| IED ID |
IndEnz0002003709 |
| Enzyme Type ID |
protease003709 |
| Protein Name |
Apoptosis regulator Bcl-2
|
| Gene Name |
Bcl2 Bcl-2 |
| Organism |
Rattus norvegicus (Rat) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Rattus
Rattus norvegicus (Rat)
|
| Enzyme Sequence |
MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDTGDEDSAPLRAAPTPGIFSFQPESNRTPAVHRDTAARTSPLRPLVANAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK |
| Enzyme Length |
236 |
| Uniprot Accession Number |
P49950 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: 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). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Modified residue (3); Motif (4); Sequence conflict (4); Site (1); Transmembrane (1) |
| Keywords |
Apoptosis;Cytoplasm;Endoplasmic reticulum;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleus;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}. |
| Modified Residue |
MOD_RES 69; /note=Phosphothreonine; by MAPK8; /evidence=ECO:0000250|UniProtKB:P10415; MOD_RES 70; /note=Phosphoserine; by MAPK8 and PKC; /evidence=ECO:0000250|UniProtKB:P10415; MOD_RES 84; /note=Phosphoserine; by MAPK8; /evidence=ECO:0000250|UniProtKB:P10415 |
| Post Translational Modification |
PTM: 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-84, wich stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250|UniProtKB:P10415, ECO:0000250|UniProtKB:P10417}.; PTM: 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 (By similarity). {ECO:0000250|UniProtKB:P10415}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P10415}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
11299004;
11879647;
12167434;
12234300;
12394778;
12787069;
14572466;
15004018;
15332118;
15341589;
15362690;
15469889;
15585409;
15649569;
15686664;
15994315;
16084662;
16216918;
16249675;
16256253;
16265626;
16289365;
16309543;
16388103;
16445580;
16732092;
17029665;
17131910;
17236787;
17302035;
17404573;
17562391;
17570453;
17639989;
17693937;
17700647;
17938867;
17967740;
18058945;
18076646;
18083315;
18086876;
18093155;
18097624;
18156304;
18202171;
18221257;
18259862;
18284815;
18289470;
18374914;
18384965;
18441466;
18758938;
18832793;
18931364;
18938189;
18959742;
18991018;
19574995;
19879923;
20037173;
20065158;
20131282;
20424483;
20663300;
20669351;
20821058;
20849813;
20888848;
21062263;
21085184;
21092002;
21161352;
21189961;
21199477;
21212266;
21214291;
21235725;
21296063;
21473886;
21474815;
21503946;
21585051;
22014268;
22153006;
22509406;
22648569;
22668016;
22700048;
22842798;
22847887;
22932950;
22978269;
23032698;
23143152;
23364609;
23381833;
23404339;
23406865;
23789224;
23940949;
23953793;
24166353;
24218972;
24228095;
24357921;
24378970;
24906198;
25535961;
25744447;
25820375;
25937801;
25996932;
26004897;
26163325;
26261574;
26459859;
26692938;
26754107;
26769958;
26897372;
27031958;
27131981;
27255231;
27256506;
29129468;
29285062;
29324390;
29587274;
29635023;
29713367;
29746994;
29777699;
9356461;
9731187;
9731710;
9813151;
|
| Motif |
MOTIF 10..30; /note=BH4; MOTIF 90..104; /note=BH3; MOTIF 133..152; /note=BH1; MOTIF 184..199; /note=BH2 |
| Gene Encoded By |
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| Mass |
26,622 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
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