S100P

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S100 calcium binding protein P
File:PBB Protein S100P image.jpg
PDB rendering based on 1j55.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols S100P ; MIG9
External IDs Template:OMIM5 HomoloGene: 81743
RNA expression pattern
File:PBB GE S100P 204351 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

S100 calcium binding protein P, also known as S100P, is a human gene.[1]

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.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: S100P S100 calcium binding protein P".

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. PMID 8701470.
  • 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. PMID 1540168.
  • Becker T, Gerke V, Kube E, Weber K (1992). "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. PMID 1633809.
  • Schäfer BW, Wicki R, Engelkamp D; et al. (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. PMID 7759097.
  • Engelkamp D, Schäfer BW, Mattei MG; et al. (1993). "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. PMID 8341667.
  • 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. PMID 9784376.
  • 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. PMID 10924150.
  • Harvell JD, Fulton R, Jones CD; et al. (2001). "Composite dendritic cell neoplasm (NOS) and small lymphocytic lymphoma". Appl. Immunohistochem. Mol. Morphol. 8 (4): 322–8. PMID 11127925.
  • 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. PMID 11747429.
  • Gribenko AV, Guzmán-Casado M, Lopez MM, Makhatadze GI (2003). "Conformational and thermodynamic properties of peptide binding to the human S100P protein". Protein Sci. 11 (6): 1367–75. PMID 12021435.
  • Filipek A, Jastrzebska B, Nowotny M, Kuznicki J (2002). "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family". J. Biol. Chem. 277 (32): 28848–52. doi:10.1074/jbc.M203602200. PMID 12042313.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Zhang H, Wang G, Ding Y; et al. (2003). "The crystal structure at 2A resolution of the Ca2+ -binding protein S100P". J. Mol. Biol. 325 (4): 785–94. PMID 12507480.
  • Nowotny M, Spiechowicz M, Jastrzebska B; et al. (2003). "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins". J. Biol. Chem. 278 (29): 26923–8. doi:10.1074/jbc.M211518200. PMID 12746458.
  • Koltzscher M, Neumann C, König S, Gerke V (2004). "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Mol. Biol. Cell. 14 (6): 2372–84. doi:10.1091/mbc.E02-09-0553. PMID 12808036.
  • Arumugam T, Simeone DM, Schmidt AM, Logsdon CD (2004). "S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE)". J. Biol. Chem. 279 (7): 5059–65. doi:10.1074/jbc.M310124200. PMID 14617629.
  • Jin G, Wang S, Hu X; et al. (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. PMID 14672411.
  • 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. PMID 14716296.
  • Lee YC, Volk DE, Thiviyanathan V; et al. (2005). "NMR structure of the Apo-S100P protein". J. Biomol. NMR. 29 (3): 399–402. doi:10.1023/B:JNMR.0000032617.88899.4b. PMID 15213440.

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