• Version:
  • 11.0 [archived version]
STRINGSTRING
SCG5 SCG5 POMC POMC GCG GCG PCSK1N PCSK1N CPE CPE GIP GIP INS INS PCSK1 PCSK1 RIPK1 RIPK1 MLKL MLKL RIPK3 RIPK3
"PCSK1" - Neuroendocrine convertase 1 in Homo sapiens
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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PCSK1Neuroendocrine convertase 1; Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP; Belongs to the peptidase S8 family. Furin subfamily (753 aa)    
Predicted Functional Partners:
POMC
Pro-opiomelanocortin; Met-enkephalin- Endogenous opiate; Belongs to the POMC family (267 aa)
     
 
  0.965
INS
Insulin; Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver (110 aa)
     
 
  0.957
GCG
Glucagon; Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life; Belongs to the glucagon family (180 aa)
         
  0.955
GIP
Gastric inhibitory polypeptide; Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion; Endogenous ligands (153 aa)
         
  0.928
RIPK3
Receptor-interacting serine/threonine-protein kinase 3; Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes- GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (518 aa)
     
 
  0.809
RIPK1
Receptor-interacting serine/threonine-protein kinase 1; Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at ’Ser-728’ in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via ’Lys-63’-link chains acts as a critical enhancer of communication with do [...] (671 aa)
     
 
  0.807
MLKL
Mixed lineage kinase domain-like protein; Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity (471 aa)
     
 
  0.804
PCSK1N
ProSAAS; May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the further processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 84 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timi [...] (260 aa)
     
 
  0.786
CPE
Carboxypeptidase E; Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin; Belongs to the peptidase M14 family (476 aa)
     
   
  0.713
SCG5
Neuroendocrine protein 7B2; Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro; Granins (212 aa)
     
 
  0.703
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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