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S100P (S100 calcium binding protein P)

Written2008-07Sayka Barry, Tatjana Crnogorac-Jurcevic
Institute of Cancer, Barts, The London, Queen Mary's School of Medicine, Dentistry, Queen Mary, University of London, Charterhouse Square, London EC1M 6BQ, United Kingdom

(Note : for Links provided by Atlas : click)

Identity

Alias_namesS100 calcium-binding protein P
Other aliasMIG9
S100E
HGNC (Hugo) S100P
LocusID (NCBI) 6286
Atlas_Id 42196
Location 4p16.1  [Link to chromosome band 4p16]
Location_base_pair Starts at 6693839 and ends at 6697170 bp from pter ( according to hg19-Feb_2009)  [Mapping S100P.png]
Fusion genes
(updated 2016)
KIAA0232 (4p16.1) / S100P (4p16.1)S100P (4p16.1) / CHD1 (5q15)

DNA/RNA

Description S100P gene contains two exons and one intron. Genomic size of 3,332 bases.
Transcription 1279 bases mRNA; 288 bases coding sequences. The transcript is on Chromosome 4 at location 6,745,697-6,749,797.
Pseudogene None identified.

Protein

Description S100P protein consists of 95 amino acids with a molecular weight of 10.4 kDa.
S100P is a Ca2+ binding protein that belongs to S100 family ("Soluble in 100% saturated solution with ammonium sulfate") which was first isolated from human placenta and is therefore designated as "P". S100 family includes at least 26 members, which are thought to be expressed only in vertebrates and are present in a tissue and cell-specific manner. S100 proteins are characterized by common structural motifs including 2 EF-hands (helix-loop-helix calcium binding domains) with different affinities for calcium ions, a central hinge region and the C-terminal extension. The N-terminal half of the protein contains an unconventional EF hand that binds calcium with lower affinity, while the C-terminal is canonical and binds calcium with high affinity. The connecting hinge region and the C-terminal extension are the most variable regions and thus determine the functional specificity of S100 family members, including S100P. In addition to Ca2+, S100P also binds Zn2+ and Mg2+ and can form homo- and heterodimers.
Expression S100P is expressed in various normal tissues including placenta, lung, heart, kidney, bladder, skeletal muscle, bone marrow, spleen, mammary epithelium, epidermis, prostate gland, gastric and intestinal mucosa, and malignant tissues such as pancreatic ductal adenocarcinoma, pancreatic intraductal papillary mucinous neoplasm, non-small-cell lung cancer, melanoma, gastric adenocarcinoma, ovarian, breast, colon and prostate carcinoma as well as in the body fluids such as tear, pancreatic juice, blood and urine.
Localisation Cytoplasm, nucleus, also secreted in the culture media.
Function S100P is involved in diverse biological functions but the exact role or mechanism of its action is still largely unknown. Upon binding of calcium ions S100P undergoes a conformational change that results in an exposure of a hydrophobic surface which allows the interaction with specific target proteins. To date, several S100P interacting partners have been identified including S100P binding protein S100PBP, EZR, S100A1, ECD, CacyBP, RAGE, S100Z and S100A6, but the consequences of their interactions are not fully understood.
Homology S100P shares 50% sequence identity with human S100A1 and 44% identity with S100B.

Mutations

Note Mutations have not been reported.

Implicated in

Note
  
Entity Cancers
Disease S100P has been associated with the progression of several types of cancer including pancreatic, prostate, non-small cell lung, breast, and colorectal cancer.
Oncogenesis S100P has been implicated in migration, invasion, proliferation and survival of cancer cells in vitro and increased tumour growth in vivo. In fibroblasts, S100P has been shown to function as an autocrine growth and survival factor that enhanced cell proliferation and survival by activating RAGE receptor through MAPK and NF-kB signaling.
  
  
Entity Pancreatic cancer
Oncogenesis The up-regulation of S100P is an early event in the development of pancreatic cancer and its expression increases throughout the progression of pancreatic intraepithelial neoplasia (PanINs) to invasive pancreatic ductal adenocarcinoma. S100P plays a critical role in the maintenance of the structural organization of intermediate filaments (cytokeratins 8, 18 and 19) and actin cytoskeleton, and its over-expression changes the phosphorylation status of the actin regulatory protein cofilin. Over-expression of S100P also increases the expression of S100A6 and cathepsin D, both of which are involved in cellular invasion. As S100P is expressed early in pancreatic ductal adenocarcinoma and is secreted into body fluids, it can serve as an useful diagnostic marker.
  
