BH3-interacting domain death agonist (BID)
The protein contains 195 amino acids for an estimated molecular weight of 21995 Da.
The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs8190315 | |
| dbSNP:rs17853595 | |
| dbSNP:rs59225839 |
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process
Apoptotic mitochondrial changes
Apoptotic process
Brain development
Establishment of protein localization to membrane
Extrinsic apoptotic signaling pathway via death domain receptors
Glial cell apoptotic process
Hepatocyte apoptotic process
Intrinsic apoptotic signaling pathway
Mitochondrial ATP synthesis coupled electron transport
Mitochondrial outer membrane permeabilization
Negative regulation of apoptotic process
Negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
Neuron apoptotic process
Positive regulation of apoptotic process
Positive regulation of extrinsic apoptotic signaling pathway
Positive regulation of fibroblast apoptotic process
Positive regulation of intrinsic apoptotic signaling pathway
Positive regulation of mitochondrial membrane potential
Positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
Positive regulation of protein homooligomerization
Positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
Positive regulation of protein oligomerization
Positive regulation of protein-containing complex assembly
Positive regulation of release of cytochrome c from mitochondria
Protein homooligomerization
Protein targeting to mitochondrion
Protein-containing complex assembly
Regulation of apoptotic process
Regulation of cell population proliferation
Regulation of G1/S transition of mitotic cell cycle
Release of cytochrome c from mitochondria
Response to estradiol
Signal transduction in response to DNA damage
The reference OMIM entry for this protein is 601997
Bh3-interacting domain death agonist; bid
CLONING
The BCL2 family of proteins consists of both antagonists (e.g., BCL2; 151430) and agonists (e.g., BAX; 600040 and BAK; 600516) that regulate apoptosis and compete through dimerization. The BH1 and BH2 domains of BCL2 are required to heterodimerize with BAX and to repress cell death. Conversely, the BH3 domain of BAX is required to heterodimerize with BCL2 and to promote cell death. Wang et al. (1996) identified a gene they termed BID (BH3 Interacting domain Death agonist) that encodes a novel death agonist that heterodimerizes with either agonists (BAX) or antagonists (BCL2). BID possesses only the BH3 domain, lacks a C-terminal signal-anchor segment, and is found in both cytosolic and membrane locations. BID's only homology with the BCL2 family is the conserved BH3 domain. BID counters the protective effect of BCL2. Expression of BID induces ICE-like proteases which are thought to be downstream of BCL2, activated in apoptosis, and required for aspects of cell death. Wang et al. (1996) stated that the discovery of this BH3-only molecule supports the identification of BH3 as a death domain and favors a model in which BID represents a death ligand for the membrane-bound receptor BAX.GENE FUNCTION
Luo et al. (1998) reported the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8 (CASP8; 601763), the apical caspase activated by cell surface death receptors such as FAS (134637) and TNF (191160). Peptide mass fingerprinting identified this protein as BID. CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Immunodepletion of BID from cell extracts eliminated the cytochrome c releasing activity. The cytochrome c releasing activity of BID was antagonized by BCL2. A mutation at the BH3 domain diminished its cytochrome c releasing activity. BID, therefore, relays an apoptotic signal from the cell surface to mitochondria. Li et al. (1998) reported that BID is a specific proximal substrate of CASP8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. Truncated BID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. The results of Li et al. (1998) indicated that BID is a mediator of mitochondrial damage induced by CASP8. Zha et al. (2000) found that BID underwent posttranslational (rather than classic cotranslocational) N-myristoylation when cleavage by CASP8 caused exposure of a glycine residue at position 60. N-myristoylation enabled the targeting of a complex of p7 and myristoylated p15 fragments of BID to artificial membranes bearing the lipid composition of mitochondria, as well as to intact mitochondria. Zha et al. (2000) found that this post-proteolytic N-myristoylation serves as an activating switch, enhancing BID-induced release of cytochrome c and cell death. The caspase-activated form of BID, tBID, triggers the homooligomerization of multidomain conserved proapoptotic family members BAK or BAX, resulting in the release of cytochrome c from mitochondria. Wei et al. (2001) found that cells lacking both BAK and BAX, but not cells lacking ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601997 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed