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Q9JJV8 (BCL2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Apoptosis regulator Bcl-2
Gene names
Name:BCL2
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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) By similarity.

Subunit structure

Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity By similarity. Also interacts with APAF1, BBC3, BCL2L1, BNIPL, EI24, 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 By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.

Domain

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

Post-translational modification

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 By similarity. In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases By similarity. 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.

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. Ref.2

Monoubiquitinated by PARK2, leading to increase its stability By similarity.

Sequence similarities

Belongs to the Bcl-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Apoptosis regulator Bcl-2
PRO_0000143047

Regions

Transmembrane209 – 23022Helical; Potential
Motif10 – 3021BH4
Motif90 – 10415BH3
Motif133 – 15220BH1
Motif184 – 19916BH2

Sites

Site64 – 652Cleavage; by caspase-3 and caspase-9

Amino acid modifications

Modified residue691Phosphothreonine; by MAPK8 By similarity
Modified residue701Phosphoserine; by MAPK8 and PKC By similarity
Modified residue841Phosphoserine; by MAPK8 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JJV8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BECADF1EF3337228

FASTA23626,491
        10         20         30         40         50         60 
MAQAGRTGYD NREIVMKYIH YKLSQRGYEW DVGDVDAAPL GAAPTPGIFS FQPESNPTPA 

        70         80         90        100        110        120 
VHRDMAARTS PLRPIVATTG PTLSPVPPVV HLTLRRAGDD FSRRYRRDFA EMSSQLHLTP 

       130        140        150        160        170        180 
FTARGRFATV VEELFRDGVN WGRIVAFFEF GGVMCVESVN REMSPLVDNI ALWMTEYLNR 

       190        200        210        220        230 
HLHTWIQDNG GWDAFVELYG PSVRPLFDFS WLSLKTLLSL ALVGACITLG TYLGHK 

« Hide

References

[1]"Cloning and functional analysis of cDNA encoding the hamster Bcl-2 protein."
Tomicic M.T., Christmann M., Kaina B.
Biochem. Biophys. Res. Commun. 275:899-903(2000) [PubMed: 10973819] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Hamster Bcl-2 protein is cleaved in vitro and in cells by caspase-9 and caspase-3."
Tomicic M.T., Kaina B.
Biochem. Biophys. Res. Commun. 281:404-408(2001) [PubMed: 11181062] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CLEAVAGE BY CASPASES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271720 mRNA. Translation: CAB92245.1.
PIRJC7383.

3D structure databases

ProteinModelPortalQ9JJV8.
SMRQ9JJV8. Positions 3-204.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9JJV8. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004472.

Family and domain databases

InterProIPR013278. Apop_reg_Bcl2.
IPR002475. Bcl2-like_apoptosis.
IPR000712. Bcl2_BH.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR004725. Bcl2_reg.
[Graphical view]
PfamPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSPR01863. APOPREGBCL2.
PR01862. BCL2FAMILY.
SMARTSM00337. BCL. 1 hit.
SM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00865. Bcl-2. 1 hit.
PROSITEPS50062. 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]
ProtoNetSearch...

Other

PMAP-CutDBQ9JJV8.

Entry information

Entry nameBCL2_CRIGR
AccessionPrimary (citable) accession number: Q9JJV8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families