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S100A2 (S100 calcium binding protein A2)

Written2011-11Christopher J Scarlett, Andrew V Biankin
Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria St Darlinghurst, NSW 2010, Australia

(Note : for Links provided by Atlas : click)


Alias (NCBI)CAN19
HGNC (Hugo) S100A2
HGNC Alias symbCAN19
HGNC Previous nameS100L
HGNC Previous nameS100 calcium-binding protein A2
LocusID (NCBI) 6273
Atlas_Id 42191
Location 1q21.3  [Link to chromosome band 1q21]
Location_base_pair Starts at 153561109 and ends at 153565844 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping S100A2.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)
EIF3D (22q12.3)::S100A2 (1q21.3)MID1 (Xp22.2)::S100A2 (1q21.3)RPRD2 (1q21.2)::S100A2 (1q21.3)
RPRD2 (1q21.3)::S100A2 (1q21.3)S100A2 (1q21.3)::EIF3D (22q12.3)S100A2 (1q21.3)::SUMO2P13 (6p22.3)


  The S100A2 gene spans a total region of 4723 bp (NM_005978.3) consisting of three exons. Exon 1 is untranslated, exon 2 codes for the N-terminal 47 amino acids and exon 3 codes for the C-terminal 50 amino acids.
Description The nucleotide sequence and genomic organization of the S100A2 gene was originally described by Wicki et al. (1997), using a normal and a tumorigenic breast epithelial cell line. The structure of S100A2 was originally deduced by the analysis of cDNA from a positive genomic clone from an EMBL-3 SP6/T7 human female peripheral blood leukocyte genomic library (Clontech, no. HL 1111j). The human S100A2 gene is located next to the S100A4 locus on chromosome 1q21.3 within a cluster of S100 genes (Wolf et al., 2011), and part of the epidermal differentiation complex (Wolf et al., 2011). The S100A2 gene spans a total region of 4723 bp (NM_005978.3) consisting of three exons. The three-exon-structure contains the coding sequence within exons two and three, reflecting the common composition of S100 genes. Exon 1 is untranslated, exon 2 codes for the N-terminal 47 amino acids and exon 3 codes for the C-terminal 50 amino acids.
The S100A2 gene has a total length of 4723 bp and seven splice variants, which can be categorized into five variants with protein product and two transcripts without an open-reading frame. Four of the variants contain the three-exon structure with the coding sequences in exon 2 and exon 3, while also sharing identical protein sequences only differing in their untranslated 5' region (Wolf et al., 2011).
Transcription The S100A2 mRNA product length, including the poly-adenylate stretch, is 970 bp (NM_005978.3). The S100A2 gene has an open-reading frame of 294 nucleotides encoding for a protein of 97 amino acid residues with a molecular mass of 11,117 kDa (NM_005969.1; see below).
Wicki et al. (1997) identified an enhancer element in the promoter region necessary for the transcription of the S100A2 gene. This enhancer element is active in both orientations and either upstream or downstream of the reporter gene, and is both necessary and sufficient for transcription of the gene (Wicki et al., 1997).


Note The S100A2 gene encodes for a protein of 97 amino acid residues, with a molecular mass of 11,117 kDa (P29034; UniProtKB).
  The protein structure and amino acid sequence of S100A2 (human). Modified from Wolf et al., Amino Acids, 2011.
Description S100A2 is a member of the S100 family of calcium-binding proteins. The S100A2 gene encodes for a protein of 98 amino acid residues, with a molecular mass of 11,117 kDa (P29034; UniProtKB). S100 proteins are a family of low-molecular weight (9-12 kD), calcium-binding proteins that initiate a number of cellular processes such as cell division, motility, secretion, protein synthesis, and membrane permeability through both calcium dependent and independent mechanism. Greater than twenty five different S100 proteins have so far been identified with many mapping closely together on chromosome 1q21.
S100A2 calcium-binding protein is characterized by four helices, two distinct calcium-binding EF-hand motifs, a central hinge region and C- and N-terminal variable domains. S100 proteins are found in the cytoplasm as preassembled dimers. A potential role for S100 proteins in cancer originated from observations that the evolutionarily conserved gene cluster containing S100 genes on human chromosome 1q21 underwent several rearrangements during tumour development.
