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Protein

Apoptosis regulator Bcl-2

Gene

BCL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei34 – 352Cleavage; by caspase-3

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • channel activity Source: BHF-UCL
  • channel inhibitor activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • sequence-specific DNA binding Source: MGI
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_549. Activation of BAD and translocation to mitochondria.
REACT_75927. The NLRP1 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator Bcl-2
Gene namesi
Name:BCL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:990. BCL2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei212 – 23322HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • membrane Source: MGI
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nuclear membrane Source: UniProtKB
  • nucleus Source: MGI
  • pore complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341D → A: Abolishes cleavage by caspase-3.
Mutagenesisi64 – 641D → A: No effect on cleavage by caspase-3.
Mutagenesisi145 – 1451G → A: No heterodimerization with BAX and loss of anti-apoptotic activity.
Mutagenesisi188 – 1881W → A: No heterodimerization with BAX and loss of anti-apoptotic activity.

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi151430. gene+phenotype.
Orphaneti545. Follicular lymphoma.
98839. Intravascular large B-cell lymphoma.
PharmGKBiPA25302.

Chemistry

DrugBankiDB01248. Docetaxel.
DB01050. Ibuprofen.
DB01229. Paclitaxel.
DB01367. Rasagiline.

Polymorphism and mutation databases

BioMutaiBCL2.
DMDMi231632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Apoptosis regulator Bcl-2PRO_0000143048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691Phosphothreonine; by MAPK81 Publication
Modified residuei70 – 701Phosphoserine; by MAPK8 and PKC1 Publication
Modified residuei87 – 871Phosphoserine; by MAPK81 Publication

Post-translational modificationi

Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity. Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle. In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases. Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-87, wich stimulates starvation-induced autophagy. Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity).By similarity
Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity.1 Publication
Monoubiquitinated by PARK2, leading to increase its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10415.
PaxDbiP10415.
PRIDEiP10415.

PTM databases

PhosphoSiteiP10415.

Miscellaneous databases

PMAP-CutDBP10415.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

BgeeiP10415.
CleanExiHS_BCL2.
ExpressionAtlasiP10415. baseline and differential.
GenevisibleiP10415. HS.

Organism-specific databases

HPAiCAB000003.

Interactioni

Subunit structurei

Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (By similarity). Interacts with EI24 (By similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts (via the BH4 domain) with EGLN3; the interaction prevents the formation of the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2. Interacts with G0S2; this interaction also prevents the formation of the anti-apoptotic BAX-BCL2 complex. Interacts with BOP. Interacts with the SCF(FBXO10) complex.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-77694,EBI-77694
AMBRA1Q9C0C710EBI-77694,EBI-2512975
BADQ929345EBI-77694,EBI-700771
BadQ613376EBI-77694,EBI-400328From a different organism.
BAXQ078129EBI-77694,EBI-516580
BBC3Q9BXH15EBI-77694,EBI-519884
BCAP31P515722EBI-77694,EBI-77683
BCL2L11O435217EBI-77694,EBI-526406
BCL2L11O43521-13EBI-77694,EBI-526416
BCL2L11O43521-24EBI-77694,EBI-526420
BCLAF1Q9NYF82EBI-77694,EBI-437804
BECN1Q1445716EBI-77694,EBI-949378
BIDP559578EBI-77694,EBI-519672
BIKQ133233EBI-77694,EBI-700794
BmfQ91ZE92EBI-77694,EBI-708032From a different organism.
BNIP3LO602382EBI-77694,EBI-849893
BRCA1P383986EBI-77694,EBI-349905
LRRK2Q5S0072EBI-4370304,EBI-5323863
MDM4O151514EBI-77694,EBI-398437
NAF1Q96HR82EBI-77694,EBI-2515597
NLRP1Q9C00012EBI-77694,EBI-1220518
NR4A1P227367EBI-77694,EBI-721550
PMAIP1Q137943EBI-77694,EBI-707392
SIVA1O153042EBI-77694,EBI-520756
TP53P046375EBI-77694,EBI-366083
TP53BP2Q1362513EBI-77694,EBI-77642

