NME2

NME2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3BBB, 3BBF, 1NSK, 3BBC, 1NUE
Identifiers
Aliases	NME2 , NDKB, NDPK-B, NDPKB, NM23-H2, NM23B, PUF, NME/NM23 nucleoside diphosphate kinase 2
External IDs	OMIM: 156491 MGI: 97356 HomoloGene: 133879 GeneCards: NME2
Gene location (Human)
Chr.	Chromosome 17 (human)
End	51,171,744 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	93,847,085 bp
RNA expression pattern
	Top expressed in
	skin of abdomen; ; left coronary artery; ; canal of the cervix; ; body of pancreas; ; subcutaneous adipose tissue; ; vagina; ; stromal cell of endometrium; ; myometrium; ; minor salivary gland; ; body of stomach;
	Top expressed in
	pancreas; ; quadriceps femoris muscle; ; morula; ; kidney; ; islet of Langerhans; ; muscle tissue; ; uterus; ; skeletal muscle tissue; ; mirror; ; renal cortex;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity ; DNA binding ; nucleotide binding ; protein histidine kinase activity ; DNA-binding transcription factor activity ; metal ion binding ; kinase activity ; protein binding ; ATP binding ; nucleoside diphosphate kinase activity ; protein serine/threonine kinase activity ; fatty acid binding ; intermediate filament binding ; enzyme binding ; transcription coactivator activity ; GDP binding ; G-quadruplex DNA binding ;
Cellular component	cytoplasm ; cytosol ; cell projection ; focal adhesion ; ruffle ; extracellular exosome ; nucleus ; cell periphery ; lamellipodium ; extracellular region ; secretory granule lumen ; ficolin-1-rich granule lumen ; intermediate filament ; mitochondrial membrane ; perinuclear region of cytoplasm ;
Biological process	UTP biosynthetic process ; peptidyl-histidine phosphorylation ; nucleobase-containing small molecule interconversion ; CTP biosynthetic process ; regulation of transcription, DNA-templated ; phosphorylation ; positive regulation of epithelial cell proliferation ; positive regulation of keratinocyte differentiation ; negative regulation of apoptotic process ; nucleotide metabolic process ; nucleoside diphosphate phosphorylation ; transcription, DNA-templated ; cell adhesion ; nucleoside triphosphate biosynthetic process ; integrin-mediated signaling pathway ; GTP biosynthetic process ; regulation of epidermis development ; positive regulation of transcription by RNA polymerase II ; neutrophil degranulation ; negative regulation of myeloid leukocyte differentiation ; positive regulation of neuron projection development ; cellular response to oxidative stress ; protein autophosphorylation ; protein complex oligomerization ; response to growth hormone ; cellular response to glucose stimulus ; cellular response to fatty acid ; adenylate cyclase-activating G protein-coupled receptor signaling pathway ; positive regulation of transcription, DNA-templated ;
	Sources:Amigo / QuickGO
Orthologs
	4831
	18103
	ENSG00000243678
	ENSMUSG00000020857
	P22392
	Q01768
	NM_002512 ; NM_001018137 ; NM_001018138 ; NM_001018139 ; NM_001198682 Contents Function ; Interactions ; References ; Further reading ;
	NM_001077529 ; NM_008705
NP_001018147 ; NP_001018148 ; NP_001018149 ; NP_001185611 ; NP_002503 ;
	NP_001018146
	NP_001070997 ; NP_032731
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 14, 2022

Nucleoside diphosphate kinase B is an enzyme that in humans is encoded by the NME2 gene.^[5]^[6]

Function

Nucleoside diphosphate kinase (NDK) exists as a hexamer composed of 'A' (encoded by NME1) and 'B' (encoded by this gene) isoforms. Multiple alternatively spliced transcript variants encoding the same isoform have been found for this gene. Co-transcription of this gene and the neighboring upstream gene (NME1) generates naturally occurring transcripts (NME1-NME2) which encode a fusion protein consisting of sequence sharing identity with each individual gene product.^[6]