Expression S100A2 appears to be tissue specific as it is expressed in many normal and tumour tissues. Expression of S100A2 occurs in normal breast, lung, kidney, prostate, skin and oral squamous cell tissue, with loss of expression observed in associated carcinomas suggesting a putative tumour suppressor role; while in some malignant tissues, such as pancreatic, esophageal, gastric, papillary and follicular thyroid, some subsets of lung cancer and non-small cell lung cancer high expression of S100A2 is associated with poor prognosis and increased metastases. Clearly, expression of S100A2 is not ubiquitous for all tissues and there is evidently an element of tissue-specific expression.
Localisation S100A2 is primarily localised in the nucleus with translocation to the cytoplasm evident in a number of tissue types.
Function Little is known about S100A2 function and its potential contribution as either a tumour suppressor or contributor to tumorigenesis and metastases. Upon calcium binding a conformational change occurs exposing a target protein recognition site. Once in the calcium-activated state each monomer can interact with one target protein. In this state the S100 proteins act as calcium sensors and play a role in protein phosphorylation, enzyme activation via phosphorylation, inflammation, cellular contraction and relaxation by regulating cytoskeletal constituents including actin and myosin, and nuclear transcription promoting cell proliferation and differentiation.
Homology Close relation to S100A4 has been confirmed by sequence analysis. Both proteins share over 60% amino acid sequence identity (Glenney et al., 1989).


Note Mutations have not been reported.

Implicated in

Entity Pancreatic cancer
Note For pancreatic cancer high S100A2 expression co-segregated with a poor response to pancreatectomy. Patients with tumours that demonstrated high S100A2 expression did not have a significant survival benefit from pancreatectomy compared to biopsy alone, whereas S100A2 negative tumours did. In the subgroup of patients who had resections with clear surgical margins, those whose tumours demonstrated high, or mod/high expression of S100A2 co-segregated with a poor outcome suggesting that occult distant metastatic disease may have been present in patients with tumours that had high S100A2 expression at the time of pancreatectomy. In a supportive study, invasive pancreatic ductal carcinoma cells were shown to express higher levels of S100A2 than did intraductal papillary mucinous neoplasms (IPMN), pancreatitis affected epithelia or normal cells, while cell lines derived from metastatic sites expressed higher levels of S100A2 than those from primary sites. This study also demonstrated that patients with high S100A2 expression had poorer overall survival. Together, these data demonstrate that S100A2 expression is a good predictor of response to pancreatectomy for pancreatic cancer and suggests that high S100A2 expression may be a marker of a metastatic phenotype (Ohuchida et al., 2007; Biankin et al., 2009; Pinese et al., 2009).
Entity Esophageal squamous cell carcinoma (ESCC)
Note S100A2 was initially reported to be downregulated in a cohort of ESCC patients as measured by RT-PCR, with node-negative ESCC patients without S100A2 expression considered to be a high-risk group with poor survival. More recently, however, S100A2-overexpressing cancers showed a trend toward preferentially developing lymph node metastases and distant metastases, suggesting that S100A2 might be related to the progression of esophageal SCC (Kyriazanos et al., 2002; Ji et al., 2004; Imazawa et al., 2005; Cao et al., 2009).
Entity Barrett's adenocarcinomas
Note Expression of S100A2 mRNA and protein in Barrett's adenocarcinoma samples were performed by RT-PCR, and immunohistochemistry respectively. Frequent overexpression of S100A2 mRNA was observed in Barrett's adenocarcinomas, while overexpression of S100A2 protein was more frequently seen in well-differentiated tumours than in others. Contrary to the nuclear expression of S100A2 in normal esophageal mucosa, two thirds of Barrett's dysplasia and Barrett's adenocarcinomas that overexpressed S100A2 demonstrated stronger cytosolic staining than nuclear staining (Lee et al., 2006).
Entity Non-small cell lung cancer (NSCLC)
Note Many studies have been performed invetigating S100A2 expression in non-small cell lung cancer (NSCLC). Increased expression of S100A2 has been demonstrated in tumour cells, with S100A2 providing valuable prognostic parameters. Patients whose tumours had positive S100A2 expression had a significantly lower overall survival and disease-specific survival rate at 5 years after surgery than did patients with negative S100A2 expression. S100A2 was overexpressed in tumours that metastasized during the course of the disease. Overexpression of S100A2 in NSCLC cell cultures has been shown to increase transendothelial migration, corroborating the role of S100A2 in the metastatic process. High expression of S100A2 is associated with metastasis and predicts survival in early stages of NSCLC. These findings are supported by studies in a mouse model of non-small cell lung cancer (NSCLC) where NOD/SCID mice xenografted with NSCLC cells overexpressing S100A2 demonstrated significantly more metastases than vector alone transfected cells (Heighway et al., 2002; Diederichs et al., 2004; Smith et al., 2004; Wang et al., 2005; Zech et al., 2006; Bartling et al., 2007; Bulk et al., 2009; Strazisar et al., 2009a; Strazisar et al., 2009b).
