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NM23 (human)

Overview NM23 nucleoside diphosphate kinase A. Major role in the synthesis of nucleoside triphosphates other than ATP. Holoenzyme is a hexamer of the A and B subunits. Mutations have been identified in aggressive neuroblastomas. Two transcript variants encoding different isoforms have been described. Note: This description may include information from UniProtKB. Protein type: Nucleotide Metabolism - purine; Nucleotide Metabolism - pyrimidine; EC 2.7.4.6; Tumor suppressor; Kinase, other Cellular Component: cytoplasm; cytosol; nucleus Molecular Function: identical protein binding; protein binding; GTP binding; nucleoside diphosphate kinase activity; magnesium ion binding; deoxyribonuclease activity; ATP binding Biological Process: regulation of apoptosis; GTP biosynthetic process; nervous system development; negative regulation of cell proliferation; CTP biosynthetic process; nucleobase, nucleoside and nucleotide metabolic process; nucleobase, nucleoside and nucleotide interconversion; UTP biosynthetic process; endocytosis; cell differentiation; positive regulation of epithelial cell proliferation; positive regulation of DNA binding Reference #:  P15531 (UniProtKB) Alt. Names/Synonyms: AWD; GAAD; Granzyme A-activated DNase; Metastasis inhibition factor nm23; NB; NBS; NDK A; NDKA; NDP kinase A; NDPK-A; NDPKA; NM23; nm23-H1; NME1; non-metastatic cells 1, protein (NM23A) expressed in; Nucleoside diphosphate kinase A; Tumor metastatic process-associated protein Gene Symbols: NME1 Molecular weight: 17,149 Da Basal Isoelectric point: 5.83  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below NM23 1JXV - A/B/C/D/E/F=1-152 (human) 1UCN - A/B/C=1-152 (human) 2HVD - A/B/C=1-152 (human) 2HVE - A/B/C=1-152 (human) 3L7U - A/C/B=1-152 (human) 4ENO - A/B=1-152 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1JXV 1UCN 2HVD 2HVE 3L7U 4ENO  |  ENZYME  |  Phospho3D  |  DISEASE 156490 256700  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein

	Sites Implicated In
cell growth, altered: S44‑p, S120‑p enzymatic activity, induced: S120‑p molecular association, regulation: S120‑p protein conformation: S120‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	107		K12-u	ERTFIAIkPDGVQRG
0	4		K26-a	GLVGEIIkRFEQkGF
0	3		K26-u	GLVGEIIkRFEQkGF
0	3		K31-a	IIkRFEQkGFRLVGL
0	2		K39-u	GFRLVGLkFMQAsED
4	1		S44-p	GLkFMQAsEDLLkEH
0	1		K49-a	QAsEDLLkEHyVDLk
0	9		K49-u	QAsEDLLkEHyVDLk
0	9		Y52-p	EDLLkEHyVDLkDRP
0	1		K56-a	kEHyVDLkDRPFFAG
0	67		K56-u	kEHyVDLkDRPFFAG
0	2		K66-a	PFFAGLVkyMHSGPV
0	12		K66-u	PFFAGLVkyMHSGPV
0	1		Y67-p	FFAGLVkyMHSGPVV
0	1		K85-a	WEGLNVVkTGRVMLG
0	2		K85-u	WEGLNVVkTGRVMLG
1	24		T94-p	GRVMLGEtNPADskP
0	14		S99-p	GEtNPADskPGTIRG
0	11		K100-a	EtNPADskPGTIRGD
0	97		K100-u	EtNPADskPGTIRGD
4	0		H118-p	QVGRNIIhGsDsVES
6	4		S120-p	GRNIIhGsDsVESAE
1	5		S122-p	NIIhGsDsVESAEkE
0	11		E124	IhGsDsVESAEkEIG
0	1		E124	IhGsDsVESAEkEIG
0	3		K128-u	DsVESAEkEIGLWFH
0	1		Y151	SCAQNWIYE______

	mouse
K12-u	ERTFIAIkPDGVQRG
K26-a	GLVGEIIkRFEQkGF
K26-u	GLVGEIIkRFEQkGF
K31-a	IIkRFEQkGFRLVGL
K39-u	GFRLVGLkFLQASED
S44	GLkFLQASEDLLkEH
K49	QASEDLLKEHYTDLk
K49-u	QASEDLLkEHYTDLk
Y52	EDLLkEHYTDLkDRP
K56	kEHYTDLKDRPFFTG
K56-u	kEHYTDLkDRPFFTG
K66	PFFTGLVKYMHSGPV
K66	PFFTGLVKYMHSGPV
Y67	FFTGLVKYMHSGPVV
K85	WEGLNVVKTGRVMLG
K85	WEGLNVVKTGRVMLG
T94-p	GRVMLGEtNPADskP
S99-p	GEtNPADskPGTIRG
K100-a	EtNPADskPGTIRGD
K100-u	EtNPADskPGTIRGD
H118	QVGRNIIHGsDsVkS
S120-p	GRNIIHGsDsVkSAE
S122-p	NIIHGsDsVkSAEkE
K124-u	IHGsDsVkSAEkEIS
K124-a	IHGsDsVkSAEkEIS
K128-u	DsVkSAEkEISLWFQ
Y151-p	SCAQNWIyE______

	rat
K12-u	ERTFIAIkPDGVQRG
K26	GLVGEIIKRFEQKGF
K26	GLVGEIIKRFEQKGF
K31	IIKRFEQKGFRLVGL
K39	GFRLVGLKFIQASED
S44	GLKFIQASEDLLKEH
K49	QASEDLLKEHYIDLk
K49	QASEDLLKEHYIDLk
Y52	EDLLKEHYIDLkDRP
K56	KEHYIDLKDRPFFSG
K56-u	KEHYIDLkDRPFFSG
K66	PFFSGLVKYMHSGPV
K66	PFFSGLVKYMHSGPV
Y67	FFSGLVKYMHSGPVV
K85	WEGLNVVKTGRVMLG
K85	WEGLNVVKTGRVMLG
T94-p	GRVMLGEtNPADSKP
S99	GEtNPADSKPGTIRG
K100	EtNPADSKPGTIRGD
K100	EtNPADSKPGTIRGD
H118	QVGRNIIHGsDSVES
S120-p	GRNIIHGsDSVESAE
S122	NIIHGsDSVESAEkE
E124	IHGsDSVESAEkEIS
E124	IHGsDSVESAEkEIS
K128-u	DSVESAEkEISLWFQ
Y151	SCAQNWIYE______

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