Nme1
entrez
18102
canonical
uniprot
P15532
canonical
ensembl
ENSMUSG00000037601
resolver
ensp
ENSMUSP00000103475
resolver
ensp
ENSMUSP00000117022
resolver
ensp
ENSMUSP00000269499
resolver
enst
ENSMUST00000107844
resolver
enst
ENSMUST00000135884
resolver
genesymbol
Nme1
resolver
genesymbol_syn
Nm23
resolver
uniprot
Q5NC79
resolver
uniprot
Q5NC81
resolver
uniprot_entry
NDKA_MOUSE
resolver
uniprot_entry
Q5NC79_MOUSE
resolver
uniprot_entry
Q5NC81_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Autophosphorylation at His-118 increases nucleoside diphosphate kinase activity and serine/threonine protein kinase activity. Nucleoside diphosphate kinase activity is inhibited through a non-covalent binding of coenzyme A (CoA) via its ADP moiety to the nucleotide-binding pocket of NME1 (PubMed:37672589). Under cellular stress conditions, nucleoside diphosphate kinase activity is inhibited through a covalent binding of CoA through CoAlation (disulfide linkage to cysteine) at Cys-109 (By similarity). Interaction with the SET complex inhibits the DNA endonuclease activity. 3'-5'-DNA exonuclease activity is inhibited by potassium chloride (KCL), with the optimal KCl concentration less than or equal to 20 mM and ATP (By similarity). {ECO:0000250|UniProtKB:P15531, ECO:0000269|PubMed:37672589}.
uniprot
proteins
amino_acid_sequence
MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFLQASEDLLKEHYTDLKDRPFFTGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFQPEELVEYKSCAQNWIYE
uniprot
proteins
disease_involvement
DISEASE: Note=This protein is found in reduced amount in tumor cells of high metastatic potential.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.13.3
uniprot
proteins
ec_number
2.7.4.18
uniprot
proteins
ec_number
2.7.4.6
uniprot
proteins
ec_number
3.1.11.-
uniprot
proteins
ec_number
3.1.24.-
uniprot
proteins
function
FUNCTION: 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 (PubMed:37672589). 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 (By similarity). Involved in the regulation of tumor metastasis and cellular differentiation (PubMed:2013093, PubMed:3346912). Also required for cell motility (By similarity). 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) (PubMed:37672589). {ECO:0000250|UniProtKB:P15531, ECO:0000269|PubMed:2013093, ECO:0000269|PubMed:3346912, ECO:0000269|PubMed:37672589}.
uniprot
proteins
mass_dalton
17208
uniprot
proteins
mutagenesis
MUTAGEN 94; /note="T->D: Does not affect phosphorylation at His-118. Decreases nucleoside diphosphate kinase activity. Impairs CoA-binding."; /evidence="ECO:0000269|PubMed:37672589
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated at His-118 results in the formation of a phospho-enzyme intermediate and consequently activation of nucleoside diphosphate kinase activity and serine/threonine protein kinase activity. {ECO:0000269|PubMed:37672589}.; PTM: CoAlation at Cys-109, in response to oxidative stress, negatively regulates the nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:P15531}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P52175}.; PTM: Acetylated by GCN5, which prevents recognition by the SCF-FBXO24 E3 ubiquitin ligase, thereby protecting the protein from ubiquitination and proteasomal degradation. {ECO:0000250|UniProtKB:P15531}.; PTM: Ubiquitinated by the SCF-FBXO24 E3 ubiquitin ligase, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P15531}.
uniprot
proteins
protein_family
NDK family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
2013093
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
2509941
uniprot
proteins
pubmed
3346912
uniprot
proteins
pubmed
37672589
uniprot
proteins
sequence_length
152
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15531}. Nucleus {ECO:0000250|UniProtKB:P15531}. Cell membrane {ECO:0000250|UniProtKB:P52175}. Note=Cell-cycle dependent nuclear localization which can be induced by degradation of the SET complex by GzmA. In response to DNA damage, translocates to the nucleus where it might participate in DNA nucleolytic processing. {ECO:0000250|UniProtKB:P15531}.
uniprot
proteins