Identifiers
BCL2-like 1
HUGO:BCL2L1, HGNC:992, ENTREZ:598, UNIPROT:Q07817, GENECARDS:GC20M030252
HUGO:BCL2L1 HGNC:992 ENTREZ:598 UNIPROT:Q07817
BCL2-like 1BCL2-associated agonist of cell death
HUGO:BCL2L1 HGNC:992 ENTREZ:598 UNIPROT:Q07817 GENECARDS:BCL2L1 REACTOME:50772 KEGG:598 ATLASONC:BCL2L1ID129ch20q11 WIKI:BCL2L1

Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
 EMT Senescence   / EMT_REGULATORS 
 EMT Senescence   / MITOCHONDRIA_OXIDATIVE_STRESS 
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / CASPASES 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / MITOCHONDRIAL_METABOLISM 
 Regulated Cell Death   / MOMP_REGULATION 
 Regulated Cell Death   / NECROPTOSIS 
 Regulated Cell Death   / RCD_GENES 
HMC:EVADING_GROWTH_SUPPRESSORS
 Survival   / PI3K_AKT_MTOR 
 Survival   / WNT_NON_CANONICAL 

References
PMID:12667443
PMID:22039431
The Bcl2 family proteins regulate and mediate the mitochondrial outer membrane permeabilization, a crucial event in the mitochondrial pathway of apoptosis in vertebrates.
The regulation of apoptosis is governed largely by interactions between the pro-survival and pro-death members of the Bcl2 protein family.
Some members of this family (e.g., Bax, Bak, and Bid: pro-apoptotic proteins) promote apoptosis, while others such as BCL2, BCL2L1, BCL2L2 (anti-apoptotic proteins) work against programmed cell death.
The BCL2 family proteins are characterized by regions of specific sequence homology named as BCL2 homology (BH) motifs that number from 1 to 4 and are critical for function.
Especially a helical BH3 motif of pro-apoptotic proteins occupy and form strong interactions with hydrophobic groove of anti-apoptotic BCL2 family proteins which leads to the activation of the essential death mediators Bax and Bak, thereby committing cells to apoptosis
PMID:22836101
BCL2L1 (BCL-X) promotes survival of adult and developing retinal ganglion cells.
The activation of the pro-death family member BAX is often the final step before cell death in neurons.
Pro-survival family members such as BCL2L1 act to inhibit BAX activation
PMID:23064052
PMID:11085534
BCL2 and BCL2L1 are known to be overexpressed in several cancers.
In particular, BCL2L1 overexpression has been correlated with cancer cells resistance to chemotherapeutic agents
synonym:BCL2-XL
PMID:10949026
PMID:18097445

References
em_emtc_emtc_re425( EMT Senescence  ):
PMID:11463392
BBC3 (so-called PUMA, p53 upregulated modulator of apoptosis) as a target for activation by p53.
This gene encodes two BH3 domain???containing proteins that are induced in cells following p53 activation.
BBC3 binds to BCL2, localize to the mitochondria to induce cytochrome c release, and activate the rapid induction of programmed cell death.
Antisense inhibition of PUMA expression reduced the apoptotic response to p53, and PUMA is likely to play a role inmediating p53-induced cell death through the cytochrome c/Apaf-1???dependent pathway.
PMID:11463391
PUMA was found to be exclusively mitochondrial and to bind to BCL2 and BCL2L1 through a BH3 domain.
em_emtc_emtc_re426( EMT Senescence  ):
PMID:12667443
p53 induces apoptosis by target gene regulation and transcription-independent signaling.
A fraction of induced p53 translocates to the mitochondria of apoptosing tumor cells. Targeting p53 to mitochondria is sufficient to launch apoptosis.
Evidence that p53 translocation to the mitochondria occurs in vivo in irradiatedthymocytes was shown.
Further, p53 can directly induce permeabilization of the outer mitochondrial membrane by forming complexes with the protective BCL2L1, resulting in cytochrome c release.
p53 binds to BCL2L1 via its DNA binding domain.
Tumor-derived transactivation-deficient mutants of p53 concomitantly lose the ability to interact with BCL2L1 and promote cytochrome c release.
em_emtc_emtc_re429( EMT Senescence  ):
PMID:22039431
The Bcl2 family proteins regulate and mediate the mitochondrial outer membrane permeabilization, a crucial event in the mitochondrial pathway of apoptosis in vertebrates.
The regulation of apoptosis is governed largely by interactions between the pro-survival and pro-death members of the Bcl2 protein family.
Some members of this family (e.g., Bax, Bak, and Bid: pro-apoptotic protines) promote apoptosis, while others such as BCL2, BCL2L1, BCL2L2 (anti-apoptotic protines)work against programmed cell death.
The BCL2 family proteins are characterized by regions of specific sequence homology named as BCL2 homology (BH) motifs that number from 1 to 4 and are critical for function.
Especially a helical BH3 motif of pro-apoptotic proteins occupy and form strong interactions with hydrophobic groove of anti-apoptotic BCL2 family proteins which leads to the activation of the essential death mediators Bax and Bak, thereby committing cells to apoptosis
PMID:22836101
BCL2L1 (BCL-X) promotes survival of adult and developing retinal ganglion cells.
The activation of the pro-death family member BAX is often the final step before cell death in neurons.
Pro-survival family members such as BCL2L1 act to inhibit BAX activation
em_emtc_emtc_re432( EMT Senescence  ):