Protein-protein interaction databases

BioGridi107068. 96 interactions.
DIPiDIP-1043N.
IntActiP10415. 46 interactions.
MINTiMINT-87089.
STRINGi9606.ENSP00000329623.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2515Combined sources
Turni32 – 343Combined sources
Helixi93 – 10715Combined sources
Helixi109 – 11810Combined sources
Turni123 – 1253Combined sources
Helixi126 – 13712Combined sources
Turni138 – 1403Combined sources
Helixi144 – 16320Combined sources
Helixi169 – 18416Combined sources
Helixi186 – 1916Combined sources
Helixi194 – 2029Combined sources
Helixi203 – 2053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5MNMR-A1-34[»]
A92-207[»]
1GJHNMR-A1-34[»]
A92-207[»]
1YSWNMR-A3-33[»]
A92-206[»]
2O21NMR-A3-34[»]
A92-207[»]
2O22NMR-A3-34[»]
A92-207[»]
2O2FNMR-A8-31[»]
A92-204[»]
2W3LX-ray2.10A/B92-206[»]
2XA0X-ray2.70A/B1-207[»]
4AQ3X-ray2.40A/B/C/D/E/F1-33[»]
A/B/C/D/E/F92-207[»]
4IEHX-ray2.10A1-34[»]
A92-207[»]
4LVTX-ray2.05A/B1-34[»]
A/B92-207[»]
4LXDX-ray1.90A1-34[»]
A92-207[»]
4MANX-ray2.07A/B1-34[»]
A/B92-207[»]
DisProtiDP00297.
ProteinModelPortaliP10415.
SMRiP10415. Positions 3-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10415.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 3021BH4Add
BLAST
Motifi93 – 10715BH3Add
BLAST
Motifi136 – 15520BH1Add
BLAST
Motifi187 – 20216BH2Add
BLAST

Domaini

The BH4 motif is required for anti-apoptotic activity and for interaction with RAF1 and EGLN3.

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG275924.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
InParanoidiP10415.
KOiK02161.
OMAiIVLKYIH.
OrthoDBiEOG70GMGD.
PhylomeDBiP10415.
TreeFamiTF315834.

Family and domain databases

InterProiIPR013278. Apop_reg_Bcl2.
IPR002475. Bcl2-like.
IPR004725. Bcl2/BclX.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF11. PTHR11256:SF11. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01863. APOPREGBCL2.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00865. bcl-2. 1 hit.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: P10415-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS
60 70 80 90 100
SQPGHTPHPA ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA
110 120 130 140 150
GDDFSRRYRR DFAEMSSQLH LTPFTARGRF ATVVEELFRD GVNWGRIVAF
160 170 180 190 200
FEFGGVMCVE SVNREMSPLV DNIALWMTEY LNRHLHTWIQ DNGGWDAFVE
210 220 230
LYGPSMRPLF DFSWLSLKTL LSLALVGACI TLGAYLGHK
Length:239
Mass (Da):26,266
Last modified:April 1, 1993 - v2
Checksum:i3C49F2B714DC9CCB
GO
Isoform Beta (identifier: P10415-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     196-239: DAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK → VGALGDVSLG

Show »
Length:205
Mass (Da):22,337
Checksum:iE3B15A271F900A84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481I → F in CAA29778 (PubMed:2834197).Curated
Sequence conflicti59 – 591P → T in AAA35591 (PubMed:2875799).Curated
Sequence conflicti96 – 961T → A in AAD14111 (PubMed:1339299).Curated
Sequence conflicti110 – 1101R → G in AAD14111 (PubMed:1339299).Curated
Sequence conflicti117 – 1171S → R in AAA35591 (PubMed:2875799).Curated
Sequence conflicti129 – 1291R → C in CAA29778 (PubMed:2834197).Curated
Isoform Beta (identifier: P10415-2)
Sequence conflicti199 – 1991L → S in AAA51814 (PubMed:3523487).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71T → S.2 Publications
VAR_000827
Natural varianti43 – 431A → T.1 Publication
Corresponds to variant rs1800477 [ dbSNP | Ensembl ].
VAR_014716
Natural varianti59 – 591P → S in non-Hodgkin lymphoma; somatic mutation. 1 Publication
VAR_000828
Natural varianti93 – 931V → I in non-Hodgkin lymphoma; somatic mutation. 1 Publication
VAR_000829

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei196 – 23944DAFVE…YLGHK → VGALGDVSLG in isoform Beta. 1 PublicationVSP_000512Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13994 mRNA. Translation: AAA51813.1. Sequence problems.
M13995 mRNA. Translation: AAA51814.1. Sequence problems.
M14745 mRNA. Translation: AAA35591.1.
X06487 mRNA. Translation: CAA29778.1.
AY220759 Genomic DNA. Translation: AAO26045.1.
AC021803 Genomic DNA. No translation available.
AC022726 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW63137.1.
BC027258 mRNA. Translation: AAH27258.1.
S72602 Genomic DNA. Translation: AAD14111.1. Sequence problems.
CCDSiCCDS11981.1. [P10415-1]
CCDS45882.1. [P10415-2]
PIRiB29409. TVHUB1.
C37332. TVHUA1.
RefSeqiNP_000624.2. NM_000633.2. [P10415-1]
NP_000648.2. NM_000657.2. [P10415-2]
UniGeneiHs.150749.

Genome annotation databases

EnsembliENST00000333681; ENSP00000329623; ENSG00000171791. [P10415-1]
ENST00000398117; ENSP00000381185; ENSG00000171791. [P10415-1]
ENST00000589955; ENSP00000466417; ENSG00000171791. [P10415-2]
GeneIDi596.
KEGGihsa:596.
UCSCiuc002lit.1. human. [P10415-1]
uc002liv.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Bcl-2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13994 mRNA. Translation: AAA51813.1. Sequence problems.
M13995 mRNA. Translation: AAA51814.1. Sequence problems.
M14745 mRNA. Translation: AAA35591.1.
X06487 mRNA. Translation: CAA29778.1.
AY220759 Genomic DNA. Translation: AAO26045.1.
AC021803 Genomic DNA. No translation available.
AC022726 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW63137.1.
BC027258 mRNA. Translation: AAH27258.1.
S72602 Genomic DNA. Translation: AAD14111.1. Sequence problems.
CCDSiCCDS11981.1. [P10415-1]
CCDS45882.1. [P10415-2]
PIRiB29409. TVHUB1.
C37332. TVHUA1.
RefSeqiNP_000624.2. NM_000633.2. [P10415-1]
NP_000648.2. NM_000657.2. [P10415-2]
UniGeneiHs.150749.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5MNMR-A1-34[»]
A92-207[»]
1GJHNMR-A1-34[»]
A92-207[»]
1YSWNMR-A3-33[»]
A92-206[»]
2O21NMR-A3-34[»]
A92-207[»]
2O22NMR-A3-34[»]
A92-207[»]
2O2FNMR-A8-31[»]
A92-204[»]
2W3LX-ray2.10A/B92-206[»]
2XA0X-ray2.70A/B1-207[»]
4AQ3X-ray2.40A/B/C/D/E/F1-33[»]
A/B/C/D/E/F92-207[»]
4IEHX-ray2.10A1-34[»]
A92-207[»]
4LVTX-ray2.05A/B1-34[»]
A/B92-207[»]
4LXDX-ray1.90A1-34[»]
A92-207[»]
4MANX-ray2.07A/B1-34[»]
A/B92-207[»]
DisProtiDP00297.
ProteinModelPortaliP10415.
SMRiP10415. Positions 3-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107068. 96 interactions.
DIPiDIP-1043N.
IntActiP10415. 46 interactions.
MINTiMINT-87089.
STRINGi9606.ENSP00000329623.

