ID   NDKM_HUMAN              Reviewed;         187 AA.
AC   O00746; A2IDD0; Q5U0M9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Nucleoside diphosphate kinase, mitochondrial {ECO:0000305};
DE            Short=NDK;
DE            Short=NDP kinase, mitochondrial;
DE            EC=2.7.4.6 {ECO:0000269|PubMed:10799505};
DE   AltName: Full=Nucleoside diphosphate kinase D;
DE            Short=NDPKD;
DE   AltName: Full=nm23-H4;
DE   Flags: Precursor;
GN   Name=NME4 {ECO:0000312|HGNC:HGNC:7852}; Synonyms=NM23D;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Stomach;
RX   PubMed=9099850; DOI=10.1007/s004390050405;
RA   Milon L., Rousseau-Merck M.-F., Munier A., Erent M., Lascu I., Capeau J.,
RA   Lacombe M.-L.;
RT   "nm23-H4, a new member of the family of human nm23/nucleoside diphosphate
RT   kinase genes localised on chromosome 16p13.";
RL   Hum. Genet. 99:550-557(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA   Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT   the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=17028143; DOI=10.1529/biophysj.106.092353;
RA   Epand R.F., Schlattner U., Wallimann T., Lacombe M.L., Epand R.M.;
RT   "Novel lipid transfer property of two mitochondrial proteins that bridge
RT   the inner and outer membranes.";
RL   Biophys. J. 92:126-137(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, FUNCTION, PHOSPHOLIPID-BINDING, MUTAGENESIS OF
RP   ARG-90, AND ACTIVITY REGULATION.
RX   PubMed=18635542; DOI=10.1074/jbc.m803132200;
RA   Tokarska-Schlattner M., Boissan M., Munier A., Borot C., Mailleau C.,
RA   Speer O., Schlattner U., Lacombe M.L.;
RT   "The nucleoside diphosphate kinase D (NM23-H4) binds the inner
RT   mitochondrial membrane with high affinity to cardiolipin and couples
RT   nucleotide transfer with respiration.";
RL   J. Biol. Chem. 283:26198-26207(2008).
RN   [9]
RP   FUNCTION, MUTAGENESIS OF ARG-90, INTERACTION WITH OPA1, CATALYTIC ACTIVITY,
RP   AND ACTIVITY REGULATION.
RX   PubMed=23150663; DOI=10.1074/jbc.m112.408633;
RA   Schlattner U., Tokarska-Schlattner M., Ramirez S., Tyurina Y.Y.,
RA   Amoscato A.A., Mohammadyani D., Huang Z., Jiang J., Yanamala N.,
RA   Seffouh A., Boissan M., Epand R.F., Epand R.M., Klein-Seetharaman J.,
RA   Lacombe M.L., Kagan V.E.;
RT   "Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and
RT   intermembrane lipid transfer: a cardiolipin-dependent switch.";
RL   J. Biol. Chem. 288:111-121(2013).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24970086; DOI=10.1126/science.1253768;
RA   Boissan M., Montagnac G., Shen Q., Griparic L., Guitton J., Romao M.,
RA   Sauvonnet N., Lagache T., Lascu I., Raposo G., Desbourdes C.,
RA   Schlattner U., Lacombe M.L., Polo S., van der Bliek A.M., Roux A.,
RA   Chavrier P.;
RT   "Membrane trafficking. Nucleoside diphosphate kinases fuel dynamin
RT   superfamily proteins with GTP for membrane remodeling.";
RL   Science 344:1510-1515(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), CHARACTERIZATION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=10799505; DOI=10.1074/jbc.275.19.14264;
RA   Milon L., Meyer P., Chiadmi M., Munier A., Johansson M., Karlsson A.,
RA   Lascu I., Capeau J., Janin J., Lacombe M.-L.;
RT   "The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate
RT   kinase.";
RL   J. Biol. Chem. 275:14264-14272(2000).
