Bcl-2-interacting killer

BIK
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2IPE
Identifiers
Aliases	BIK , BIP1, BP4, NBK, BCL2 interacting killer
External IDs	OMIM: 603392 MGI: 1206591 HomoloGene: 924 GeneCards: BIK
Gene location (Human)
Chr.	Chromosome 22 (human)
End	43,129,712 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	83,428,835 bp
RNA expression pattern
	Top expressed in
	palpebral conjunctiva; ; bronchial epithelial cell; ; minor salivary gland; ; prostate; ; epithelium of esophagus; ; trachea; ; pancreatic epithelial cell; ; pancreatic ductal cell; ; lactiferous duct; ; body of stomach;
	Top expressed in
	proximal tubule; ; conjunctival fornix; ; right lung lobe; ; ascending aorta; ; stria vascularis; ; submandibular gland; ; morula; ; kidney; ; secondary oocyte; ; atrium;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding ; BH domain binding ; protein heterodimerization activity ;
Cellular component	integral component of membrane ; endomembrane system ; mitochondrial membrane ; mitochondrion ; membrane ;
Biological process	regulation of apoptotic process ; positive regulation of protein homooligomerization ; positive regulation of release of cytochrome c from mitochondria ; apoptotic process ; male gonad development ; apoptotic mitochondrial changes ;
	Sources:Amigo / QuickGO
Orthologs
	638
	12124
	ENSG00000100290
	ENSMUSG00000016758
	Q13323
	O70337
	NM_001197
	NM_007546
	NP_001188 ; NP_001188.1
	NP_031572
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 02, 2023

Bcl-2-interacting killer is a protein that in humans is encoded by the BIK gene.^[5]^[6]^[7]

Function

The protein encoded by this gene is known to interact with cellular and viral survival-promoting proteins, such as BCL2 and the Epstein–Barr virus in order to enhance programmed cell death. Because its activity is suppressed in the presence of survival-promoting proteins, this protein is suggested as a likely target for antiapoptotic proteins. This protein shares a critical BH3 domain with other death-promoting proteins, BAX and BAK.^[7]

Interactions

Bcl-2-interacting killer has been shown to interact with BCL2-like 1 ^[8]^[9]^[10]^[11] and Bcl-2.^[9]^[10]

Related Research Articles

Bcl-2, encoded in humans by the BCL2 gene, is the founding member of the Bcl-2 family of regulator proteins that regulate cell death (apoptosis), by either inhibiting (anti-apoptotic) or inducing (pro-apoptotic) apoptosis. It was the first apoptosis regulator identified in any organism.

Apoptosis regulator BAX, also known as bcl-2-like protein 4, is a protein that in humans is encoded by the BAX gene. BAX is a member of the Bcl-2 gene family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis.

The BH3 interacting-domain death agonist, or BID, gene is a pro-apoptotic member of the Bcl-2 protein family. Bcl-2 family members share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains, and can form hetero- or homodimers. Bcl-2 proteins act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities.

The p53 upregulated modulator of apoptosis (PUMA) also known as Bcl-2-binding component 3 (BBC3), is a pro-apoptotic protein, member of the Bcl-2 protein family. In humans, the Bcl-2-binding component 3 protein is encoded by the BBC3 gene. The expression of PUMA is regulated by the tumor suppressor p53. PUMA is involved in p53-dependent and -independent apoptosis induced by a variety of signals, and is regulated by transcription factors, not by post-translational modifications. After activation, PUMA interacts with antiapoptotic Bcl-2 family members, thus freeing Bax and/or Bak which are then able to signal apoptosis to the mitochondria. Following mitochondrial dysfunction, the caspase cascade is activated ultimately leading to cell death.

Phorbol-12-myristate-13-acetate-induced protein 1 is a protein that in humans is encoded by the PMAIP1 gene, and is also known as Noxa.

Bcl-2 homologous antagonist/killer is a protein that in humans is encoded by the BAK1 gene on chromosome 6. The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.

The BCL2 associated agonist of cell death (BAD) protein is a pro-apoptotic member of the Bcl-2 gene family which is involved in initiating apoptosis. BAD is a member of the BH3-only family, a subfamily of the Bcl-2 family. It does not contain a C-terminal transmembrane domain for outer mitochondrial membrane and nuclear envelope targeting, unlike most other members of the Bcl-2 family. After activation, it is able to form a heterodimer with anti-apoptotic proteins and prevent them from stopping apoptosis.

