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P15531

- NDKA_HUMAN

UniProt

P15531 - NDKA_HUMAN

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Protein
Nucleoside diphosphate kinase A
Gene
NME1, NDPKA, NM23
Organism
Homo sapiens (Human)
Status
Reviewed - 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.4 Publications

Catalytic activityi

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Cofactori

Magnesium.

Enzyme regulationi

Autophosphorylation at His-118 increases serine/threonine protein kinase activity of the enzyme. Interaction with the SET complex inhibits the endonuclease activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121ATP
Binding sitei60 – 601ATP
Binding sitei88 – 881ATP
Binding sitei94 – 941ATP
Binding sitei105 – 1051ATP
Binding sitei115 – 1151ATP
Active sitei118 – 1181Pros-phosphohistidine intermediate1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  4. deoxyribonuclease activity Source: UniProtKB
  5. identical protein binding Source: IntAct
  6. magnesium ion binding Source: UniProtKB
  7. nucleoside diphosphate kinase activity Source: UniProtKB
  8. poly(A) RNA binding Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. ribosomal small subunit binding Source: UniProtKB
  11. single-stranded DNA binding Source: Ensembl

GO - Biological processi

  1. CTP biosynthetic process Source: InterPro
  2. DNA catabolic process Source: GOC
  3. GTP biosynthetic process Source: InterPro
  4. UTP biosynthetic process Source: InterPro
  5. cellular response to drug Source: Ensembl
  6. cellular response to fatty acid Source: Ensembl
  7. cellular response to glucose stimulus Source: Ensembl
  8. endocytosis Source: UniProtKB-KW
  9. hippocampus development Source: Ensembl
  10. lactation Source: Ensembl
  11. negative regulation of cell proliferation Source: UniProtKB
  12. negative regulation of gene expression Source: Ensembl
  13. negative regulation of myeloid leukocyte differentiation Source: Ensembl
  14. nucleobase-containing small molecule interconversion Source: Reactome
  15. nucleobase-containing small molecule metabolic process Source: Reactome
  16. positive regulation of DNA binding Source: UniProtKB
  17. positive regulation of epithelial cell proliferation Source: HGNC
  18. positive regulation of neuron projection development Source: Ensembl
  19. regulation of apoptotic process Source: UniProtKB
  20. response to amine Source: Ensembl
  21. response to cAMP Source: Ensembl
  22. response to testosterone Source: Ensembl
  23. small molecule metabolic process Source: Reactome
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

BioCyciMetaCyc:ENSG00000011052-MONOMER.
ReactomeiREACT_21330. 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):
Granzyme A-activated DNase
Short name:
GAAD
Metastasis inhibition factor nm23
NM23-H1
Tumor metastatic process-associated protein
Gene namesi
Name:NME1
Synonyms:NDPKA, NM23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7849. NME1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Cell-cycle dependent nuclear localization which can be induced by interaction with Epstein-barr viral proteins or by degradation of the SET complex by GzmA.1 Publication

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: Ensembl
  6. nucleus Source: UniProtKB
  7. perinuclear region of cytoplasm Source: Ensembl
  8. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601F → W: No loss of activity or substrate binding. 1 Publication
Mutagenesisi96 – 961P → S: Increased motility of carcinoma cells. 1 Publication
Mutagenesisi118 – 1181H → F: Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells. 2 Publications
Mutagenesisi118 – 1181H → G: Loss of activity. 2 Publications
Mutagenesisi120 – 1201S → A: Limited increase in motility of carcinoma cells. 1 Publication

Organism-specific databases

PharmGKBiPA249.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 152151Nucleoside diphosphate kinase AUniRule annotation
PRO_0000137114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki100 – 100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)UniRule annotation

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP15531.
PaxDbiP15531.
PRIDEiP15531.

2D gel databases

DOSAC-COBS-2DPAGEP15531.
OGPiP15531.

PTM databases

PhosphoSiteiP15531.

