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NPY2R NPY2R ADK ADK WDYHV1 WDYHV1 HPRT1 HPRT1 AK3 AK3 ICAM1 ICAM1 UPRT UPRT ADA ADA APRT APRT ATIC ATIC PNP PNP GUK1 GUK1 CDA CDA NT5C1A NT5C1A DCK DCK UMPS UMPS NAMPT NAMPT TYMS TYMS DTYMK DTYMK ITPA ITPA CMPK2 CMPK2 QPRT QPRT NUDT12 NUDT12 DUT DUT DCTPP1 DCTPP1 DCTD DCTD
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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NAMPTNicotinamide phosphoribosyltransferase; Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock fun [...] (491 aa)
NUDT12Peroxisomal NADH pyrophosphatase NUDT12; Hydrolyzes NAD(P)H to NMNH and AMP (2’,5’-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle; Belongs to the Nudix hydrolase family. NudC subfamily (462 aa)
UMPSUridine 5’-monophosphate synthase; Uridine monophosphate synthetase; In the C-terminal section; belongs to the OMP decarboxylase family (480 aa)
NT5C1ACytosolic 5’-nucleotidase 1A; Dephosphorylates the 5’ and 2’(3’)-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia; 5’-nucleotidases (368 aa)
ATICBifunctional purine biosynthesis protein PURH; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family (592 aa)
CMPK2UMP-CMP kinase 2, mitochondrial; May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs. Also displays broad nucleoside diphosphate kinase activity (449 aa)
ICAM1Intercellular adhesion molecule 1; ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans- endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation; CD molecules (532 aa)
ADKAdenosine kinase; ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides; Belongs to the carbohydrate kinase PfkB family (362 aa)
DCKDeoxycytidine kinase; Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents; Belongs to the DCK/DGK family (260 aa)
WDYHV1Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N- terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C- terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested s [...] (205 aa)
HPRT1Hypoxanthine-guanine phosphoribosyltransferase; Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5- phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (218 aa)
DTYMKThymidylate kinase; Catalyzes the conversion of dTMP to dTDP; Belongs to the thymidylate kinase family (212 aa)
TYMSThymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway (313 aa)
DCTPP1dCTP pyrophosphatase 1; Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism (170 aa)
NPY2RNeuropeptide Y receptor type 2; Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PYY > NPY > PYY (3-36) > NPY (2-36) > [Ile-31, Gln-34] PP > [Leu- 31, Pro-34] NPY > PP, [Pro-34] PYY and NPY free acid (381 aa)
DCTDDeoxycytidylate deaminase; Supplies the nucleotide substrate for thymidylate synthetase (189 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)
GUK1Guanylate kinase; Essential for recycling GMP and indirectly, cGMP (241 aa)
ADAAdenosine deaminase; Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte- epithelial cell adhesion. Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ [...] (363 aa)
UPRTUracil phosphoribosyltransferase homolog; Belongs to the UPRTase family (309 aa)
CDACytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2’-deoxycytidine for UMP synthesis (146 aa)
APRTAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis (180 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)
DUTDeoxyuridine 5’-triphosphate nucleotidohydrolase, mitochondrial; This enzyme is involved in nucleotide metabolism- it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family (252 aa)
AK3GTP-AMP phosphotransferase AK3, mitochondrial; Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP-AMP phosphotransferase and ITP-AMP phosphotransferase activities; Belongs to the adenylate kinase family. AK3 subfamily (227 aa)
QPRTNicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA); Belongs to the NadC/ModD family (297 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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