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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | C5 | complement 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) | ||
 | GCLC | glutamate-cysteine ligase, catalytic subunit (637 aa) | ||
 | UMPS | uridine monophosphate synthetase (480 aa) | ||
 | GGT1 | gamma-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) | ||
 | KLB | klotho 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) | ||
 | LCT | lactase; LPH splits lactose in the small intestine (1927 aa) | ||
 | GGTLC1 | gamma-glutamyltransferase light chain 1 (225 aa) | ||
 | RNPEP | arginyl aminopeptidase (aminopeptidase B); Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(- 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity) (650 aa) | ||
 | TRIM25 | tripartite motif containing 25; Functions as an ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates ’Lys-63’-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs (630 aa) | ||
 | GGT7 | gamma-glutamyltransferase 7; Cleaves glutathione conjugates (By similarity) (662 aa) | ||
 | RIMKLB | ribosomal 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) | ||
 | GCLM | glutamate-cysteine ligase, modifier subunit (274 aa) | ||
 | PABPC4 | poly(A) binding protein, cytoplasmic 4 (inducible form); Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity) (660 aa) | ||
 | KL | klotho; 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) | ||
 | DENND4C | DENN/MADD domain containing 4C (1673 aa) | ||
 | FAM98B | family with sequence similarity 98, member B (433 aa) | ||
 | GGT5 | gamma-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) | ||
 | GGT2 | gamma-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) | ||
 | DENND4A | DENN/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) | ||
 | C4A | complement component 4A (Rodgers blood group) (1744 aa) | ||
 | RIMKLA | ribosomal modification protein rimK-like family member A; Catalyzes the synthesis of N-acetylaspartyl-glutamate (NAAG) (391 aa) | ||
 | GGTLC3 | gamma-glutamyltransferase light chain 3 (236 aa) | ||
 | C4B | complement component 4B (Chido blood group) (1744 aa) | ||
 | GGTLC2 | gamma-glutamyltransferase light chain 2 (218 aa) | ||
 | GGT6 | gamma-glutamyltransferase 6; Cleaves glutathione conjugates (By similarity) (493 aa) | ||
 | KLRP | glucosidase, beta, acid 3 (cytosolic) (EC-3.2.1.21) (162 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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