1722 aa)
           
  0.618
RALGAPA2
Ral GTPase-activating protein subunit alpha-2; Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB; Armadillo-like helical domain containing (1873 aa)
           
  0.578
DNAH1
Dynein heavy chain 1, axonemal; Force generating protein of cilia required for sperm flagellum motility. 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 in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme; Belongs to the dynein heavy chain family (4265 aa)
           
  0.578
DNAH7
Dynein heavy chain 7, 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 (By similarity); Dyneins, axonemal (4024 aa)
           
  0.578
MYO7B
Unconventional myosin-VIIb; Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli (Probable); FERM domain containing (2116 aa)
           
  0.567
CDH24
Cadherin-24; Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-24 mediate strong cell-cell adhesion (819 aa)
           
  0.557
DNAJC13
DnaJ homolog subfamily C member 13; Involved in membrane trafficking through early endosomes, such as the early endosome to recycling endosome transport implicated in the recycling of transferrin and the early endosome to late endosome transport implicated in degradation of EGF and EGFR. Involved in the regulation of endosomal membrane tubulation and regulates th dynamics of SNX1 on the endosomal membrane; via association with WASHC2 may link the WASH complex to the retromer SNX-BAR subcomplex; Armadillo-like helical domain containing (2243 aa)
       
 
  0.546
FRAS1
Fraser extracellular matrix complex subunit 1 (1976 aa)
           
  0.542
LIMCH1
LIM and calponin homology domains 1 (1083 aa)
           
  0.537
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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