S100P

Protein-coding gene in the species Homo sapiens
S100P
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

1J55, 1OZO, 2MJW

Identifiers
AliasesS100P, MIG9, S100 calcium binding protein P
External IDsOMIM: 600614; HomoloGene: 81743; GeneCards: S100P; OMA:S100P - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for S100P
Genomic location for S100P
Band4p16.1Start6,693,878 bp[1]
End6,697,170 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of urinary bladder

  • palpebral conjunctiva

  • bone marrow

  • amniotic fluid

  • periodontal fiber

  • pylorus

  • gastric mucosa

  • trabecular bone

  • urethra

  • rectum
    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
SpeciesHumanMouse
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 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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

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. ^ a b c 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. Bibcode:1993PNAS...90.6547E. 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. ^ a b "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. ^ a b 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. Bibcode:2014PLoSO...9j3947P. 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. S2CID 2276667.
  • 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. S2CID 8156903.
  • 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. S2CID 86444278.


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