S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100Pgene.[3][4][5]
Function
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21; however, this gene is located at 4p16. This protein, in addition to binding Ca2+, also binds Zn2+ and Mg2+. This protein may play a role in the etiology of prostate cancer.[5]
Interactions
S100P has been shown to interact with EZR[6] and RAGE.[7] The interactions between S100P and RAGE are disrupted by cromolyn[8] and pentamidine.[7]
^Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (Jun 1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638–43. doi:10.1016/0888-7543(95)80005-7. PMID7759097.
^Penumutchu SR, Chou RH, Yu C (Oct 2014). "Interaction between S100P and the anti-allergy drug cromolyn". Biochemical and Biophysical Research Communications. 454 (3): 404–409. doi:10.1016/j.bbrc.2014.10.048. PMID25450399.
Further reading
Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID8701470.
Emoto Y, Kobayashi R, Akatsuka H, Hidaka H (1992). "Purification and characterization of a new member of the S-100 protein family from human placenta". Biochem. Biophys. Res. Commun. 182 (3): 1246–53. doi:10.1016/0006-291X(92)91865-N. PMID1540168.
Gribenko AV, Makhatadze GI (1998). "Oligomerization and divalent ion binding properties of the S100P protein: a Ca2+/Mg2+-switch model". J. Mol. Biol. 283 (3): 679–94. doi:10.1006/jmbi.1998.2116. PMID9784376.
Koltzscher M, Gerke V (2000). "Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo". Biochemistry. 39 (31): 9533–9. doi:10.1021/bi000257+. PMID10924150.
Harvell JD, Fulton R, Jones CD, Terris DJ, Warnke RA (2001). "Composite dendritic cell neoplasm (NOS) and small lymphocytic lymphoma". Appl. Immunohistochem. Mol. Morphol. 8 (4): 322–8. doi:10.1097/00022744-200012000-00010. PMID11127925.
Gribenko AV, Hopper JE, Makhatadze GI (2002). "Molecular characterization and tissue distribution of a novel member of the S100 family of EF-hand proteins". Biochemistry. 40 (51): 15538–48. doi:10.1021/bi0114731. PMID11747429.
Zhang H, Wang G, Ding Y, Wang Z, Barraclough R, Rudland PS, Fernig DG, Rao Z (2003). "The crystal structure at 2A resolution of the Ca2+ -binding protein S100P". J. Mol. Biol. 325 (4): 785–94. doi:10.1016/S0022-2836(02)01278-0. PMID12507480.
Jin G, Wang S, Hu X, Jing Z, Chen J, Ying K, Xie Y, Mao Y (2004). "Characterization of the tissue-specific expression of the s100P gene which encodes an EF-hand Ca2+-binding protein". Mol. Biol. Rep. 30 (4): 243–8. doi:10.1023/A:1026311423326. PMID14672411. S2CID2276667.
Sato N, Fukushima N, Matsubayashi H, Goggins M (2004). "Identification of maspin and S100P as novel hypomethylation targets in pancreatic cancer using global gene expression profiling". Oncogene. 23 (8): 1531–8. doi:10.1038/sj.onc.1207269. PMID14716296. S2CID8156903.
Lee YC, Volk DE, Thiviyanathan V, Kleerekoper Q, Gribenko AV, Zhang S, Gorenstein DG, Makhatadze GI, Luxon BA (2005). "NMR structure of the Apo-S100P protein". J. Biomol. NMR. 29 (3): 399–402. doi:10.1023/B:JNMR.0000032617.88899.4b. PMID15213440. S2CID86444278.
