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Gene Review

CSN1S1  -  casein alpha s1

Homo sapiens

Synonyms: Alpha-S1-casein, CASA, CSN1
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Disease relevance of CSN1S1


Psychiatry related information on CSN1S1


High impact information on CSN1S1


Chemical compound and disease context of CSN1S1


Biological context of CSN1S1

  • From qPCR data, the four casein transcripts appeared to be present approximately at the same level of abundance (ca. 25%, except for defective genotypes at the CSN1S1 locus, in the goat) whereas the amounts of the corresponding proteins in milk were ranging between 9 and 38% of the whole casein fraction [21].
  • In addition, two cryptic exons were localized in the bovine alpha s1-casein gene [22].
  • The casein gene family was localized to chromosome 4q21.1 by FISH analysis [23].
  • Five yeast artificial chromosome (YAC) clones containing the human casein gene family were isolated and characterized to study the control mechanisms for the expression of these genes [23].
  • Amino acid sequence analysis of the closely spaced bands all resulted in the same N-terminal sequence which was found to be homologous with alpha s1-casein from other species [24].

Anatomical context of CSN1S1

  • Human alpha s1-casein has been reported to exist naturally as a multimer in complex with kappa-casein in mature human milk, thereby being unique among alpha s1-caseins [Rasmussen, Due and Petersen (1995) Comp. Biochem. Physiol., in the press] [22].
  • GC kinase immunoprecipitated from transfected COS cells phosphorylated the substrates casein and myelin basic protein [25].
  • Casein kinase II activity does not change during oocyte maturation, and therefore, cannot be responsible for the activation of translation [26].
  • Two-hundred twenty subjects provided a semen sample for computer-aided sperm analysis (CASA) and a urine sample for measurement of phthalate monoesters, monoethyl (MEP), monobenzyl (MBzP), mono-n-butyl (MBP), mono-2-ethylhexyl (MEHP), and monomethyl (MMP) [27].
  • Pre-treatment of human neutrophils with myelin basic protein selectively inhibits the formyl-peptide-induced chemotaxis, without affecting chemotaxis evoked by casein and activated serum [28].

Associations of CSN1S1 with chemical compounds


Physical interactions of CSN1S1


Enzymatic interactions of CSN1S1

  • Here, we report that BACE can be phosphorylated within its cytoplasmic domain at serine residue 498 by casein kinase 1 [37].
  • In this report, we demonstrate that mammalian Cdc37 is phosphorylated on Ser13 in situ in rabbit reticulocyte lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphorylating recombinant Cdc37 at this site [38].
  • These results demonstrate that the hER is phosphorylated on serine 167 by casein kinase II in a hormone-dependent manner [39].
  • The human 1,25-dihydroxyvitamin D3 receptor (hVDR) has been recently shown to be phosphorylated in vitro by casein kinase-II [40].
  • Furthermore, human casein enhanced t-PA-catalyzed plasminogen activation, comparable to the enhancing effect obtained with fibrinogen fragments [41].

Co-localisations of CSN1S1

  • Casein autography of isolated platelets revealed a approximately 90 kDa band of activity which comigrated with plasma prekallikrein (PK)/kallikrein, a known activator of pro-UK [42].

Regulatory relationships of CSN1S1


Other interactions of CSN1S1


Analytical, diagnostic and therapeutic context of CSN1S1

  • Here we report the molecular cloning and sequencing of three types of human alpha s1-casein transcripts and present evidence indicating that exon skipping is responsible for deleted mRNA transcripts [22].
  • Tissue-specific expression of human alpha s1-casein was indicated by Northern-blot analysis [22].
  • Partial restriction analysis in conjunction with the chromosomal fragmentation method and fluorescence in situ hybridization (FISH) analysis were performed to construct a detailed physical map of the casein gene family and to determine the chromosomal localization of these genes [23].
  • The relative proportions of each specific messenger (% of casein mRNA) were compared to the relative amounts of the corresponding caseins (% of whole casein) in milks sampled from the same animals, determined after fractionation by reverse phase HPLC and integration of the corresponding peak areas [21].
  • The human counterpart of alpha s1-casein has been purified by a combination of gel-filtration and ion-exchange chromatography under denaturing conditions [24].


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  12. Monopolar attachment of sister kinetochores at meiosis I requires casein kinase 1. Petronczki, M., Matos, J., Mori, S., Gregan, J., Bogdanova, A., Schwickart, M., Mechtler, K., Shirahige, K., Zachariae, W., Nasmyth, K. Cell (2006) [Pubmed]
  13. A one-sided view of kinetochore attachment in meiosis. Watanabe, Y. Cell (2006) [Pubmed]
  14. Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase I and MEKK1. Zhu, J., Shibasaki, F., Price, R., Guillemot, J.C., Yano, T., Dötsch, V., Wagner, G., Ferrara, P., McKeon, F. Cell (1998) [Pubmed]
  15. Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes. Fan, H., Sakulich, A.L., Goodier, J.L., Zhang, X., Qin, J., Maraia, R.J. Cell (1997) [Pubmed]
  16. A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network. Alconada, A., Bauer, U., Hoflack, B. EMBO J. (1996) [Pubmed]
  17. Urea cycle enzyme activities are normal and inducible by a high-protein diet in CCl4 cirrhosis of rats. Snodgrass, P.J. Hepatology (1989) [Pubmed]
  18. The MYCN protein of human neuroblastoma cells is phosphorylated by casein kinase II in the central region and at serine 367. Hamann, U., Wenzel, A., Frank, R., Schwab, M. Oncogene (1991) [Pubmed]
  19. Influence of vegetable protein on gallstone formation in hamsters. Kritchevsky, D., Klurfeld, D.M. Am. J. Clin. Nutr. (1979) [Pubmed]
  20. Phosphorylation at the carboxy terminus of the 55-kilodalton adenovirus type 5 E1B protein regulates transforming activity. Teodoro, J.G., Halliday, T., Whalen, S.G., Takayesu, D., Graham, F.L., Branton, P.E. J. Virol. (1994) [Pubmed]
  21. Translational efficiency of casein transcripts in the mammary tissue of lactating ruminants. Bevilacqua, C., Helbling, J.C., Miranda, G., Martin, P. Reprod. Nutr. Dev. (2006) [Pubmed]
  22. Characterization of three types of human alpha s1-casein mRNA transcripts. Johnsen, L.B., Rasmussen, L.K., Petersen, T.E., Berglund, L. Biochem. J. (1995) [Pubmed]
  23. Genomic organization and chromosomal localization of the human casein gene family. Fujiwara, Y., Miwa, M., Nogami, M., Okumura, K., Nobori, T., Suzuki, T., Ueda, M. Hum. Genet. (1997) [Pubmed]
  24. Human alpha s1-casein: purification and characterization. Rasmussen, L.K., Due, H.A., Petersen, T.E. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1995) [Pubmed]
  25. Differential expression of a novel protein kinase in human B lymphocytes. Preferential localization in the germinal center. Katz, P., Whalen, G., Kehrl, J.H. J. Biol. Chem. (1994) [Pubmed]
  26. Maturation hormone induced an increase in the translational activity of starfish oocytes coincident with the phosphorylation of the mRNA cap binding protein, eIF-4E, and the activation of several kinases. Xu, Z., Dholakia, J.N., Hille, M.B. Dev. Genet. (1993) [Pubmed]
  27. The relationship between environmental exposure to phthalates and computer-aided sperm analysis motion parameters. Duty, S.M., Calafat, A.M., Silva, M.J., Brock, J.W., Ryan, L., Chen, Z., Overstreet, J., Hauser, R. J. Androl. (2004) [Pubmed]
  28. Myelin basic protein inhibits formyl-peptide induced chemotaxis in human neutrophils. Bellini, T., Dallocchio, F., Degani, D., Spisani, S., Gavioli, R., Traniello, S. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  29. In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase. Ren, M., Zeng, J., De Lemos-Chiarandini, C., Rosenfeld, M., Adesnik, M., Sabatini, D.D. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  30. Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. Sato, S., Cerny, R.L., Buescher, J.L., Ikezu, T. J. Neurochem. (2006) [Pubmed]
  31. Molecular cloning and expression of a unique receptor-like protein-tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate family. Zhang, W.R., Hashimoto, N., Ahmad, F., Ding, W., Goldstein, B.J. Biochem. J. (1994) [Pubmed]
