BCL2L2: Difference between revisions

BCL2L2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1MK3, 1O0L, 1ZY3, 2Y6W, 4CIM
Identifiers
Aliases	BCL2L2, BCL-W, BCL2-L-2, BCLW, PPP1R51, BCL2 like 2
External IDs	OMIM: 601931; MGI: 108052; HomoloGene: 2989; GeneCards: BCL2L2; OMA:BCL2L2 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	23,311,751 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	55,125,691 bp
RNA expression pattern
	Top expressed in
	C1 segment; ; prefrontal cortex; ; amygdala; ; right frontal lobe; ; postcentral gyrus; ; lateral nuclear group of thalamus; ; Brodmann area 9; ; orbitofrontal cortex; ; cingulate gyrus; ; muscle layer of sigmoid colon;
	Top expressed in
	medial dorsal nucleus; ; lobe of cerebellum; ; habenula; ; subiculum; ; cerebellar vermis; ; medial geniculate nucleus; ; pontine nuclei; ; ventral tegmental area; ; medial vestibular nucleus; ; lateral geniculate nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding; protein homodimerization activity; disordered domain specific binding; identical protein binding; protein heterodimerization activity; BH domain binding;
Cellular component	cytoplasm; cytosol; mitochondrial membranes; mitochondrion; membrane; mitochondrial outer membrane; Bcl-2 family protein complex; nucleus; nuclear inclusion body;
Biological process	spermatogenesis; regulation of apoptotic process; negative regulation of apoptotic process; Sertoli cell proliferation; apoptotic process; intrinsic apoptotic signaling pathway in response to DNA damage; extrinsic apoptotic signaling pathway in absence of ligand; negative regulation of intrinsic apoptotic signaling pathway; cellular response to estradiol stimulus; cellular response to amyloid-beta;
	Sources:Amigo / QuickGO
Orthologs
	599
	12050
	ENSG00000129473
	ENSMUSG00000089682
	Q92843
	P70345
	NM_004050; NM_001199839
	NM_007537
	NP_001186768; NP_004041
	NP_031563
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 06:07, 15 January 2024

Bcl-2-like protein 2 is a 193-amino acid protein that in humans is encoded by the BCL2L2 gene on chromosome 14 (band q11.2-q12).^[5]^[6]^[7] It was originally discovered by Leonie Gibson, Suzanne Cory and colleagues at the Walter and Eliza Hall Institute of Medical Research, who called it Bcl-w.^[8]

Function

This gene encodes a pro-survival (anti-apoptotic) member of the bcl-2 protein family, and is most similar to Bcl-xL.^[7] The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of NGF- and BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult spermatogenesis.^[6]^[9]^[7]

Clinical significance

High levels of Bcl-w are seen in many cancers, including glioblastoma, colorectal cancer, non-small-cell lung carcinoma, and breast cancer.^[7] Breast cancer patients with metastasis have higher Bcl-w than breast cancer patients only having primary tumor.^[7] Elevated levels of Bcl-w has been shown to protect neurons from cell death induced by amyloid beta.^[7] Parkinson's disease patients with a mutant PARK2 gene have elevated Bcl-w.^[7] Bcl-w has been shown to contribute to cellular senescence.^[7]

Quercetin has been shown to inhibit the PI3K/AKT pathway leading to downregulation of Bcl-w.^[10]^[7]

