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STRINGSTRING
LRIG3 LRIG3 LRIG1 LRIG1 PIGW PIGW NEU1 NEU1 NEU2 NEU2 CHST8 CHST8 GAL3ST1 GAL3ST1 PSG4 PSG4 UGT8 UGT8 GALC GALC NDUFA3 NDUFA3 GLA GLA ARSA ARSA NEU4 NEU4 NEU3 NEU3 SDCBP SDCBP
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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.
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experimentally determined
Predicted Interactions
gene neighborhood
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textmining
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ARSAArylsulfatase A; Hydrolyzes cerebroside sulfate; Belongs to the sulfatase family (509 aa)
GLAGalactosidase alpha; Belongs to the glycosyl hydrolase 27 family (429 aa)
NEU2Sialidase-2; Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides (380 aa)
SDCBPSyntenin-1; Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1- mediated SMAD2/3 activation and TGFB1-induced epithelial-to- mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6I [...] (298 aa)
GALCGalactocerebrosidase; Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon; Belongs to the glycosyl hydrolase 59 family (685 aa)
CHST8Carbohydrate sulfotransferase 8; Catalyzes the transfer of sulfate to position 4 of non- reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin; Belongs to the sulfotransferase 2 family (424 aa)
LRIG1Leucine-rich repeats and immunoglobulin-like domains protein 1; Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation; I-set domain containing (1093 aa)
NEU3Sialidase-3; Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates; Belongs to the glycosyl hydrolase 33 family (461 aa)
UGT82-hydroxyacylsphingosine 1-beta-galactosyltransferase; Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system; Belongs to the UDP-glycosyltransferase family (541 aa)
NEU4Sialidase-4; May function in lysosomal catabolism of sialylated glycoconjugates. Has sialidase activity towards synthetic substrates, such as 2’-(4-methylumbelliferyl)-alpha-D-N- acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad substrate specificity being active on glycoproteins, oligosaccharides and sialylated glycolipids (497 aa)
LRIG3Leucine-rich repeats and immunoglobulin-like domains protein 3; May play a role in craniofacial and inner ear morphogenesis during embryonic development. May act within the otic vesicle epithelium to control formation of the lateral semicircular canal in the inner ear, possibly by restricting the expression of NTN1 (By similarity); I-set domain containing (1119 aa)
NEU1Sialidase-1; Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (415 aa)
PSG4Pregnancy specific beta-1-glycoprotein 4 (419 aa)
GAL3ST1Galactosylceramide sulfotransferase; Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (By similarity). Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro); Belongs to the galactose-3-O-sulfotransferase family (423 aa)
NDUFA3NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3; Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone; NADH-ubiquinone oxidoreductase supernumerary subunits (84 aa)
PIGWPhosphatidylinositol-glycan biosynthesis class W protein; Required for the transport of GPI-anchored proteins to the plasma membrane. Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins (By similarity); Belongs to the PIGW family (504 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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