Entity Gastric cancer
Note Early assessment of S100A2 expression in gastric cancer using serial analysis of gene expression (SAGE) revealed that over 90% of gastric tumours overexpressed S100A2 when compared to normal gastric mucosa. More recently, however, S100A2 protein expression in normal and benign gastric tissues has been reported with a loss of S100A2 expression in 52% of gastric adenocarcinomas. Loss of S100A2 expression was associated with histological differentiation, depth of invasion, lymphatic vessel invasion and lymph node metastasis. These conflicting data demonstrate the need for further studies into S100A2 expression and gastric adenocarcinomas to further elucidate the tumorigenic mechanisms underpinning gastric carcinogenesis (El-Rifai et al., 2002; Liu et al., 2008; Luo et al., 2011).
Entity Thyroid carcinomas
Note For thyroid carcinomas, S100A2 has been demonstrated to contribute to carcinogenic events in papillary carcinoma progression (90% positive), with S100A2 expression being one of the biological characteristics of anaplastic carcinoma (Ito et al., 2005).
Entity Ovarian carcinomas (various subtypes) / ovarian serous papillary tumours
Note S100A2 is highly overexpressed in the majority of ovarian carcinomas irrespective of the subtype, in particular S100A2 is overexpressed in ovarian serous papillary carcinomas compared to normal ovarian cell lines (Hough et al., 2001; Santin et al., 2004).
Entity Breast cancer
Note S100A2 expression in normal mammary epithelium is usually high, with loss of S100A2 associated with the development of malignant breast carcinoma. Studies have revealed that loss of S100A2 expression is not associated with early carcinogenesis from normal mammary epithelium to benign hyperplasia. These experiments provided early evidence that S100A2 repression in tumour cells may be mediated by site-specific methylation. Interestingly, recent investigations have demonstrated that the highly invasive basal breast cancers express significantly higher levels of S100A2 than non-basal breast malignancies (Wicki et al., 1997; Liu et al., 2000; McKiernan et al., 2011).
Entity Oral squamous cell carcinoma (OSCC) / laryngeal squamous cell carcinoma (LSCC)
Note Recent data has emerged surrounding the potential antitumour role of S100A2 in squamous cell carcinomas, partly via reduced expression of COX-2. For oral squamous cell carcinomas (OSCC) a higher rate of late cervical metastasis has been shown in patients with S100A2-negative tumours than those with S100A2-positive tumours, indicating that patients with stage I or II invasive OSCC without S100A2 expression should be considered a high-risk group for late cervical metastasis (poor overall survival). Loss of nuclear S100A2 may also serve as an independent prognostic marker for early-stage oral cancer patients at high risk of recurrence. A more aggressive treatment modality and intensive follow-up may be recommended for the patients with reduced expression of S100A2 in tumour cell nuclei. In laryngeal squamous cell carcinoma, a correlation was found between S100A2 tumour positivity and longer relapse-free and overall survival (Lauriola et al., 2000; Suzuki et al., 2005; Tsai et al., 2005; Tsai et al., 2006; Almadori et al., 2009).
Entity Bladder cancer
Note Conflicting data has emerged concerning S100A2 expression in bladder cancers. Overexpression of S100A2 mRNA has been demonstrated in bladder cancers using RT-PCR, however a study investigating S100A2 expression at the protein level demonstrated that S100A2 expression was significantly decreased in the bladder cancer specimens compared with the controls. The loss of expression of S100A2 and increased expression of another calcium binding protein, S100A4, were associated with muscle invasion with alterations in expression also associated with a greater risk of disease progression and a decreased chance of cancer-specific survival (Matsumoto et al., 2007; Yao et al., 2007).
