S100P

S100 calcium binding protein P

PDB rendering based on 1j55.

Available structures
PDB	1J55, 1OZO

Identifiers

Symbols

S100P; MIG9

External IDs

OMIM: 600614 HomoloGene: 81743 GeneCards: S100P Gene

Gene Ontology
Molecular function	• magnesium ion binding • calcium ion binding • protein binding • calcium-dependent protein binding
Cellular component	• nucleus • cytoplasm • cytoplasm
Biological process	• endothelial cell migration
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

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

[1]

n/a

Protein S100-P is a protein that in humans is encoded by the S100P gene.^[1]^[2]^[3]

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]

References

^ Engelkamp D, Schafer 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=46969.
^ Schafer 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.
^ ^a ^b "Entrez Gene: S100P S100 calcium binding protein P". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6286.
^ Koltzscher, Max; Neumann Claudia, König Simone, Gerke Volker (Jun. 2003). "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P". Mol. Biol. Cell (United States) 14 (6): 2372–84. doi:10.1091/mbc.E02-09-0553. ISSN 1059-1524. PMC 194886. PMID 12808036. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=194886.

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. 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, 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2373636.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. doi:10.1016/S0022-2836(02)01278-0. 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. PMC 194886. PMID 12808036. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=194886.
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. 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, 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.

PDB gallery

1j55: The Crystal Structure of Ca+-bound Human S100P Determined at 2.0A Resolution by X-ray

1ozo: Three-dimensional solution structure of apo-S100P protein determined by NMR spectroscopy

S100P

Interactions

References

Further reading