NME1

Catalyzes the transfer of a gamma-phosphoryl group from a nucleoside triphosphate, mainly ATP, to a nucleoside diphosphate via a ping-pong mechanism involving a phosphohistidine intermediate, therefore contributing to the nucleoside triphosphate homeostasis. Also phosphorylates geranyl pyrophosphate (GPP) and farnesyl pyrophosphate (FPP), linking it to isoprenoid metabolism. Additionally, functions as a non-specific serine/threonine kinase and histidine protein kinase, transferring phosphoryl groups from its active site to target proteins. May function as a Mg(2+)-dependent single-stranded DNA endonuclease as part of the SET complex, cooperating with the 3'-5' exonuclease TREX1 to mediate apoptotic DNA fragmentation in cytotoxic T lymphocytes. Reported to nick one DNA strand, enabling TREX1 to remove nucleotides from the free 3' end, enhancing DNA damage and suppressing DNA end reannealing and repair. Has been shown to cleave double strands DNA within the 3'-portions of both 5'-SHS silencer and NHE basal promoter element of the PDGFA gene, potentially repressing its transcription. May also function as a Mg(2+)-dependent 3'-5' DNA exonuclease, excising nucleotides from 3' single-stranded DNA or DNA with 3' single strand overhangs, suggesting a role in DNA nucleolytic processing. Involved in the regulation of tumor metastasis and cellular differentiation (By similarity). Also required for cell motility. May control, with NME2, AcCoA usage between histone acetylation and fatty acid synthesis, possibly by binding and releasing AcCoA at transcriptionally active chromatin regions in proximity to histone acetyltransferase (HAT) (By similarity)..

Function from UniProtKB (P15531), read 2026-09-23. CC BY 4.0.