  
Entity Prostate cancer
Oncogenesis In prostate cancer over-expression of S100P increases cell growth both in vitro and in vivo. S100P over-expression also up-regulates androgen receptor that leads to prostate cancer progression. Its expression has also been associated with poor clinical prognosis of patients with this malignancy.
  
  
Entity Non-small-cell lung cancer
Oncogenesis Higher levels of S100P have been correlated with progression to metastasis and decreased survival in patients with lung cancer. This may also serve as a predictor of distant metastasis and poor survival in non-small cell lung carcinomas.
  
  
Entity Colorectal cancer
Oncogenesis In colon cancer, expression of S100P correlates with resistance to chemotherapy and has also been associated with doxorubicin resistance in colon cancer cell lines.
  
  
Entity Breast cancer
Oncogenesis S100P has been associated with immortalization of breast cancer cells in vitro and tumour progression in vivo. Higher level of S100P expression has also been correlated with decreased survival in patients with breast cancer.
  
  
Entity Other cancer types
Note S100P is also expressed at higher levels in gastric, ovarian and cervical carcinomas.
  

Bibliography

The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins.
Adachi J, Kumar C, Zhang Y, Olsen JV, Mann M.
Genome Biol. 2006;7(9):R80.
PMID 16948836
 
S100P promotes pancreatic cancer growth, survival, and invasion.
Arumugam T, Simeone DM, Van Golen K, Logsdon CD.
Clin Cancer Res. 2005 Aug 1;11(15):5356-64.
PMID 16061848
 
Functional evidence implicating S100P in prostate cancer progression.
Basu GD, Azorsa DO, Kiefer JA, Rojas AM, Tuzmen S, Barrett MT, Trent JM, Kallioniemi O, Mousses S.
Int J Cancer. 2008 Jul 15;123(2):330-9.
PMID 18452169
 
S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties.
Becker T, Gerke V, Kube E, Weber K.
Eur J Biochem. 1992 Jul 15 ;207(2): 541-7.
PMID 1633809
 
Gene-expression profiles predict survival of patients with lung adenocarcinoma.
Beer DG, Kardia SL, Huang CC, Giordano TJ, Levin AM, Misek DE, Lin L, Chen G, Gharib TG, Thomas DG, Lizyness ML, Kuick R, Hayasaka S, Taylor JM, Iannettoni MD, Orringer MB, Hanash S.
Nat Med. 2002 Aug; 8(8): 816-24.
PMID 12118244
 
Elevated expression of S100P, CAPL and MAGE 3 in doxorubicin-resistant cell lines: comparison of mRNA differential display reverse transcription-polymerase chain reaction and subtractive suppressive hybridization for the analysis of differential gene expression.
Bertram J, Palfner K, Hiddemann W, Kneba M.
Anticancer Drugs. 1998 Apr ;9(4): 311-7.
PMID 9635921
 
Molecular alterations in pancreatic carcinoma: expression profiling shows that dysregulated expression of S100 genes is highly prevalent.
Crnogorac-Jurcevic T, Missiaglia E, Blaveri E, Gangeswaran R, Jones M, Terris B, Costello E, Neoptolemos JP, Lemoine NR.
J Pathol. 2003 Sep;201(1):63-74.
PMID 12950018
 
S100 family members and trypsinogens are predictors of distant metastasis and survival in early-stage non-small cell lung cancer.
Diederichs S, Bulk E, Steffen B, Ji P, Tickenbrock L, Lang K, Zänker KS, Metzger R, Schneider PM, Gerke V, Thomas M, Berdel WE, Serve H, Müller-Tidow C.
Cancer Res. 2004 Aug 15;64(16):5564-9.
PMID 15313892
 
Intracellular and extracellular roles of S100 proteins.
Donato R.
Microsc Res Tech. 2003 Apr 15;60(6):540-51
PMID 12645002
 
Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer.
Dowen SE, Crnogorac-Jurcevic T, Gangeswaran R, Hansen M, Eloranta JJ, Bhakta V, Brentnall TA, Lüttges J, Klöppel G, Lemoine NR.
Am J Pathol. 2005 Jan;166(1):81-92.
PMID 15632002
 
CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family.
Filipek A, Jastrzebska B, Nowotny M, Kuznicki J.
J Biol Chem. 2002 Aug 9; 277(32): 28848-52.
PMID 12042313
 
RAGE activation by S100P in colon cancer stimulates growth, migration, and cell signaling pathways.
Fuentes MK, Nigavekar SS, Arumugam T, Logsdon CD, Schmidt AM, Park JC, Huang EH.
Dis Colon Rectum. 2007 Aug;50(8):1230-40.
PMID 17587138
 
S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo.
Guerreiro Da Silva ID, Hu YF, Russo IH, Ao X, Salicioni AM, Yang X, Russo J.
Int J Oncol. 2000 Feb; 16(2): 231-40.
PMID 10639564
 
Discovery of novel tumor markers of pancreatic cancer using global gene expression technology.
Iacobuzio-Donahue CA, Maitra A, Shen-Ong GL, van Heek T, Ashfaq R, Meyer R, Walter K, Berg K, Hollingsworth MA, Cameron JL, Yeo CJ, Kern SE, Goggins M, Hruban RH.
Am J Pathol. 2002 Apr;160(4):1239-49.
PMID 11943709
 
Characterization of the tissue-specific expression of the s100P gene which encodes an EF-hand Ca2+-binding protein.
Jin G, Wang S, Hu X, Jing Z, Chen J, Ying K, Xie Y, Mao Y.
Mol Biol Rep. 2003 Dec;30(4):243-8.
PMID 14672411
 
Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P.
Koltzscher M, Neumann C, König S, Gerke V.
Mol Biol Cell. 2003 Jun;14(6):2372-84.
PMID 12808036
 
Diagnostic utility of S100P and von Hippel-Lindau gene product (pVHL) in pancreatic adenocarcinoma-with implication of their roles in early tumorigenesis.
Lin F, Shi J, Liu H, Hull ME, Dupree W, Prichard JW, Brown RE, Zhang J, Wang HL, Schuerch C.
Am J Surg Pathol. 2008 Jan;32(1):78-91.
PMID 18162774
 
Molecular profiling of pancreatic adenocarcinoma and chronic pancreatitis identifies multiple genes differentially regulated in pancreatic cancer.
Logsdon CD, Simeone DM, Binkley C, Arumugam T, Greenson JK, Giordano TJ, Misek DE, Kuick R, Hanash S.
Cancer Res. 2003 May 15;63(10):2649-57.
PMID 12750293
 
Clinical validation of candidate genes associated with prostate cancer progression in the CWR22 model system using tissue microarrays.
Mousses S, Bubendorf L, Wagner U, Hostetter G, Kononen J, Cornelison R, Goldberger N, Elkahloun AG, Willi N, Koivisto P, Ferhle W, Raffeld M, Sauter G, Kallioniemi OP.
Cancer Res. 2002 Mar 1;62(5):1256-60.
PMID 11888886
 
Genome-wide cDNA microarray analysis of gene expression profiles in pancreatic cancers using populations of tumor cells and normal ductal epithelial cells selected for purity by laser microdissection.
Nakamura T, Furukawa Y, Nakagawa H, Tsunoda T, Ohigashi H, Murata K, Ishikawa O, Ohgaki K, Kashimura N, Miyamoto M, Hirano S, Kondo S, Katoh H, Nakamura Y, Katagiri T.
Oncogene. 2004 Mar 25;23(13):2385-400.
PMID 14767473
 
Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins.
Nowotny M, Spiechowicz M, Jastrzebska B, Filipek A, Kitagawa K, Kuznicki J.
J Biol Chem. 2003 Jul 18;278(29):26923-8.
PMID 12746458
 
S100P is an early developmental marker of pancreatic carcinogenesis.
Ohuchida K, Mizumoto K, Egami T, Yamaguchi H, Fujii K, Konomi H, Nagai E, Yamaguchi K, Tsuneyoshi M, Tanaka M.
Clin Cancer Res. 2006 Sep 15;12(18):5411-6.
PMID 17000674
 
