S100P

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)
End	6,697,170 bp
RNA expression pattern
	Top expressed in
	mucosa of urinary bladder; ; palpebral conjunctiva; ; bone marrow; ; amniotic fluid; ; periodontal fiber; ; pylorus; ; gastric mucosa; ; cancellous bone; ; urethra; ; rectum;
	n/a
	More reference expression data
	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
	6286
	n/a
	ENSG00000163993
	n/a
	P25815
	n/a
	NM_005980
	n/a
	NP_005971
	n/a
	Wikidata
View/Edit Human

Last updated March 04, 2023

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]

Related Research Articles

Oncomodulin is a parvalbumin-family calcium-binding protein expressed and secreted by macrophages.

Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.

Protein S100-A4 (S100A4) is a protein that in humans is encoded by the S100A4 gene.

S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.

S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene and it is located on chromosome 1q21 with other S100 proteins.

S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family.

S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene. It is also known as calgranulin A.

S100 calcium-binding protein A9 (S100A9) also known as migration inhibitory factor-related protein 14 (MRP14) or calgranulin B is a protein that in humans is encoded by the S100A9 gene.

Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post-myocardially infarcted cardiac tissue.

S100 calcium-binding protein A10 (S100A10), also known as p11, is a protein that is encoded by the S100A10 gene in humans and the S100a10 gene in other species. S100A10 is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells. They regulate a number of cellular processes such as cell cycle progression and differentiation. The S100 protein is implicated in exocytosis and endocytosis by reorganization of F-actin.

S100 calcium-binding protein A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene.

S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene.

S100 calcium-binding protein A12 (S100A12) is a protein that in humans is encoded by the S100A12 gene. Human S100A12, also known as calgranulin C, was first described in 1995.

S100 calcium-binding protein A13 (S100A13) is a protein that in humans is encoded by the S100A13 gene.

Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.

F-actin-capping protein subunit alpha-1 is a protein that in humans is encoded by the CAPZA1 gene.

S100 calcium-binding protein A3 (S100A3) is a protein that in humans is encoded by the S100A3 gene.

Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene.

Grancalcin is a protein that in humans is encoded by the GCA gene.

S100 calcium-binding protein A5 (S100A5) is a protein that in humans is encoded by the S100A5 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000163993 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: S100P S100 calcium binding protein P".
↑ 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.
1 2 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.
↑ 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.

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.
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.

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000163993 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8341667-3] 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.

[pmid7759097-4] 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.

[entrez-5] 1 2 "Entrez Gene: S100P S100 calcium binding protein P".

[pmid12808036-6] 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.

[pmid25084534-7] 1 2 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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

S100P

Contents

Function

Interactions

Related Research Articles

References

Further reading