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STRINGSTRING
PGP PGP AGL AGL CPLX1 CPLX1 GRHPR GRHPR IMPA2 IMPA2 FABP5 FABP5 PRDX6 PRDX6 GLOD4 GLOD4 AKR1B1 AKR1B1 PGAM1 PGAM1 ALDOC ALDOC AKR1B15 AKR1B15 PPA1 PPA1 QDPR QDPR GLO1 GLO1 PREP PREP PNP PNP UMPS UMPS ITPA ITPA GMPS GMPS IGBP1 IGBP1 ATIC ATIC PGM3 PGM3 ACY1 ACY1 PSMG4 PSMG4 HSD17B14 HSD17B14
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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
Node Content
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.
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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ALDOCAldolase, fructose-bisphosphate C (364 aa)
UMPSUridine 5’-monophosphate synthase; Uridine monophosphate synthetase; In the C-terminal section; belongs to the OMP decarboxylase family (480 aa)
ATICBifunctional purine biosynthesis protein PURH; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family (592 aa)
HSD17B1417-beta-hydroxysteroid dehydrogenase 14; Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3- beta,17-beta-diol (in vitro); Short chain dehydrogenase/reductase superfamily (270 aa)
IMPA2Inositol monophosphatase 2; Can use myo-inositol monophosphates, scylloinositol 1,4- diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2’- AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain (288 aa)
QDPRDihydropteridine reductase; The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases; Short chain dehydrogenase/reductase superfamily (244 aa)
AKR1B1Aldose reductase; Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies; Belongs to the aldo/keto reductase family (316 aa)
AGLGlycogen debranching enzyme; Multifunctional enzyme acting as 1,4-alpha-D-glucan-1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation; Belongs to the glycogen debranching enzyme family (1532 aa)
FABP5Fatty acid-binding protein, epidermal; High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation; Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family (135 aa)
GLOD4Glyoxalase domain containing 4 (298 aa)
CPLX1Complexin-1; Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior (134 aa)
GRHPRGlyoxylate reductase/hydroxypyruvate reductase; Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate (328 aa)
PGPGlycerol-3-phosphate phosphatase; Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3- phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear. In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity) (321 aa)
PRDX6Peroxiredoxin-6; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role [...] (224 aa)
PNPPurine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (289 aa)
PREPProlyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family (710 aa)
PGAM1Phosphoglycerate mutase 1; Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity (254 aa)
PPA1Pyrophosphatase 1 (289 aa)
GLO1Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF- kappa-B. Required for normal osteoclastogenesis (184 aa)
IGBP1Immunoglobulin-binding protein 1; Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits (339 aa)
ITPAInosine triphosphate pyrophosphatase; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2’-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5’-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (194 aa)
ACY1Aminoacylase-1; Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate); Belongs to the peptidase M20A family (408 aa)
AKR1B15Aldo-keto reductase family 1 member B15; Isoform 1- Mainly acts as a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. Has a strong selectivity towards NADP(H); Belongs to the aldo/keto reductase family (344 aa)
PSMG4Proteasome assembly chaperone 4 (162 aa)
GMPSGMP synthase [glutamine-hydrolyzing]; Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division; Glutamine amidotransferase like class 1 domain containing (693 aa)
PGM3Phosphoacetylglucosamine mutase; Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation (570 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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