Chemistry

BindingDBiP10415.
ChEMBLiCHEMBL4860.
DrugBankiDB01248. Docetaxel.
DB01050. Ibuprofen.
DB01229. Paclitaxel.
DB01367. Rasagiline.

PTM databases

PhosphoSiteiP10415.

Polymorphism and mutation databases

BioMutaiBCL2.
DMDMi231632.

Proteomic databases

MaxQBiP10415.
PaxDbiP10415.
PRIDEiP10415.

Protocols and materials databases

DNASUi596.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333681; ENSP00000329623; ENSG00000171791. [P10415-1]
ENST00000398117; ENSP00000381185; ENSG00000171791. [P10415-1]
ENST00000589955; ENSP00000466417; ENSG00000171791. [P10415-2]
GeneIDi596.
KEGGihsa:596.
UCSCiuc002lit.1. human. [P10415-1]
uc002liv.1. human.

Organism-specific databases

CTDi596.
GeneCardsiGC18M060763.
HGNCiHGNC:990. BCL2.
HPAiCAB000003.
MIMi151430. gene+phenotype.
neXtProtiNX_P10415.
Orphaneti545. Follicular lymphoma.
98839. Intravascular large B-cell lymphoma.
PharmGKBiPA25302.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275924.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
InParanoidiP10415.
KOiK02161.
OMAiIVLKYIH.
OrthoDBiEOG70GMGD.
PhylomeDBiP10415.
TreeFamiTF315834.

Enzyme and pathway databases

ReactomeiREACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_549. Activation of BAD and translocation to mitochondria.
REACT_75927. The NLRP1 inflammasome.

Miscellaneous databases

ChiTaRSiBCL2. human.
EvolutionaryTraceiP10415.
GeneWikiiBcl-2.
GenomeRNAii596.
NextBioi2423.
PMAP-CutDBP10415.
PROiP10415.
SOURCEiSearch...

Gene expression databases

BgeeiP10415.
CleanExiHS_BCL2.
ExpressionAtlasiP10415. baseline and differential.
GenevisibleiP10415. HS.

