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ENSG00000114786 ENSG00000114786 ENPP3 ENPP3 MALSU1 MALSU1 NMNAT2 NMNAT2 NT5C NT5C PNP PNP NT5C3 NT5C3 NMNAT3 NMNAT3 ENSG00000250741 ENSG00000250741 APRT APRT NT5M NT5M NMNAT1 NMNAT1 ENPP1 ENPP1 NT5C2 NT5C2 ACY1 ACY1 NT5C1A NT5C1A NAPRT1 NAPRT1 CNDP2 CNDP2 NT5C3L NT5C3L CNDP1 CNDP1 NUDT12 NUDT12 QRSL1 QRSL1 PM20D1 PM20D1 FAAH FAAH FAAH2 FAAH2 NUDT15 NUDT15
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NUDT12nudix (nucleoside diphosphate linked moiety X)-type motif 12; 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 (462 aa)
NT5C1A5’-nucleotidase, cytosolic IA; 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 (368 aa)
NT5C35’-nucleotidase, cytosolic III (336 aa)
FAAHfatty acid amide hydrolase; Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (579 aa)
NT5C5’, 3’-nucleotidase, cytosolic; Dephosphorylates the 5’ and 2’(3’)-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP (201 aa)
NUDT15nudix (nucleoside diphosphate linked moiety X)-type motif 15; Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8- oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A-T to C-G transversions. Its substrate specificity in vivo however remains unclear (By similarity). May have a role in DNA synthesis and cell cycle progression through the interaction with PCNA (164 aa)
NMNAT2nicotinamide nucleotide adenylyltransferase 2; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides [...] (307 aa)
CNDP2CNDP dipeptidase 2 (metallopeptidase M20 family); Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells (475 aa)
NT5C25’-nucleotidase, cytosolic II; May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5’-monophosphate (IMP) and other purine nucleotides (561 aa)
NMNAT3nicotinamide nucleotide adenylyltransferase 3; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as subs [...] (215 aa)
ENPP3ectonucleotide pyrophosphatase/phosphodiesterase 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity) (875 aa)
CNDP1carnosine dipeptidase 1 (metallopeptidase M20 family) (507 aa)
ENPP1ectonucleotide pyrophosphatase/phosphodiesterase 1; By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. In vitro, has a broad specificity, hydrolyzing other nucleoside 5’ triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3’,5’-cAMP to AMP. May also be involved in the regu [...] (925 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 (By similarity) (289 aa)
PM20D1peptidase M20 domain containing 1 (502 aa)
QRSL1glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity) (528 aa)
FAAH2fatty acid amide hydrolase 2; Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates (532 aa)
NMNAT1nicotinamide nucleotide adenylyltransferase 1; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails [...] (279 aa)
APRTadenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis (180 aa)
NT5M5’,3’-nucleotidase, mitochondrial; Dephosphorylates specifically the 5’ and 2’(3’)- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP (228 aa)
ACY1aminoacylase 1; Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) (408 aa)
NT5C3L5’-nucleotidase, cytosolic III-like; Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates (300 aa)
NAPRT1nicotinate phosphoribosyltransferase domain containing 1; Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells (538 aa)
MALSU1mitochondrial assembly of ribosomal large subunit 1; May function as a ribosomal silencing factor. Addition to isolated mitochondrial ribosomal subunits partially inhibits translation. Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome (234 aa)
ENSG00000114786ABHD14A-ACY1 readthrough (non-protein coding) (509 aa)
ENSG00000250741NT5C1B-RDH14 readthrough (602 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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