Expressioni

Tissue specificityi

Isoform 1 is expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen and thymus. Expressed in lung carcinoma cell lines but not in normal lung tissues. Isoform 2 is ubiquitously expressed and its expression is also related to tumor differentiation. Isoform 3 is ubiquitously expressed.3 Publications

Gene expression databases

ArrayExpressiP15531.
BgeeiP15531.
CleanExiHS_NME1.
GenevestigatoriP15531.

Organism-specific databases

HPAiHPA008467.
HPA041113.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-741141,EBI-741141
Ksr1Q610977EBI-741141,EBI-1536336From a different organism.
MCF2P109114EBI-741141,EBI-1914514
NME2P223922EBI-741141,EBI-713693
PRUNEQ86TP12EBI-741141,EBI-2127112
STRAPQ9Y3F49EBI-741141,EBI-727414
WDYHV1Q96HA83EBI-741141,EBI-741158

Protein-protein interaction databases

BioGridi110894. 46 interactions.
DIPiDIP-39164N.
IntActiP15531. 22 interactions.
MINTiMINT-221462.
STRINGi9606.ENSP00000013034.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43
Beta strandi6 – 116
Helixi13 – 175
Helixi21 – 3111
Beta strandi34 – 418
Helixi45 – 517
Helixi53 – 553
Beta strandi56 – 583
Helixi61 – 699
Beta strandi73 – 808
Helixi83 – 919
Helixi96 – 983
Helixi104 – 1085
Helixi112 – 1143
Beta strandi116 – 1194
Helixi123 – 13311
Helixi136 – 1383
Helixi147 – 1504

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXVX-ray2.20A/B/C/D/E/F1-152[»]
1UCNX-ray2.00A/B/C1-152[»]
2HVDX-ray2.15A/B/C1-152[»]
2HVEX-ray2.40A/B/C1-152[»]
3L7UX-ray2.10A/B/C1-152[»]
4ENOX-ray2.80A/B1-152[»]
ProteinModelPortaliP15531.
SMRiP15531. Positions 1-152.

Miscellaneous databases

EvolutionaryTraceiP15531.

Family & Domainsi

Sequence similaritiesi

Belongs to the NDK family.

Phylogenomic databases

eggNOGiCOG0105.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
KOiK00940.
OMAiCAHEWIY.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP15531.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15531-1) [UniParc]FASTAAdd to Basket

Also known as: NM23-H1A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE    50
HYVDLKDRPF FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK 100
PGTIRGDFCI QVGRNIIHGS DSVESAEKEI GLWFHPEELV DYTSCAQNWI 150
YE 152
Length:152
Mass (Da):17,149
Last modified:April 1, 1990 - v1
Checksum:iAAE9C0DF63CB70A1
GO
Isoform 2 (identifier: P15531-2) [UniParc]FASTAAdd to Basket

Also known as: NM23-H1B

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVLLSTLGIVFQGEGPPISSCDTGTM

Show »
Length:177
Mass (Da):19,654
Checksum:iDEA9961E992D0378
GO
Isoform 3 (identifier: P22392-2) [UniParc]FASTAAdd to Basket

Also known as: NM23-LV

The sequence of this isoform can be found in the external entry P22392.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a naturally occurring readthrough transcript which produces an NME1-NME2 fusion protein.

Length:267
Mass (Da):30,137
GO

Sequence cautioni

The sequence CAA35621.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201S → G in a neuroblastoma sample; increased motility of carcinoma cells. 1 Publication
Corresponds to variant rs121917887 [ dbSNP | Ensembl ].
VAR_004625

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVLLSTLGIVFQGEGPPISS CDTGTM in isoform 2.
VSP_036707