CC   -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC       than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC       phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC       intermediate. Through the catalyzed exchange of gamma-phosphate between
CC       di- and triphosphonucleosides participates in regulation of
CC       intracellular nucleotide homeostasis (PubMed:10799505). Binds to
CC       anionic phospholipids, predominantly to cardiolipin; the binding
CC       inhibits its phosphotransfer activity (PubMed:18635542,
CC       PubMed:23150663). Acts as a mitochondria-specific NDK; its association
CC       with cardiolipin-containing mitochondrial inner membrane is coupled to
CC       respiration suggesting that ADP locally regenerated in the
CC       mitochondrion innermembrane space by its activity is directly taken up
CC       via ANT ADP/ATP translocase into the matrix space to stimulate
CC       respiratory ATP regeneration (PubMed:18635542). Proposed to increase
CC       GTP-loading on dynamin-related GTPase OPA1 in mitochondria
CC       (PubMed:24970086). In vitro can induce liposome cross-linking
CC       suggesting that it can cross-link inner and outer membranes to form
CC       contact sites, and promotes intermembrane migration of anionic
CC       phosphoplipids. Promotes the redistribution of cardiolipin between the
CC       mitochondrial inner membrane and outer membrane which is implicated in
CC       pro-apoptotic signaling (PubMed:18635542, PubMed:17028143,
CC       PubMed:23150663). {ECO:0000269|PubMed:10799505,
CC       ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542,
CC       ECO:0000269|PubMed:23150663, ECO:0000305, ECO:0000305|PubMed:24970086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:10799505};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:10799505};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cardiolipin(in) = a cardiolipin(out); Xref=Rhea:RHEA:38695,
CC         ChEBI:CHEBI:62237; Evidence={ECO:0000269|PubMed:23150663};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38696;
CC         Evidence={ECO:0000305|PubMed:23150663};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Binding to anionic phospholipids, predominantly to
CC       cardiolipin inhibits its phosphotransfer activity.
CC       {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663}.
CC   -!- SUBUNIT: Homohexamer (PubMed:10799505). Interacts with OPA1
CC       (PubMed:23150663). Interacts with CAPN8 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WV84, ECO:0000269|PubMed:10799505,
CC       ECO:0000269|PubMed:23150663}.
CC   -!- INTERACTION:
CC       O00746; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-744871, EBI-11096309;
CC       O00746; P01019: AGT; NbExp=3; IntAct=EBI-744871, EBI-751728;
CC       O00746; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-744871, EBI-8643161;
CC       O00746; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-744871, EBI-742909;
CC       O00746; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-744871, EBI-1166928;
CC       O00746; P54253: ATXN1; NbExp=6; IntAct=EBI-744871, EBI-930964;
CC       O00746; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-744871, EBI-2837444;
CC       O00746; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-744871, EBI-725606;
CC       O00746; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-744871, EBI-12011224;
CC       O00746; Q9NP86: CABP5; NbExp=3; IntAct=EBI-744871, EBI-10311131;
CC       O00746; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-744871, EBI-10171570;
CC       O00746; Q2TAC2-2: CCDC57; NbExp=5; IntAct=EBI-744871, EBI-10961624;
CC       O00746; P55273: CDKN2D; NbExp=3; IntAct=EBI-744871, EBI-745859;
CC       O00746; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-744871, EBI-749051;
CC       O00746; Q99828: CIB1; NbExp=3; IntAct=EBI-744871, EBI-372594;
CC       O00746; Q96Q77: CIB3; NbExp=3; IntAct=EBI-744871, EBI-10292696;
CC       O00746; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-744871, EBI-7062247;
CC       O00746; Q86UW9: DTX2; NbExp=3; IntAct=EBI-744871, EBI-740376;
CC       O00746; P02042: HBD; NbExp=3; IntAct=EBI-744871, EBI-6152722;
CC       O00746; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-744871, EBI-12094670;
CC       O00746; O75031: HSF2BP; NbExp=3; IntAct=EBI-744871, EBI-7116203;