Entity Squamous cell carcinoma of the head and neck (SCCHN)
Note In oral cancer cells the Ca2+ and cell cycle-dependent p53-S100A2 interaction might modulate proliferation, while for squamous cell carcinomas of the head and neck (SCCHN) it has been postulated that S100A2 may play a role in the metastasis of SCCHN, however most tumours expressed S100A2 but lymph node metastases showed a pattern of reduced staining for S100A2 compared with primary tumours (Mueller et al., 2005; Zhang et al., 2007).
Entity Lung adenocarcinoma / lung squamous cell carcinoma (LSCC)
Note Expression of S100A2 is reportedly downregulated in some lung squamous cell carcinomas, with S100A2 positivity being a favourable prognostic indicator in patients with p53-negative tumours (Feng et al., 2001; Shen et al., 2002; Matsubara et al., 2005).
Entity Prostate cancer
Note S100A2 expression was observed in the basal cells of non-malignant epithelium, while absent S100A2 expression was demonstrated in a cohort of 41 prostate cancer specimens, potentially due to promoter hypermethylation. In benign conditions such as benign prostate hyperplasia and prostatitis, high levels of S100A2 are observed with a progressive loss of S100A2 expression occurring with increasing tumour grade and metastases indicating that loss of S100A2 may be an important event during progression of prostate cancer. More recently, high S100A2 protein expression was observed in a cohort of benign prostatic hyperplasia, with little or no expression in prostate cancer cells, while a concomitant increase of S100A4 expression was observed in prostate cancer cells. These data suggest that the analysis of both S100A2 and S100A4 expression in prostatic tissues may be a useful prognostic indicator for prostate cancer (Gupta et al., 2003; Rehman et al., 2005; Kwon et al., 2010).
Entity Malignant melanoma
Note For malignant melanoma, loss of S100A2 gene expression may be an early event in the development of melanoma. All nevi showed moderate to high expression levels of S100A2, while the expression levels were low in cell lines established from primary melanomas and metastases did not express S100A2 mRNA (Maelandsmo et al., 1997).


Diminished expression of S100A2, a putative tumour suppressor, is an independent predictive factor of neck node relapse in laryngeal squamous cell carcinoma.
Almadori G, Bussu F, Galli J, Rigante M, Lauriola L, Michetti F, Maggiano N, Schafer BW, Heizmann CW, Ranelletti FO, Paludetti G.
J Otolaryngol Head Neck Surg. 2009 Feb;38(1):16-22.
PMID 19344608
S100A2-S100P expression profile and diagnosis of non-small cell lung carcinoma: impairment by advanced tumour stages and neoadjuvant chemotherapy.
Bartling B, Rehbein G, Schmitt WD, Hofmann HS, Silber RE, Simm A.
Eur J Cancer. 2007 Sep;43(13):1935-43. Epub 2007 Aug 3.
PMID 17689067
Expression of S100A2 calcium-binding protein predicts response to pancreatectomy for pancreatic cancer.
Biankin AV, Kench JG, Colvin EK, Segara D, Scarlett CJ, Nguyen NQ, Chang DK, Morey AL, Lee CS, Pinese M, Kuo SC, Susanto JM, Cosman PH, Lindeman GJ, Visvader JE, Nguyen TV, Merrett ND, Warusavitarne J, Musgrove EA, Henshall SM, Sutherland RL; NSW Pancreatic Cancer Network.
Gastroenterology. 2009 Aug;137(2):558-68, 568.e1-11. Epub 2009 Apr 16.
PMID 19376121
S100A2 induces metastasis in non-small cell lung cancer.
Bulk E, Sargin B, Krug U, Hascher A, Jun Y, Knop M, Kerkhoff C, Gerke V, Liersch R, Mesters RM, Hotfilder M, Marra A, Koschmieder S, Dugas M, Berdel WE, Serve H, Muller-Tidow C.
Clin Cancer Res. 2009 Jan 1;15(1):22-9.
PMID 19118029
Expression and clinical significance of S100A2 and p63 in esophageal carcinoma.
Cao LY, Yin Y, Li H, Jiang Y, Zhang HF.
World J Gastroenterol. 2009 Sep 7;15(33):4183-8.
PMID 19725154
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, Zanker KS, Metzger R, Schneider PM, Gerke V, Thomas M, Berdel WE, Serve H, Muller-Tidow C.
Cancer Res. 2004 Aug 15;64(16):5564-9.
