S100P

S100P
Available structures PDB Human UniProt search:PDBeRCSB 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;OMA:S100P - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4p16.1 Start 6,693,878bp End 6,697,170bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in nasal epithelium mucosa of urinary bladder palpebral conjunctiva olfactory zone of nasal mucosa bone marrow amniotic fluid periodontal fiber epithelium of nasopharynx pylorus testicle n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding 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 plasma membrane cell projection extracellular exosome membrane 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 PubMedsearch n/a
Wikidata
View/Edit Human

S100calcium-binding protein P(S100P) is aproteinthat in humans is encoded by theS100Pgene.

Function

The protein encoded by this gene is a member of theS100 family of proteinscontaining 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.

Interactions

S100P has been shown tointeractwithEZRand RAGE.The interactions between S100P and RAGE are disrupted by cromolynand pentamidine.

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.
• 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.PMID1633809.
• 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.
• 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.PMC2373636.PMID12021435.
• 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.PMID12042313.
• 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.
• 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.PMID12746458.
• 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.PMC194886.PMID12808036.
• 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.PMID14617629.
• 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.