BCL2-associated X protein

mammalian protein found in Mus musculus

Protein protein Q14905404

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BCL2-associated X protein

Summary

BCL2-associated X protein is a protein^[1].

Key Facts

BCL2-associated X protein's instance of is recorded as protein^[2].
BCL2-associated X protein's UniProt protein ID is recorded as Q07813^[3].
BCL2-associated X protein's part of is recorded as Blc2-like superfamily^[4].
BCL2-associated X protein's part of is recorded as Apoptosis regulator BAX^[5].
BCL2-associated X protein's part of is recorded as Apoptosis regulator, Bcl-2, BH3 motif, conserved site, protein family^[6].
BCL2-associated X protein's part of is recorded as Apoptosis regulator, Bcl-2, BH1 motif, conserved site, protein family^[7].
BCL2-associated X protein's part of is recorded as Apoptosis regulator, Bcl-2, BH2 motif, conserved site, protein family^[8].
BCL2-associated X protein's has part is recorded as Apoptosis regulator, Bcl-2, BH2 motif, conserved site^[9].
BCL2-associated X protein's has part is recorded as Apoptosis regulator, Bcl-2, BH1 motif, conserved site^[10].
BCL2-associated X protein's has part is recorded as Apoptosis regulator, Bcl-2, BH3 motif, conserved site^[11].
BCL2-associated X protein's RefSeq protein ID is recorded as NP_031553^[12].
BCL2-associated X protein's RefSeq protein ID is recorded as XP_006540647^[13].
BCL2-associated X protein's RefSeq protein ID is recorded as XP_011249082^[14].
BCL2-associated X protein's PDB structure ID is recorded as 2XA0^[15].
BCL2-associated X protein's molecular function is recorded as protein homodimerization activity^[16].
BCL2-associated X protein's molecular function is recorded as protein binding^[17].
BCL2-associated X protein's molecular function is recorded as BH3 domain binding^[18].
BCL2-associated X protein's molecular function is recorded as protein heterodimerization activity^[19].
BCL2-associated X protein's molecular function is recorded as lipid binding^[20].
BCL2-associated X protein's molecular function is recorded as chaperone binding^[21].
BCL2-associated X protein's molecular function is recorded as Hsp70 protein binding^[22].
BCL2-associated X protein's molecular function is recorded as channel activity^[23].
BCL2-associated X protein's molecular function is recorded as identical protein binding^[24].
BCL2-associated X protein's molecular function is recorded as heat shock protein binding^[25].
BCL2-associated X protein's molecular function is recorded as identical protein binding^[26].

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Quick Facts

Instance of protein

Part of Blc2-like superfamily, Apoptosis regulator BAX, Apoptosis regulator, Bcl-2, BH3 motif, conserved site, protein family, Apoptosis regulator, Bcl-2, BH1 motif, conserved site, protein family, Apoptosis regulator, Bcl-2, BH2 motif, conserved site, protein family

