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Gene Review

NUCKS1  -  nuclear casein kinase and cyclin-dependent...

Homo sapiens

Synonyms: JC7, NUCKS, Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1, P1
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Disease relevance of NUCKS1

  • One of these (P1), which has significant sequence homology to the cytomegalovirus IE2 protein, binds with high affinity to the N-terminal domain of CK2beta without disrupting the formation of the CK2 holoenzyme [1].
  • Potato spindle tuber viroid (PSTV), a small infectios RNA, has been completely digested with RNase T1 and RNase A, and the resulting oligonucleotides have been sequenced using 5'-terminal 32p-labelling with gamma-32p ATP and T4 polynucleotide kinase, fingerprinting and controlled nuclease P1 digestion [2].
  • A major determinant of neurovirulence for the GDVII strain of Theiler's virus, a murine picornavirus, was mapped to the P1 capsid protein region [3].
  • Immunogenicity of synthetic peptides of Haemophilus influenzae type b outer membrane protein P1 [4].
  • In the present study, we investigated whether P1 agonist-induced Cl- secretion is preserved in cystic fibrosis airway epithelium and which signalling mechanism is involved [5].

Psychiatry related information on NUCKS1


High impact information on NUCKS1

  • The activated mutant, hbetacFIDelta, is able to confer growth factor-independent proliferation on the murine myeloid cell line FDC-P1, and on primary committed myeloid progenitors [7].
  • Passage 1 (P1) and P10 cells have identical morphology, immunophenotype, telomere length, and differentiation capacity [8].
  • It appears that in adipocytes, P1 3-kinase prevents activation of GAP [9].
  • Despite a negative effect on intrinsic Abl kinase activity, both P210 SH2 mutants were still able to transform the hematopoietic factor-dependent cell lines Ba/F3 and FDC-P1 to growth factor independence [10].
  • Therefore, expression of the Harvey RAS oncogene in FDC-P1 myeloid cells leads to at least two pathways of cytoplasmic signaling [11].

Chemical compound and disease context of NUCKS1

  • Statistical analysis revealed that the incidence of promoter hypermethylation of any single gene, of multiple genes, or of glutathione S -transferase P1 was significantly associated with atypical and anaplastic meningiomas ( P < .0001, P = .004, and P = .004, respectively) [12].
  • Stimulation of chloride secretion by P1 purinoceptor agonists in cystic fibrosis phenotype airway epithelial cell line CFPEo- [5].
  • Tamoxifen prevention still remains contentious, with a significant reduction in risk of breast cancer in women given tamoxifen in the NSABP P1 study but no effect in the Italian and Royal Marsden trials [13].

Biological context of NUCKS1

  • In all the species investigated, the protein contains several consensus phosphorylation sites for cyclin-dependent kinases and CK-2, and we have shown that the fish protein (like mammalian NUCKS) indeed is a substrate for CDK1 and CK-2 in vitro [14].
  • Characterisation of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species [14].
  • The NUCKS gene is located on human chromosome 1q32.1 and consists of seven exons and six introns [14].
  • Phosphopeptide mapping and back-phosphorylation experiments employing NUCKS from HeLa interphase and metaphase cells show that the protein is phosphorylated by Cdk1 during mitosis of the cell cycle [15].
  • Retroviral expression vectors carrying the tyrosine kinase oncogenes abl, fms, src, and trk abrogate the requirements of murine myeloid FDC-P1 cells for interleukin-3 (IL-3) [16].

Anatomical context of NUCKS1

  • We have isolated variant cell lines from FDC-P1 that grow in response to phorbol myristate acetate (PMA) [17].
  • Preincubation of human granules with calcium, a treatment which totally inactivates the hemolytic and cytotoxic activity of murine lymphocyte granules [perforin 1 (P1)] had no effect on human LAK granule cytotoxicity for nucleated cells [18].
  • In addition, Northern blot analysis of polyadenylated RNA isolated from human LAK cells using a murine P1 complementary DNA probe showed a cross-hybridizing 2.8- to 3.0-kilobase mRNA species identical in size to murine P1 mRNA [18].
  • Transcriptional start sites were identified in parathyroid gland and TT cells; that for promoter P1 lies 27 bp downstream of a TATA box, whereas that for promoter P2, which lacks a TATA box, lies in a GC-rich region [19].
  • All hydrophobic amino acid substitutions were transforming when tested in FDC-P1 cells yet inactivating when tested in Rat-2 fibroblasts [20].

