S100P

S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.[3][4][5]

S100P
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1J55, 1OZO, 2MJW
Identifiers
Aliases	S100P, MIG9, S100 calcium binding protein P
External IDs	OMIM: 600614 HomoloGene: 81743 GeneCards: S100P
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p16.1 Start 6,693,878 bp[1] End 6,697,170 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • GO:0001948 protein binding • RAGE receptor binding • metal ion binding • calcium-dependent protein binding • magnesium ion binding • cadherin binding • transition metal ion binding • protein homodimerization activity Cellular component • cell membrane • cell projection • extracellular exosome • membrane • cell nucleus • microvillus membrane • cytoplasm • extracellular region • nuclear body • secretory granule lumen Biological process • response to organic substance • endothelial cell migration • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6286	n/a
Ensembl	ENSG00000163993	n/a
UniProt	P25815	n/a
RefSeq (mRNA)	NM_005980	n/a
RefSeq (protein)	NP_005971	n/a
Location (UCSC)	Chr 4: 6.69 – 6.7 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

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]

References

1. GRCh38: Ensembl release 89: ENSG00000163993 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Engelkamp D, Schäfer BW, Mattei MG, Erne P, Heizmann CW (Aug 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. doi:10.1073/pnas.90.14.6547. PMC 46969. PMID 8341667.
4. 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. PMID 7759097.
5. "Entrez Gene: S100P S100 calcium binding protein P".
6. Koltzscher M, Neumann C, König S, Gerke V (Jun 2003). "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Molecular Biology of the Cell. 14 (6): 2372–84. doi:10.1091/mbc.E02-09-0553. PMC 194886. PMID 12808036.
7. Penumutchu SR, Chou RH, Yu C (2014-08-01). "Structural insights into calcium-bound S100P and the V domain of the RAGE complex". PLOS ONE. 9 (8): e103947. doi:10.1371/journal.pone.0103947. PMC 4118983. PMID 25084534.
8. 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. PMID 25450399.

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. 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. doi:10.1016/0006-291X(92)91865-N. 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. doi:10.1111/j.1432-1033.1992.tb17080.x. PMID 1633809.
• 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. doi:10.1021/bi000257+. PMID 10924150.
• 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. 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. doi:10.1021/bi0114731. 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. doi:10.1110/ps.0202202. PMC 2373636. 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.
• 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. PMID 12507480.
• Nowotny M, Spiechowicz M, Jastrzebska B, Filipek A, Kitagawa K, Kuznicki J (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. PMC 194886. 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, 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. 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, 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. PMID 15213440.