The calcium-binding protein S100P in normal and malignant human tissues.
Parkkila S, Pan PW, Ward A, Gibadulinova A, Oveckova I, Pastorekova S, Pastorek J, Martinez AR, Helin HO, Isola J.
BMC Clin Pathol. 2008 Feb 18;8:2.
PMID 18282279
 
Identification of maspin and S100P as novel hypomethylation targets in pancreatic cancer using global gene expression profiling.
Sato N, Fukushima N, Matsubayashi H, Goggins M.
Oncogene. 2004 Feb 26;23(8):1531-8.
PMID 14716296
 
Induction of metastasis by S100P in a rat mammary model and its association with poor survival of breast cancer patients.
Wang G, Platt-Higgins A, Carroll J, de Silva Rudland S, Winstanley J, Barraclough R, Rudland PS.
Cancer Res. 2006 Jan 15;66(2):1199-207.
PMID 16424059
 
The role of S100P in the invasion of pancreatic cancer cells is mediated through cytoskeletal changes and regulation of cathepsin D.
Whiteman HJ, Weeks ME, Dowen SE, Barry S, Timms JF, Lemoine NR, Crnogorac-Jurcevic T.
Cancer Res. 2007 Sep 15;67(18):8633-42.
PMID 17875703
 
The crystal structure at 2A resolution of the Ca2+ -binding protein S100P.
Zhang H, Wang G, Ding Y, Wang Z, Barraclough R, Rudland PS, Fernig DG, Rao Z.
J Mol Biol. 2003 Jan 24;325(4):785-94.
PMID 12507480
 
Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors.
de Souza GA, Godoy LM, Mann M.
Genome Biol. 2006;7(8):R72.
PMID 16901338
 

Citation

This paper should be referenced as such :
Barry, S ; Crnogorac-Jurcevic, T
S100P (S100 calcium binding protein P)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(6):429-431.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/S100PID42196ch4p16.html


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  i(4p) in myeloid malignancies


