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PPP2R2D PPP2R2D PPP2R2A PPP2R2A ENTPD5 ENTPD5 PPP2R2C PPP2R2C ENTPD7 ENTPD7 ATP6V1H ATP6V1H PPP2R2B PPP2R2B ACPP ACPP ENTPD6 ENTPD6
"ENTPD7" - ectonucleoside triphosphate diphosphohydrolase 7 in Homo sapiens
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protein of unknown 3D structure
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Score
ENTPD7ectonucleoside triphosphate diphosphohydrolase 7; Preferentially hydrolyzes nucleoside 5’-triphosphates. The order of activity with respect to possible substrates is UTP > GTP > CTP (604 aa)    
Predicted Functional Partners:
ATP6V1H
ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (483 aa)
        score_image   score_image   0.806
ENTPD6
ectonucleoside triphosphate diphosphohydrolase 6 (putative); Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5’-diphosphates, nucleoside 5’-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5’-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP (By similarity) (484 aa)
        score_image   score_image score_image 0.752
ENTPD5
ectonucleoside triphosphate diphosphohydrolase 5; Uridine diphosphatase (UDPase) that promotes protein N- glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. Also hydrolyzes GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a ke [...] (428 aa)
        score_image   score_image score_image 0.744
PPP2R2D
protein phosphatase 2, regulatory subunit B, delta; B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55- delta) fluctuate during the cell cycle- the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of t [...] (422 aa)
            score_image   0.696
PPP2R2B
protein phosphatase 2, regulatory subunit B, beta (446 aa)
            score_image   0.696
PPP2R2C
protein phosphatase 2, regulatory subunit B, gamma; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (447 aa)
            score_image   0.696
PPP2R2A
protein phosphatase 2, regulatory subunit B, alpha; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (457 aa)
            score_image   0.696
ACPP
acid phosphatase, prostate; A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (418 aa)
            score_image   0.416
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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