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17620 mRNA. Translation: CAA35621.1. Different initiation.
X73066 mRNA. Translation: CAA51527.1.
X75598 Genomic DNA. Translation: CAA53270.1.
AF487339 mRNA. Translation: AAO85436.1.
AK291105 mRNA. Translation: BAF83794.1.
CR542104 mRNA. Translation: CAG46901.1.
CR542115 mRNA. Translation: CAG46912.1.
AC005839 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94568.1.
BC000293 mRNA. Translation: AAH00293.1.
BC018994 mRNA. Translation: AAH18994.1.
CCDSiCCDS11578.1. [P15531-2]
CCDS11579.1. [P15531-1]
PIRiA33386.
RefSeqiNP_000260.1. NM_000269.2. [P15531-1]
NP_937818.1. NM_198175.1. [P15531-2]
UniGeneiHs.463456.

Genome annotation databases

EnsembliENST00000013034; ENSP00000013034; ENSG00000239672. [P15531-2]
ENST00000336097; ENSP00000337060; ENSG00000239672. [P15531-2]
ENST00000393196; ENSP00000376892; ENSG00000239672. [P15531-1]
GeneIDi4830.
KEGGihsa:4830.
UCSCiuc002ith.2. human. [P15531-2]
uc002iti.2. human. [P15531-1]

Polymorphism databases

DMDMi127981.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17620 mRNA. Translation: CAA35621.1 . Different initiation.
X73066 mRNA. Translation: CAA51527.1 .
X75598 Genomic DNA. Translation: CAA53270.1 .
AF487339 mRNA. Translation: AAO85436.1 .
AK291105 mRNA. Translation: BAF83794.1 .
CR542104 mRNA. Translation: CAG46901.1 .
CR542115 mRNA. Translation: CAG46912.1 .
AC005839 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94568.1 .
BC000293 mRNA. Translation: AAH00293.1 .
BC018994 mRNA. Translation: AAH18994.1 .
CCDSi CCDS11578.1. [P15531-2 ]
CCDS11579.1. [P15531-1 ]
PIRi A33386.
RefSeqi NP_000260.1. NM_000269.2. [P15531-1 ]
NP_937818.1. NM_198175.1. [P15531-2 ]
UniGenei Hs.463456.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JXV X-ray 2.20 A/B/C/D/E/F 1-152 [» ]
1UCN X-ray 2.00 A/B/C 1-152 [» ]
2HVD X-ray 2.15 A/B/C 1-152 [» ]
2HVE X-ray 2.40 A/B/C 1-152 [» ]
3L7U X-ray 2.10 A/B/C 1-152 [» ]
4ENO X-ray 2.80 A/B 1-152 [» ]
ProteinModelPortali P15531.
SMRi P15531. Positions 1-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110894. 46 interactions.
DIPi DIP-39164N.
IntActi P15531. 22 interactions.
MINTi MINT-221462.
STRINGi 9606.ENSP00000013034.

Chemistry

ChEMBLi CHEMBL2159.
DrugBanki DB00441. Gemcitabine.
DB00396. Progesterone.

PTM databases

PhosphoSitei P15531.

Polymorphism databases

DMDMi 127981.

2D gel databases

DOSAC-COBS-2DPAGE P15531.
OGPi P15531.

Proteomic databases

MaxQBi P15531.
PaxDbi P15531.
PRIDEi P15531.

Protocols and materials databases

DNASUi 4830.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000013034 ; ENSP00000013034 ; ENSG00000239672 . [P15531-2 ]
ENST00000336097 ; ENSP00000337060 ; ENSG00000239672 . [P15531-2 ]
ENST00000393196 ; ENSP00000376892 ; ENSG00000239672 . [P15531-1 ]
GeneIDi 4830.
KEGGi hsa:4830.
UCSCi uc002ith.2. human. [P15531-2 ]
uc002iti.2. human. [P15531-1 ]

Organism-specific databases

CTDi 4830.
GeneCardsi GC17P049231.
HGNCi HGNC:7849. NME1.
HPAi HPA008467.
HPA041113.
MIMi 156490. gene.
neXtProti NX_P15531.
PharmGKBi PA249.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0105.
HOGENOMi HOG000224564.
HOVERGENi HBG000423.
KOi K00940.
OMAi CAHEWIY.
OrthoDBi EOG7GJ6FG.
PhylomeDBi P15531.
TreeFami TF106373.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000011052-MONOMER.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTracei P15531.
GeneWikii NME1.
GenomeRNAii 4830.
NextBioi 18606.
PROi P15531.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15531.
Bgeei P15531.
CleanExi HS_NME1.
Genevestigatori P15531.