Interactions

NME2 has been shown to interact with NME3 ^[7]^[8] and HERC5.^[9]

Related Research Articles

Nucleoside-diphosphate kinases are enzymes that catalyze the exchange of terminal phosphate between different nucleoside diphosphates (NDP) and triphosphates (NTP) in a reversible manner to produce nucleotide triphosphates. Many NDP serve as acceptor while NTP are donors of phosphate group. The general reaction via ping-pong mechanism is as follows: XDP + YTP ←→ XTP + YDP. NDPK activities maintain an equilibrium between the concentrations of different nucleoside triphosphates such as, for example, when guanosine triphosphate (GTP) produced in the citric acid (Krebs) cycle is converted to adenosine triphosphate (ATP). Other activities include cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor, endocytosis, and gene expression.

RAR-related orphan receptor beta (ROR-beta), also known as NR1F2 is a nuclear receptor that in humans is encoded by the RORB gene.

RAR-related orphan receptor alpha (RORα), also known as NR1F1 is a nuclear receptor that in humans is encoded by the RORA gene. RORα participates in the transcriptional regulation of some genes involved in circadian rhythm. In mice, RORα is essential for development of cerebellum through direct regulation of genes expressed in Purkinje cells. It also plays an essential role in the development of type 2 innate lymphoid cells (ILC2) and mutant animals are ILC2 deficient. In addition, although present in normal numbers, the ILC3 and Th17 cells from RORα deficient mice are defective for cytokine production.

Myc box-dependent-interacting protein 1, also known as Bridging Integrator-1 and Amphiphysin-2 is a protein that in humans is encoded by the BIN1 gene.

Nucleoside diphosphate kinase A is an enzyme that in humans is encoded by the NME1 gene. It is thought to be a metastasis suppressor.

T-cell lymphoma invasion and metastasis-inducing protein 1 is a protein that in humans is encoded by the TIAM1 gene.

RAC-gamma serine/threonine-protein kinase is an enzyme that in humans is encoded by the AKT3 gene.

Telomeric repeat-binding factor 1 is a protein that in humans is encoded by the TERF1 gene.

Protein NDRG1 is a protein that in humans is encoded by the NDRG1 gene.

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 is a protein that in humans is encoded by the GNG2 gene.

Oxidoreductase HTATIP2 is an enzyme that in humans is encoded by the HTATIP2 gene. It may be a metastasis suppressor.

Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene.

Myc-associated zinc finger protein is a protein that in humans is encoded by the MAZ gene.

Integrin beta-1-binding protein 1 is a protein that in humans is encoded by the ITGB1BP1 gene.

Ras Related Glycolysis Inhibitor and Calcium Channel Regulator (RRAD) is a protein that in humans is encoded by the RRAD gene. RRAD is a Ras-related small GTPase that is regulated by p53 and plays a role in the regulation of aerobic glycolysis.

Connector enhancer of kinase suppressor of ras 1 is an enzyme that in humans is encoded by the CNKSR1 gene.

Histidine triad nucleotide-binding protein 1 also known as adenosine 5'-monophosphoramidase is an enzyme that in humans is encoded by the HINT1 gene.

Nucleoside diphosphate kinase 3 is an enzyme that in humans is encoded by the NME3 gene.

Non-metastatic cells 4, protein expressed in, also known as NME4, is a protein which in humans is encoded by the NME4 gene.