External links

Nomenclature
HGNC (Hugo)S100P   10504
Cards
AtlasS100PID42196ch4p16
Entrez_Gene (NCBI)S100P  6286  S100 calcium binding protein P
AliasesMIG9
GeneCards (Weizmann)S100P
Ensembl hg19 (Hinxton)ENSG00000163993 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000163993 [Gene_View]  chr4:6693839-6697170 [Contig_View]  S100P [Vega]
ICGC DataPortalENSG00000163993
TCGA cBioPortalS100P
AceView (NCBI)S100P
Genatlas (Paris)S100P
WikiGenes6286
SOURCE (Princeton)S100P
Genetics Home Reference (NIH)S100P
Genomic and cartography
GoldenPath hg38 (UCSC)S100P  -     chr4:6693839-6697170 +  4p16.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)S100P  -     4p16.1   [Description]    (hg19-Feb_2009)
EnsemblS100P - 4p16.1 [CytoView hg19]  S100P - 4p16.1 [CytoView hg38]
Mapping of homologs : NCBIS100P [Mapview hg19]  S100P [Mapview hg38]
OMIM600614   
Gene and transcription
Genbank (Entrez)AF539739 AI202505 AY423724 BC006819 BI259919
RefSeq transcript (Entrez)NM_005980
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)S100P
Cluster EST : UnigeneHs.2962 [ NCBI ]
CGAP (NCI)Hs.2962
Alternative Splicing GalleryENSG00000163993
Gene ExpressionS100P [ NCBI-GEO ]   S100P [ EBI - ARRAY_EXPRESS ]   S100P [ SEEK ]   S100P [ MEM ]
Gene Expression Viewer (FireBrowse)S100P [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6286
GTEX Portal (Tissue expression)S100P
Protein : pattern, domain, 3D structure
UniProt/SwissProtP25815   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP25815  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP25815
Splice isoforms : SwissVarP25815
PhosPhoSitePlusP25815
Domaine pattern : Prosite (Expaxy)EF_HAND_2 (PS50222)    S100_CABP (PS00303)   
Domains : Interpro (EBI)EF-hand-dom_pair    EF_hand_dom    S-100_dom    S100/CaBP-9k_CS    S100_Ca-bd_sub    S100P   
Domain families : Pfam (Sanger)S_100 (PF01023)   
Domain families : Pfam (NCBI)pfam01023   
Domain families : Smart (EMBL)EFh (SM00054)  S_100 (SM01394)  
Conserved Domain (NCBI)S100P
DMDM Disease mutations6286
Blocks (Seattle)S100P
PDB (SRS)1J55    1OZO    2MJW   
PDB (PDBSum)1J55    1OZO    2MJW   
PDB (IMB)1J55    1OZO    2MJW   
PDB (RSDB)1J55    1OZO    2MJW   
Structural Biology KnowledgeBase1J55    1OZO    2MJW   
SCOP (Structural Classification of Proteins)1J55    1OZO    2MJW   
CATH (Classification of proteins structures)1J55    1OZO    2MJW   
SuperfamilyP25815
Human Protein AtlasENSG00000163993
Peptide AtlasP25815
HPRD02792
IPIIPI00017526   
Protein Interaction databases
DIP (DOE-UCLA)P25815
IntAct (EBI)P25815
FunCoupENSG00000163993
BioGRIDS100P
STRING (EMBL)S100P
ZODIACS100P
Ontologies - Pathways
QuickGOP25815
Ontology : AmiGOmagnesium ion binding  calcium ion binding  protein binding  extracellular region  nucleus  cytoplasm  cytoplasm  response to organic substance  nuclear body  microvillus membrane  secretory granule lumen  neutrophil degranulation  endothelial cell migration  cadherin binding  transition metal ion binding  calcium-dependent protein binding  RAGE receptor binding  extracellular exosome  
Ontology : EGO-EBImagnesium ion binding  calcium ion binding  protein binding  extracellular region  nucleus  cytoplasm  cytoplasm  response to organic substance  nuclear body  microvillus membrane  secretory granule lumen  neutrophil degranulation  endothelial cell migration  cadherin binding  transition metal ion binding  calcium-dependent protein binding  RAGE receptor binding  extracellular exosome  
REACTOMEP25815 [protein]
REACTOME PathwaysR-HSA-6798695 [pathway]   
NDEx NetworkS100P
Atlas of Cancer Signalling NetworkS100P
Wikipedia pathwaysS100P
Orthology - Evolution
OrthoDB6286
GeneTree (enSembl)ENSG00000163993
Phylogenetic Trees/Animal Genes : TreeFamS100P
HOVERGENP25815
HOGENOMP25815
Homologs : HomoloGeneS100P
Homology/Alignments : Family Browser (UCSC)S100P
Gene fusions - Rearrangements
Fusion : MitelmanS100P/CHD1 [4p16.1/5q15]  
Fusion: TCGAS100P 4p16.1 CHD1 5q15 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerS100P [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)S100P
dbVarS100P
ClinVarS100P
1000_GenomesS100P 
Exome Variant ServerS100P
ExAC (Exome Aggregation Consortium)S100P (select the gene name)
Genetic variants : HAPMAP6286
Genomic Variants (DGV)S100P [DGVbeta]
DECIPHERS100P [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisS100P 
Mutations
ICGC Data PortalS100P 
TCGA Data PortalS100P 
Broad Tumor PortalS100P
OASIS PortalS100P [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICS100P  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDS100P
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch S100P
DgiDB (Drug Gene Interaction Database)S100P
DoCM (Curated mutations)S100P (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)S100P (select a term)
intoGenS100P
NCG5 (London)S100P
Cancer3DS100P(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM600614   
Orphanet
MedgenS100P
Genetic Testing Registry S100P
NextProtP25815 [Medical]
TSGene6286
GENETestsS100P
Target ValidationS100P
Huge Navigator S100P [HugePedia]
snp3D : Map Gene to Disease6286
BioCentury BCIQS100P
ClinGenS100P
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD6286
Chemical/Pharm GKB GenePA34913
Clinical trialS100P
Miscellaneous
canSAR (ICR)S100P (select the gene name)
Probes
Litterature
PubMed101 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineS100P
EVEXS100P
GoPubMedS100P
iHOPS100P
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Mon Sep 18 17:14:01 CEST 2017

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