  32. Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex. Gao, Z.H., Seeling, J.M., Hill, V., Yochum, A., Virshup, D.M. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  33. Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. Pflum, M.K., Tong, J.K., Lane, W.S., Schreiber, S.L. J. Biol. Chem. (2001) [Pubmed]
  34. Alterations in C3 activation and binding caused by phosphorylation by a casein kinase released from activated human platelets. Ekdahl, K.N., Nilsson, B. J. Immunol. (1999) [Pubmed]
  35. Casein kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity. Lin, A., Frost, J., Deng, T., Smeal, T., al-Alawi, N., Kikkawa, U., Hunter, T., Brenner, D., Karin, M. Cell (1992) [Pubmed]
  36. The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation. Kaiser, K., Stelzer, G., Meisterernst, M. EMBO J. (1995) [Pubmed]
  37. Phosphorylation regulates intracellular trafficking of beta-secretase. Walter, J., Fluhrer, R., Hartung, B., Willem, M., Kaether, C., Capell, A., Lammich, S., Multhaup, G., Haass, C. J. Biol. Chem. (2001) [Pubmed]
  38. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. Shao, J., Prince, T., Hartson, S.D., Matts, R.L. J. Biol. Chem. (2003) [Pubmed]
  39. Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Arnold, S.F., Obourn, J.D., Jaffe, H., Notides, A.C. Mol. Endocrinol. (1994) [Pubmed]
  40. Vitamin D receptor phosphorylation in transfected ROS 17/2.8 cells is localized to the N-terminal region of the hormone-binding domain. Jones, B.B., Jurutka, P.W., Haussler, C.A., Haussler, M.R., Whitfield, G.K. Mol. Endocrinol. (1991) [Pubmed]
  41. Plasminogen activation system in human milk. Heegaard, C.W., Larsen, L.B., Rasmussen, L.K., Højberg, K.E., Petersen, T.E., Andreasen, P.A. J. Pediatr. Gastroenterol. Nutr. (1997) [Pubmed]
  42. Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: a mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Loza, J.P., Gurewich, V., Johnstone, M., Pannell, R. Thromb. Haemost. (1994) [Pubmed]
  43. Effect of yak milk casein hydrolysate on TH1/TH2 cytokines production by murine spleen lymphocytes in vitro. Mao, X.Y., Yang, H.Y., Song, J.P., Li, Y.H., Ren, F.Z. J. Agric. Food Chem. (2007) [Pubmed]
  44. Sensitization of tumor cells to Apo2 ligand/TRAIL-induced apoptosis by inhibition of casein kinase II. Ravi, R., Bedi, A. Cancer Res. (2002) [Pubmed]
  45. Mechanism of stimulation of human DNA ligase I by the Rad9-rad1-Hus1 checkpoint complex. Wang, W., Lindsey-Boltz, L.A., Sancar, A., Bambara, R.A. J. Biol. Chem. (2006) [Pubmed]
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  47. HPV-16 E7 and adenovirus E1a complex formation with TATA box binding protein is enhanced by casein kinase II phosphorylation. Massimi, P., Pim, D., Storey, A., Banks, L. Oncogene (1996) [Pubmed]
  48. Activation of a Ca2+-inhibitable protein kinase that phosphorylates microtubule-associated protein 2 in vitro by growth factors, phorbol esters, and serum in quiescent cultured human fibroblasts. Hoshi, M., Nishida, E., Sakai, H. J. Biol. Chem. (1988) [Pubmed]
  49. Phosphorylation of the regulatory subunit of type II beta cAMP-dependent protein kinase by cyclin B/p34cdc2 kinase impairs its binding to microtubule-associated protein 2. Keryer, G., Luo, Z., Cavadore, J.C., Erlichman, J., Bornens, M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
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  51. Autotaxin is an exoenzyme possessing 5'-nucleotide phosphodiesterase/ATP pyrophosphatase and ATPase activities. Clair, T., Lee, H.Y., Liotta, L.A., Stracke, M.L. J. Biol. Chem. (1997) [Pubmed]
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