Interactions

BCL2L2 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000129473 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000089682 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S (October 1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.
^ ^a ^b "Entrez Gene: BCL2L2 BCL2-like 2".
^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ Hartman ML, Czyz M (2020). "BCL-w: apoptotic and non-apoptotic role in health and disease". Cell Death & Disease. 11 (4): 2260. doi:10.1038/s41419-020-2417-0. PMC 7174325. PMID 32317622.
^ Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.
^ Kelly GL, Strasser A (2020). "Toward Targeting Antiapoptotic MCL-1 for Cancer Therapy". Annual Review of Cancer Biology. 4: 299–313. doi:10.1146/annurev-cancerbio-030419-033510. hdl:11343/252362.
^ Paez-Ribes M, González-Gualda E, Doherty GJ, Muñoz-Espín D (2019). "Targeting senescent cells in translational medicine". EMBO Molecular Medicine. 11 (12): e10234. doi:10.15252/emmm.201810234. PMC 6895604. PMID 31746100.
^ Hsu SY, Lin P, Hsueh AJ (September 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members". Mol. Endocrinol. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.
^ O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (January 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
^ ^a ^b Ayllón V, Cayla X, García A, Fleischer A, Rebollo A (July 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.
^ Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
^ Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (October 2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30. doi:10.1023/A:1011319901057. PMID 11483855. S2CID 23119757.
^ Holmgreen SP, Huang DC, Adams JM, Cory S (June 1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID 10381646.

External links

Human BCL2L2 genome location and BCL2L2 gene details page in the UCSC Genome Browser.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000129473 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000089682 – 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.

[pmid8761287-5] Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S (October 1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.

[entrez-6] "Entrez Gene: BCL2L2 BCL2-like 2".

[pmid32317622-7] ^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ Hartman ML, Czyz M (2020). "BCL-w: apoptotic and non-apoptotic role in health and disease". Cell Death & Disease. 11 (4): 2260. doi:10.1038/s41419-020-2417-0. PMC 7174325. PMID 32317622.

[Gibson1996-8] Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75. PMID 8761287.

[9] Kelly GL, Strasser A (2020). "Toward Targeting Antiapoptotic MCL-1 for Cancer Therapy". Annual Review of Cancer Biology. 4: 299–313. doi:10.1146/annurev-cancerbio-030419-033510. hdl:11343/252362.

[pmid31746100-10] Paez-Ribes M, González-Gualda E, Doherty GJ, Muñoz-Espín D (2019). "Targeting senescent cells in translational medicine". EMBO Molecular Medicine. 11 (12): e10234. doi:10.15252/emmm.201810234. PMC 6895604. PMID 31746100.

[pmid9731710-11] Hsu SY, Lin P, Hsueh AJ (September 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members". Mol. Endocrinol. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.

[pmid9430630-12] O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (January 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.

[pmid12115603-13] Ayllón V, Cayla X, García A, Fleischer A, Rebollo A (July 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.

[pmid15694340-14] Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.

[pmid11483855-15] Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (October 2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30. doi:10.1023/A:1011319901057. PMID 11483855. S2CID 23119757.

[pmid10381646-16] Holmgreen SP, Huang DC, Adams JM, Cory S (June 1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID 10381646.

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+{{cs1 config|name-list-style=vanc}}
+{{Short description|Protein-coding gene in the species Homo sapiens}}
 {{Infobox_gene}}
-'''Bcl-2-like protein 2''' is a [[protein]] that in humans is encoded by the ''BCL2L2'' [[gene]].<ref name="pmid8761287">{{cite journal | vauthors = Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S | title = bcl-w, a novel member of the bcl-2 family, promotes cell survival | journal = Oncogene | volume = 13 | issue = 4 | pages = 665–75 |date=October 1996 | pmid = 8761287 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BCL2L2 BCL2-like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=599| accessdate = }}</ref> It was originally discovered by Leonie Gibson, [[Suzanne Cory]] and colleagues at the [[Walter and Eliza Hall Institute of Medical Research]], who called it '''Bcl-w'''.<ref name="Gibson1996">{{cite journal  | vauthors=Gibson L, Holmgreen SP, Huang DC |title=bcl-w, a novel member of the bcl-2 family, promotes cell survival. |journal=Oncogene |volume=13 |issue= 4 |pages= 665–75 |year= 1996 |pmid= 8761287 |doi=  |display-authors=etal}}</ref>
+'''Bcl-2-like protein 2''' is a 193-amino acid [[protein]] that in humans is encoded by the ''BCL2L2'' [[gene]] on [[chromosome 14]] ([[Locus (genetics)|band]] q11.2-q12).<ref name="pmid8761287">{{cite journal | vauthors = Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA, Sutherland GR, Baker E, Adams JM, Cory S |authorlink7=Grant Robert Sutherland | title = bcl-w, a novel member of the bcl-2 family, promotes cell survival | journal = Oncogene | volume = 13 | issue = 4 | pages = 665–75 |date=October 1996 | pmid = 8761287 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BCL2L2 BCL2-like 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=599}}</ref><ref name="pmid32317622">{{cite journal | vauthors=Hartman ML, Czyz M | title=BCL-w: apoptotic and non-apoptotic role in health and disease | journal= Cell Death & Disease| volume=11 | issue=4 | pages=2260 | year=2020 | doi = 10.1038/s41419-020-2417-0 | pmc=7174325  | pmid=32317622}}</ref> It was originally discovered by Leonie Gibson, [[Suzanne Cory]] and colleagues at the [[Walter and Eliza Hall Institute of Medical Research]], who called it '''Bcl-w'''.<ref name="Gibson1996">{{cite journal  | vauthors=Gibson L, Holmgreen SP, Huang DC |title=bcl-w, a novel member of the bcl-2 family, promotes cell survival. |journal=Oncogene |volume=13 |issue= 4 |pages= 665–75 |year= 1996 |pmid= 8761287 |display-authors=etal}}</ref>
 == Function ==
+This gene encodes a pro-survival (anti-[[apoptosis|apoptotic]]) member of the [[Bcl-2 family| bcl-2 protein family]], and is most similar to [[Bcl-xL]].<ref name="pmid32317622" /> The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under [[cytotoxicity|cytotoxic]] conditions. Studies of the related gene in mice indicated a role in the survival of [[Nerve growth factor|NGF]]- and [[BDNF]]-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult [[spermatogenesis]].<ref name="entrez"/><ref>{{cite journal|doi=10.1146/annurev-cancerbio-030419-033510|doi-access=free|title=Toward Targeting Antiapoptotic MCL-1 for Cancer Therapy|year=2020|last1=Kelly|first1=Gemma L.|last2=Strasser|first2=Andreas|journal=Annual Review of Cancer Biology|volume=4|pages=299–313|hdl=11343/252362|hdl-access=free}}</ref><ref name="pmid32317622" />
+== Clinical significance==
-This gene encodes a pro-survival (anti-[[apoptosis|apoptotic]]) member of the [[bcl-2]] [[protein]] family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under [[cytotoxicity|cytotoxic]] conditions. Studies of the related gene in mice indicated a role in the survival of [[Nerve growth factor|NGF]]- and [[BDNF]]-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult [[spermatogenesis]].<ref name="entrez"/>