PMID 15313892
Gastric cancers overexpress S100A calcium-binding proteins.
El-Rifai W, Moskaluk CA, Abdrabbo MK, Harper J, Yoshida C, Riggins GJ, Frierson HF Jr, Powell SM.
Cancer Res. 2002 Dec 1;62(23):6823-6.
PMID 12460893
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Feng G, Xu X, Youssef EM, Lotan R.
Cancer Res. 2001 Nov 1;61(21):7999-8004.
PMID 11691825
Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution.
Glenney JR Jr, Kindy MS, Zokas L.
J Cell Biol. 1989 Feb;108(2):569-78.
PMID 2521861
Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma.
Gupta S, Hussain T, MacLennan GT, Fu P, Patel J, Mukhtar H.
J Clin Oncol. 2003 Jan 1;21(1):106-12.
PMID 12506178
Expression profiling of primary non-small cell lung cancer for target identification.
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Oncogene. 2002 Oct 31;21(50):7749-63.
PMID 12400018
Coordinately up-regulated genes in ovarian cancer.
Hough CD, Cho KR, Zonderman AB, Schwartz DR, Morin PJ.
Cancer Res. 2001 May 15;61(10):3869-76.
PMID 11358798
S100A2 overexpression is frequently observed in esophageal squamous cell carcinoma.
Imazawa M, Hibi K, Fujitake S, Kodera Y, Ito K, Akiyama S, Nakao A.
Anticancer Res. 2005 Mar-Apr;25(2B):1247-50.
PMID 15865073
Expression of S100A2 and S100A6 in thyroid carcinomas.
Ito Y, Yoshida H, Tomoda C, Uruno T, Miya A, Kobayashi K, Matsuzuka F, Kakudo K, Kuma K, Miyauchi A.
Histopathology. 2005 May;46(5):569-75.
PMID 15842639
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Ji J, Zhao L, Wang X, Zhou C, Ding F, Su L, Zhang C, Mao X, Wu M, Liu Z.
J Cancer Res Clin Oncol. 2004 Aug;130(8):480-6. Epub 2004 Jun 4.
PMID 15185146
Significance of S100A2 and S100A4 Expression in the Progression of Prostate Adenocarcinoma.
Kwon YW, Chang IH, Kim KD, Kim YS, Myung SC, Kim MK, Kim TH.
Korean J Urol. 2010 Jul;51(7):456-62. Epub 2010 Jul 20.
PMID 20664777
Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus.
Kyriazanos ID, Tachibana M, Dhar DK, Shibakita M, Ono T, Kohno H, Nagasue N.
Oncol Rep. 2002 May-Jun;9(3):503-10.
PMID 11956617
Prognostic significance of the Ca(2+) binding protein S100A2 in laryngeal squamous-cell carcinoma.
Lauriola L, Michetti F, Maggiano N, Galli J, Cadoni G, Schafer BW, Heizmann CW, Ranelletti FO.
Int J Cancer. 2000 Jul 20;89(4):345-9.
PMID 10956408
Expression of calcium-binding proteins S100A2 and S100A4 in Barrett's adenocarcinomas.
Lee OJ, Hong SM, Razvi MH, Peng D, Powell SM, Smoklin M, Moskaluk CA, El-Rifai W.
Neoplasia. 2006 Oct;8(10):843-50.
PMID 17032501
Expression of calcium-binding protein S100A2 in breast lesions.
Liu D, Rudland PS, Sibson DR, Platt-Higgins A, Barraclough R.
Br J Cancer. 2000 Dec;83(11):1473-9.
PMID 11076656
In silico analysis and verification of S100 gene expression in gastric cancer.
Liu J, Li X, Dong GL, Zhang HW, Chen DL, Du JJ, Zheng JY, Li JP, Wang WZ.
BMC Cancer. 2008 Sep 16;8:261.
PMID 18793447
Loss of Reprimo and S100A2 expression in human gastric adenocarcinoma.
Luo J, Zhu Y, Yang G, Gong L, Wang B, Liu H.
Diagn Cytopathol. 2011 Oct;39(10):752-7. doi: 10.1002/dc.21461. Epub 2010 Oct 14.
PMID 20949468
Differential expression patterns of S100A2, S100A4 and S100A6 during progression of human malignant melanoma.
Maelandsmo GM, Florenes VA, Mellingsaeter T, Hovig E, Kerbel RS, Fodstad O.