Associations of NUCKS1 with chemical compounds

  • We have previously reported transformation to growth factor-independent proliferation in the interleukin-3 (IL-3)-dependent cell line FDC-P1 by high-level expression of the valine 12 Harvey RAS oncogene, following from a nonautocrine mechanism [11].
  • Like the papain protease family, SspB cleaved substrates with a hydrophobic amino acid at P2 but had a strong preference for arginine at P1 [21].
  • The present work describes the detection, purification, and characterization of a serine endopeptidase with preference for a phosphoserine in the P1' position of the substrate [22].
  • The site P1 (position -1 relative to the cleavage site) is mainly leucine [23].
  • The effects of P1 and verapamil on drug accumulation in MCF7-MDR cells were additive [24].

Analytical, diagnostic and therapeutic context of NUCKS1

  • Both data searches and Western immunoblotting experiments show that a homologous protein is present in fish, amphibians, and birds but not in insects and yeast, suggesting that NUCKS is a vertebrate specific gene [14].
  • Northern blot analyses revealed that human and rat tissues contain three NUCKS transcripts varying in size from 1.5 to 6.5 kb [15].
  • By partial sequence analysis, this protein was identified as the 60 kDa human heat-shock protein (hsp) that is the P1 mitochondrial protein, and which is 50% homologous to the mycobacterial 65 kDa hsp [25].
  • Fluorescence in situ hybridization analysis with P1 and cosmid probes containing D9S126 also confirmed these data [26].
  • Chromatin immunoprecipitation assay results also confirm that LMP1 activates P1 promoter via the JNK-AP-1 pathway [27].


