Biology:S100P
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.[1][2][3]
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.[3]
Interactions
S100P has been shown to interact with EZR[4] and RAGE.[5] The interactions between S100P and RAGE are disrupted by cromolyn[6] and pentamidine.[5]
References
- ↑ "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proc Natl Acad Sci U S A 90 (14): 6547–51. Aug 1993. doi:10.1073/pnas.90.14.6547. PMID 8341667. Bibcode: 1993PNAS...90.6547E.
- ↑ "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. Jun 1995. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
- ↑ 3.0 3.1 "Entrez Gene: S100P S100 calcium binding protein P". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6286.
- ↑ "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Molecular Biology of the Cell 14 (6): 2372–84. Jun 2003. doi:10.1091/mbc.E02-09-0553. PMID 12808036.
- ↑ 5.0 5.1 "Structural insights into calcium-bound S100P and the V domain of the RAGE complex". PLOS ONE 9 (8): e103947. 2014-08-01. doi:10.1371/journal.pone.0103947. PMID 25084534. Bibcode: 2014PLoSO...9j3947P.
- ↑ "Interaction between S100P and the anti-allergy drug cromolyn". Biochemical and Biophysical Research Communications 454 (3): 404–409. Oct 2014. doi:10.1016/j.bbrc.2014.10.048. PMID 25450399.
Further reading
- "The S100 family of EF-hand calcium-binding proteins: functions and pathology.". Trends Biochem. Sci. 21 (4): 134–40. 1996. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
- "Purification and characterization of a new member of the S-100 protein family from human placenta.". Biochem. Biophys. Res. Commun. 182 (3): 1246–53. 1992. doi:10.1016/0006-291X(92)91865-N. PMID 1540168.
- "S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties.". Eur. J. Biochem. 207 (2): 541–7. 1992. doi:10.1111/j.1432-1033.1992.tb17080.x. PMID 1633809.
- "Oligomerization and divalent ion binding properties of the S100P protein: a Ca2+/Mg2+-switch model.". J. Mol. Biol. 283 (3): 679–94. 1998. doi:10.1006/jmbi.1998.2116. PMID 9784376.
- "Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo.". Biochemistry 39 (31): 9533–9. 2000. doi:10.1021/bi000257+. PMID 10924150.
- "Composite dendritic cell neoplasm (NOS) and small lymphocytic lymphoma.". Appl. Immunohistochem. Mol. Morphol. 8 (4): 322–8. 2001. doi:10.1097/00022744-200012000-00010. PMID 11127925.
- "Molecular characterization and tissue distribution of a novel member of the S100 family of EF-hand proteins.". Biochemistry 40 (51): 15538–48. 2002. doi:10.1021/bi0114731. PMID 11747429.
- "Conformational and thermodynamic properties of peptide binding to the human S100P protein.". Protein Sci. 11 (6): 1367–75. 2003. doi:10.1110/ps.0202202. PMID 12021435.
- "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family.". J. Biol. Chem. 277 (32): 28848–52. 2002. doi:10.1074/jbc.M203602200. PMID 12042313.
- "The crystal structure at 2A resolution of the Ca2+ -binding protein S100P.". J. Mol. Biol. 325 (4): 785–94. 2003. doi:10.1016/S0022-2836(02)01278-0. PMID 12507480.
- "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins.". J. Biol. Chem. 278 (29): 26923–8. 2003. doi:10.1074/jbc.M211518200. PMID 12746458.
- "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P.". Mol. Biol. Cell 14 (6): 2372–84. 2004. doi:10.1091/mbc.E02-09-0553. PMID 12808036.
- "S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE).". J. Biol. Chem. 279 (7): 5059–65. 2004. doi:10.1074/jbc.M310124200. PMID 14617629.
- "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. 2004. doi:10.1023/A:1026311423326. PMID 14672411.
- "Identification of maspin and S100P as novel hypomethylation targets in pancreatic cancer using global gene expression profiling.". Oncogene 23 (8): 1531–8. 2004. doi:10.1038/sj.onc.1207269. PMID 14716296.
- "NMR structure of the Apo-S100P protein.". J. Biomol. NMR 29 (3): 399–402. 2005. doi:10.1023/B:JNMR.0000032617.88899.4b. PMID 15213440.
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