Int J Cancer. 1997 Aug 22;74(4):464-9.
PMID 9291441
Differential expression of S100A2 and S100A4 in lung adenocarcinomas: clinicopathological significance, relationship to p53 and identification of their target genes.
Matsubara D, Niki T, Ishikawa S, Goto A, Ohara E, Yokomizo T, Heizmann CW, Aburatani H, Moriyama S, Moriyama H, Nishimura Y, Funata N, Fukayama M.
Cancer Sci. 2005 Dec;96(12):844-57.
PMID 16367903
Expression of S100A2 and S100A4 predicts for disease progression and patient survival in bladder cancer.
Matsumoto K, Irie A, Satoh T, Ishii J, Iwabuchi K, Iwamura M, Egawa S, Baba S.
Urology. 2007 Sep;70(3):602-7. Epub 2007 Aug 3.
PMID 17688917
The role of S100 genes in breast cancer progression.
McKiernan E, McDermott EW, Evoy D, Crown J, Duffy MJ.
Tumour Biol. 2011 Jun;32(3):441-50. Epub 2010 Dec 14.
PMID 21153724
The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity.
Mueller A, Schafer BW, Ferrari S, Weibel M, Makek M, Hochli M, Heizmann CW.
J Biol Chem. 2005 Aug 12;280(32):29186-93. Epub 2005 Jun 7.
PMID 15941720
Over-expression of S100A2 in pancreatic cancer correlates with progression and poor prognosis.
Ohuchida K, Mizumoto K, Miyasaka Y, Yu J, Cui L, Yamaguchi H, Toma H, Takahata S, Sato N, Nagai E, Yamaguchi K, Tsuneyoshi M, Tanaka M.
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PMID 17940995
Messina: a novel analysis tool to identify biologically relevant molecules in disease.
Pinese M, Scarlett CJ, Kench JG, Colvin EK, Segara D, Henshall SM, Sutherland RL, Biankin AV.
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PMID 19399185
Promoter hyper-methylation of calcium binding proteins S100A6 and S100A2 in human prostate cancer.
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Prostate. 2005 Dec 1;65(4):322-30.
PMID 16015609
Gene expression profiles in primary ovarian serous papillary tumors and normal ovarian epithelium: identification of candidate molecular markers for ovarian cancer diagnosis and therapy.
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PMID 15305371
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PMID 12445744
S100A2 is strongly expressed in airway basal cells, preneoplastic bronchial lesions and primary non-small cell lung carcinomas.
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Br J Cancer. 2004 Oct 18;91(8):1515-24.
PMID 15467767
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PMID 18656279
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PMID 15792606
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PMID 15800916
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Cell Calcium. 1997 Oct;22(4):243-54.
PMID 9481475
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Anticancer Res. 2007 Sep-Oct;27(5A):3051-8.
PMID 17970044
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PMID 17067748
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PMID 17123307


This paper should be referenced as such :
Scarlett, CJ ; Biankin, AV
S100A2 (S100 calcium binding protein A2)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(4):280-285.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)S100A2   10492
Atlas Explorer : (Salamanque)S100A2
Entrez_Gene (NCBI)S100A2    S100 calcium binding protein A2
AliasesCAN19; S100L
GeneCards (Weizmann)S100A2
Ensembl hg19 (Hinxton)ENSG00000196754 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000196754 [Gene_View]  ENSG00000196754 [Sequence]  chr1:153561109-153565844 [Contig_View]  S100A2 [Vega]
ICGC DataPortalENSG00000196754
TCGA cBioPortalS100A2
AceView (NCBI)S100A2
Genatlas (Paris)S100A2
SOURCE (Princeton)S100A2
Genetics Home Reference (NIH)S100A2
Genomic and cartography
GoldenPath hg38 (UCSC)S100A2  -     chr1:153561109-153565844 -  1q21.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)S100A2  -     1q21.3   [Description]    (hg19-Feb_2009)
GoldenPathS100A2 - 1q21.3 [CytoView hg19]  S100A2 - 1q21.3 [CytoView hg38]
Genome Data Viewer NCBIS100A2 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF086003 AW195797 BC002829 BC105787 BQ953250