  1. p53-dependent inhibition of mammalian cell survival by a genetically selected peptide aptamer that targets the regulatory subunit of protein kinase CK2. Martel, V., Filhol, O., Colas, P., Cochet, C. Oncogene (2006) [Pubmed]
  2. Studies on the primary and secondary structure of potato spindle tuber viroid: products of digestion with ribonuclease A and ribonuclease T1, and modification with bisulfite. Domdey, H., Jank, P., Sänger, L., Gross, H.J. Nucleic Acids Res. (1978) [Pubmed]
  3. Assembly of Theiler's virus recombinants used in mapping determinants of neurovirulence. Pritchard, A.E., Jensen, K., Lipton, H.L. J. Virol. (1993) [Pubmed]
  4. Immunogenicity of synthetic peptides of Haemophilus influenzae type b outer membrane protein P1. Chong, P., Yang, Y.P., Persaud, D., Haer, M., Tripet, B., Tam, E., Sia, C., Klein, M. Infect. Immun. (1995) [Pubmed]
  5. Stimulation of chloride secretion by P1 purinoceptor agonists in cystic fibrosis phenotype airway epithelial cell line CFPEo-. Chao, A.C., Zifferblatt, J.B., Wagner, J.A., Dong, Y.J., Gruenert, D.C., Gardner, P. Br. J. Pharmacol. (1994) [Pubmed]
  6. Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases. Zhao, Y., Loyer, P., Li, H., Valentine, V., Kidd, V., Kraft, A.S. J. Biol. Chem. (1997) [Pubmed]
  7. Dysregulated hematopoiesis and a progressive neurological disorder induced by expression of an activated form of the human common beta chain in transgenic mice. D'Andrea, R.J., Harrison-Findik, D., Butcher, C.M., Finnie, J., Blumbergs, P., Bartley, P., McCormack, M., Jones, K., Rowland, R., Gonda, T.J., Vadas, M.A. J. Clin. Invest. (1998) [Pubmed]
  8. Isolation of multipotent progenitor cells from human fetal liver capable of differentiating into liver and mesenchymal lineages. Dan, Y.Y., Riehle, K.J., Lazaro, C., Teoh, N., Haque, J., Campbell, J.S., Fausto, N. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  9. Functional interactions of phosphatidylinositol 3-kinase with GTPase-activating protein in 3T3-L1 adipocytes. DePaolo, D., Reusch, J.E., Carel, K., Bhuripanyo, P., Leitner, J.W., Draznin, B. Mol. Cell. Biol. (1996) [Pubmed]
  10. The SH2 domain of P210BCR/ABL is not required for the transformation of hematopoietic factor-dependent cells. Ilaria, R.L., Van Etten, R.A. Blood (1995) [Pubmed]
  11. Dissociation of nuclear events on p21 RAS transformation of FDC-P1 myeloid cells: c-jun/AP-1 expression versus c-myc transcription. Litz-Jackson, S., Miller, A.H., Burgess, G.S., Boswell, H.S. Blood (1992) [Pubmed]
  12. Aberrant CpG island hypermethylation profile is associated with atypical and anaplastic meningiomas. Liu, Y., Pang, J.C., Dong, S., Mao, B., Poon, W.S., Ng, H.K. Hum. Pathol. (2005) [Pubmed]
  13. 14. Breast cancer prevention. Salih, A.K., Fentiman, I.S. International journal of clinical practice. (2002) [Pubmed]
  14. Characterisation of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species. Grundt, K., Haga, I.V., Aleporou-Marinou, V., Drosos, Y., Wanvik, B., Østvold, A.C. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  15. Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo. Ostvold, A.C., Norum, J.H., Mathiesen, S., Wanvik, B., Sefland, I., Grundt, K. Eur. J. Biochem. (2001) [Pubmed]
  16. Tyrosine kinase oncogenes abrogate interleukin-3 dependence of murine myeloid cells through signaling pathways involving c-myc: conditional regulation of c-myc transcription by temperature-sensitive v-abl. Cleveland, J.L., Dean, M., Rosenberg, N., Wang, J.Y., Rapp, U.R. Mol. Cell. Biol. (1989) [Pubmed]
  17. Effects of phorbol esters on an interleukin-3-dependent cell line. McCubrey, J.A., Steelman, L.S., Sandlin, G., Riddle, R.S., Ways, D.K. Blood (1990) [Pubmed]
  18. Isolation and characterization of cytotoxic granules from human lymphokine (interleukin 2) activated killer cells. Lowrey, D.M., Hameed, A., Lichtenheld, M., Podack, E.R. Cancer Res. (1988) [Pubmed]
  19. Human calcium-sensing receptor gene. Vitamin D response elements in promoters P1 and P2 confer transcriptional responsiveness to 1,25-dihydroxyvitamin D. Canaff, L., Hendy, G.N. J. Biol. Chem. (2002) [Pubmed]
  20. Cell specific transformation by c-fms activating loop mutations is attributable to constitutive receptor degradation. Morley, G.M., Uden, M., Gullick, W.J., Dibb, N.J. Oncogene (1999) [Pubmed]
  21. Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus. Massimi, I., Park, E., Rice, K., Muller-Esterl, W., Sauder, D., McGavin, M.J. J. Biol. Chem. (2002) [Pubmed]
  22. A human serine endopeptidase, purified with respect to activity against a peptide with phosphoserine in the P1' position, is apparently identical with prolyl endopeptidase. Rosén, J., Tomkinson, B., Pettersson, G., Zetterqvist, O. J. Biol. Chem. (1991) [Pubmed]
  23. A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii. Yokoyama, H., Matsui, I. J. Biol. Chem. (2005) [Pubmed]
  24. Partial reversal of multidrug resistance in human breast cancer cells by an N-myristoylated protein kinase C-alpha pseudosubstrate peptide. Gupta, K.P., Ward, N.E., Gravitt, K.R., Bergman, P.J., O'Brian, C.A. J. Biol. Chem. (1996) [Pubmed]
  25. Antibodies to the human 60 kDa heat-shock protein in patients with schizophrenia. Kilidireas, K., Latov, N., Strauss, D.H., Gorig, A.D., Hashim, G.A., Gorman, J.M., Sadiq, S.A. Lancet (1992) [Pubmed]
  26. Identification of a novel region of homozygous deletion on chromosome 9p in squamous cell carcinoma of the lung: the location of a putative tumor suppressor gene. Wiest, J.S., Franklin, W.A., Otstot, J.T., Forbey, K., Varella-Garcia, M., Rao, K., Drabkin, H., Gemmill, R., Ahrent, S., Sidransky, D., Saccomanno, G., Fountain, J.W., Anderson, M.W. Cancer Res. (1997) [Pubmed]
  27. Activation of DNA methyltransferase 1 by EBV LMP1 Involves c-Jun NH(2)-terminal kinase signaling. Tsai, C.L., Li, H.P., Lu, Y.J., Hsueh, C., Liang, Y., Chen, C.L., Tsao, S.W., Tse, K.P., Yu, J.S., Chang, Y.S. Cancer Res. (2006) [Pubmed]
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