Because of a lapse in government funding, the information on this
website may not be up to date, transactions submitted via the
website may not be processed, and the agency may not be able to
respond to inquiries until appropriations are enacted. The NIH
Clinical Center (the research hospital of NIH) is open. For more
details about its operating status, please visit
cc.nih.gov. Updates
regarding government operating status and resumption of normal
operations can be found at
opm.gov.
NM23 Nucleoside Diphosphate Kinases MeSH Descriptor Data 2026
A family of nucleotide diphosphate kinases that play a role in a variety of cellular signaling pathways that effect CELL DIFFERENTIATION; CELL PROLIFERATION; and APOPTOSIS. They are considered multifunctional proteins that interact with a variety of cellular proteins and have functions that are unrelated to their enzyme activity.
Entry Term(s)
DR-NM23 Nucleoside Diphosphate Kinase
Expressed in Non-Metastatic Cells 2 Protein
Granzyme A-activated DNase
NDP Kinase A
NM23-H2 Nucleoside Diphosphate Kinase
NM23-H3 Nucleoside Diphosphate Kinase
NM23A Nucleoside Diphosphate Kinases
NM23B Nucleoside Diphosphate Kinase
NME1 Nucleoside Diphosphate Kinase
Nm23-H1 Nucleoside Diphosphate Kinase
Non-Metastatic Cells 1 Protein
Nucleoside Diphosphate Kinase 3
Nucleoside Diphosphate Kinase A
Nucleoside Diphosphate Kinase B
Nucleoside Diphosphate Kinase C
Tumor Metastatic Process-Associated Protein
Registry Numbers
0
EC 2.7.4.6
EC 2.7.4.6
EC 2.7.4.6
Related Numbers
EC 2.7.4.6
Public MeSH Note
2008; NUCLEOSIDE DIPHOSPHATE KINASE A (now NM23 NUCLEOSIDE DIPHOSPHATE KINASES) was indexed under NUCLEOSIDE-DIPHOSPHATE KINASE 2005-2007, under GENES, TUMOR SUPPRESSOR 2005, under MONOMERIC GTP-BINDING PROTEINS 1994-2004, under TRANSCRIPTION FACTORS 1994-2004, & under PROTEINS 1989-1993
A family of nucleotide diphosphate kinases that play a role in a variety of cellular signaling pathways that effect CELL DIFFERENTIATION; CELL PROLIFERATION; and APOPTOSIS. They are considered multifunctional proteins that interact with a variety of cellular proteins and have functions that are unrelated to their enzyme activity.