Family and domain databases

Gene3Di 3.30.70.141. 1 hit.
HAMAPi MF_00451. NDP_kinase.
InterProi IPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view ]
Pfami PF00334. NDK. 1 hit.
[Graphical view ]
PRINTSi PR01243. NUCDPKINASE.
SMARTi SM00562. NDK. 1 hit.
[Graphical view ]
SUPFAMi SSF54919. SSF54919. 1 hit.
PROSITEi PS00469. NDP_KINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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] (ISOFORM 1).
  2. "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme."
    Gilles A.-M., Presecan E., Vonica A., Lascu I.
    J. Biol. Chem. 266:8784-8789(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, ACTIVE SITE.
  3. "Mutation in the nm23 gene is associated with metastasis in colorectal cancer."
    Wang L., Patel U., Ghosh L., Chen H.C., Banerjee S.
    Cancer Res. 53:717-720(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1."
    Dooley S., Seib T., Engel M., Theisinger B., Janz H., Piontek K., Zang K.D., Welter C.
    Hum. Genet. 93:63-66(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  5. "Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1."
    Ni X., Gu S., Dai J., Cheng H., Guo L., Li L., Ji C., Xie Y., Ying K., Mao Y.
    J. Hum. Genet. 48:96-100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 1).
    Tissue: Brain and Lung.
  11. "High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification."
    Hailat N., Keim D.R., Melhem R.F., Zhu X.X., Eckerskorn C., Brodeur G.M., Reynolds C.P., Seeger R.C., Lottspeich F., Strahler J.R., Hanash S.J.
    J. Clin. Invest. 88:341-345(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-18; 40-49 AND 89-94 (ISOFORMS 1/2), DISCUSSION OF THE ROLE IN TUMOR PROGRESSION.
    Tissue: Neuroblastoma.
  12. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-26; 40-49; 57-85 AND 89-128 (ISOFORMS 1/2), IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  13. "Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells."
    MacDonald N.J., Freije J.M., Stracke M.L., Manrow R.E., Steeg P.S.
    J. Biol. Chem. 271:25107-25116(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PRO-96; HIS-118 AND SER-120.
  14. "Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display."
    Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.
    Genomics 61:5-14(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
    Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
    Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SET, IDENTIFICATION IN THE SET COMPLEX.
  16. "Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV."
    Valentijn L.J., Koster J., Versteeg R.
    Genomics 87:483-489(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
    Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
    Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX.
  18. "Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility."
    Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C., Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.
    Oncogene 27:1853-1864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRUNE.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor."
    Min K., Song H.K., Chang C., Kim S.Y., Lee K.J., Suh S.W.
    Proteins 46:340-342(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  22. "Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases."
    Chen Y., Gallois-Montbrun S., Schneider B., Veron M., Morera S., Deville-Bonne D., Janin J.
    J. Mol. Biol. 332:915-926(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF PHE-60 AND HIS-118.
  23. Cited for: VARIANT GLY-120.

Entry informationi

Entry nameiNDKA_HUMAN
AccessioniPrimary (citable) accession number: P15531
Secondary accession number(s): Q6FGK3, Q86XQ2, Q9UDJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The role of this protein in tumor development and progression is uncertain. This protein is found in reduced amount in some tumor cells of high metastatic potential. However, increased NME1 levels correlate with aggressive tumor features in neuroblastoma. May have distinct if not opposite roles in different tumors.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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