Thioredoxin domain-containing protein 3 (TXNDC3), also known as spermatid-specific thioredoxin-2 (Sptrx-2), is a protein that in humans is encoded by the NME8 gene on chromosome 7.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000243678 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020857 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS (February 1991). "Identification of a second human nm23 gene, nm23-H2". Cancer Res. 51 (1): 445–9. PMID 1988104.
1 2 "Entrez Gene: NME2 non-metastatic cells 2, protein (NM23B) expressed in".
↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID 16169070. S2CID 8235923.
↑ Negroni A, Venturelli D, Tanno B, Amendola R, Ransac S, Cesi V, Calabretta B, Raschellà G (September 2000). "Neuroblastoma specific effects of DR-nm23 and its mutant forms on differentiation and apoptosis". Cell Death Differ. 7 (9): 843–50. doi: 10.1038/sj.cdd.4400720 . PMID 11042679.
↑ Hochrainer K, Kroismayr R, Baranyi U, Binder BR, Lipp J (July 2008). "Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B". Cell. Mol. Life Sci. 65 (13): 2105–17. doi:10.1007/s00018-008-8148-5. PMID 18535780. S2CID 6897759.

Thakur RK, Kumar P, Halder K, Verma A, Kar A, Parent JL, Basundra R, Kumar A, Chowdhury S (2009). "Metastases suppressor NM23-H2 interaction with G-quadruplex DNA within c-MYC promoter nuclease hypersensitive element induces c-MYC expression". Nucleic Acids Res. 37 (1): 172–83. doi:10.1093/nar/gkn919. PMC 2615625 . PMID 19033359.
Gilles AM, Presecan E, Vonica A, Lascu I (1991). "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme". J. Biol. Chem. 266 (14): 8784–9. doi: 10.1016/S0021-9258(18)31515-1 . PMID 1851158.
Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS (1989). "Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development". Nature. 342 (6246): 177–80. Bibcode:1989Natur.342..177R. doi:10.1038/342177a0. PMID 2509941. S2CID 4340066.
Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL (1995). "The crystal structure of a human nucleoside diphosphate kinase, NM23-H2". J. Mol. Biol. 251 (4): 574–87. doi:10.1006/jmbi.1995.0457. PMID 7658474.
Chandrasekharappa SC, Gross LA, King SE, Collins FS (1993). "The human NME2 gene lies within 18kb of NME1 in chromosome 17". Genes Chromosomes Cancer. 6 (4): 245–8. doi:10.1002/gcc.2870060411. PMID 7685630. S2CID 28992233.
Ji L, Arcinas M, Boxer LM (1995). "The transcription factor, Nm23H2, binds to and activates the translocated c-myc allele in Burkitt's lymphoma". J. Biol. Chem. 270 (22): 13392–8. doi: 10.1074/jbc.270.22.13392 . PMID 7768941.
MacDonald NJ, De la Rosa A, Benedict MA, Freije JM, Krutsch H, Steeg PS (1993). "A serine phosphorylation of Nm23, and not its nucleoside diphosphate kinase activity, correlates with suppression of tumor metastatic potential". J. Biol. Chem. 268 (34): 25780–9. doi: 10.1016/S0021-9258(19)74458-5 . PMID 8245015.
Backer JM, Mendola CE, Kovesdi I, Fairhurst JL, O'Hara B, Eddy RL, Shows TB, Mathew S, Murty VV, Chaganti RS (1993). "Chromosomal localization and nucleoside diphosphate kinase activity of human metastasis-suppressor genes NM23-1 and NM23-2". Oncogene. 8 (2): 497–502. PMID 8381224.
Postel EH, Berberich SJ, Flint SJ, Ferrone CA (1993). "Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis". Science. 261 (5120): 478–80. Bibcode:1993Sci...261..478P. doi:10.1126/science.8392752. PMID 8392752.
Kelsell DP, Black DM, Solomon E, Spurr NK (1993). "Localization of a second NM23 gene, NME2, to chromosome 17q21-q22". Genomics. 17 (2): 522–4. doi:10.1006/geno.1993.1362. PMID 8406509.