CC       O00746; P42858: HTT; NbExp=20; IntAct=EBI-744871, EBI-466029;
CC       O00746; P03952: KLKB1; NbExp=3; IntAct=EBI-744871, EBI-10087153;
CC       O00746; P61968: LMO4; NbExp=3; IntAct=EBI-744871, EBI-2798728;
CC       O00746; P06858: LPL; NbExp=3; IntAct=EBI-744871, EBI-715909;
CC       O00746; Q13064: MKRN3; NbExp=3; IntAct=EBI-744871, EBI-2340269;
CC       O00746; P40692: MLH1; NbExp=3; IntAct=EBI-744871, EBI-744248;
CC       O00746; P15531: NME1; NbExp=11; IntAct=EBI-744871, EBI-741141;
CC       O00746; P22392: NME2; NbExp=5; IntAct=EBI-744871, EBI-713693;
CC       O00746; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-744871, EBI-744782;
CC       O00746; P61970: NUTF2; NbExp=3; IntAct=EBI-744871, EBI-591778;
CC       O00746; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-744871, EBI-398874;
CC       O00746; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-744871, EBI-721769;
CC       O00746; O15160: POLR1C; NbExp=5; IntAct=EBI-744871, EBI-1055079;
CC       O00746; P20618: PSMB1; NbExp=3; IntAct=EBI-744871, EBI-372273;
CC       O00746; P37840: SNCA; NbExp=3; IntAct=EBI-744871, EBI-985879;
CC       O00746; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-744871, EBI-742688;
CC       O00746; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-744871, EBI-740595;
CC       O00746; Q13148: TARDBP; NbExp=6; IntAct=EBI-744871, EBI-372899;
CC       O00746; O14656-2: TOR1A; NbExp=3; IntAct=EBI-744871, EBI-25847109;
CC       O00746; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-744871, EBI-11961968;
CC       O00746; Q15645: TRIP13; NbExp=4; IntAct=EBI-744871, EBI-358993;
CC       O00746; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-744871, EBI-3918381;
CC       O00746; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-744871, EBI-948354;
CC       O00746; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-744871, EBI-607755;
CC       O00746; P40337-2: VHL; NbExp=3; IntAct=EBI-744871, EBI-12157263;
CC       O00746; Q05516: ZBTB16; NbExp=3; IntAct=EBI-744871, EBI-711925;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:18635542}; Peripheral membrane protein.
CC       Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly
CC       localized in the mitochondrion intermembrane space (PubMed:18635542).
CC       Colocalizes with OPA1 in mitochondria (PubMed:24970086).
CC       {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00746-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00746-2; Sequence=VSP_054743;
CC   -!- TISSUE SPECIFICITY: Widely distributed. Found at very high levels in
CC       prostate, heart, liver, small intestine, and skeletal muscle tissues,
CC       and in low amounts in the brain and in blood leukocytes.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; Y07604; CAA68877.1; -; mRNA.
DR   EMBL; BT019438; AAV38245.1; -; mRNA.
DR   EMBL; AE006463; AAK61230.1; -; Genomic_DNA.
DR   EMBL; Z97634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85818.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85819.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85820.1; -; Genomic_DNA.
DR   EMBL; BC004880; AAH04880.1; -; mRNA.
DR   EMBL; BC017067; AAH17067.1; -; mRNA.
DR   CCDS; CCDS10408.1; -. [O00746-1]
DR   CCDS; CCDS66886.1; -. [O00746-2]
DR   RefSeq; NP_001273362.1; NM_001286433.1.
DR   RefSeq; NP_001273364.1; NM_001286435.1.
DR   RefSeq; NP_001273365.1; NM_001286436.1. [O00746-2]
DR   RefSeq; NP_001273367.1; NM_001286438.1. [O00746-2]
DR   RefSeq; NP_001273368.1; NM_001286439.1. [O00746-2]
DR   RefSeq; NP_001273369.1; NM_001286440.1. [O00746-2]
DR   RefSeq; NP_005000.1; NM_005009.2. [O00746-1]
DR   PDB; 1EHW; X-ray; 2.40 A; A/B=33-175.
DR   PDBsum; 1EHW; -.
DR   AlphaFoldDB; O00746; -.
DR   SMR; O00746; -.
DR   BioGRID; 110897; 187.
DR   IntAct; O00746; 123.
DR   MINT; O00746; -.
DR   STRING; 9606.ENSP00000219479; -.
DR   BindingDB; O00746; -.
DR   ChEMBL; CHEMBL4488; -.
DR   SwissLipids; SLP:000000360; -.
DR   GlyGen; O00746; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O00746; -.
DR   PhosphoSitePlus; O00746; -.
DR   BioMuta; NME4; -.
DR   EPD; O00746; -.
DR   jPOST; O00746; -.
DR   MassIVE; O00746; -.
DR   MaxQB; O00746; -.
DR   PaxDb; 9606-ENSP00000219479; -.
DR   PeptideAtlas; O00746; -.
DR   ProteomicsDB; 449; -.
DR   ProteomicsDB; 48013; -. [O00746-1]
DR   Pumba; O00746; -.
DR   Antibodypedia; 34896; 461 antibodies from 26 providers.
