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Details on Person UniProt:O00746-1 NME4
| Class:Id | ReferenceIsoform:8972029 |
|---|---|
| _chainChangeLog | transit peptide:1-33 added on Fri February 17 2017;chain:34-187 added on Fri February 17 2017 |
| _displayName | UniProt:O00746-1 NME4 |
| _timestamp | 2026-02-20 22:24:20 |
| chain | transit peptide:1-28 chain:29-187 |
| checksum | A56FEF18A7D712D4 |
| comment | 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).CATALYTIC ACTIVITY a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADPCATALYTIC ACTIVITY a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADPCATALYTIC ACTIVITY dTDP + ATP = dTTP + ADPCATALYTIC ACTIVITY a cardiolipin(in) = a cardiolipin(out)CATALYTIC ACTIVITY GDP + ATP = GTP + ADPCATALYTIC ACTIVITY CDP + ATP = CTP + ADPCATALYTIC ACTIVITY UDP + ATP = UTP + ADPCATALYTIC ACTIVITY dCDP + ATP = dCTP + ADPCATALYTIC ACTIVITY dGDP + ATP = dGTP + ADPCOFACTOR Binding to anionic phospholipids, predominantly to cardiolipin inhibits its phosphotransfer activity.SUBUNIT Homohexamer (PubMed:10799505). Interacts with OPA1 (PubMed:23150663). Interacts with CAPN8 (By similarity).INTERACTION 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).ALTERNATIVE PRODUCTS Widely distributed. Found at very high levels in prostate, heart, liver, small intestine, and skeletal muscle tissues, and in low amounts in the brain and in blood leukocytes.SIMILARITY Belongs to the NDK family. |
| created | [InstanceEdit:8964659] Weiser, JD |
| description | recommendedName: fullName evidence="16"Nucleoside diphosphate kinase D, mitochondrial shortName evidence="11"NDPK-D ecNumber evidence="4 5 7 8"2.7.4.6 alternativeName: fullName evidence="15"Nucleoside diphosphate kinase 4 shortName evidence="10"NDK4 alternativeName: fullName evidence="12"nm23-H4 |
| geneName | NME4 NM23D |
| identifier | O00746 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing ATP-binding Direct protein sequencing Kinase Lipid-binding Magnesium Membrane Metal-binding Mitochondrion Mitochondrion outer membrane Nucleotide metabolism Nucleotide-binding Proteomics identification Reference proteome Transferase Transit peptide |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | NME4 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9004831] ENSEMBL:ENSG00000103202 NME4 [Homo sapiens] |
| secondaryIdentifier | NDKD_HUMAN A2IDD0 Q5U0M9 |
| sequenceLength | 187 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | O00746-1 |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:O00746-1 NME4 (8972029)
