Nme1
entrez
191575
canonical
uniprot
Q05982
canonical
ensembl
ENSRNOG00000002693
resolver
ensembl
ENSRNOG00055032674
resolver
ensembl
ENSRNOG00060030298
resolver
ensp
ENSRNOP00000083790
resolver
ensp
ENSRNOP00055046568
resolver
ensp
ENSRNOP00060043780
resolver
enst
ENSRNOT00000112785
resolver
enst
ENSRNOT00055056462
resolver
enst
ENSRNOT00060052647
resolver
genesymbol
Nme1
resolver
uniprot_entry
NDKA_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Autophosphorylation at His-118 increases nucleoside diphosphate kinase activity and serine/threonine protein kinase activity. Under cellular stress conditions, nucleoside diphosphate kinase activity is inhibited through both covalent and non-covalent binding by CoenzymeA (CoA); a non-covalent binding of coenzyme A (CoA) via its ADP moiety to the nucleotide-binding pocket of NME1 and a covalent binding of CoA through CoAlation (disulfide linkage to cysteine) at Cys-109. 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. {ECO:0000250|UniProtKB:P15531}.
uniprot
proteins
amino_acid_sequence
MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFIQASEDLLKEHYIDLKDRPFFSGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEISLWFQPEELVDYKSCAQNWIYE
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:7665595). Also phosphorylates geranyl pyrophosphate (GPP) and farnesyl pyrophosphate (FPP), linking it to isoprenoid metabolism (PubMed:10952986). Additionally, functions as a non-specific serine/threonine kinase and histidine protein kinase, transferring phosphoryl groups from its active site to target proteins (PubMed:7665595). 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 (By similarity). 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) (By similarity). {ECO:0000250|UniProtKB:P15531, ECO:0000250|UniProtKB:P15532, ECO:0000269|PubMed:10952986, ECO:0000269|PubMed:7665595}.
uniprot
proteins
mass_dalton
17193
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated at His-118 results in the formation of a phospho-enzyme intermediate (PubMed:7665595). Consequently, activates nucleoside diphosphate kinase activity and serine/threonine protein kinase activity (By similarity). {ECO:0000250|UniProtKB:P15531, ECO:0000269|PubMed:7665595}.; 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
10952986
uniprot
proteins
pubmed
33903070
uniprot
proteins
pubmed
7665595
uniprot
proteins
pubmed
8381409
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