logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0075 : BAK, BCL2-antagonist/killer 1

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesbcl-2 homologous antagonist/killer [Homo sapiens]; bcl-2 homologous antagonist/killer; pro-apoptotic protein BAK; apoptosis regulator BAK; BCL2-like 7 protein; bcl2-L-7; bcl-2-like protein 7; Bcl-2 homologous antagonist/killer; Apoptosis regulator BAK; Bcl-2-like protein 7; Bcl2-L-7
Gene NamesBAK1; BAK, BCL2L7, CDN1; BAK; BCL2L7; CDN1; BCL2-antagonist/killer 1
Gene Locus6p21.3; chromosome 6
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001179 NM_001188 578 Q16611 600516 HGNC:949 02744 hsa:578

* Information From OMIM

Function: Chittenden et al. (1995) and Kiefer et al. (1995) described the functional analysis of BAK, which promotes cell death and counteracts the protection from apoptosis provided by BCL2. Chittenden et al. (1995) found that enforced expression of BAK induced rapid and extensive apoptosis of serum-deprived fibroblasts. This suggested that BAK may be directly involved in activating the cell death machinery. Kiefer et al. (1995) pointed out that, like BAX (OMIM:600040), the BAK gene product primarily enhances apoptotic cell death following an appropriate stimulus. Unlike BAX, however, BAK can inhibit cell death in an Epstein-Barr virus-transformed cell line.

* Structure Information

1. Primary Information

Length: 211 aa

Average Mass: 23.408 kDa

Monoisotopic Mass: 23.394 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 15 ---
Apoptosis regulator proteins, Bcl-2 family 1. 26457.00.1
Apoptosis regulator M11, B cell 2 leukaemia/lymphoma like 1. 7913535.00.0

3. Sequence Information

Fasta Sequence: SB0075.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1BXL (NMR; -; B=72-87), 2IMS (X-ray; 148 A; A=16-186), 2IMT (X-ray; 149 A; A=16-186), 2JBY (X-ray; 241 A; B=67-92), 2JCN (X-ray; 180 A; A=21-190), 2LP8 (NMR; -; B=72-87), 2M5B (NMR; -; A=18-186), 2XPX (X-ray; 205 A; B=67-92), 2YV6 (X-ray; 250 A; A=23-185), 3I1H (X-ray; 220 A; B=72-87), 3QBR (X-ray; 260 A; B/Y=63-96), 4D2L (X-ray; 290 A; B=67-91), 4U2U (X-ray; 290 A; A/B=23-186), 4U2V (X-ray; 230 A; A/B/C/D=68-148), 5AJK (X-ray; 255 A; B/D/F/H/J/L=67-92)

* Cleavage Information

1 [sites] cleaved by Calpain 1 and 2

Source Reference: [PubMed ID: 17157251] Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K, The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell. 2006 Dec 8;24(5):677-88.

Cleavage sites (±10aa)


Gly15 Glu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24265320] Dai H, Pang YP, Ramirez-Alvarado M, Kaufmann SH, Evaluation of the BH3-only protein Puma as a direct Bak activator. J Biol Chem. 2014 Jan 3;289(1):89-99. doi: 10.1074/jbc.M113.505701. Epub 2013 Nov

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