Bcl-2-like protein 1 is a protein encoded in humans by the BCL2L1 gene. Through alternative splicing, the gene encodes both of the human proteins Bcl-xL and Bcl-xS.

BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the BAG1 gene.

Induced myeloid leukemia cell differentiation protein Mcl-1 is a protein that in humans is encoded by the MCL1 gene.

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 is a protein found in humans that is encoded by the BNIP3 gene.

Bcl-2-like protein 11, commonly called BIM, is a protein that in humans is encoded by the BCL2L11 gene.

Bcl-2-related protein A1 is a protein in humans which is encoded by the BCL2A1 gene.

Bcl-2-like protein 2 is a 193-amino acid protein that in humans is encoded by the BCL2L2 gene on chromosome 14. It was originally discovered by Leonie Gibson, Suzanne Cory and colleagues at the Walter and Eliza Hall Institute of Medical Research, who called it Bcl-w.

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like is a protein that in humans is encoded by the BNIP3L gene.

Activator of apoptosis harakiri is a protein that in humans is encoded by the HRK gene.

Bcl-2-modifying factor is a protein that in humans is encoded by the BMF gene.

Apoptosis facilitator Bcl-2-like protein 14 is a protein that in humans is encoded by the BCL2L14 gene.

Bok is a protein-coding gene of the Bcl-2 family that is found in many invertebrates and vertebrates. It induces apoptosis, a special type of cell death. Currently, the precise function of Bok in this process is unknown.

Bcl-2-like protein 10 is a protein that in humans is encoded by the BCL2L10 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100290 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000016758 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Boyd JM, Gallo GJ, Elangovan B, Houghton AB, Malstrom S, Avery BJ, Ebb RG, Subramanian T, Chittenden T, Lutz RJ (Dec 1995). "Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins". Oncogene. 11 (9): 1921–8. PMID 7478623.
↑ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi: 10.1038/990031 . PMID 10591208.
1 2 "Entrez Gene: BIK BCL2-interacting killer (apoptosis-inducing)".
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
1 2 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi: 10.1016/j.molcel.2004.12.030 . PMID 15694340.
1 2 Gillissen B, Essmann F, Graupner V, Stärck L, Radetzki S, Dörken B, Schulze-Osthoff K, Daniel PT (July 2003). "Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway". EMBO J. 22 (14): 3580–90. doi:10.1093/emboj/cdg343. PMC 165613 . PMID 12853473.
↑ Jiang A, Clark EA (May 2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. 166 (10): 6025–33. doi: 10.4049/jimmunol.166.10.6025 . PMID 11342619.

External links

Human BIK genome location and BIK gene details page in the UCSC Genome Browser .

Chittenden T, Flemington C, Houghton AB, Ebb RG, Gallo GJ, Elangovan B, Chinnadurai G, Lutz RJ (1996). "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions". EMBO J. 14 (22): 5589–96. doi:10.1002/j.1460-2075.1995.tb00246.x. PMC 394673 . PMID 8521816.
Han J, Sabbatini P, White E (1996). "Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K". Mol. Cell. Biol. 16 (10): 5857–64. doi:10.1128/MCB.16.10.5857. PMC 231587 . PMID 8816500.
Inohara N, Ding L, Chen S, Núñez G (1997). "harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)". EMBO J. 16 (7): 1686–94. doi:10.1093/emboj/16.7.1686. PMC 1169772 . PMID 9130713.
Huang DC, Adams JM, Cory S (1998). "The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4". EMBO J. 17 (4): 1029–39. doi:10.1093/emboj/17.4.1029. PMC 1170452 . PMID 9463381.
Hegde R, Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES (1998). "Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist". J. Biol. Chem. 273 (14): 7783–6. doi: 10.1074/jbc.273.14.7783 . PMID 9525867.
Ohi N, Tokunaga A, Tsunoda H, Nakano K, Haraguchi K, Oda K, Motoyama N, Nakajima T (1999). "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region". Cell Death Differ. 6 (4): 314–25. doi: 10.1038/sj.cdd.4400493 . PMID 10381623.
Holmgreen SP, Huang DC, Adams JM, Cory S (1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi: 10.1038/sj.cdd.4400519 . PMID 10381646.
Castells A, Ino Y, Louis DN, Ramesh V, Gusella JF, Rustgi AK (1999). "Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer". Gastroenterology. 117 (4): 831–7. doi: 10.1016/S0016-5085(99)70341-0 . PMID 10500065.
Verma S, Budarf ML, Emanuel BS, Chinnadurai G (2000). "Structural analysis of the human pro-apoptotic gene Bik: chromosomal localization, genomic organization and localization of promoter sequences". Gene. 254 (1–2): 157–62. doi:10.1016/S0378-1119(00)00276-6. PMID 10974546.
Jiang A, Clark EA (2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. 166 (10): 6025–33. doi: 10.4049/jimmunol.166.10.6025 . PMID 11342619.
Federici M, Hribal M, Perego L, Ranalli M, Caradonna Z, Perego C, Usellini L, Nano R, Bonini P, Bertuzzi F, Marlier LN, Davalli AM, Carandente O, Pontiroli AE, Melino G, Marchetti P, Lauro R, Sesti G, Folli F (2001). "High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: a potential role for regulation of specific Bcl family genes toward an apoptotic cell death program". Diabetes. 50 (6): 1290–301. doi: 10.2337/diabetes.50.6.1290 . PMID 11375329.
Zou Y, Peng H, Zhou B, Wen Y, Wang SC, Tsai EM, Hung MC (2002). "Systemic tumor suppression by the proapoptotic gene bik". Cancer Res. 62 (1): 8–12. PMID 11782349.
Germain M, Mathai JP, Shore GC (2002). "BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria". J. Biol. Chem. 277 (20): 18053–60. doi: 10.1074/jbc.M201235200 . PMID 11884414.
Gillissen B, Essmann F, Graupner V, Stärck L, Radetzki S, Dörken B, Schulze-Osthoff K, Daniel PT (2003). "Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway". EMBO J. 22 (14): 3580–90. doi:10.1093/emboj/cdg343. PMC 165613 . PMID 12853473.
Arena V, Martini M, Luongo M, Capelli A, Larocca LM (2003). "Mutations of the BIK gene in human peripheral B-cell lymphomas". Genes Chromosomes Cancer. 38 (1): 91–6. doi:10.1002/gcc.10245. PMID 12874789. S2CID 23761640.
Hur J, Chesnes J, Coser KR, Lee RS, Geck P, Isselbacher KJ, Shioda T (2004). "The Bik BH3-only protein is induced in estrogen-starved and antiestrogen-exposed breast cancer cells and provokes apoptosis". Proc. Natl. Acad. Sci. U.S.A. 101 (8): 2351–6. Bibcode:2004PNAS..101.2351H. doi: 10.1073/pnas.0307337101 . PMC 356954 . PMID 14983013.
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi: 10.1186/gb-2004-5-10-r84 . PMC 545604 . PMID 15461802.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100290 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000016758 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7478623-5] Boyd JM, Gallo GJ, Elangovan B, Houghton AB, Malstrom S, Avery BJ, Ebb RG, Subramanian T, Chittenden T, Lutz RJ (Dec 1995). "Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins". Oncogene. 11 (9): 1921–8. PMID 7478623.

[pmid10591208-6] Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi: 10.1038/990031 . PMID 10591208.

[entrez-7] 1 2 "Entrez Gene: BIK BCL2-interacting killer (apoptosis-inducing)".

[pmid16189514-8] Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

[pmid15694340-9] 1 2 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi: 10.1016/j.molcel.2004.12.030 . PMID 15694340.

[pmid12853473-10] 1 2 Gillissen B, Essmann F, Graupner V, Stärck L, Radetzki S, Dörken B, Schulze-Osthoff K, Daniel PT (July 2003). "Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway". EMBO J. 22 (14): 3580–90. doi:10.1093/emboj/cdg343. PMC 165613 . PMID 12853473.

[pmid11342619-11] Jiang A, Clark EA (May 2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. 166 (10): 6025–33. doi: 10.4049/jimmunol.166.10.6025 . PMID 11342619.

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