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Protein

Nucleoside diphosphate kinase A

Gene

Nme1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity).By similarity

Catalytic activityi

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.

Cofactori

Mg2+By similarity

Enzyme regulationi

Autophosphorylation at His-118 increases serine/threonine protein kinase activity of the enzyme. Interaction with the SET complex inhibits exonuclease activity (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121ATPBy similarity
Binding sitei60 – 601ATPBy similarity
Binding sitei88 – 881ATPBy similarity
Binding sitei94 – 941ATPBy similarity
Binding sitei105 – 1051ATPBy similarity
Binding sitei115 – 1151ATPBy similarity
Active sitei118 – 1181Pros-phosphohistidine intermediate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Differentiation, Endocytosis, Neurogenesis, Nucleotide metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside diphosphate kinase A (EC:2.7.4.6)
Short name:
NDK A
Short name:
NDP kinase A
Alternative name(s):
Metastasis inhibition factor NM23
NDPK-A
Tumor metastatic process-associated protein
nm23-M1
Gene namesi
Name:Nme1
Synonyms:Nm23
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97355. Nme1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

This protein is found in reduced amount in tumor cells of high metastatic potential.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 152151Nucleoside diphosphate kinase APRO_0000137115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki100 – 100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei124 – 1241N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP15532.
PaxDbiP15532.
PRIDEiP15532.

2D gel databases

REPRODUCTION-2DPAGEP15532.
SWISS-2DPAGEP15532.

PTM databases

PhosphoSiteiP15532.

Expressioni

Gene expression databases

BgeeiP15532.
ExpressionAtlasiP15532. baseline and differential.
GenevisibleiP15532. MM.

Interactioni

Subunit structurei

Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with PRUNE. Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, interacts directly with SET. Also interacts with TREX1, but only following translocation to the nucleus (By similarity).By similarity

Protein-protein interaction databases

BioGridi201788. 2 interactions.
IntActiP15532. 5 interactions.
MINTiMINT-1868955.
STRINGi10090.ENSMUSP00000117022.

Structurei

3D structure databases

ProteinModelPortaliP15532.
SMRiP15532. Positions 5-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

eggNOGiCOG0105.
GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP15532.
KOiK00940.
OMAiNASRAWI.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP15532.
TreeFamiTF106373.

Family and domain databases

Gene3Di3.30.70.141. 1 hit.
HAMAPiMF_00451. NDP_kinase.
InterProiIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamiPF00334. NDK. 1 hit.
[Graphical view]
PRINTSiPR01243. NUCDPKINASE.
SMARTiSM00562. NDK. 1 hit.
[Graphical view]
SUPFAMiSSF54919. SSF54919. 1 hit.
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15532-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF LQASEDLLKE
60 70 80 90 100
HYTDLKDRPF FTGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK
110 120 130 140 150
PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFQPEELV EYKSCAQNWI

YE
Length:152
Mass (Da):17,208
Last modified:April 1, 1990 - v1
Checksum:iEE2E4DB218024686
GO

Sequence cautioni

The sequence AAA39826.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25247.1.
PIRiA46557.
RefSeqiNP_032730.1. NM_008704.2.
UniGeneiMm.439702.

Genome annotation databases

EnsembliENSMUST00000135884; ENSMUSP00000117022; ENSMUSG00000037601.
GeneIDi18102.
KEGGimmu:18102.
UCSCiuc007kxu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25247.1.
PIRiA46557.
RefSeqiNP_032730.1. NM_008704.2.
UniGeneiMm.439702.

3D structure databases

ProteinModelPortaliP15532.
SMRiP15532. Positions 5-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201788. 2 interactions.
IntActiP15532. 5 interactions.
MINTiMINT-1868955.
STRINGi10090.ENSMUSP00000117022.

PTM databases

PhosphoSiteiP15532.

2D gel databases

REPRODUCTION-2DPAGEP15532.
SWISS-2DPAGEP15532.

Proteomic databases

MaxQBiP15532.
PaxDbiP15532.
PRIDEiP15532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000135884; ENSMUSP00000117022; ENSMUSG00000037601.
GeneIDi18102.
KEGGimmu:18102.
UCSCiuc007kxu.1. mouse.

Organism-specific databases

CTDi4830.
MGIiMGI:97355. Nme1.

Phylogenomic databases

eggNOGiCOG0105.
GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP15532.
KOiK00940.
OMAiNASRAWI.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP15532.
TreeFamiTF106373.

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSiNme1. mouse.
NextBioi293271.
PROiP15532.
SOURCEiSearch...

Gene expression databases

BgeeiP15532.
ExpressionAtlasiP15532. baseline and differential.
GenevisibleiP15532. MM.

Family and domain databases

Gene3Di3.30.70.141. 1 hit.
HAMAPiMF_00451. NDP_kinase.
InterProiIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamiPF00334. NDK. 1 hit.
[Graphical view]
PRINTSiPR01243. NUCDPKINASE.
SMARTiSM00562. NDK. 1 hit.
[Graphical view]
SUPFAMiSSF54919. SSF54919. 1 hit.
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. 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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNDKA_MOUSE
AccessioniPrimary (citable) accession number: P15532
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.