DR   DNASU; 4833; -.
DR   Ensembl; ENST00000219479.7; ENSP00000219479.2; ENSG00000103202.13. [O00746-1]
DR   Ensembl; ENST00000397722.5; ENSP00000380834.1; ENSG00000103202.13. [O00746-2]
DR   Ensembl; ENST00000450036.1; ENSP00000389048.1; ENSG00000103202.13. [O00746-2]
DR   Ensembl; ENST00000620944.4; ENSP00000479996.1; ENSG00000103202.13. [O00746-2]
DR   GeneID; 4833; -.
DR   KEGG; hsa:4833; -.
DR   MANE-Select; ENST00000219479.7; ENSP00000219479.2; NM_005009.3; NP_005000.1.
DR   UCSC; uc002cgz.4; human. [O00746-1]
DR   AGR; HGNC:7852; -.
DR   CTD; 4833; -.
DR   DisGeNET; 4833; -.
DR   GeneCards; NME4; -.
DR   HGNC; HGNC:7852; NME4.
DR   HPA; ENSG00000103202; Low tissue specificity.
DR   MIM; 601818; gene.
DR   neXtProt; NX_O00746; -.
DR   OpenTargets; ENSG00000103202; -.
DR   PharmGKB; PA31657; -.
DR   VEuPathDB; HostDB:ENSG00000103202; -.
DR   eggNOG; KOG0888; Eukaryota.
DR   GeneTree; ENSGT00940000160286; -.
DR   HOGENOM; CLU_060216_6_3_1; -.
DR   InParanoid; O00746; -.
DR   OMA; LLNWECC; -.
DR   OrthoDB; 3075753at2759; -.
DR   PhylomeDB; O00746; -.
DR   TreeFam; TF106373; -.
DR   BRENDA; 2.7.4.6; 2681.
DR   PathwayCommons; O00746; -.
DR   Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR   SignaLink; O00746; -.
DR   BioGRID-ORCS; 4833; 8 hits in 1159 CRISPR screens.
DR   ChiTaRS; NME4; human.
DR   EvolutionaryTrace; O00746; -.
DR   GeneWiki; NME4; -.
DR   GenomeRNAi; 4833; -.
DR   Pharos; O00746; Tbio.
DR   PRO; PR:O00746; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; O00746; Protein.
DR   Bgee; ENSG00000103202; Expressed in stromal cell of endometrium and 202 other cell types or tissues.
DR   ExpressionAtlas; O00746; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:BHF-UCL.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1901612; F:cardiolipin binding; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR   GO; GO:0009116; P:nucleoside metabolic process; TAS:ProtInc.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04413; NDPk_I; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR   HAMAP; MF_00451; NDP_kinase; 1.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR11349:SF49; NUCLEOSIDE DIPHOSPHATE KINASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS00469; NDPK; 1.
DR   PROSITE; PS51374; NDPK_LIKE; 1.
DR   Genevisible; O00746; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Direct protein sequencing;
KW   Kinase; Lipid-binding; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW   Nucleotide metabolism; Nucleotide-binding; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..187
FT                   /note="Nucleoside diphosphate kinase, mitochondrial"
FT                   /id="PRO_0000019432"
FT   ACT_SITE        151
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..70
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054743"
FT   MUTAGEN         90
FT                   /note="R->D: Abolishes cardiolipin-containing membrane
FT                   binding; decreases lipid transfer and pro-apoptotic
FT                   activity; does not change phosphotransfer activity."
FT                   /evidence="ECO:0000269|PubMed:18635542,
FT                   ECO:0000269|PubMed:23150663"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           54..63
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   STRAND          67..74
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           94..101
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           116..124
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           137..141
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   STRAND          149..152
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           156..166
FT                   /evidence="ECO:0007829|PDB:1EHW"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1EHW"
SQ   SEQUENCE   187 AA;  20659 MW;  A56FEF18A7D712D4 CRC64;
     MGGLFWRSAL RGLRCGPRAP GPSLLVRHGS GGPSWTRERT LVAVKPDGVQ RRLVGDVIQR
     FERRGFTLVG MKMLQAPESV LAEHYQDLRR KPFYPALIRY MSSGPVVAMV WEGYNVVRAS
     RAMIGHTDSA EAAPGTIRGD FSVHISRNVI HASDSVEGAQ REIQLWFQSS ELVSWADGGQ
     HSSIHPA
//