Family and domain databases

InterProiIPR013278. Apop_reg_Bcl2.
IPR002475. Bcl2-like.
IPR004725. Bcl2/BclX.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF11. PTHR11256:SF11. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01863. APOPREGBCL2.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00865. bcl-2. 1 hit.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma."
    Tsujimoto Y., Croce C.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:5214-5218(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
  2. "Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo."
    Eguchi Y., Ewert D.L., Tsujimoto Y.
    Nucleic Acids Res. 20:4187-4192(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 96; 110 AND 237.
  3. "Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation."
    Cleary M.L., Smith S.D., Sklar J.
    Cell 47:19-28(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  4. "Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma."
    Seto M., Jaeger U., Hockett R.D., Graninger W., Bennett S., Goldman P., Korsmeyer S.J.
    EMBO J. 7:123-131(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT SER-7.
  5. "Consequences of the t(14;18) chromosomal translocation in follicular lymphoma: deregulated expression of a chimeric and mutated BCL-2 gene."
    Hua C., Zorn S., Jensen J.P., Coupland R.W., Ko H.S., Wright J.J., Bakhshi A.
    Oncogene Res. 2:263-275(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-7.
  6. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-43.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Testis.
  10. "Frequent incidence of somatic mutations in translocated BCL2 oncogenes of non-Hodgkin's lymphomas."
    Tanaka S., Louie D.C., Kant J.A., Reed J.C.
    Blood 79:229-237(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131 (ISOFORM ALPHA), VARIANTS NON-HODGKIN LYMPHOMA SER-59 AND ILE-93.
  11. "Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death."
    Hockenbery D., Nunez G., Milliman C., Schreiber R.D., Korsmeyer S.J.
    Nature 348:334-336(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax."
    Yin X.-M., Oltvai Z.N., Korsmeyer S.J.
    Nature 369:321-323(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. Cited for: INTERACTION WITH BAG1.
  14. "Conversion of Bcl-2 to a Bax-like death effector by caspases."
    Cheng E.H.-Y., Kirsch D.G., Clem R.J., Ravi R., Kastan M.B., Bedi A., Ueno K., Hardwick J.M.
    Science 278:1966-1968(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY CASPASES, MUTAGENESIS.
  15. "The p53-binding protein 53BP2 also interacts with Bcl2 and impedes cell cycle progression at G2/M."
    Naumovski L., Cleary M.L.
    Mol. Cell. Biol. 16:3884-3892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53BP2.
  16. "Phosphorylation of Bcl2 and regulation of apoptosis."
    Ruvolo P.P., Deng X., May W.S.
    Leukemia 15:515-522(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON PHOSPHORYLATION.
  17. "BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M."
    Yamamoto K., Ichijo H., Korsmeyer S.J.
    Mol. Cell. Biol. 19:8469-8478(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ASK1/JNK1.
  18. "PUMA induces the rapid apoptosis of colorectal cancer cells."
    Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B.
    Mol. Cell 7:673-682(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBC3 AND BCL2L1.
  19. "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis."
    Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P., Shen L., Wan D., Gu J.
    Biochem. Biophys. Res. Commun. 308:379-385(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BNIPL.
  20. "The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)."
    Kang C.B., Tai J., Chia J., Yoon H.S.
    FEBS Lett. 579:1469-1476(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP8.
  21. "p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1 regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association."
    Jin S., Zhuo Y., Guo W., Field J.
    J. Biol. Chem. 280:24698-24705(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAF1.
  22. Cited for: INTERACTION WITH MRPL41.
  23. "Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression."
    Portier B.P., Taglialatela G.
    J. Biol. Chem. 281:40493-40502(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP8.
  24. "JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy."
    Wei Y., Pattingre S., Sinha S., Bassik M., Levine B.
    Mol. Cell 30:678-688(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-69; SER-70 AND SER-87 BY MAPK8/JNK1, FUNCTION.
  25. "Identification of a protein, G0S2, that lacks Bcl-2 homology domains and interacts with and antagonizes Bcl-2."
    Welch C., Santra M.K., El-Assaad W., Zhu X., Huber W.E., Keys R.A., Teodoro J.G., Green M.R.
    Cancer Res. 69:6782-6789(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH G0S2.
  26. "Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect."
    Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J., Gunter T.E.
    J. Biol. Chem. 284:9692-9699(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPIF.
  27. "Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-induced apoptosis in H9c2 cells."
    Liu Y., Huo Z., Yan B., Lin X., Zhou Z.N., Liang X., Zhu W., Liang D., Li L., Liu Y., Zhao H., Sun Y., Chen Y.H.
    Biochem. Biophys. Res. Commun. 401:231-237(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EGLN3.
  28. "Parkin mono-ubiquitinates Bcl-2 and regulates autophagy."
    Chen D., Gao F., Li B., Wang H., Xu Y., Zhu C., Wang G.
    J. Biol. Chem. 285:38214-38223(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY PARK2.
  29. "Human Bop is a novel BH3-only member of the Bcl-2 protein family."
    Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L., Tang H.
    Protein Cell 3:790-801(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BOP/C22ORF29.
  30. Cited for: INTERACTION WITH FBXO10, UBIQUITINATION, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX.
  31. Cited for: STRUCTURE BY NMR OF 1-207.
  32. Cited for: STRUCTURE BY NMR OF 45-207.
  33. Cited for: STRUCTURE BY NMR OF 44-207.

Entry informationi

Entry nameiBCL2_HUMAN
AccessioniPrimary (citable) accession number: P10415
Secondary accession number(s): C9JHD5
, P10416, Q13842, Q16197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1993
Last modified: June 24, 2015
This is version 201 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.