+High levels of Bcl-w are seen in many cancers, including [[glioblastoma]], [[colorectal cancer]], [[non-small-cell lung carcinoma]], and [[breast cancer]].<ref name="pmid32317622" /> Breast cancer patients with [[metastasis]] have higher Bcl-w than breast cancer patients only having [[primary tumor]].<ref name="pmid32317622" /> Elevated levels of Bcl-w has been shown to protect [[neuron]]s from cell death induced by [[amyloid beta]].<ref name="pmid32317622" /> [[Parkinson's disease]] patients with a mutant [[Parkin (ligase)|PARK2]] gene have elevated Bcl-w.<ref name="pmid32317622" /> Bcl-w has been shown to contribute to [[cellular senescence]].<ref name="pmid32317622" />
+[[Quercetin]] has been shown to inhibit the [[PI3K/AKT/mTOR pathway|PI3K/AKT pathway]] leading to [[Downregulation and upregulation|downregulation]] of Bcl-w.<ref name="pmid31746100">{{cite journal | vauthors=Paez-Ribes M, González-Gualda E, Doherty GJ, Muñoz-Espín D | title=Targeting senescent cells in translational medicine | journal=[[EMBO Molecular Medicine]] | volume=11 | issue=12 | pages=e10234 | year=2019 | doi = 10.15252/emmm.201810234 | pmc=6895604 | pmid=31746100}}</ref><ref name="pmid32317622" />
-Relative to its [[Bcl-2]] counterparts there is considerably less data on this particular protein. Located on chromosome 14q11 it appears to be redundant in most tissues apart from specific examples.
 ==Interactions==
 BCL2L2 has been shown to [[Protein-protein interaction|interact]] with:
-* [[BCL2L11]]<ref name="pmid9731710">{{cite journal | vauthors = Hsu SY, Lin P, Hsueh AJ | title = BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members | journal = Mol. Endocrinol. | volume = 12 | issue = 9 | pages = 1432–40 |date=September 1998  | pmid = 9731710 | doi = 10.1210/mend.12.9.0166 }}</ref><ref name = pmid9430630>{{cite journal | date = January 1998 | vauthors = O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC | title = Bim: a novel member of the Bcl-2 family that promotes apoptosis | journal = EMBO J. | volume = 17 | issue = 2 | pages = 384–95  | pmid = 9430630 | pmc = 1170389 | doi = 10.1093/emboj/17.2.384}}</ref>
+* [[BCL2L11]]<ref name="pmid9731710">{{cite journal | vauthors = Hsu SY, Lin P, Hsueh AJ | title = BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members | journal = Mol. Endocrinol. | volume = 12 | issue = 9 | pages = 1432–40 |date=September 1998  | pmid = 9731710 | doi = 10.1210/mend.12.9.0166 | doi-access = free }}</ref><ref name = pmid9430630>{{cite journal | date = January 1998 | vauthors = O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC | title = Bim: a novel member of the Bcl-2 family that promotes apoptosis | journal = EMBO J. | volume = 17 | issue = 2 | pages = 384–95  | pmid = 9430630 | pmc = 1170389 | doi = 10.1093/emboj/17.2.384}}</ref>
-* [[Bcl-2-associated death promoter|BAD]],<ref name = pmid12115603/><ref name = pmid15694340>{{cite journal | date = February 2005 | vauthors = Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC | title = Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | journal = Mol. Cell | volume = 17 | issue = 3 | pages = 393–403  | pmid = 15694340 | doi = 10.1016/j.molcel.2004.12.030}}</ref><ref name = pmid11483855>{{cite journal | date = October 2001 | vauthors = Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ | title = Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis | journal = Apoptosis | volume = 6 | issue = 5 | pages = 319–30  | pmid = 11483855 | doi = 10.1023/A:1011319901057}}</ref><ref name = pmid10381646>{{cite journal | date = June 1999 | vauthors = Holmgreen SP, Huang DC, Adams JM, Cory S | title = Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members | journal = Cell Death Differ. | volume = 6 | issue = 6 | pages = 525–32  | pmid = 10381646 | doi = 10.1038/sj.cdd.4400519}}</ref> and