RefSeq transcript (Entrez)NM_001366406 NM_001366407 NM_005978
Consensus coding sequences : CCDS (NCBI)S100A2
Gene ExpressionS100A2 [ NCBI-GEO ]   S100A2 [ EBI - ARRAY_EXPRESS ]   S100A2 [ SEEK ]   S100A2 [ MEM ]
Gene Expression Viewer (FireBrowse)S100A2 [ Firebrowse - Broad ]
GenevisibleExpression of S100A2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6273
GTEX Portal (Tissue expression)S100A2
Human Protein AtlasENSG00000196754-S100A2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP29034   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP29034  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP29034
Domaine pattern : Prosite (Expaxy)EF_HAND_1 (PS00018)    EF_HAND_2 (PS50222)    S100_CABP (PS00303)   
Domains : Interpro (EBI)EF-hand-dom_pair    EF_Hand_1_Ca_BS    EF_hand_dom    S-100_dom    S100/CaBP-9k_CS    S100_Ca-bd_sub   
Domain families : Pfam (Sanger)S_100 (PF01023)   
Domain families : Pfam (NCBI)pfam01023   
Domain families : Smart (EMBL)S_100 (SM01394)  
Conserved Domain (NCBI)S100A2
PDB Europe2RGI    4DUQ   
PDB (PDBSum)2RGI    4DUQ   
PDB (IMB)2RGI    4DUQ   
Structural Biology KnowledgeBase2RGI    4DUQ   
SCOP (Structural Classification of Proteins)2RGI    4DUQ   
CATH (Classification of proteins structures)2RGI    4DUQ   
AlphaFold pdb e-kbP29034   
Human Protein Atlas [tissue]ENSG00000196754-S100A2 [tissue]
Protein Interaction databases
IntAct (EBI)P29034
Ontologies - Pathways
Ontology : AmiGOcalcium ion binding  calcium ion binding  protein binding  cellular_component  identical protein binding  endothelial cell migration  endothelial cell migration  transition metal ion binding  calcium-dependent protein binding  
Ontology : EGO-EBIcalcium ion binding  calcium ion binding  protein binding  cellular_component  identical protein binding  endothelial cell migration  endothelial cell migration  transition metal ion binding  calcium-dependent protein binding  
NDEx NetworkS100A2
Atlas of Cancer Signalling NetworkS100A2
Wikipedia pathwaysS100A2
Orthology - Evolution
GeneTree (enSembl)ENSG00000196754
Phylogenetic Trees/Animal Genes : TreeFamS100A2
Homologs : HomoloGeneS100A2
Homology/Alignments : Family Browser (UCSC)S100A2
Gene fusions - Rearrangements
Fusion : MitelmanMID1::S100A2 [Xp22.2/1q21.3]  
Fusion : MitelmanRPRD2::S100A2 [1q21.3/1q21.3]  
Fusion : FusionHubAHNAK--S100A2    CHTOP--S100A2    CX3CL1--S100A2    EIF3D--S100A2    FLG-AS1--S100A2    GNB2L1--S100A2    MID1--S100A2    RPRD2--S100A2    S100A16--S100A2    S100A2--CD74   
S100A2--CHD1    S100A2--CXCR5    S100A2--DDX21    S100A2--EIF3D    S100A2--FXYD3    S100A2--HSA-MIR-6723    S100A2--KRT7    S100A2--KRT81    S100A2--LAMC1    S100A2--MTMR2   
S100A2--NDUFV1    S100A2--RPL30    S100A2--SGK223    TPRA1--S100A2   
Fusion : QuiverS100A2
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerS100A2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)S100A2
Exome Variant ServerS100A2
GNOMAD BrowserENSG00000196754
Varsome BrowserS100A2
ACMGS100A2 variants
Genomic Variants (DGV)S100A2 [DGVbeta]
DECIPHERS100A2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisS100A2 
ICGC Data PortalS100A2 
TCGA Data PortalS100A2 
Broad Tumor PortalS100A2
OASIS PortalS100A2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICS100A2  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DS100A2
Mutations and Diseases : HGMDS100A2
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)S100A2
DoCM (Curated mutations)S100A2
CIViC (Clinical Interpretations of Variants in Cancer)S100A2
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry S100A2
NextProtP29034 [Medical]
Target ValidationS100A2
Huge Navigator S100A2 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDS100A2
Pharm GKB GenePA34904
Clinical trialS100A2
canSAR (ICR)S100A2
DataMed IndexS100A2
PubMed93 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Jan 20 14:16:53 CET 2022

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