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UniProtKB - P10415 (BCL2_HUMAN)

Protein

Apoptosis regulator Bcl-2

Gene

BCL2

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processApoptosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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

SIGNOR Signaling Network Open Resource

More...SIGNORi		P10415

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Apoptosis regulator Bcl-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BCL2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000171791.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:990 BCL2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		151430 gene+phenotype

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P10415

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei212 – 233HelicalSequence analysisAdd BLAST22

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		596

MalaCards human disease database

More...MalaCardsi		BCL2
MIMi151430 gene+phenotype

Open Targets

More...OpenTargetsi		ENSG00000171791

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		545 Follicular lymphoma
480541 High grade B-cell lymphoma with MYC and/ or BCL2 and/or BCL6 rearrangement
98839 Intravascular large B-cell lymphoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA25302

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4860

Drug and drug target database

More...DrugBanki		DB05764 ABT-263
DB05297 DHA-paclitaxel
DB01248 Docetaxel
DB04940 E7389
DB01050 Ibuprofen
DB01229 Paclitaxel
DB01367 Rasagiline
DB05281 S-8184
DB11581 Venetoclax

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2844

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		BCL2

Domain mapping of disease mutations (DMDM)

More...DMDMi		231632

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001430481 – 239Apoptosis regulator Bcl-2Add BLAST239

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei69Phosphothreonine; by MAPK81 Publication1
Modified residuei70Phosphoserine; by MAPK8 and PKC1 Publication1
Modified residuei87Phosphoserine; by MAPK81 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei34 – 35Cleavage; by caspase-32

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P10415

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P10415

MaxQB - The MaxQuant DataBase

More...MaxQBi		P10415

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P10415

PeptideAtlas

More...PeptideAtlasi		P10415

PRoteomics IDEntifications database

More...PRIDEi		P10415

ProteomicsDB human proteome resource

More...ProteomicsDBi		52603
52604 [P10415-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P10415

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P10415

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P10415

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000171791 Expressed in 227 organ(s), highest expression level in thyroid gland

CleanEx database of gene expression profiles

More...CleanExi		HS_BCL2

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P10415 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P10415 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000003
HPA055295

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107068, 102 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-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

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P10415

Database of interacting proteins

More...DIPi		DIP-1043N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P10415

Protein interaction database and analysis system

More...IntActi		P10415, 50 interactors

Molecular INTeraction database

More...MINTi		P10415

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000329623

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P10415

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
6GL8X-ray1.40A9-206[»]

Database of protein disorder

More...DisProti		DP00297

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P10415

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P10415

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P10415

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi10 – 30BH4Add BLAST21
Motifi93 – 107BH3Add BLAST15
Motifi136 – 155BH1Add BLAST20
Motifi187 – 202BH2Add BLAST16

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4728 Eukaryota
ENOG41123S0 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00530000062935

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000056452

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004472

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10415

KEGG Orthology (KO)

More...KOi		K02161

Identification of Orthologs from Complete Genome Data

More...OMAi		QRGYEWE

Database of Orthologous Groups

More...OrthoDBi		1218929at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P10415

TreeFam database of animal gene trees

More...TreeFami		TF315834

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

The PANTHER Classification System

More...PANTHERi		PTHR11256 PTHR11256, 1 hit
PTHR11256:SF11 PTHR11256:SF11, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00452 Bcl-2, 1 hit
PF02180 BH4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01863 APOPREGBCL2
PR01862 BCL2FAMILY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00265 BH4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56854 SSF56854, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00865 bcl-2, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000512196 – 239DAFVE…YLGHK → VGALGDVSLG in isoform Beta. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11981.1 [P10415-1]
CCDS45882.1 [P10415-2]

Protein sequence database of the Protein Information Resource

More...PIRi		B29409 TVHUB1
C37332 TVHUA1

NCBI Reference Sequences

More...RefSeqi		NP_000624.2, NM_000633.2 [P10415-1]
NP_000648.2, NM_000657.2 [P10415-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.150749

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000333681; ENSP00000329623; ENSG00000171791 [P10415-1]
ENST00000398117; ENSP00000381185; ENSG00000171791 [P10415-1]
ENST00000589955; ENSP00000466417; ENSG00000171791 [P10415-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		596

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:596

UCSC genome browser

More...UCSCi		uc002lit.2 human [P10415-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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[»]
6GL8X-ray1.40A9-206[»]
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
jPOSTiP10415
MaxQBiP10415
PaxDbiP10415
PeptideAtlasiP10415
PRIDEiP10415
ProteomicsDBi52603
52604 [P10415-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		596
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

Comparative Toxicogenomics Database

More...CTDi		596
DisGeNETi596
EuPathDBiHostDB:ENSG00000171791.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		BCL2
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

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4728 Eukaryota
ENOG41123S0 LUCA
GeneTreeiENSGT00530000062935
HOGENOMiHOG000056452
HOVERGENiHBG004472
InParanoidiP10415
KOiK02161
OMAiQRGYEWE
OrthoDBi1218929at2759
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		BCL2 human
EvolutionaryTraceiP10415

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Bcl-2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		596
PMAP-CutDBiP10415

Protein Ontology

More...PROi		PR:P10415

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBCL2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10415
Secondary accession number(s): C9JHD5
, P10416, Q13842, Q16197
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1993
Last modified: January 16, 2019
This is version 238 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
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