Properties

Biological process negative regulation of neuron apoptotic process, response to ionizing radiation, germ cell development, positive regulation of calcium ion transport into cytosol, glycosphingolipid metabolic process, B cell apoptotic process, response to salt stress, Sertoli cell proliferation, thymocyte apoptotic process, T cell homeostatic proliferation, post-embryonic development, negative regulation of protein binding, regulation of mitochondrial membrane permeability involved in apoptotic process, cellular response to DNA damage stimulus, regulation of mitochondrial membrane permeability involved in programmed necrotic cell death, odontogenesis of dentin-containing tooth, intrinsic apoptotic signaling pathway, positive regulation of extrinsic apoptotic signaling pathway in absence of ligand, blood vessel remodeling, positive regulation of neuron apoptotic process, apoptotic process involved in blood vessel morphogenesis, activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c, spermatogenesis, intrinsic apoptotic signaling pathway in response to DNA damage, apoptotic signaling pathway, cell population proliferation, mitochondrion morphogenesis, activation of cysteine-type endopeptidase activity involved in apoptotic process, negative regulation of cell population proliferation, apoptotic process, regulation of apoptotic process, cellular response to organic substance, B cell homeostatic proliferation, limb morphogenesis, release of matrix enzymes from mitochondria, extrinsic apoptotic signaling pathway, kidney development, activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway, negative regulation of apoptotic signaling pathway, myeloid cell homeostasis, regulation of neuron apoptotic process, regulation of cysteine-type endopeptidase activity involved in apoptotic process, response to wounding, intrinsic apoptotic signaling pathway by p53 class mediator, hypothalamus development, protein homooligomerization, response to gamma radiation, negative regulation of fibroblast proliferation, positive regulation of intrinsic apoptotic signaling pathway, response to toxic substance, B cell negative selection, mitochondrial fusion, neuron apoptotic process, male gonad development, positive regulation of B cell apoptotic process, regulation of protein heterodimerization activity, cellular response to UV, sex differentiation, neuron migration, B cell homeostasis, positive regulation of release of sequestered calcium ion into cytosol, positive regulation of apoptotic process involved in mammary gland involution, nervous system development, spermatid differentiation, development of secondary sexual characteristics, positive regulation of developmental pigmentation, retina development in camera-type eye, response to axon injury, positive regulation of mitochondrial membrane permeability involved in apoptotic process, fertilization, ectopic germ cell programmed cell death, homeostasis of number of cells within a tissue, positive regulation of release of cytochrome c from mitochondria, B cell receptor apoptotic signaling pathway, negative regulation of endoplasmic reticulum calcium ion concentration, regulation of protein homodimerization activity, protein insertion into mitochondrial membrane involved in apoptotic signaling pathway, apoptotic process involved in embryonic digit morphogenesis, leukocyte homeostasis, positive regulation of apoptotic DNA fragmentation, mitochondrial fragmentation involved in apoptotic process, positive regulation of endoplasmic reticulum unfolded protein response, establishment or maintenance of transmembrane electrochemical gradient, homeostasis of number of cells, vagina development, post-embryonic camera-type eye morphogenesis, regulation of mammary gland epithelial cell proliferation, retinal cell programmed cell death, regulation of cell cycle, regulation of mitochondrial membrane potential, intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress, apoptotic mitochondrial changes, protein complex oligomerization, regulation of nitrogen utilization, negative regulation of peptidyl-serine phosphorylation, positive regulation of protein oligomerization, positive regulation of apoptotic process, extrinsic apoptotic signaling pathway in absence of ligand, extrinsic apoptotic signaling pathway via death domain receptors, release of cytochrome c from mitochondria, ovarian follicle development, cerebral cortex development, release of cytochrome c from mitochondria, activation of cysteine-type endopeptidase activity involved in apoptotic process, inner mitochondrial membrane organization, outer mitochondrial membrane organization, mitochondrial fusion, intrinsic apoptotic signaling pathway in response to DNA damage, viral process, positive regulation of apoptotic process, cellular respiration, extrinsic apoptotic signaling pathway in absence of ligand, negative regulation of mitochondrial membrane potential, negative regulation of mitochondrial membrane potential

Cell component cytosol, nuclear envelope, Bcl-2 family protein complex, mitochondrion, nucleus, mitochondrial permeability transition pore complex, BAX complex, endoplasmic reticulum, pore complex, integral component of membrane, intracellular anatomical structure, endoplasmic reticulum membrane, mitochondrial outer membrane, mitochondrial membranes, cytoplasm, cell periphery, membrane, mitochondrion, mitochondrial outer membrane, mitochondrial membranes, perinuclear region of cytoplasm

Encoded by Bax

Exact match identifiers.org, purl.uniprot.org, www.ncbi.nlm.nih.gov

Found in taxon house mouse

Has part(s) Apoptosis regulator, Bcl-2, BH2 motif, conserved site, Apoptosis regulator, Bcl-2, BH1 motif, conserved site, Apoptosis regulator, Bcl-2, BH3 motif, conserved site

