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DENND4A DENND4A GGTLC3 GGTLC3 GGTLC1 GGTLC1 ME3 ME3 RIMKLB RIMKLB RIMKLA RIMKLA LCT LCT GGTLC2 GGTLC2 RNPEPL1 RNPEPL1 GGT6 GGT6 KL KL C4A C4A GCLM GCLM GGT7 GGT7 DENND4C DENND4C GGT5 GGT5 GCLC GCLC C3 C3 C5 C5 KLB KLB GGT1 GGT1 A2ML1 A2ML1 C4B C4B GGT2 GGT2 KLRP KLRP GBA3 GBA3
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
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C5complement component 5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled (1676 aa)
GCLCglutamate-cysteine ligase, catalytic subunit (637 aa)
C3complement component 3; C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (1663 aa)
GGT1gamma-glutamyltransferase 1; Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive (569 aa)
KLBklotho beta; Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21 (By similarity) (1044 aa)
LCTlactase; LPH splits lactose in the small intestine (1927 aa)
RNPEPL1arginyl aminopeptidase (aminopeptidase B)-like 1 (494 aa)
GGTLC1gamma-glutamyltransferase light chain 1 (225 aa)
A2ML1alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] (1454 aa)
GGT7gamma-glutamyltransferase 7; Cleaves glutathione conjugates (By similarity) (662 aa)
RIMKLBribosomal modification protein rimK-like family member B; Catalyzes the synthesis of beta-citryl-glutamate and N- acetyl-aspartyl-glutamate. Beta-citryl-glutamate is synthesized more efficiently than N-acetyl-aspartyl-glutamate (By similarity) (386 aa)
ME3malic enzyme 3, NADP(+)-dependent, mitochondrial (604 aa)
GCLMglutamate-cysteine ligase, modifier subunit (274 aa)
KLklotho; May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity) (1012 aa)
DENND4CDENN/MADD domain containing 4C (1673 aa)
GGT5gamma-glutamyltransferase 5; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4) (587 aa)
GGT2gamma-glutamyltransferase 2; Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors (By similarity) (569 aa)
DENND4ADENN/MADD domain containing 4A; Probable guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP- bound form. According to PubMed-8056341, it may bind to ISRE-like element (interferon-stimulated response element) of MYC P2 promoter (1906 aa)
C4Acomplement component 4A (Rodgers blood group) (1744 aa)
RIMKLAribosomal modification protein rimK-like family member A; Catalyzes the synthesis of N-acetylaspartyl-glutamate (NAAG) (391 aa)
GGTLC3gamma-glutamyltransferase light chain 3 (236 aa)
C4Bcomplement component 4B (Chido blood group) (1744 aa)
GGTLC2gamma-glutamyltransferase light chain 2 (218 aa)
GGT6gamma-glutamyltransferase 6; Cleaves glutathione conjugates (By similarity) (493 aa)
KLRPglucosidase, beta, acid 3 (cytosolic) (EC-3.2.1.21) (162 aa)
GBA3Cytosolic beta-glucosidase ; Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta- glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide (469 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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