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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). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785).2 Publications

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • channel activity Source: BHF-UCL
  • channel inhibitor activity Source: BHF-UCL
  • 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

BioCyciZFISH:ENSG00000171791-MONOMER.
ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-844455. The NLRP1 inflammasome.
SIGNORiP10415.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator Bcl-2
Gene namesi
Name:BCL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:990. BCL2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei212 – 233HelicalSequence analysisAdd BLAST22

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)DescriptionActionsGraphical viewLength
Mutagenesisi34D → A: Abolishes cleavage by caspase-3. 1
Mutagenesisi64D → A: No effect on cleavage by caspase-3. 1
Mutagenesisi138 – 141FRDG → AAAA: Loss of BAX-binding and of anti-apoptotic activity. 1 Publication4
Mutagenesisi144W → A: Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146. 1 Publication1
Mutagenesisi145G → A: Loss of BAX-binding and of anti-apoptotic activity. No effect on NLRP1-induced IL1B release, nor on homodimerization. Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146. 2 Publications1
Mutagenesisi145G → E: Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization. 2 Publications1
Mutagenesisi146R → A: Loss of BAX-binding and of anti-apoptotic activity; when associated with A-144 and A145. 1 Publication1
Mutagenesisi188W → A: Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization. 1 Publication1
Mutagenesisi190Q → L: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with A-191 and A-192. No effect on homodimerization; when associated with L-190 and A-191. 1 Publication1
Mutagenesisi191D → A: No effect on BAX-binding, nor on anti-apoptotic activity. Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-192. No effect on homodimerization; when associated with L-190 and A-191. 1 Publication1
Mutagenesisi192N → A: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-191. No effect on homodimerization; when associated with L-190 and A-191. 1 Publication1
Mutagenesisi194 – 197Missing : Loss of BAX-binding and of anti-apoptotic activity. May also affect protein stability. 1 Publication4
Mutagenesisi200E → A: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi596.
MalaCardsiBCL2.
MIMi151430. gene+phenotype.
OpenTargetsiENSG00000171791.
Orphaneti545. Follicular lymphoma.
98839. Intravascular large B-cell lymphoma.
PharmGKBiPA25302.

Chemistry databases

ChEMBLiCHEMBL4860.
DrugBankiDB01248. Docetaxel.
DB01050. Ibuprofen.
DB01229. Paclitaxel.
DB01367. Rasagiline.
GuidetoPHARMACOLOGYi2844.

Polymorphism and mutation databases

BioMutaiBCL2.
DMDMi231632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001430481 – 239Apoptosis regulator Bcl-2Add BLAST239

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei69Phosphothreonine; by MAPK81 Publication1
Modified residuei70Phosphoserine; by MAPK8 and PKC1 Publication1
Modified residuei87Phosphoserine; by MAPK81 Publication1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei34 – 35Cleavage; by caspase-32

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP10415.
MaxQBiP10415.
PaxDbiP10415.
PeptideAtlasiP10415.
PRIDEiP10415.

PTM databases

iPTMnetiP10415.
PhosphoSitePlusiP10415.

Miscellaneous databases

PMAP-CutDBP10415.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

BgeeiENSG00000171791.
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 (PubMed:8183370). 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. Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (PubMed:17418785).By similarity15 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.
BAK1Q166113EBI-77694,EBI-519866
BAXQ0781211EBI-77694,EBI-516580
BBC3Q9BXH15EBI-77694,EBI-519884
BCAP31P515722EBI-77694,EBI-77683
BCL2L11O435218EBI-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
BIKQ133235EBI-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-4370304,EBI-707392
SIVA1O153042EBI-77694,EBI-520756
TP53P046375EBI-77694,EBI-366083
TP53BP2Q1362513EBI-77694,EBI-77642

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107068. 98 interactors.
DIPiDIP-1043N.
IntActiP10415. 47 interactors.
MINTiMINT-87089.
STRINGi9606.ENSP00000329623.

Chemistry databases

BindingDBiP10415.

