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PLSCR4 PLSCR4 PLSCR1 PLSCR1 PLN PLN PLSCR2 PLSCR2 PRKACA PRKACA CEP76 CEP76 PRKACB PRKACB PRKAR2B PRKAR2B PRKAR2A PRKAR2A USP4 USP4 PRKAR1A PRKAR1A MEPCE MEPCE AKAP7 AKAP7 PLSCR5 PLSCR5 PLSCR3 PLSCR3 SPA17 SPA17 ROPN1 ROPN1
Nodes:
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
ROPN1rhophilin associated tail protein 1 (212 aa)
SPA17sperm autoantigenic protein 17; Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity) (151 aa)
CEP76centrosomal protein 76kDa; Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication (659 aa)
USP4ubiquitin specific peptidase 4 (proto-oncogene); Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. Plays a role in the regulation of quality control in the ER (963 aa)
PRKAR2Aprotein kinase, cAMP-dependent, regulatory, type II, alpha; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (404 aa)
PRKAR2Bprotein kinase, cAMP-dependent, regulatory, type II, beta; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (418 aa)
MEPCEmethylphosphate capping enzyme; S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5’-end of 7SK snRNA, leading to stabilize it (689 aa)
PRKACAprotein kinase, cAMP-dependent, catalytic, alpha; Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, TRPC1 and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in th [...] (351 aa)
PLSCR3phospholipid scramblase 3; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mit [...] (295 aa)
PLSCR1phospholipid scramblase 1; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system (318 aa)
PLSCR4phospholipid scramblase 4; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system (329 aa)
PLNphospholamban; Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum (52 aa)
PRKAR1Aprotein kinase, cAMP-dependent, regulatory, type I, alpha; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells (381 aa)
PRKACBprotein kinase, cAMP-dependent, catalytic, beta (398 aa)
PLSCR5phospholipid scramblase family, member 5 (271 aa)
AKAP7A kinase (PRKA) anchor protein 7; Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (348 aa)
PLSCR2phospholipid scramblase 2; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system (297 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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