Imported from wholeness_audit_2026-05-02

Molecular function protein homodimerization activity, protein binding, BH3 domain binding, protein heterodimerization activity, lipid binding, chaperone binding, Hsp70 protein binding, channel activity, identical protein binding, heat shock protein binding, identical protein binding, protein homodimerization activity, protein-containing complex binding, protein heterodimerization activity, chaperone binding, BH domain binding

External References (4)

Ensembl protein id ENSMUSP00000033093, ENSMUSP00000147753, ENSMUSP00000148182, ENSMUSP00000148240, ENSMUSP00000148265

Pdb structure id 2XA0

Refseq protein id NP_031553, XP_006540647, XP_011249082

Uniprot protein id Q07813

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ BCL2-associated X protein — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ BCL2-associated X protein — UniProt protein ID (P352): Q07813. Q905695. Retrieved 2022-05-25. wikidata.org.
[4] ↑ BCL2-associated X protein — part of (P361): Blc2-like superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ BCL2-associated X protein — part of (P361): Apoptosis regulator BAX. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ BCL2-associated X protein — part of (P361): Apoptosis regulator, Bcl-2, BH3 motif, conserved site, protein family. wikidata.org.
[7] ↑ BCL2-associated X protein — part of (P361): Apoptosis regulator, Bcl-2, BH1 motif, conserved site, protein family. wikidata.org.
[8] ↑ BCL2-associated X protein — part of (P361): Apoptosis regulator, Bcl-2, BH2 motif, conserved site, protein family. wikidata.org.
[9] ↑ BCL2-associated X protein — has part(s) (P527): Apoptosis regulator, Bcl-2, BH2 motif, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ BCL2-associated X protein — has part(s) (P527): Apoptosis regulator, Bcl-2, BH1 motif, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[11] ↑ BCL2-associated X protein — has part(s) (P527): Apoptosis regulator, Bcl-2, BH3 motif, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[12] ↑ BCL2-associated X protein — RefSeq protein ID (P637): NP_031553. Q20641742. Retrieved 2022-03-20. wikidata.org.
[13] ↑ BCL2-associated X protein — RefSeq protein ID (P637): XP_006540647. Q20641742. Retrieved 2022-03-20. wikidata.org.
[14] ↑ BCL2-associated X protein — RefSeq protein ID (P637): XP_011249082. Q20641742. Retrieved 2022-03-20. wikidata.org.
[15] ↑ BCL2-associated X protein — PDB structure ID (P638): 2XA0. Q905695. Retrieved 2016-08-09. wikidata.org.
[16] ↑ BCL2-associated X protein — molecular function (P680): protein homodimerization activity. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ BCL2-associated X protein — molecular function (P680): protein binding. BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ BCL2-associated X protein — molecular function (P680): BH3 domain binding. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ BCL2-associated X protein — molecular function (P680): protein heterodimerization activity. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ BCL2-associated X protein — molecular function (P680): lipid binding. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ BCL2-associated X protein — molecular function (P680): chaperone binding. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ BCL2-associated X protein — molecular function (P680): Hsp70 protein binding. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ BCL2-associated X protein — molecular function (P680): channel activity. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ BCL2-associated X protein — molecular function (P680): identical protein binding. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ BCL2-associated X protein — molecular function (P680): heat shock protein binding. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ BCL2-associated X protein — molecular function (P680): identical protein binding. GOA. Retrieved 2019-04-08. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ BCL2-associated X protein is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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APA

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MLA

“BCL2-associated X protein.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/bcl2-associated-x-protein.

BibTeX

@misc{4ortxyz_bcl2-associated-x-protein_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{BCL2-associated X protein}}, year = {2026}, url = {https://4ort.xyz/entity/bcl2-associated-x-protein}, note = {Accessed: 2026-05-03}}

LLM prompt

According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): BCL2-associated X protein — https://4ort.xyz/entity/bcl2-associated-x-protein (retrieved 2026-05-03)

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