Engel M, Véron M, Theisinger B, Lacombe ML, Seib T, Dooley S, Welter C (1995). "A novel serine/threonine-specific protein phosphotransferase activity of Nm23/nucleoside-diphosphate kinase". Eur. J. Biochem. 234 (1): 200–7. doi:10.1111/j.1432-1033.1995.200_c.x. PMID 8529641.
Guignard F, Markert M (1996). "The nucleoside diphosphate kinase of human neutrophils". Biochem. J. 316 ( Pt 1) (1): 233–8. doi:10.1042/bj3160233. PMC 1217327 . PMID 8645210.
Moréra S, Lacombe ML, Xu Y, LeBras G, Janin J (1995). "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution". Structure. 3 (12): 1307–14. doi: 10.1016/S0969-2126(01)00268-4 . PMID 8747457.
Paravicini G, Steinmayr M, André E, Becker-André M (1996). "The metastasis suppressor candidate nucleotide diphosphate kinase NM23 specifically interacts with members of the ROR/RZR nuclear orphan receptor subfamily". Biochem. Biophys. Res. Commun. 227 (1): 82–7. doi:10.1006/bbrc.1996.1471. PMID 8858107.
Nosaka K, Kawahara M, Masuda M, Satomi Y, Nishino H (1998). "Association of nucleoside diphosphate kinase nm23-H2 with human telomeres". Biochem. Biophys. Res. Commun. 243 (2): 342–8. doi:10.1006/bbrc.1997.8097. PMID 9480811.
Pinon VP, Millot G, Munier A, Vassy J, Linares-Cruz G, Capeau J, Calvo F, Lacombe ML (1999). "Cytoskeletal association of the A and B nucleoside diphosphate kinases of interphasic but not mitotic human carcinoma cell lines: specific nuclear localization of the B subunit". Exp. Cell Res. 246 (2): 355–67. doi:10.1006/excr.1998.4318. PMID 9925751.
Negroni A, Venturelli D, Tanno B, Amendola R, Ransac S, Cesi V, Calabretta B, Raschellà G (2000). "Neuroblastoma specific effects of DR-nm23 and its mutant forms on differentiation and apoptosis". Cell Death Differ. 7 (9): 843–50. doi: 10.1038/sj.cdd.4400720 . PMID 11042679.
Roymans D, Willems R, Vissenberg K, De Jonghe C, Grobben B, Claes P, Lascu I, Van Bockstaele D, Verbelen JP, Van Broeckhoven C, Slegers H (2000). "Nucleoside diphosphate kinase beta (Nm23-R1/NDPKbeta) is associated with intermediate filaments and becomes upregulated upon cAMP-induced differentiation of rat C6 glioma". Exp. Cell Res. 261 (1): 127–38. doi:10.1006/excr.2000.5037. PMID 11082283.
Baillat G, Gaillard S, Castets F, Monneron A (2002). "Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and Dynamin I". J. Biol. Chem. 277 (21): 18961–6. doi: 10.1074/jbc.M108818200 . PMID 11872741.
Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C (2002). "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement". J. Biol. Chem. 277 (23): 20895–902. doi: 10.1074/jbc.M200200200 . PMID 11919189.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000243678 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020857 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1988104-5] Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS (February 1991). "Identification of a second human nm23 gene, nm23-H2". Cancer Res. 51 (1): 445–9. PMID 1988104.

[entrez-6] 1 2 "Entrez Gene: NME2 non-metastatic cells 2, protein (NM23B) expressed in".

[pmid16169070-7] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID 16169070. S2CID 8235923.

[pmid11042679-8] Negroni A, Venturelli D, Tanno B, Amendola R, Ransac S, Cesi V, Calabretta B, Raschellà G (September 2000). "Neuroblastoma specific effects of DR-nm23 and its mutant forms on differentiation and apoptosis". Cell Death Differ. 7 (9): 843–50. doi: 10.1038/sj.cdd.4400720 . PMID 11042679.

[pmid18535780-9] Hochrainer K, Kroismayr R, Baranyi U, Binder BR, Lipp J (July 2008). "Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B". Cell. Mol. Life Sci. 65 (13): 2105–17. doi:10.1007/s00018-008-8148-5. PMID 18535780. S2CID 6897759.

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NME2

Contents

Function

Interactions

Related Research Articles

References

Further reading