Atlas of Genetics and Cytogenetics in Oncology and Haematology

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BCL2L12 (BCL2-like 12 (proline-rich))

Written2008-08Christos Kontos, Hellinida Thomadaki, Andreas Scorilas
Department of Biochemistry, Molecular Biology, Faculty of Biology, University of Athens. 157 01, Panepistimiopolis, Athens, Greece

(Note : for Links provided by Atlas : click)


Other aliasBPR
LocusID (NCBI) 83596
Atlas_Id 773
Location 19q13.33  [Link to chromosome band 19q13]
Location_base_pair Starts at and ends at bp from pter
Local_order Telomere to centromere.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BCL2L12 (19q13.33) / LENG8 (19q13.42)BCL2L12 (19q13.33) / LOC100507412 (-)BCL2L12 (19q13.33) / PRMT1 (19q13.33)
PRMT1 (19q13.33) / BCL2L12 (19q13.33)TBC1D17 (19q13.33) / BCL2L12 (19q13.33)


Description Spanning 8.8 kb of genomic DNA, the BCL2L12 gene consists of 6 introns and 7 exons.
Transcription The BCL2L12 gene has three splice variants with differences in exon 3. The predominant form is 1855 bp and encodes the full-length protein. The second splice variant lacks exon 3, which consists of 143 bp, thus resulting in no ORF. The third splice variant lacks 3 bp at the beginning of exon 3 and encodes a protein having one amino acid residue less than the full-lengh protein.
Pseudogene Not identified so far.


Description The BCL2L12 protein is composed of 334 amino acids, with a calculated molecular mass of 36.8 kDa and an isoelectric point of 9.45. The BCL2L12 protein contains one BH2 and one putative BH3 domain, one proline-rich region similar to the TC21 protein, and five consensus PXXP tetrapeptide sequences.
BCL2L12 protein also includes various putative posttranslational modification sites. There are numerous potential sites for O-glycosylation. Furthermore, several possible sites of phosphorylation have been identified for cAMP-dependent protein kinase, protein kinase C, and casein kinase 2. In addition, several N-myristoylation sites have been predicted. The BCL2L12 protein was found to have proline-rich sites. One PPPP site as well as five PP amino acid sites are present in this protein. Eight putative PXXP motifs were also identified. Proline-rich motifs are characterized by the presence of the consensus PXXP tetrapeptide, found in all proline-rich proteins identified to date. It is known that SH3 domains recognize proline-rich sequences and that all known SH3-binding proteins contain proline-rich regions with at least one PXXP motif. Proline-rich domains have been identified in a number of diverse proteins such as epidermal growth factors, phosphatidylinositol 3-kinase, and, more recently, the small GTPase RRAS protein and members of the RRAS superfamily such as the TC21 protein. Moreover, the amino acid loop (PPSPEP) at positions 271-276 of the BCL2L12 protein is identical with the PXXP motif present in the RRAS and TC21 oncogenes. This motif is required for integrin activation.
The splice variant BCL2L12-A is expected to encode a truncated protein of 176 amino acids with five PP proline sites, two putative PXXP motifs, and no BH2 homology domain.
Expression High levels of BCL2L12 expression are typically found in glandular epithelia in various organs, such as gastrointestinal tract and/or breast. Lower BCL2L12 protein expression has been found in prostate tissue.
Function BCL2L12 is involved in apoptosis. However, its proapoptotic or antiapoptotic role in different types of cells and conditions remains unclear.
Homology Human BCL2L12 shares 98% and 96% identity with chimpanzee and Rhesus monkey Bcl2l12, respectively, and 83% identity with rat/mouse Bc2l12 as well.


Note No germinal or somatic mutations are identified to be associated with cancer so far.

Implicated in

Entity Human Leukemias, Solid Tumors.
Note Significant alterations of BCL2L12 mRNA expression have been noticed in HL-60 leukemia cells as well as in MCF7 breast cancer cells, after treatment with various antineoplastic agents including cisplatin, carboplatin, doxorubicin, methotrexate, and etoposide. These important modulations of BCL2L12 mRNA levels seem to depend on both the apoptotic inducer and the specific apoptotic pathway, implying a strong relationship between alterations in BCL2L12 mRNA levels and apoptosis.
Expression analysis of the BCL2L12 gene has showed that BCL2L12 mRNA expression may be considered as a new prognostic marker for breast cancer, as breast tumours of lower stage or grade are more often BCL2L12-positive. Moreover, breast cancer patients with BCL2L12 mRNA expression are less likely to relapse or die, in comparison with BCL2L12-negative patients. Regarding BCL2L12 gene expression in colon cancer, the BCL2L12-A transcript is overexpressed in cancer tissues as compared to their normal mucosa counterparts. BCL2L12-A mRNA expression is also associated with colon cancer progression, since it is usually greater in patients being at the initial stages of the disease or having negative nodal status. BCL2L12 were found also to inhibits post-mitochondrial apoptosis signaling in glioblastoma.
Cytogenetics No cytogenetic abnormalities are identified so far.
Hybrid/Mutated Gene Not identified so far.


Alterations in mRNA expression of apoptosis-related genes BCL2, BAX, FAS, caspase-3, and the novel member BCL2L12 after treatment of human leukemic cell line HL60 with the antineoplastic agent etoposide.
Floros KV, Thomadaki H, Florou D, Talieri M, Scorilas A.
Ann N Y Acad Sci 2006; 1090: 89-97.
PMID 17384250
Expression analysis of BCL2L12, a new member of apoptosis-related genes, in colon cancer.
Mathioudaki K, Scorilas A, Papadokostopoulou A, Xynopoulos D, Arnogianaki N, Agnanti N, Talieri M.
Biol Chem 2004; 385: 779-783.
PMID 15493871
Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family.
Scorilas A, Kyriakopoulou L, Yousef GM, Ashworth LK, Kwamie A, Diamandis EP.
Genomics 2001; 72: 217-221.
PMID 11401436
BCL2L12 inhibits post-mitochondrial apoptosis signaling in glioblastoma.
Stegh AH, Kim H, Bachoo RM, Forloney KL, Zhang J, Schulze H, Park K, Hannon GJ, Yuan J, Louis DN, DePinho RA, Chin L.
Genes Dev. 2007 Jan 1;21(1):98-111.
PMID 17210792
Expression of BCL2L12, a new member of apoptosis-related genes, in breast tumors.
Talieri M, Diamandis EP, Katsaros N, Gourgiotis D, Scorilas A.
Thromb Haemost 2003; 89: 1081-1088.
PMID 12783122
Prognostic value of the apoptosis related genes BCL2 and BCL2L12 in breast cancer.
Thomadaki H, Talieri M, Scorilas A.
Cancer Lett 2007; 247: 48-55.
PMID 16647810


This paper should be referenced as such :
Kontos, C ; Thomadaki, H ; Scorilas, A
BCL2L12 (BCL2-like 12 (proline-rich))
Atlas Genet Cytogenet Oncol Haematol. 2009;13(7):467-468.
Free journal version : [ pdf ]   [ DOI ]
On line version :

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  BCL2L12/PRMT1 (19q13)

External links

Genomic and cartography
Gene and transcription
RefSeq transcript (Entrez)
RefSeq genomic (Entrez)
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
BioGPS (Tissue expression)83596
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Protein Interaction databases
Ontologies - Pathways
Clinical trials, drugs, therapy
canSAR (ICR) (select the gene name)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Oct 18 17:29:34 CEST 2018

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