BCL2L12

Bcl-2-like protein 12 is a protein that in humans is encoded by the BCL2L12 gene.[5][6]

BCL2L12
Identifiers
Aliases	BCL2L12, BCL2 like 12
External IDs	OMIM: 610837 MGI: 1922986 HomoloGene: 12619 GeneCards: BCL2L12
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.33 Start 49,665,142 bp[1] End 49,673,916 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 B3 Start 44,991,222 bp[2] End 44,998,712 bp[2]
Gene ontology Molecular function • p53 binding • GO:0001948 protein binding Cellular component • membrane • cell nucleus Biological process • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator • positive regulation of transcription from RNA polymerase II promoter • inhibition of cysteine-type endopeptidase activity involved in apoptotic process • negative regulation of cellular senescence • apoptotic process • regulation of apoptotic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	83596	75736
Ensembl	ENSG00000126453	ENSMUSG00000003190
UniProt	Q9HB09	n/a
RefSeq (mRNA)	NM_001040668 NM_001282516 NM_001282517 NM_001282519 NM_001282520 NM_001282521 NM_138639	NM_029410
RefSeq (protein)	NP_001035758 NP_001269445 NP_001269446 NP_001269448 NP_001269449 NP_001269450 NP_619580	n/a
Location (UCSC)	Chr 19: 49.67 – 49.67 Mb	Chr 7: 44.99 – 45 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the Bcl-2 protein family. Bcl-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a Bcl-2 homology domain 2 (BH2). The function of this gene has not yet been determined. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.[5]

Bcl2L12 expression is upregulated in most human glioblastomas. Expression of Bcl2L12 results in resistance to apoptosis. Bcl2L12 directly neutralizes caspase-7 (CASP7) and indirectly neutralizes caspase-3 (CASP3) by an indirect mechanism.[7] Both caspase enzymes are known to play essential roles in the execution phase of apoptosis.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000126453 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000003190 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Bcl2L12 Bcl2-like 12 (proline rich)".
6. Scorilas A, Kyriakopoulou L, Yousef GM, Ashworth LK, Kwamie A, Diamandis EP (March 2001). "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". Genomics. 72 (2): 217–21. doi:10.1006/geno.2000.6455. PMID 11401436.
7. Stegh AH, Kim H, Bachoo RM, Forloney KL, Zhang J, Schulze H, Park K, Hannon GJ, Yuan J, Louis DN, DePinho RA, Chin L (January 2007). "Bcl2L12 inhibits post-mitochondrial apoptosis signaling in glioblastoma". Genes Dev. 21 (1): 98–111. doi:10.1101/gad.1480007. PMC 1759904. PMID 17210792.
8. Wilson MR (August 1998). "Apoptosis: unmasking the executioner". Cell Death Differ. 5 (8): 646–52. doi:10.1038/sj.cdd.4400394. PMID 10200519.

External links

• Human BCL2L12 genome location and BCL2L12 gene details page in the UCSC Genome Browser.

Further reading

• Hammond PW, Alpin J, Rise CE, et al. (2001). "In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries". J. Biol. Chem. 276 (24): 20898–906. doi:10.1074/jbc.M011641200. PMID 11283018.
• Scorilas A, Kyriakopoulou L, Yousef GM, et al. (2001). "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". Genomics. 72 (2): 217–21. doi:10.1006/geno.2000.6455. PMID 11401436.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Talieri M, Diamandis EP, Katsaros N, et al. (2004). "Expression of BCL2L12, a new member of apoptosis-related genes, in breast tumors". Thromb. Haemost. 89 (6): 1081–8. doi:10.1055/s-0037-1613411. PMID 12783122.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Mathioudaki K, Scorilas A, Papadokostopoulou A, et al. (2005). "Expression analysis of BCL2L12, a new member of apoptosis-related genes, in colon cancer". Biol. Chem. 385 (9): 779–83. doi:10.1515/BC.2004.101. PMID 15493871.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.