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 25Combined sources15
Turni32 – 34Combined sources3
Helixi93 – 107Combined sources15
Helixi109 – 118Combined sources10
Turni123 – 125Combined sources3
Helixi126 – 137Combined sources12
Turni138 – 140Combined sources3
Helixi144 – 163Combined sources20
Helixi169 – 184Combined sources16
Helixi186 – 191Combined sources6
Helixi194 – 202Combined sources9
Helixi203 – 205Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5AGWX-ray2.69A/B1-34[»]
A/B92-207[»]
5AGXX-ray2.24A/B1-34[»]
A/B92-207[»]
5FCGX-ray2.10A1-207[»]
DisProtiDP00297.
ProteinModelPortaliP10415.
SMRiP10415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10415.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi10 – 30BH4Add BLAST21
Motifi93 – 107BH3Add BLAST15
Motifi136 – 155BH1Add BLAST20
Motifi187 – 202BH2Add BLAST16

Domaini

BH1 and BH2 domains are required for the interaction with BAX and for anti-apoptotic activity.1 Publication
The BH4 motif is required for anti-apoptotic activity and for interaction with RAF1 and EGLN3.
The loop between motifs BH4 and BH3 is required for the interaction with NLRP1.1 Publication

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
InParanoidiP10415.
KOiK02161.
OMAiIVLKYIH.
OrthoDBiEOG091G0OCU.
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)DescriptionActionsGraphical viewLength
Sequence conflicti48I → F in CAA29778 (PubMed:2834197).Curated1
Sequence conflicti59P → T in AAA35591 (PubMed:2875799).Curated1
Sequence conflicti96T → A in AAD14111 (PubMed:1339299).Curated1
Sequence conflicti110R → G in AAD14111 (PubMed:1339299).Curated1
Sequence conflicti117S → R in AAA35591 (PubMed:2875799).Curated1
Sequence conflicti129R → C in CAA29778 (PubMed:2834197).Curated1
Isoform Beta (identifier: P10415-2)
Sequence conflicti199L → S in AAA51814 (PubMed:3523487).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0008277T → S.2 Publications1
Natural variantiVAR_01471643A → T.1 PublicationCorresponds to variant rs1800477dbSNPEnsembl.1
Natural variantiVAR_00082859P → S in non-Hodgkin lymphoma; somatic mutation. 1 Publication1
Natural variantiVAR_00082993V → I in non-Hodgkin lymphoma; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000512196 – 239DAFVE…YLGHK → VGALGDVSLG in isoform Beta. 1 PublicationAdd BLAST44

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.2. human. [P10415-1]

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
PDB 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[»]
5AGWX-ray2.69A/B1-34[»]
A/B92-207[»]
5AGXX-ray2.24A/B1-34[»]
A/B92-207[»]
5FCGX-ray2.10A1-207[»]
DisProtiDP00297.
ProteinModelPortaliP10415.
SMRiP10415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107068. 98 interactors.
DIPiDIP-1043N.
IntActiP10415. 47 interactors.
MINTiMINT-87089.
STRINGi9606.ENSP00000329623.

Chemistry databases

BindingDBiP10415.
ChEMBLiCHEMBL4860.
DrugBankiDB01248. Docetaxel.
DB01050. Ibuprofen.
DB01229. Paclitaxel.
DB01367. Rasagiline.
GuidetoPHARMACOLOGYi2844.

PTM databases

iPTMnetiP10415.
PhosphoSitePlusiP10415.

Polymorphism and mutation databases

BioMutaiBCL2.
DMDMi231632.

Proteomic databases

EPDiP10415.
MaxQBiP10415.
PaxDbiP10415.
PeptideAtlasiP10415.
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.2. human. [P10415-1]

Organism-specific databases

CTDi596.
DisGeNETi596.
GeneCardsiBCL2.
HGNCiHGNC:990. BCL2.
HPAiCAB000003.
MalaCardsiBCL2.
MIMi151430. gene+phenotype.
neXtProtiNX_P10415.
OpenTargetsiENSG00000171791.
Orphaneti545. Follicular lymphoma.
98839. Intravascular large B-cell lymphoma.
PharmGKBiPA25302.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
InParanoidiP10415.
KOiK02161.
OMAiIVLKYIH.
OrthoDBiEOG091G0OCU.
PhylomeDBiP10415.
TreeFamiTF315834.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171791-MONOMER.
ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-844455. The NLRP1 inflammasome.
SIGNORiP10415.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000171791.
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...

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: November 30, 2016
This is version 216 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

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 one 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.