Maps_Modules
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / CASPASES 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / MITOCHONDRIAL_METABOLISM 
 Regulated Cell Death   / MOMP_REGULATION 
 Regulated Cell Death   / NECROPTOSIS 
 Regulated Cell Death   / RCD_GENES 

Maps_Modules
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / CASPASES 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / MITOCHONDRIAL_METABOLISM 
 Regulated Cell Death   / MOMP_REGULATION 
 Regulated Cell Death   / NECROPTOSIS 
 Regulated Cell Death   / RCD_GENES 

References
rc_re583( Regulated Cell Death  ):
PMID:15724238
in human tonsil B cells, constitutive interaction
PMID:9430630
rc_re593:( Regulated Cell Death  ) PMID:16608847
rc_re603( Regulated Cell Death  ):
PMID:11546872
in HEK293T, coIP
Y2H
rc_re606( Regulated Cell Death  ):
PMID:9130713
PMID:10075695
in 293T, IP
rc_re1003:( Regulated Cell Death  ) PMID:9660918
rc_re1131:( Regulated Cell Death  ) PMID:12011449
rc_re1246( Regulated Cell Death  ):
influenceDelete: reactants to re
hierarchical:post-MOMP
reactionType:casp.cleavage
PMID:9435230

Maps_Modules
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / CASPASES 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / MITOCHONDRIAL_METABOLISM 
 Regulated Cell Death   / MOMP_REGULATION 
 Regulated Cell Death   / NECROPTOSIS 
 Regulated Cell Death   / RCD_GENES 

Maps_Modules
HMC:RESISTING_CELL_DEATH
HMC:DEREGULATING_CELLULAR_ENERGETICS
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / CASPASES 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / MITOCHONDRIAL_METABOLISM 
 Regulated Cell Death   / MOMP_REGULATION 
 Regulated Cell Death   / NECROPTOSIS 
 Regulated Cell Death   / RCD_GENES 

References
s_wnc2_re19:( Survival  ) PMID:21486225

1. BCL2-XL*@Cytoplasm

1. BCL2-XL*@Cytosol

1. BCL2-XL*@Endopasmic Reticulum
2. BCL2-XL*@Endopasmic Reticulum

1. BCL2-XL*@Mitochondria

1. BCL2-XL*@Mitochondrial inner membrane

1. BCL2-XL*:​Cleaved ATG5*@Cytosol
2. BAD|​S91_unk|​active:​BCL2-XL*@Cytosol
3. BCL2-XL*:​BECN1:​UVRAG@Cytosol

1. BAX:​BCL2-XL*@Endopasmic Reticulum
2. BAK1:​BCL2-XL*@Endopasmic Reticulum
3. BCL2-XL*:​TMBIM6@Endopasmic Reticulum

1. BAX:​BCL2-XL*@Mitochondria
2. BAK1:​BCL2-XL*@Mitochondria
3. BBC3:​BCL2-XL*@Mitochondria
4. BCL2-XL*:​p53*@Mitochondria

1. BCL2-XL*:​HRK@Mitochondrial inner membrane
2. BBC3:​BCL2-XL*@Mitochondrial inner membrane
3. BCL2-XL*:​p53*@Mitochondrial inner membrane
4. BCL2-XL*:​SIVA1@Mitochondrial inner membrane
5. BCL2-XL*:​TMBIM6@Mitochondrial inner membrane
6. BCL2-XL*:​BCL2L11@Mitochondrial inner membrane
7. BCL2-XL*:​BMF|​unk@Mitochondrial inner membrane
8. BAD|​S91_unk:​BCL2-XL*@Mitochondrial inner membrane
9. BCL2-XL*:​cleaved_BID*|​myr@Mitochondrial inner membrane
10. BAX|​S163_unk|​T167_unk:​BCL2-XL*@Mitochondrial inner membrane

1. BAD_binding partners*@Mitochondria → BCL2-XL*@Mitochondria
2. BBC3@Mitochondria + BCL2-XL*@Mitochondria → BBC3:​BCL2-XL*@Mitochondria
3. BCL2-XL*@Mitochondria + p53*@Mitochondria → BCL2-XL*:​p53*@Mitochondria
4. BCL2-XL*@Mitochondria + BAX@Cytosol → BAX:​BCL2-XL*@Mitochondria
5. BCL2-XL*@Mitochondria + BAK1@Mitochondria → BAK1:​BCL2-XL*@Mitochondria
6. rBCL2-XL*@Nucleus → BCL2-XL*@Mitochondria
7. TMBIM6@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​TMBIM6@Mitochondrial inner membrane
8. SIVA1@Cytosol + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​SIVA1@Mitochondrial inner membrane
9. BCL2-XL*@Mitochondrial inner membrane → cleaved~BCL2_XL*@Mitochondrial inner membrane
10. BCL2-XL*@Cytosol + BECN1@Cytosol + UVRAG@Cytosol → BCL2-XL*:​BECN1:​UVRAG@Cytosol
11. BCL2-XL*@Mitochondrial inner membrane + BAX|​S163_unk|​T167_unk@Mitochondrial inner membrane → BAX|​S163_unk|​T167_unk:​BCL2-XL*@Mitochondrial inner membrane
12. BCL2-XL*@Mitochondrial inner membrane + p53*|​S15_unk@Cytosol → BCL2-XL*:​p53*@Mitochondrial inner membrane
13. BCL2-XL*:​BECN1:​UVRAG@Cytosol → BCL2-XL*@Cytosol + BECN1|​ubi@Cytosol + UVRAG@Cytosol
14. BCL2-XL*@Cytosol + BAD|​S91_unk|​active@Cytosol → BAD|​S91_unk|​active:​BCL2-XL*@Cytosol
15. BCL2-XL*@Cytosol + Cleaved ATG5*@Cytosol → BCL2-XL*:​Cleaved ATG5*@Cytosol
16. rBCL2-XL*@Nucleus → BCL2-XL*@Cytosol
17. TMBIM6@Endopasmic Reticulum + BCL2-XL*@Endopasmic Reticulum → BCL2-XL*:​TMBIM6@Endopasmic Reticulum
18. BCL2-XL*:​TMBIM6@Endopasmic Reticulum → Ca2+ homeostasis@Endopasmic Reticulum
19. BCL2-XL*@Endopasmic Reticulum + BAX@Endopasmic Reticulum → BAX:​BCL2-XL*@Endopasmic Reticulum
20. BCL2-XL*@Endopasmic Reticulum + BAK1@Endopasmic Reticulum → BAK1:​BCL2-XL*@Endopasmic Reticulum
21. BCL2-XL*@Endopasmic Reticulum → BCL2-XL*@Endopasmic Reticulum
22. BCL2L11@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​BCL2L11@Mitochondrial inner membrane
23. cleaved_BID*|​myr@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​cleaved_BID*|​myr@Mitochondrial inner membrane
24. BBC3@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BBC3:​BCL2-XL*@Mitochondrial inner membrane
25. BAD|​S91_unk|​active@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BAD|​S91_unk:​BCL2-XL*@Mitochondrial inner membrane
26. BMF|​unk@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​BMF|​unk@Mitochondrial inner membrane
27. HRK@Mitochondrial inner membrane + BCL2-XL*@Mitochondrial inner membrane → BCL2-XL*:​HRK@Mitochondrial inner membrane
28. 14-3-3*:​BAD|​S112_pho|​S136_pho|​S155_pho@Mitochondria → 14-3-3*:​BAD|​S112_pho|​S136_pho|​S155_pho@Mitochondria + BCL2-XL*@Mitochondria
29. BCL2-XL*@Mitochondria → Prosurvival@Mitochondria
30. BAX@Cytoplasm + BCL2-XL*@Cytoplasm → BAX:​BCL2-XL*@Mitochondria
31. BAX:​BCL2-XL*@Mitochondria + BAX_sub_TRUNC_endsub_*@Cytoplasm → su_wnc1_s_wnc2_s64 + BAX@Cytoplasm

1. Sphingomyelin@Cytosol + H2O@Cytosol → Ceramide@Cytosol + Choline Phosphate@Cytosol
2. IRE1-alpha*:​Unfolded protein*@Endopasmic Reticulum + TRAF2@Cytosol → MCL1|​pho|​hm2:​TRAF2:​Unfolded protein*@Endopasmic Reticulum
3. ITPR*@Endopasmic Reticulum → low Ca2+ level@Endopasmic Reticulum
4. Mitochondria outer~membrane integrity@Mitochondrial inner membrane → MOMP@Mitochondrial inner membrane