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Gene Review

STOML2  -  stomatin (EPB72)-like 2

Homo sapiens

Synonyms: EPB72-like protein 2, HSPC108, Paraprotein target 7, Paratarg-7, SLP-2, ...
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Disease relevance of STOML2


High impact information on STOML2

  • Unlike SLP-1, SLP-2 is also present in mature human erythrocytes ( approximately 4,000 +/- 5,600 (+/- 2 S.D.) copies/cell) [2].
  • The gene for human SLP-2, HUSLP2, is present on chromosome 9p13 [2].
  • Northern and Western blots for SLP-1 and SLP-2 reveal a wide but incompletely overlapping tissue distribution [2].
  • We hypothesize that SLP-2 may link stomatin or other integral membrane proteins to the peripheral cytoskeleton and thereby play a role in regulating ion channel conductances or the organization of sphingolipid and cholesterol-rich lipid rafts [2].
  • SLP-2 partitions into both Triton X-100-soluble and -insoluble pools in erythrocyte ghost membranes or when expressed in cultured COS cells and migrates anomalously on SDS-polyacrylamide gel electrophoresis analysis with apparent mobilities of approximately 45,500, 44,600, and 34,300 M(r) [2].

Biological context of STOML2

  • Comparison of the STOML2 cDNA sequence with human genomic DNA indicated that the gene encoding STOML2 was 3,250 bp long and consisted of ten exons interrupted by nine introns [3].
  • We have mapped STOML2 to HSA chromosome 9p13.1, a region that is rearranged in some cancers and thought to contain the gene responsible for acromesomelic dysplasia [3].
  • KYSE450 cells transfected with antisense SLP-2 showed decreased cell growth, proliferation, tumorigenecity, and cell adhesion [1].
  • Decreased cell growth, cell adhesion, and tumorigenesis in the antisense transfectants revealed that SLP-2 may be important in tumorigenesis [1].
  • Antisense SLP-2 eukaryotic expression plasmids were constructed and transfected into human ESCC cell line KYSE450 [1].

Anatomical context of STOML2

  • Northern blot analysis of a panel of poly(A)(+) mRNA from normal human adult tissues showed that a single 1.3-kb mRNA transcript encoding STOML2 was ubiquitously expressed, with relatively higher levels in skeletal muscle and heart compared to other tissues [3].

Other interactions of STOML2

  • The predicted polypeptide sequence of STOML2 could be delineated into three major domains: an N-terminal alpha-helical region; a domain with significant similarity to a 172 amino acid region of the HSA stomatin polypeptide, composed of an alternating alpha-helical and beta-sheet structure and a C-terminal domain that was mostly alpha-helical [3].
  • A cDNA encoding a novel second member of the Band7/stomatin-like/SPFH domain family in humans designated stomatin-like 2 (STOML2) has been isolated using the technique of cDNA Representational Difference Analysis [3].

Analytical, diagnostic and therapeutic context of STOML2


  1. Stomatin-like protein 2 is overexpressed in cancer and involved in regulating cell growth and cell adhesion in human esophageal squamous cell carcinoma. Zhang, L., Ding, F., Cao, W., Liu, Z., Liu, W., Yu, Z., Wu, Y., Li, W., Li, Y., Liu, Z. Clin. Cancer Res. (2006) [Pubmed]
  2. Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues. Wang, Y., Morrow, J.S. J. Biol. Chem. (2000) [Pubmed]
  3. A novel member of the STOMATIN/EPB72/mec-2 family, stomatin-like 2 (STOML2), is ubiquitously expressed and localizes to HSA chromosome 9p13.1. Owczarek, C.M., Treutlein, H.R., Portbury, K.J., Gulluyan, L.M., Kola, I., Hertzog, P.J. Cytogenet. Cell Genet. (2001) [Pubmed]
  4. Mass spectrometrical verification of stomatin-like protein 2 (SLP-2) primary structure. John, J.P., Anrather, D., Pollak, A., Lubec, G. Proteins (2006) [Pubmed]
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