NME4
entrez
4833
canonical
uniprot
O00746
canonical
ensembl
ENSG00000103202
resolver
ensp
ENSP00000219479
resolver
ensp
ENSP00000380834
resolver
ensp
ENSP00000389048
resolver
ensp
ENSP00000405925
resolver
ensp
ENSP00000479681
resolver
ensp
ENSP00000479996
resolver
enst
ENST00000621774
resolver
genesymbol
NME4
resolver
genesymbol_syn
NM23D
resolver
hgnc
HGNC:7852
resolver
uniprot
A0A087WVT9
resolver
uniprot
A2IDD0
resolver
uniprot
Q5U0M9
resolver
uniprot_entry
A0A087WVT9_HUMAN
resolver
uniprot_entry
NDKD_HUMAN
resolver
uniprot_sec
A2IDD0
resolver
uniprot_sec
Q5U0M9
resolver
activity_regulation
ACTIVITY REGULATION: Binding to anionic phospholipids, predominantly to cardiolipin inhibits its phosphotransfer activity. {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663}.
uniprot
proteins
amino_acid_sequence
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
uniprot
proteins
ec_number
2.7.4.6
uniprot
proteins
function
FUNCTION: Mitochondria-specific nucleoside diphosphate kinase that catalyzes the transfer of a gamma-phosphoryl group from ATP to a nucleoside diphosphate via a ping-pong mechanism involving a phosphohistidine intermediate, participating in nucleoside triphosphate homeostasis (PubMed:10799505, PubMed:16313181, PubMed:18635542, PubMed:23150663). In vitro, purine nucleoside triphosphates are much more effective as donors and acceptors than pyrimidine nucleoside triphosphates, and ribonucleosides derivatives are superior to their deoxyribonucleosides counterparts (By similarity). Associates with cardiolipin-containing mitochondrial inner membrane and locally produces ADP in the mitochondrial intermembrane space, which is directly taken up via the ADP/ATP translocase (ANT) into the matrix to stimulate respiratory ATP regeneration (PubMed:18635542, PubMed:24970086). Also directly provides GTP for mitochondrial GTPases, such as the dynamin-related GTPase OPA1 (PubMed:24970086). Additionally, catalyzes the anionic phospholipid transfer, namely cardiolipin, from the mitochondrial inner membrane (IM) to the outer membrane (OM) through the formation of contact sites between IM and OM, in a nucleoside diphosphate kinase-independent manner (PubMed:17028143, PubMed:23150663). The switch between the nucleoside diphosphate kinase and the phospholipid transfer activity may depend on the availability and accessibility of cardiolipin and other anionic phospholipids in the IM outer leaflet and OM inner leaflet (PubMed:23150663). {ECO:0000250|UniProtKB:P87355, ECO:0000269|PubMed:10799505, ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663, ECO:0000269|PubMed:24970086, ECO:0000305, ECO:0000305|PubMed:24970086}.
uniprot
proteins
mass_dalton
20659
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="R->D: Abolishes cardiolipin-containing membrane binding; decreases lipid transfer and pro-apoptotic activity; does not change phosphotransfer activity."; /evidence="ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663"; MUTAGEN 129; /note="S->P: Does not affect autophosphorylation."; /evidence="ECO:0000269|PubMed:10799505
uniprot
proteins
protein_family
NDK family
uniprot
proteins
pubmed
10799505
uniprot
proteins
pubmed
11157797
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16313181
uniprot
proteins
pubmed
17028143
uniprot
proteins
pubmed
18635542
uniprot
proteins
pubmed
23150663
uniprot
proteins
pubmed
24970086
uniprot
proteins
pubmed
9099850
uniprot
proteins
sequence_length
187
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:10799505, ECO:0000269|PubMed:18635542, ECO:0000305|PubMed:23150663}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000269|PubMed:10799505, ECO:0000305|PubMed:18635542}. Mitochondrion outer membrane {ECO:0000269|PubMed:10799505, ECO:0000305|PubMed:23150663}. Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (Probable) (PubMed:24970086). Phospholipid binding mediates mitochondrial inner membrane binding (Probable) (PubMed:18635542). Fully membrane-bound, when attached simultaneously to inner membrane (IM) and outer membrane (OM) through the formation of contact sites between IM and OM (Probable) (PubMed:17028143). The additional binding to OM may depend on the availability or accessibility of cardiolipin and/or other anionic phospholipids in the IM outer leaflet and the OM inner leaflet (Probable). {ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086, ECO:0000305|PubMed:23150663}.
uniprot
proteins