+* [[Bcl-2-associated death promoter|BAD]],<ref name = pmid12115603/><ref name = pmid15694340>{{cite journal | date = February 2005 | vauthors = Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC | title = Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | journal = Mol. Cell | volume = 17 | issue = 3 | pages = 393–403  | pmid = 15694340 | doi = 10.1016/j.molcel.2004.12.030| doi-access = free }}</ref><ref name = pmid11483855>{{cite journal | date = October 2001 | vauthors = Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ | title = Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis | journal = Apoptosis | volume = 6 | issue = 5 | pages = 319–30  | pmid = 11483855 | doi = 10.1023/A:1011319901057| s2cid = 23119757 }}</ref><ref name = pmid10381646>{{cite journal | date = June 1999 | vauthors = Holmgreen SP, Huang DC, Adams JM, Cory S | title = Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members | journal = Cell Death Differ. | volume = 6 | issue = 6 | pages = 525–32  | pmid = 10381646 | doi = 10.1038/sj.cdd.4400519| doi-access = free }}</ref> and
-* [[PPP1CA]].<ref name = pmid12115603>{{cite journal | date = July 2002 | vauthors = Ayllón V, Cayla X, García A, Fleischer A, Rebollo A | title = The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad | journal = Eur. J. Immunol. | volume = 32 | issue = 7 | pages = 1847–55  | pmid = 12115603 | doi = 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7}}</ref>
+* [[PPP1CA]].<ref name = pmid12115603>{{cite journal | date = July 2002 | vauthors = Ayllón V, Cayla X, García A, Fleischer A, Rebollo A | title = The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad | journal = Eur. J. Immunol. | volume = 32 | issue = 7 | pages = 1847–55  | pmid = 12115603 | doi = 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7| doi-access = free }}</ref>
 ==References==
 {{Reflist}}
-==External links==
-* {{UCSC gene info|BCL2L2}}
 ==Further reading==
 {{Refbegin | 2}}
-*{{cite journal  | vauthors=Nagase T, Seki N, Ishikawa K |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321–9, 341–54 |year= 1997 |pmid= 9039502 |doi=10.1093/dnares/3.5.321  |display-authors=etal}}
+*{{cite journal  | vauthors=Nagase T, Seki N, Ishikawa K |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321–9, 341–54 |year= 1997 |pmid= 9039502 |doi=10.1093/dnares/3.5.321  |display-authors=etal|doi-access=free }}
 *{{cite journal  | vauthors=O'Connor L, Strasser A, O'Reilly LA |title=Bim: a novel member of the Bcl-2 family that promotes apoptosis. |journal=EMBO J. |volume=17 |issue= 2 |pages= 384–95 |year= 1998 |pmid= 9430630 |doi= 10.1093/emboj/17.2.384  | pmc=1170389 |display-authors=etal}}
-*{{cite journal  | vauthors=Ross AJ, Waymire KG, Moss JE |title=Testicular degeneration in Bclw-deficient mice. |journal=Nat. Genet. |volume=18 |issue= 3 |pages= 251–6 |year= 1998 |pmid= 9500547 |doi= 10.1038/ng0398-251 |display-authors=etal}}
+*{{cite journal  | vauthors=Ross AJ, Waymire KG, Moss JE |title=Testicular degeneration in Bclw-deficient mice. |journal=Nat. Genet. |volume=18 |issue= 3 |pages= 251–6 |year= 1998 |pmid= 9500547 |doi= 10.1038/ng0398-251 |s2cid=32843609 |display-authors=etal}}
-*{{cite journal  | vauthors=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432–40 |year= 1998 |pmid= 9731710 |doi=10.1210/mend.12.9.0166  }}
+*{{cite journal  | vauthors=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432–40 |year= 1998 |pmid= 9731710 |doi=10.1210/mend.12.9.0166  |doi-access=free }}
-*{{cite journal  | vauthors=Middleton G, Wyatt S, Ninkina N, Davies AM |title=Reciprocal developmental changes in the roles of Bcl-w and Bcl-x(L) in regulating sensory neuron survival. |journal=Development |volume=128 |issue= 3 |pages= 447–57 |year= 2001 |pmid= 11152643 |doi=  }}
+*{{cite journal  | vauthors=Middleton G, Wyatt S, Ninkina N, Davies AM |title=Reciprocal developmental changes in the roles of Bcl-w and Bcl-x(L) in regulating sensory neuron survival. |journal=Development |volume=128 |issue= 3 |pages= 447–57 |year= 2001 |doi=10.1242/dev.128.3.447 |pmid= 11152643 |url=http://dev.biologists.org/content/128/3/447.abstract }}
-*{{cite journal  | vauthors=O'Reilly LA, Print C, Hausmann G |title=Tissue expression and subcellular localization of the pro-survival molecule Bcl-w. |journal=Cell Death Differ. |volume=8 |issue= 5 |pages= 486–94 |year= 2001 |pmid= 11423909 |doi= 10.1038/sj.cdd.4400835 |display-authors=etal}}
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 {{Refend}}
+==External links==
+* {{UCSC gene info|BCL2L2}}
 {{PDB Gallery|geneid=599}}