Written | 2012-07 | Kate E Lines, Tatjana Crnogorac-Jurcevic |
Barts Cancer Institute, Queen Mary University of London, London, UK |
Identity |
Alias_symbol (synonym) | FLJ12903 |
S100PBPR | |
Other alias | |
HGNC (Hugo) | S100PBP |
LocusID (NCBI) | 64766 |
Atlas_Id | 44308 |
Location | 1p35.1 [Link to chromosome band 1p35] |
Location_base_pair | Starts at 32817518 and ends at 32858879 bp from pter ( according to hg19-Feb_2009) [Mapping S100PBP.png] |
Fusion genes (updated 2017) | Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands) |
DNA/RNA |
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Description | There are two different transcript variants of S100PBP. Variant 1 is 4317 base pairs and contains 7 exons. Variant 2 is 1483 base pairs and also contains 7 exons. This is shown in the above alignment. The coding sequence for each isoform is indicated in red, with the non-coding sequence in grey. Unmatched base pairs between the two isoforms are highlighted in green and the position of a missing CAG codon in isoform B is circled. The end of the isoform B sequence is indicated by a bold line. |
Protein |
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Description | S100PBP isoform A codes for a 45 kDa protein and isoform B for 37 kDa protein. Secondary structure analysis of the S100PBP protein sequence was performed using the secondary structure consensus prediction tool (NPS@, Lyon, France). Based on three different methods: DSC (Discrimination of protein Secondary structure Class), MLRC (Multivariate Linear Regression Combination) and PHD neural network system, S100PBP was shown to be largely unstructured and unfolded, as seen above ("h" represents a helix, "c" a coil and "e" an extended strand). |
Expression | S100PBP is expressed in various normal tissues including prostate and lung and in both the endocrine and exocrine pancreas. S100PBP is also expressed in malignant tissues such as liver hepatocellular carcinoma and thyroid carcinoma (Lines et al., 2012). In pancreas, S100PBP is expressed in decreasing levels as cancer develops and progresses, which is an inverse pattern of expression of its binding partner, S100P. This is shown on picture below (a= acinar cells, d= ducts; PanIN= pancreatic intraepithelial neoplasia, a precursor lesion to pancreatic cancer, black arrows= PanIN-1, red arrows= PanIN-2; PDAC= pancreatic cancer). |
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Localisation | Predominantly nuclear. |
Function | The exact functions of S100PBP are currently unknown, however it has been shown that S100PBP can bind to the metastasis related protein S100P (Dowen et al., 2005). |
Homology | No homology to any currently described protein is seen. |
Mutations |
Note | No mutations have yet been reported. |
Implicated in |
Note | |
Entity | Pancreatic ductal adenocarcinoma (PDAC) |
Note | Overexpression of S100PBP in FA6 pancreatic cancer cells that show low levels of endogenous S100PBP expression and silencing of S100PBP in MiaPaCa2 cells (high levels of endogenous S100PBP) showed no effect on proliferation or wound healing. While cell migration was not affected in majority of tested pancreatic cancer cell lines after modulation of S100PBP expression, significant changes in invasion (increase in MiaPaCa2 and Panc1 cells after S100PBP silencing and decrease in RwP1 cells after overexpression) were seen. However, the most affected cellular function after modulation of S100PBP expression was adhesion. Loss of S100PBP causes an increase in pancreatic cancer cell adhesion to extracellular matrix proteins which was mediated by cysteine protease Cathepsin Z (CTSZ) and the integrin ανβ5 (Lines et al., 2012). Schematic and simplified diagram of the putative mechanism behind S100PBP mediated changes in pancreatic cell adhesion is shown below: in normal cells where S100PBP is highly expressed, low levels of CTSZ are present; no or very little ανβ5 is seen on the cellular surface. In cancer cells (PDAC), S100PBP levels decrease, which results in an increase in CTSZ expression; CTSZ is then secreted and can interact with ανβ5, promoting thus the adhesion. |
Disease | Pancreatic cancer. |
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Bibliography |
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, Luttges J, Kloppel G, Lemoine NR. |
Am J Pathol. 2005 Jan;166(1):81-92. |
PMID 15632002 |
S100P-binding protein, S100PBP, mediates adhesion through regulation of cathepsin Z in pancreatic cancer cells. |
Lines KE, Chelala C, Dmitrovic B, Wijesuriya N, Kocher HM, Marshall JF, Crnogorac-Jurcevic T. |
Am J Pathol. 2012 Apr;180(4):1485-94. Epub 2012 Feb 11. |
PMID 22330678 |
Citation |
This paper should be referenced as such : |
Lines, KE ; Crnogorac-Jurcevic, T |
S100PBP (S100P binding protein) |
Atlas Genet Cytogenet Oncol Haematol. 2013;17(1):40-44. |
Free journal version : [ pdf ] [ DOI ] |
On line version : http://AtlasGeneticsOncology.org/Genes/S100PBPID44308ch1p35.html |
External links |
REVIEW articles | automatic search in PubMed |
Last year publications | automatic search in PubMed |
© Atlas of Genetics and Cytogenetics in Oncology and Haematology | indexed on : Thu Feb 14 17:28:25 CET 2019 |
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