Nucleoside diphosphate kinase A - Mus musculus (Mouse)

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P15532 (NDKA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nucleoside diphosphate kinase A
Short name=NDK A
Short name=NDP kinase A
EC=2.7.4.6

Alternative name(s):
Metastasis inhibition factor NM23
NDPK-A
Tumor metastatic process-associated protein
nm23-M1

Gene names

Name:	Nme1
Synonyms:	Nm23

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination By similarity.
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	Autophosphorylation at His-118 increases serine/threonine protein kinase activity of the enzyme. Interaction with the SET complex inhibits exonuclease activity By similarity.
Subunit structure	Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with SET and PRUNE By similarity.
Subcellular location	Cytoplasm. Nucleus.
Involvement in disease	Note=This protein is found in reduced amount in tumor cells of high metastatic potential.
Sequence similarities	Belongs to the NDK family.
Sequence caution	The sequence AAA39826.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Neurogenesis Nucleotide metabolism
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	CTP biosynthetic process Inferred from electronic annotation. Source: InterPro GTP biosynthetic process Inferred from electronic annotation. Source: InterPro UTP biosynthetic process Inferred from electronic annotation. Source: InterPro cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW nervous system development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 152

152

Nucleoside diphosphate kinase A

PRO_0000137115

Sites

Active site

118

Pros-phosphohistidine intermediate

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

105

ATP By similarity

Binding site

115

ATP By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphothreonine By similarity

Cross-link

100

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P15532 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: EE2E4DB218024686
Show »

FASTA

152

17,208

        10         20         30         40         50         60 
MANSERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF LQASEDLLKE HYTDLKDRPF 

        70         80         90        100        110        120 
FTGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS 

       130        140        150 
DSVKSAEKEI SLWFQPEELV EYKSCAQNWI YE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development." Rosengard A.M., Krutzsch H.C., Shearn A., Biggs J.R., Barker E., Margulies I.M.K., King C.R., Liotta L.A., Steeg P.S. Nature 342:177-180(1989) [PubMed: 2509941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Evidence for a novel gene associated with low tumor metastatic potential." Steeg P.S., Bevilacqua G., Kopper L., Thorgeirsson U.P., Talmadge J.E., Liotta L.A., Sobel M.E. J. Natl. Cancer Inst. 80:200-204(1988) [PubMed: 3346912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Reduced tumor incidence, metastatic potential, and cytokine responsiveness of nm23-transfected melanoma cells." Leone A., Flatow U., King C.R., Sandeen M.A., Margulies I.M., Liotta L.A., Steeg P.S. Cell 65:25-35(1991) [PubMed: 2013093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Dabernat S., Masse K., Daniel J.Y. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Sv.
[5]	Gervasi F., Fanciulli M., Lombardi D. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss Webster / NIH.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[7]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 7-26; 67-85; 89-124 AND 129-143, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35970 mRNA. Translation: AAA39826.1. Different initiation. M65037 mRNA. Translation: AAA63391.1. U85511 mRNA. Translation: AAB42080.1. AF033377 mRNA. Translation: AAB87689.1. BC005629 mRNA. Translation: AAH05629.1.
IPI	IPI00131459.
PIR	A46557.
RefSeq	NP_032730.1. NM_008704.2.
UniGene	Mm.439702.
3D structure databases
ProteinModelPortal	P15532.
SMR	P15532. Positions 5-152.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15532. 2 interactions.
STRING	P15532.
PTM databases
PhosphoSite	P15532.
2D gel databases
SWISS-2DPAGE	P15532.
REPRODUCTION-2DPAGE	P15532.
Proteomic databases
PRIDE	P15532.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000135884; ENSMUSP00000117022; ENSMUSG00000037601.
GeneID	18102.
KEGG	mmu:18102.
Organism-specific databases
CTD	4830.
MGI	MGI:97355. Nme1.
Phylogenomic databases
eggNOG	maNOG10260.
HOGENOM	HBG445152.
HOVERGEN	HBG000423.
InParanoid	P15532.
OMA	KSCAQNW.
PhylomeDB	P15532.
Gene expression databases
ArrayExpress	P15532.
Bgee	P15532.
Genevestigator	P15532.
GermOnline	ENSMUSG00000037601. Mus musculus.
Family and domain databases
InterPro	IPR001564. Nucleoside_diP_kinase. IPR023005. Nucleoside_diP_kinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.70.141. NDK. 1 hit.
KO	K00940.
PANTHER	PTHR11349. Nuc_diP_kinase_core. 1 hit.
Pfam	PF00334. NDK. 1 hit. [Graphical view]
PRINTS	PR01243. NUCDPKINASE.
SMART	SM00562. NDK. 1 hit. [Graphical view]
SUPFAM	SSF54919. NDK. 1 hit.
PROSITE	PS00469. NDP_KINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	459792.
SOURCE	Search...

Entry information

Entry name

NDKA_MOUSE

Accession

Primary (citable) accession number: P15532

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 16, 2011
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents