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STMN1 (stathmin 1)

Written2014-05João Agostinho Machado-Neto, Fabiola Traina
Hematology, Hemotherapy Center-University of Campinas/Hemocentro-Unicamp, Instituto Nacional de Ciencia e Tecnologia do Sangue, Campinas, Sao Paulo, Brazil (JAMN, FT); Department of Internal Medicine, University of Sao Paulo at Ribeirao Preto Medical School, Ribeirao Preto, Sao Paulo, Brazil (FT)

Abstract Stathmin 1 (STMN1) is a microtubule destabilizer protein with an important role in cell cycle progression, cell proliferation, migration and survival. The present review on STMN1 contains data on DNA/RNA, on the protein encoded and where the gene is implicated.

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Alias (NCBI)C1orf215
HGNC Alias symbSMN
HGNC Alias nameoncoprotein 18
HGNC Previous nameLAP18
HGNC Previous namechromosome 1 open reading frame 215
 stathmin 1/oncoprotein 18
LocusID (NCBI) 3925
Atlas_Id 42443
Location 1p36.11  [Link to chromosome band 1p36]
Location_base_pair Starts at 25900116 and ends at 25906153 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping STMN1.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)
BTF3L4 (1p32.3)::STMN1 (1p36.11)KIAA1211 (4q12)::STMN1 (1p36.11)PHYKPL (5q35.3)::STMN1 (1p36.11)
STMN1 (1p36.11)::CSMD2 (1p35.1)STMN1 (1p36.11)::STARD7 (2q11.2)STMN1 (1p36.11)::STMN1 (1p36.11)


Note The entire STMN1 gene is about 22.8 kb and contains 5 exons (start: 26210672 bp and end: 26233482; orientation: minus strand). The STMN1 gene encodes 2 isoforms, A and B. Isoform A contains 3 transcript variants that differ in the 5' UTR and have an alternate terminal exon, compared to isoform B, resulting in a shorter and distinct C-terminus. The isoform B represents the longest transcript variant.


  Figure 1. Representation of primary structure of Stathmin 1 protein. The catastrophe promotion region (aa 1 - 99) and the four serine phosphorylation sites (S16, S25, S38 and S63) at the N-terminal, and the tubulin binding domain (aa 25 - 149) at the C-terminal are illustrated in the figure. Reproduced with permission of the editor-in-chief of BMB reports from Machado-Neto et al., 2014b.
Description Stathmin 1 belongs to the Stathmin protein family, which is characterized by the presence of a Stathmin-like domain (also known as tubulin-binding domain) that participates in interactions/sequestering of alpha/beta-tubulin heterodimers (Figure 1).
Expression Ubiquitous. Stathmin 1 is highly expressed during embryonic development. In adult cells, it is expressed during cell proliferation, and in nervous tissue and testis (revised in Curmi et al., 1999).
  Figure 2. Intracellular localization of Stathmin 1 protein in HeLa cells. Confocal analysis of HeLa cells displaying Stathmin 1 (green), Actin (red) and DAPI (blue) staining; MERGE shows the overlapped images. Scale bar: 10 μm. Note the predominant cytoplasmic localization of Stathmin 1. Anti-Stathmin 1 (OP18; sc-55531) was from Santa Cruz Biotechnology, (Santa Cruz, CA, USA), Phalloidin (A12379) and DAPI (P-36931) were from Invitrogen (Carlsbad, CA, USA). Personal data.
Localisation Stathmin 1 is predominantly found in the cytoplasm (Figure 2).
  Figure 3. Stathmin 1 signaling. Stathmin 1 may be phosphorylated on serine sites by cyclin-dependent kinases (CDKs), mitogen-activated protein kinases (MAPKs), phosphoinositide 3-kinase (PI3K), aurora kinase B (AURKB), protein kinase A (PKA), and Ca2+/calmodulin-dependent protein kinases (CamKs), leading to microtubule stability. On the other hand, Stathmin 1 may be dephosphorylated by protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 2B (PP2B), resulting in microtubule instability. Abbreviations: TKR: tyrosine kinase receptor; P: phosphorylation; Ac: acetylation. This figure was performed using Servier Medical Art tools (
Function Stathmin 1 is a phosphoprotein that participates in microtubule catastrophe and/or in the sequestering of alpha/beta-tubulin heterodimers, regulates microtubule dynamics, cell cycle progression, proliferation, motility and survival (Curmi et al., 1999; Belletti and Baldassarre, 2011). The main mechanism of regulation of Stathmin 1 activity on based in its phophorylated and unphosphorylated status at serine sites (residues 16, 25, 38 and 68). Stathmin 1 phosphorylation at serine 16 and/or 63 reduces the affinity between Stathmin 1 and alpha/beta-tubulin heterodimers. The proteins that are able to phosphorylate Stathmin 1 at serine 16 and/or 63 are: aurora kinase B, protein kinase A (PKA), P21 protein (Cdc42/Rac)-activated kinase (PAK1) and Ca2+/calmodulin-dependent protein kinases (CamKs). Serine 25 and/or 38 may be phosphorylated by cyclin-dependent kinases (CDKs), mitogen-activated protein kinases (MAPKs) and phosphoinositide 3-kinase (PI3K) (Belletti and Baldassarre, 2011). Phosphatase proteins that are able to dephosphorylate Stathmin 1 includes: protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 2B (PP2B) (Guy et al., 1992; Tournebize et al., 1997; Mistry et al., 1998) (Figure 3).
Homology Stathmin 1 shares high homology with the other members of the Stathmin protein family including Stathmin-like 2 (also named SCG10), Stathmin-like 3 (also named SCLIP) and Stathmin-like 4 (also named RB3). Stathmin 1 also shares high homology among different species (Table 1).


Note Recurrent mutations in the STMN1 gene are rare, 10 missense, 8 nonsense, 1 nonstop extension and 3 coding silent mutations are reported at COSMIC (catalogue of somatic mutations in cancer; COSMIC). In human esophageal adenocarcinoma, STMN1 Q18E mutation was identified and presented transformation potential in vitro and in vivo in NIH3T3 cells (Misek et al., 2002). Studies performed in leukemia cells indicate that the Q18E mutation results in Stathmin 1 hyperactivity and contributes to chromosomal instability (Holmfeldt et al., 2006).

Implicated in

Entity Various cancers
Note The role and clinical impact of Stathmin 1 has been extensively addressed in many types of human cancers. In general, the increased expression of Stathmin 1 is found in many cancers and confers a poor prognosis (revised in Belletti and Baldassarre, 2011 and Rana et al., 2008). Using cancer cell line models, several groups have demonstrated that Stathmin 1 inhibition may partially reverse the malignant phenotype.
Entity Hematopoietic neoplasms
Note Stathmin 1 was initially identified by proteomics analysis of HL60 leukemia cells (Feuerstein and Cooper, 1983). In primary acute leukemia and lymphoma samples, and leukemia cell lines, several independent groups have showed that Stathmin 1 is highly expressed (Hanash et al., 1988; Melhem et al., 1991; Melhem et al., 1997; Roos et al., 1993; Machado-Neto et al., 2014a; Brattsand et al., 1993); however its impact on survival outcome remains unknown. A recent study of immunophenotypic and molecular features of a large series of follicular lymphomas indicated that Stathmin 1 represents an useful novel diagnostic marker for these diseases (Marafioti et al., 2013). Importantly, Stathmin 1 silencing resulted in marked inhibition of tumorigenicity, proliferation and clonogenicity in leukemia cell lines (K562, U937 and Namalwa cells) (Machado-Neto et al., 2014a; Jeha et al., 1996; Iancu et al., 2001).
In a study that focused on the identification of biomarkers of human aging and aging-related diseases, Stathmin 1 was found upregulated in plasma samples from myelodysplastic patients (Jiang et al., 2008). Recently, increased levels of Stathmin 1 were reported in bone marrow and CD34+ cells from high-risk myelodysplastic syndromes patients and during disease progression (Machado-Neto et al., 2014a). Notably, higher Stathmin 1 expression was associated with high-risk disease and higher bone marrow blasts percentage (Machado-Neto et al., 2014a), but did not impacted survival.
Stathmin 1 was also identified as one of the 15 most relevant genes for determining the outcome in myeloma multiple patients by microarray approach (Decaux et al., 2008).
Entity Breast cancer
Note Using Western blot analysis, Brattsand (Brattsand, 2000) reported that Stathmin 1 expression positively correlated with proliferation status and aggressiveness in a panel of 151 primary breast carcinoma samples. Similar results were found by Curmi and colleagues (Curmi et al., 2000), who also reported that Stathmin 1 overexpression correlated with loss of steroid receptors, histopathological grade III and mitotic index. Importantly, Stathmin 1 expression was indicated as a potential tool for predicting the outcome of breast cancer patients with lymph node metastasis and its expression was increased in the group with poor prognosis (Oishi et al., 2007). By multivariate analysis, high Stathmin 1 expression predicted reduced disease-free survival (Saal et al., 2007; Golouh et al., 2008; Baquero et al., 2012) and overall survival (Baquero et al., 2012). Decreased Stathmin 1 phosphorylation at serine 16 (an inhibitory site) correlated with the more metastatic phenotype in breast cancers cell lines and primary tumors (Li et al., 2011). Using breast cancer cell lines and gene therapy tools, Stathmin 1 inhibition, by adenovirus-mediated gene transfer of anti-Stathmin 1 ribozyme, resulted in a dose-dependent inhibition of proliferation, apoptosis induction and had an additive effect together low concentration of taxol treatment in vitro and in vivo (Miceli et al., 2013).
Entity Ovarian cancer
Note Stathmin 1 overexpression has been described in ovarian cancer patients (Alaiya et al., 1997; Price et al., 2000). Wei and colleagues (Wei et al., 2008) observed that Stathmin 1 was expressed in all ovarian cancer samples analyzed and higher levels were observed in the metastatic tumors and negatively impacted survival by univariate analysis. In agreement, Stathmin 1 overexpression was found in primary high-grade serous ovarian carcinomas and ovarian cancer cell lines (Karst et al., 2011). High levels of Stathmin 1 predicted an unfavorable prognosis in ovarian cancer patients under paclitaxel and/or platinum therapy (Su et al., 2009; Aoki et al., 2009) also by univariate analysis. In p53 mutated ovarian cancer cell lines, Stathmin 1 silencing caused cell cycle arrest and apoptosis in vivo and in vivo (Sonego et al., 2013).
Entity Head and neck cancer
Note Using proteomics approach, Stathmin 1 was found to be differently expressed in oral squamous-cell carcinoma and laryngeal squamous-cell carcinoma (Koike et al., 2005; Sewell et al., 2007). Stathmin 1 expression was also found to be significantly increased in oral squamous-cell carcinoma cell lines and primary tumors and its high expression correlated with advanced stages of the disease and poor disease-free survival by univariate analysis (Kouzu et al., 2006). In head-neck squamous-cell carcinoma, Stathmin 1 was expressed at low levels (76% cases) and did not impact recurrence (Canzonieri et al., 2012). Cheng and colleagues (Cheng et al., 2008) identified an upregulation of Stathmin 1 in primary nasopharyngeal carcinoma and its expression was associated with recurrence and advanced stages of the disease. In agreement, Hsu and colleagues (Hsu et al., 2014) reported that Stathmin 1 was overexpressed in approximately 50% of the nasopharyngeal carcinoma samples and was associated with advanced age, high-grade tumors and was an independent predictor of worse disease-free survival. Notably, knockdown of Stathmin 1 suppressed cell cycle progression, proliferation, migration, invasion, xenograft tumor growth, induced apoptosis and potentiated paclitaxel response in nasopharyngeal carcinoma cell lines (CNE1-LMP1 and HNE2 cells) (Wu et al., 2014).
Entity Hepatocarcinoma
Note Yuan and colleagues (Yuan et al., 2006) reported a high Stathmin 1 expression in 56% of 156 hepatocarcinoma patients and high Stathmin 1 expression was associated with increased tumor size, tumor grade, metastasis, p53 mutation status and negatively impacted survival in univariate analysis. In agreement, elevated Stathmin 1 levels were also reported by Singer and colleagues (Singer et al., 2007) and were associated with the presence of undifferentiated tumors. Other studies observed an increased Stathmin 1 expression in tumor tissue compared to matched normal tissue, and a positive association between Stathmin 1 overexpression and recurrence or poor prognosis in univariate analysis (Hsieh et al., 2010; Chen et al., 2013b). In hepatocarcinoma cell lines, Stathmin 1 silencing reduced cell proliferation, viability, migration and augmented the response to paclitaxel, vinblastine and cisplatin treatment (Singer et al., 2007; Hsieh et al., 2010; Gan et al., 2010).
Entity Endometrial cancer
Note In a multicenter study including 1076 endometrial patients, Stathmin 1 overexpression was detected in 37% of cases and correlated with high grade disease and aneuploidy, and was an independent predictor of metastasis and worse disease specific survival (Trovik et al., 2011). In another study from the same group (Trovik et al., 2010), high Stathmin 1 expression was associated with a higher probability of endometrial cancer recurrence and PI3K activation. Additionally, a study conducted by Salvesen and colleagues (Salvesen et al., 2009), investigating the impact of PI3K activation in endometrial cancer, identified that high Stathmin 1 expression was an independent predictor of aggressive phenotype and worse survival. Of note, Wik and colleagues (Wik et al., 2013) reported that the levels of Stathmin 1 phosphorylation at serine 38 site were associated with poor prognosis, tumor cell proliferation, increased PIK3CA copy number and PI3K activation by multivariate analysis. Werner and colleagues (Werner et al., 2014), using endometrial cancer cell lines, showed that Stathmin 1 silencing potentiated the response to paclitaxel treatment. This finding was confirmed in vivo: endometrial cancer patients with high Stathmin 1 expression had a poor response to paclitaxel therapy (Werner et al., 2014).
Entity Bladder cancer and urothelial carcinoma
Note Using quantitative PCR targeting 110 relevant cancer genes, Dubosq and colleagues (Dubosq et al., 2012) detected Stathmin 1 as highly expressed in early recurrence, compared to late or null recurrence cancer in a cohort of 47 bladder cancer patients, suggesting a role for this protein in the time of recurrence. Bhagirath and colleagues (Bhagirath et al., 2012) reported elevated STMN1 mRNA levels in muscle invasive tumors. In agreement, patients with high Stathmin 1 expression under taxane therapy had decreased recurrence-free survival by univariate analysis (Wosnitzer et al., 2011). In a cohort of 58 urothelial carcinoma patients, multivariate analysis revealed that Stathmin 1 positivity was associated with high grade tumors, recurrence and negatively impacted survival (Lin et al., 2009).
Entity Colorectal cancer
Note In a cohort of 149 patients with colorectal cancer, high Stathmin 1 levels were an independent predictor of worse overall survival (Zheng et al., 2010). In addition, Stathmin 1 expression was associated with tumor differentiation, invasion and stage of the disease (Zheng et al., 2010). In contrast, Ogino and colleagues (Ogino et al., 2009) showed that, by multivariate analysis, Stathmin 1 positivity had a protective effect on survival in a cohort of 546 colorectal patients (stratified in obese and non-obese individuals). Interestingly, obesity had a negative impact on survival in Stathmin 1 positive patients, but not in Stathmin 1-negative patients (Ogino et al., 2009). A recent study conduced by Tan and colleagues (Tan et al., 2012) corroborated the findings from Zheng and colleagues (Zheng et al., 2010), indicating that high Stathmin 1 levels negatively impacted survival in a cohort of 324 colorectal cancer patients in univariate analysis. Tan and colleagues (Tan et al., 2012) also demonstrated functional evidences that Stathmin 1 is a positive regulator of cell proliferation, clonogenicity, migration and invasion in colorectal cancer cell lines.
Entity Gastric cancer
Note Jeon and colleagues (Jeon et al., 2010) reported that a high expression of Stathmin 1 was an independent predictor of shorter recurrence-free survival, and associated with lymph node metastasis and high grade stages in a cohort of 226 gastric cancer patients. The authors, using two different gastric cancer cell lines (SNU638 and SNU16 cells), demonstrated that Stathmin 1 silencing decreased cell proliferation, migration, invasion and xenograft tumor growth (Jeon et al., 2010). Kang and colleagues (Kang et al., 2012), and Ke and colleagues (Ke et al., 2013), identified high Stathmin 1 expression in cell lines and primary cells from gastric cancer and predicted poor prognosis by univariate analysis. Interestingly, Kang and colleagues (Kang et al., 2012) also reported that Stathmin 1 silencing reduced the malignant phenotype in vitro and in vivo, and suggested that miR-223 is involved in the regulation of Stathmin 1 expression in gastric cancer cell lines (AGS and MKN7 cells). Another study, using lentivirus mediated RNAi delivery, also demonstrated that Stathmin 1 silencing reduced cell proliferation, migration and xenograft tumor growth in MKN-45 gastric cancer cells (Akhtar et al., 2013).
Entity Prostate cancer
Note Using high-throughput immunoblotting, elevated Stathmin 1 expression was found in metastatic prostate cancer protein extracts (Varambally et al., 2005). Another study reported that Stathmin 1 expression was higher in advanced prostate tumors (Ghosh et al., 2007). Stathmin 1 silencing resulted in cell cycle arrest, reduced clonogenicity and increased apoptosis in prostate cancer cell line (LNCaP cells) (Mistry et al., 2005). In contrast, Stathmin 1 inhibition augmented the epithelial-to-mesenchymal transition and metastasis potential in another prostate cancer cell line (DU145 cells) (Williams et al., 2012).
Entity Pheochromocytomas
Note In a study conducted by Sadow and colleagues (Sadow et al., 2008), among the endocrine tumors, high levels of Stathmin 1 were observed in malignant pheochromocytomas. These results were confirmed by two other groups, who reported an overexpression of Stathmin 1 in malignant/metastatic pheochromocytomas compared to benign tumors or normal tissues (Björklund et al., 2010; Lin et al., 2011).
Entity Cervical cancer
Note A higher Stathmin 1 expression was found in primary cells and cell lines from cervical carcinoma compared to normal cervical epithelial cells and also in tumor cells compared to matched adjacent non-carcinoma tissue (Xi et al., 2009). Increased Stathmin 1 expression correlated with a worse clinical stage and metastasis (Xi et al., 2009). Another study found Stathmin 1 overexpression in all cervical and rare expression of Stathmin 1 in benign samples; the authors suggest that the analysis of Stathmin 1 may be useful diagnostically in the identification of cervical cancer (Howitt et al., 2013).
Entity Glioma
Note In a cohort of 24 glioma patients, increased Stathmin 1 levels were associated with decreased recurrence-free survival in univariate analysis (Ngo et al., 2007). Similar results were observed in a xenograft glioma nitrosourea-treated model (Ngo et al., 2007). Dong and colleagues (Dong et al., 2012) observed that Stathmin 1 expression was aberrantly expressed in vascular endothelial cells from glioma, especially in high grade cases and the Stathmin 1 silencing reduced cell proliferation and invasion, and induced apoptosis in glioma-derived microvascular endothelial cells.
Entity Lung cancer
Note Chen and colleagues (Chen et al., 2003) reported a high expression of Stathmin 1 in a cohort of 93 lung adenocarcinoma patients and this expression was associated with poorly differentiated tumors. Stathmin 1 overexpression was also found in primary non-small cell lung tumors matched with normal tissues (Singer et al., 2009). Rosell and colleagues (Rosell et al., 2003) observed that high Stathmin 1 levels negatively affected the time to progression in non-small-cell lung cancer patients, by univariate analysis. Of note, Stathmin 1 inhibition decreased proliferation, migration and invasion in non-small cell lung cancer cell lines (Calu-1 and Calu-6 cells) (Singer et al., 2009).
Entity Medulloblastoma
Note Using a microarray approach, Stathmin 1 was identified as differentially expressed in primary medulloblastoma samples and it was associated with unfavorable overall survival (Neben et al., 2004). Accordingly, Kuo and colleagues (Kuo et al., 2009) reported that Stathmin 1 correlated with tumor dissemination and predicted decreased survival in medulloblastoma patients, by univariate analysis in both studies.
Entity Pancreatic cancer
Note Lu and colleagues (Lu et al., 2014) reported that Stathmin 1 was overexpressed in pancreatic cancer samples and that high Stathmin 1 levels were correlated with vascular emboli, tumor size, and negatively impacted overall survival in univariate analysis. In addition, Stathmin 1 silencing in pancreatic cancer cells resulted in reduced cell proliferation, clonogenicity and cell cycle arrest (Lu et al., 2014; Jiang et al., 2009).
Entity Thyroid cancer
Note Using cDNA microarray approach, Onda and colleagues (Onda et al., 2004) reported that Stathmin 1 was overexpressed in all anaplastic thyroid cancer cell lines analyzed and this was confirmed by immunohistochemical analyses in primary samples. Another study also observed that Stathmin 1 was highly expressed in anaplastic thyroid carcinomas (Sadow et al., 2008).
Entity Cholangiocarcinoma
Note In a cohort of 80 extrahepatic cholangiocarcinoma patients, high levels of Stathmin 1 correlated with invasion and shorter recurrence-free survival by multivariate analysis (Watanabe et al., 2014). The authors also demonstrated that Stathmin 1 silencing resulted in reduced cell proliferation capacity and increased sensitivity to paclitaxel treatment in a cholangiocarcinoma cell line (Watanabe et al., 2014).
Entity Melanoma
Note In primary melanoma samples, Stathmin 1 was highly expressed in two independent cohorts, but did not impacts survival (Chen et al., 2013a). Stathmin 1 silencing reduced cell proliferation and migration. Furthermore, Stathmin 1 overexpression potentiated both these cell processes in melanoma cell lines (Malme-3M and A375 cells) (Chen et al., 2013a).
Entity Mesothelioma
Note Overexpression of Stathmin 1 was found in all mesothelioma cell lines tested (LRK1A, H2052, 211H, H290, MS1, H513 and H28 cells) and also in primary tumors compared to its matched normal tissue (Kim et al., 2007).
Entity Pediatric brain cancer
Note Using 2-dimensional differential in-gel electrophoresis, immunohistochemistry and quantitative PCR, Stathmin 1 was identified as highly expressed in primary primitive neuroectodermal tumors compared to ependymomas samples (de Bont et al., 2007).
Entity Renal cancer
Note In Wilms tumors, Stathmin 1 was highly expressed in high grade compared to low grade tumors (Takahashi et al., 2002).
Entity Sarcoma
Note Belletti and colleagues (Belletti et al., 2008) reported that Stathmin 1 was increased in recurrent and metastatic sarcoma samples. In addition, overexpression of the wild type Stathmin 1 or mutated Stathmin 1 (Q18E, gain-of-function mutation) potentiated the malignant phenotype in the sarcoma cell line HT1080 (Belletti et al., 2008).
Entity Salivary cancer
Note Using 2-dimensional differential in-gel electrophoresis, increased Stathmin 1 expression was found in adenoid cystic carcinoma (Nakashima et al., 2006).

To be noted

Although Stathmin 1 regulates multiple important cellular functions, Schubart and colleagues (Schubart et al., 1996) initially reported that Stmn1 knockout mice had normal growth, development, reproduction and did not show any aberrant phenotype. Later on, it was observed that Stmn1 knockout mice developed an axonopathy of the central and peripheral nervous systems with aging (Liedtke et al., 2002). In addition, Shumyatsky and colleagues (Shumyatsky et al., 2005) reported that Stmn1 knockout mice had reduced memory in amygdala-dependent fear conditioning, failed to recognize danger environments (Shumyatsky et al., 2005) and exhibited accelerated fear extinction (Martel et al., 2012). Using well-defined mouse models of carcinogenesis and Stmn1 knockout mice, D'Andrea and colleagues (D'Andrea et al., 2012) demonstrated that Stmn1 did not impact on cancer onset. Regarding hematopoietic-related processes, Stmn1 knockout mice presented two human hematopoietic disease phenotypes: megaloblastic anemia and thrombocytosis (Ramlogan-Steel et al., 2012). Notably, Stmn1 knockout mice did not have any that were alterations incompatible with life, and Stathmin 1 inhibition in several types of cancer cells reduced the malignant phenotype, making it an attractive target for anticancer therapies.


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This paper should be referenced as such :
JA Machado-Neto, F Traina
STMN1 (stathmin 1)
Atlas Genet Cytogenet Oncol Haematol. 2015;19(2):126-874.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(1;11)(p36;p11) STMN1::SPI1

External links


HGNC (Hugo)STMN1   6510
Entrez_Gene (NCBI)STMN1    stathmin 1
AliasesC1orf215; LAP18; Lag; OP18; 
PP17; PP19; PR22; SMN
GeneCards (Weizmann)STMN1
Ensembl hg19 (Hinxton)ENSG00000117632 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000117632 [Gene_View]  ENSG00000117632 [Sequence]  chr1:25900116-25906153 [Contig_View]  STMN1 [Vega]
ICGC DataPortalENSG00000117632
TCGA cBioPortalSTMN1
Genatlas (Paris)STMN1
SOURCE (Princeton)STMN1
Genetics Home Reference (NIH)STMN1
Genomic and cartography
GoldenPath hg38 (UCSC)STMN1  -     chr1:25900116-25906153 -  1p36.11   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)STMN1  -     1p36.11   [Description]    (hg19-Feb_2009)
GoldenPathSTMN1 - 1p36.11 [CytoView hg19]  STMN1 - 1p36.11 [CytoView hg38]
Genome Data Viewer NCBISTMN1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB209282 AB451319 AB451448 AK054594 AK056768
RefSeq transcript (Entrez)NM_001145454 NM_005563 NM_152497 NM_203399 NM_203401
Consensus coding sequences : CCDS (NCBI)STMN1
Gene ExpressionSTMN1 [ NCBI-GEO ]   STMN1 [ EBI - ARRAY_EXPRESS ]   STMN1 [ SEEK ]   STMN1 [ MEM ]
Gene Expression Viewer (FireBrowse)STMN1 [ Firebrowse - Broad ]
GenevisibleExpression of STMN1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)3925
GTEX Portal (Tissue expression)STMN1
Human Protein AtlasENSG00000117632-STMN1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP16949   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP16949  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP16949
Domaine pattern : Prosite (Expaxy)STATHMIN_1 (PS00563)    STATHMIN_2 (PS01041)    STATHMIN_3 (PS51663)   
Domains : Interpro (EBI)Stathmin_CS    Stathmin_fam    Stathmin_sf   
Domain families : Pfam (Sanger)Stathmin (PF00836)   
Domain families : Pfam (NCBI)pfam00836   
Conserved Domain (NCBI)STMN1
AlphaFold pdb e-kbP16949   
Human Protein Atlas [tissue]ENSG00000117632-STMN1 [tissue]
Protein Interaction databases
IntAct (EBI)P16949
Ontologies - Pathways
Ontology : AmiGOmitotic cytokinesis  protein binding  cytoplasm  cytosol  microtubule  microtubule depolymerization  microtubule depolymerization  microtubule depolymerization  mitotic spindle organization  signal transduction  axonogenesis  brain development  response to virus  tubulin binding  tubulin binding  tubulin binding  membrane  regulation of microtubule polymerization or depolymerization  regulation of microtubule polymerization or depolymerization  negative regulation of microtubule polymerization  neuron projection development  negative regulation of Rho protein signal transduction  intracellular signal transduction  neuron projection  hepatocyte growth factor receptor signaling pathway  positive regulation of cellular component movement  negative regulation of stress fiber assembly  establishment of skin barrier  extracellular exosome  negative regulation of thrombin-activated receptor signaling pathway  negative regulation of guanyl-nucleotide exchange factor activity  
Ontology : EGO-EBImitotic cytokinesis  protein binding  cytoplasm  cytosol  microtubule  microtubule depolymerization  microtubule depolymerization  microtubule depolymerization  mitotic spindle organization  signal transduction  axonogenesis  brain development  response to virus  tubulin binding  tubulin binding  tubulin binding  membrane  regulation of microtubule polymerization or depolymerization  regulation of microtubule polymerization or depolymerization  negative regulation of microtubule polymerization  neuron projection development  negative regulation of Rho protein signal transduction  intracellular signal transduction  neuron projection  hepatocyte growth factor receptor signaling pathway  positive regulation of cellular component movement  negative regulation of stress fiber assembly  establishment of skin barrier  extracellular exosome  negative regulation of thrombin-activated receptor signaling pathway  negative regulation of guanyl-nucleotide exchange factor activity  
Pathways : BIOCARTAStathmin and breast cancer resistance to antimicrotubule agents [Genes]   
Pathways : KEGGMAPK signaling pathway    MicroRNAs in cancer   
NDEx NetworkSTMN1
Atlas of Cancer Signalling NetworkSTMN1
Wikipedia pathwaysSTMN1
Orthology - Evolution
GeneTree (enSembl)ENSG00000117632
Phylogenetic Trees/Animal Genes : TreeFamSTMN1
Homologs : HomoloGeneSTMN1
Homology/Alignments : Family Browser (UCSC)STMN1
Gene fusions - Rearrangements
Fusion : MitelmanBTF3L4::STMN1 [1p32.3/1p36.11]  
Fusion : MitelmanKIAA1211::STMN1 [4q12/1p36.11]  
Fusion : QuiverSTMN1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerSTMN1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)STMN1
Exome Variant ServerSTMN1
GNOMAD BrowserENSG00000117632
Varsome BrowserSTMN1
ACMGSTMN1 variants
Genomic Variants (DGV)STMN1 [DGVbeta]
DECIPHERSTMN1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisSTMN1 
ICGC Data PortalSTMN1 
TCGA Data PortalSTMN1 
Broad Tumor PortalSTMN1
OASIS PortalSTMN1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICSTMN1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DSTMN1
Mutations and Diseases : HGMDSTMN1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)STMN1
DoCM (Curated mutations)STMN1
CIViC (Clinical Interpretations of Variants in Cancer)STMN1
NCG (London)STMN1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry STMN1
NextProtP16949 [Medical]
Target ValidationSTMN1
Huge Navigator STMN1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDSTMN1
Pharm GKB GenePA35491
Clinical trialSTMN1
DataMed IndexSTMN1
PubMed286 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 : Fri Oct 8 21:28:55 CEST 2021

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