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  • 11.0 [archived version]
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PLTP PLTP OS9 OS9 AMZ1 AMZ1 ERLEC1 ERLEC1 SPRYD7 SPRYD7 SEL1L3 SEL1L3 SPTBN1 SPTBN1 CCDC13 CCDC13 AZIN1 AZIN1 KRBA1 KRBA1 LRGUK LRGUK
"SEL1L3" - Protein sel-1 homolog 3 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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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]
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SEL1L3Protein sel-1 homolog 3; SEL1L family member 3 (1132 aa)    
Predicted Functional Partners:
PLTP
Phospholipid transfer protein; Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that [...] (493 aa)
       
 
  0.768
OS9
Protein OS-9; Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4; MRH domain containing (667 aa)
     
 
  0.675
ERLEC1
Endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins; MRH domain containing (483 aa)
     
 
  0.675
LRGUK
Leucine-rich repeat and guanylate kinase domain-containing protein; Involved in multiple aspects of sperm assembly including acrosome attachment, shaping of the sperm head and in the early aspects of axoneme development. Not essential for primary cilium biogenesis; Cilia and flagella associated (825 aa)
       
 
  0.654
KRBA1
Protein KRBA1; KRAB-A domain containing 1 (1030 aa)
           
  0.650
AZIN1
Antizyme inhibitor 1; Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme- binding. Inhibits antizyme- dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (448 aa)
           
  0.605
CCDC13
Coiled-coil domain-containing protein 13; Required for primary cilia formation and promotes the localization of the ciliopathy protein BBS4 to both centriolar satellites and cilia (715 aa)
           
  0.598
SPTBN1
Spectrin beta chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane; Pleckstrin homology domain containing (2364 aa)
       
 
  0.589
AMZ1
Archaemetzincin-1; Zinc metalloprotease. Exhibits aminopeptidase activity against neurogranin in vitro. Does not hydrolyze angiotensin-2; Belongs to the peptidase M54 family (498 aa)
           
  0.569
SPRYD7
SPRY domain containing 7 (196 aa)
     
   
  0.563
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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