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Protein

Apoptosis regulator Bcl-2

Gene

BCL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Biological processApoptosis

Enzyme and pathway databases

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-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-844455 The NLRP1 inflammasome
R-HSA-9018519 Estrogen-dependent gene expression
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

EuPathDBiHostDB:ENSG00000171791.12
HGNCiHGNC:990 BCL2
MIMi151430 gene+phenotype
neXtProtiNX_P10415

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

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

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.2 Publications

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
480541 High grade B-cell lymphoma with MYC and/ or BCL2 and/or BCL6 rearrangement
98839 Intravascular large B-cell lymphoma
PharmGKBiPA25302

Chemistry databases

ChEMBLiCHEMBL4860
DrugBankiDB05764 ABT-263
DB05297 DHA-paclitaxel
DB01248 Docetaxel
DB04940 E7389
DB01050 Ibuprofen
DB01229 Paclitaxel
DB01367 Rasagiline
DB05281 S-8184
DB11581 Venetoclax
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 PRKN, 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
ProteomicsDBi52603
52604 [P10415-2]

PTM databases

iPTMnetiP10415
PhosphoSitePlusiP10415

Miscellaneous databases

PMAP-CutDBiP10415

Expressioni

Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

BgeeiENSG00000171791 Expressed in 227 organ(s), highest expression level in thyroid gland
CleanExiHS_BCL2
ExpressionAtlasiP10415 baseline and differential
GenevisibleiP10415 HS

Organism-specific databases

HPAiCAB000003
HPA055295

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 RTL10/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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107068, 102 interactors
ComplexPortaliCPX-1981 BCL-2 dimer
CPX-1982 BAD:BCL-2 complex
CPX-1984 BID:BCL-2 complex
CPX-1986 PUMA:BCL-2 complex
CPX-1990 BIM:BCL-2 complex
CORUMiP10415
DIPiDIP-1043N
ELMiP10415
IntActiP10415, 50 interactors
MINTiP10415
STRINGi9606.ENSP00000329623

Chemistry databases

BindingDBiP10415

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiQRGYEWE
OrthoDBiEOG091G0OCU
PhylomeDBiP10415
TreeFamiTF315834

Family and domain databases

InterProiView protein in InterPro
IPR013278 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
IPR036834 Blc2-like_sf
IPR026298 Blc2_fam
PANTHERiPTHR11256 PTHR11256, 1 hit
PTHR11256:SF11 PTHR11256:SF11, 1 hit
PfamiView protein in Pfam
PF00452 Bcl-2, 1 hit
PF02180 BH4, 1 hit
PRINTSiPR01863 APOPREGBCL2
PR01862 BCL2FAMILY
SMARTiView protein in SMART
SM00265 BH4, 1 hit
SUPFAMiSSF56854 SSF56854, 1 hit
TIGRFAMsiTIGR00865 bcl-2, 1 hit
PROSITEiView protein in PROSITE
PS50062 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

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 → S2 Publications1
Natural variantiVAR_01471643A → T1 PublicationCorresponds to variant dbSNP:rs1800477Ensembl.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

Similar proteinsi

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[»]
5JSNX-ray2.10A/C1-207[»]
5VAUX-ray1.75A/B/C/D1-207[»]
5VAXX-ray2.00A/B/C/D1-207[»]
5VAYX-ray1.80A/B/C/D1-34[»]
A/B/C/D66-207[»]
DisProtiDP00297
ProteinModelPortaliP10415
SMRiP10415
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107068, 102 interactors
ComplexPortaliCPX-1981 BCL-2 dimer
CPX-1982 BAD:BCL-2 complex
CPX-1984 BID:BCL-2 complex
CPX-1986 PUMA:BCL-2 complex
CPX-1990 BIM:BCL-2 complex
CORUMiP10415
DIPiDIP-1043N
ELMiP10415
IntActiP10415, 50 interactors
MINTiP10415
STRINGi9606.ENSP00000329623

Chemistry databases

BindingDBiP10415
ChEMBLiCHEMBL4860
DrugBankiDB05764 ABT-263
DB05297 DHA-paclitaxel
DB01248 Docetaxel
DB04940 E7389
DB01050 Ibuprofen
DB01229 Paclitaxel
DB01367 Rasagiline
DB05281 S-8184
DB11581 Venetoclax
GuidetoPHARMACOLOGYi2844

PTM databases

iPTMnetiP10415
PhosphoSitePlusiP10415

Polymorphism and mutation databases

BioMutaiBCL2
DMDMi231632

Proteomic databases

EPDiP10415
MaxQBiP10415
PaxDbiP10415
PeptideAtlasiP10415
PRIDEiP10415
ProteomicsDBi52603
52604 [P10415-2]

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
EuPathDBiHostDB:ENSG00000171791.12
GeneCardsiBCL2
HGNCiHGNC:990 BCL2
HPAiCAB000003
HPA055295
MalaCardsiBCL2
MIMi151430 gene+phenotype
neXtProtiNX_P10415
OpenTargetsiENSG00000171791
Orphaneti545 Follicular lymphoma
480541 High grade B-cell lymphoma with MYC and/ or BCL2 and/or BCL6 rearrangement
98839 Intravascular large B-cell lymphoma
PharmGKBiPA25302
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-844455 The NLRP1 inflammasome
R-HSA-9018519 Estrogen-dependent gene expression
SIGNORiP10415

Miscellaneous databases

ChiTaRSiBCL2 human
EvolutionaryTraceiP10415
GeneWikiiBcl-2
GenomeRNAii596
PMAP-CutDBiP10415
PROiPR:P10415
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171791 Expressed in 227 organ(s), highest expression level in thyroid gland
CleanExiHS_BCL2
ExpressionAtlasiP10415 baseline and differential
GenevisibleiP10415 HS

Family and domain databases

InterProiView protein in InterPro
IPR013278 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
IPR036834 Blc2-like_sf
IPR026298 Blc2_fam
PANTHERiPTHR11256 PTHR11256, 1 hit
PTHR11256:SF11 PTHR11256:SF11, 1 hit
PfamiView protein in Pfam
PF00452 Bcl-2, 1 hit
PF02180 BH4, 1 hit
PRINTSiPR01863 APOPREGBCL2
PR01862 BCL2FAMILY
SMARTiView protein in SMART
SM00265 BH4, 1 hit
SUPFAMiSSF56854 SSF56854, 1 hit
TIGRFAMsiTIGR00865 bcl-2, 1 hit
PROSITEiView protein in PROSITE
PS50062 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
ProtoNetiSearch...

Entry informationi

Entry nameiBCL2_HUMAN
AccessioniPrimary (citable) accession number: P10415
Secondary accession number(s): C9JHD5
, P10416, Q13842, Q16197
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1993
Last modified: November 7, 2018
This is version 237 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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