BAX

BAX (англ. BCL2 associated X, apoptosis regulator) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 19-ї хромосоми.^[3] Довжина поліпептидного ланцюга білка становить 192 амінокислот, а молекулярна маса — 21 184^[4].

Послідовність амінокислот

10		20		30		40		50
MDGSGEQPRG		GGPTSSEQIM		KTGALLLQGF		IQDRAGRMGG		EAPELALDPV
PQDASTKKLS		ECLKRIGDEL		DSNMELQRMI		AAVDTDSPRE		VFFRVAADMF
SDGNFNWGRV		VALFYFASKL		VLKALCTKVP		ELIRTIMGWT		LDFLRERLLG
WIQDQGGWDG		LLSYFGTPTW		QTVTIFVAGV		LTASLTIWKK		MG

A: Аланін
C: Цистеїн
D: Аспарагінова кислота
E: Глутамінова кислота
F: Фенілаланін
G: Гліцин
I: Ізолейцин
K: Лізин
L: Лейцин
M: Метіонін
N: Аспарагін
P: Пролін
Q: Глутамін
R: Аргінін
S: Серин
T: Треонін
V: Валін
W: Триптофан

Y: Тирозин

BAX
Наявні структури PDB Пошук ортологів: PDBe RCSB Список кодів PDB 4BDU, 1F16, 2G5B, 2K7W, 2LR1, 3PK1, 3PL7, 4BD2, 4BD6, 4BD7, 4BD8, 4UF2, 4ZIE, 4ZIF, 4ZIG, 4ZIH, 4ZII, 4S0O
Ідентифікатори
Символи	BAX, BCL2L4, BCL2 associated X protein, BCL2 associated X, apoptosis regulator
Зовнішні ІД	OMIM: 600040 MGI: 99702 HomoloGene: 7242 GeneCards: BAX
Онтологія гена Молекулярна функція • protein homodimerization activity • channel activity • GO:0001948, GO:0016582 protein binding • BH3 domain binding • chaperone binding • protein heterodimerization activity • identical protein binding • lipid binding • Hsp70 protein binding Клітинна компонента • гіалоплазма • nuclear envelope • мембрана • Bcl-2 family protein complex • мітохондрія • клітинне ядро • mitochondrial permeability transition pore complex • мітохондріальна мембрана • BAX complex • ендоплазматичний ретикулум • екзосома • pore complex • integral component of membrane • внутрішньоклітинний • endoplasmic reticulum membrane • цитоплазма • мітохондріальна зовнішня мембрана • cell periphery Біологічний процес • GO:1904089 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 • regulation of mitochondrial membrane permeability involved in apoptotic process • negative regulation of protein binding • cellular response to DNA damage stimulus • regulation of mitochondrial membrane permeability involved in programmed necrotic cell death • odontogenesis of dentin-containing tooth • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand • positive regulation of IRE1-mediated unfolded protein response • 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 • Сперматогенез • apoptotic signaling pathway • проліферація • mitochondrion morphogenesis • activation of cysteine-type endopeptidase activity involved in apoptotic process • negative regulation of cell population proliferation • cellular response to organic substance • B cell homeostatic proliferation • limb morphogenesis • release of matrix enzymes from mitochondria • extrinsic apoptotic signaling pathway • розвиток нирки • 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 • endoplasmic reticulum calcium ion homeostasis • response to wounding • intrinsic apoptotic signaling pathway by p53 class mediator • hypothalamus development • GO:0022415 viral process • 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 • GO:1990613 mitochondrial fusion • neuron apoptotic process • male gonad development • positive regulation of B cell apoptotic process • regulation of protein heterodimerization activity • positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway • 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 • нейробіологія розвитку • 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 • cerebral cortex development • ovarian follicle development • запліднення • 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 • 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 apoptotic process • positive regulation of protein oligomerization • extrinsic apoptotic signaling pathway via death domain receptors • release of cytochrome c from mitochondria • GO:0097285 апоптоз • protein insertion into mitochondrial membrane involved in apoptotic signaling pathway • intrinsic apoptotic signaling pathway • regulation of apoptotic process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • intrinsic apoptotic signaling pathway in response to DNA damage • extrinsic apoptotic signaling pathway in absence of ligand • transcription initiation from RNA polymerase II promoter • Unfolded Protein Response • negative regulation of mitochondrial membrane potential Джерела:Amigo / QuickGO
Шаблон експресії
Більше даних
Ортологи
Види	Людина	Миша
Entrez	581	12028
Ensembl	ENSG00000087088	ENSMUSG00000003873
UniProt	Q07812 Q5ZPJ0	Q07813
RefSeq (мРНК)	NM_001291428 NM_001291429 NM_001291430 NM_001291431 NM_004324 NM_138761 NM_138762 NM_138763 NM_138764	NM_007527
RefSeq (білок)	NP_001278357 NP_001278358 NP_001278359 NP_001278360 NP_004315 NP_620116 NP_620118 NP_620119 NP_001278358.1	NP_031553
Локус (UCSC)	Хр. 19: 48.95 – 48.96 Mb	Хр. 7: 45.11 – 45.12 Mb
PubMed search	[1]	[2]
Вікідані
Див./Ред. для людей Див./Ред. для мишей

Задіяний у таких біологічних процесах, як апоптоз, взаємодія хазяїн-вірус, ацетилювання, альтернативний сплайсинг. Локалізований у цитоплазмі, мембрані, мітохондрії.

Література

• Oltvai Z.N., Milliman C.L., Korsmeyer S.J. (1993). Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 74: 609—619. PMID 8358790 DOI:10.1016/0092-8674(93)90509-O
• Apte S.S., Mattei M.-G., Olsen B.R. (1995). Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta. Genomics. 26: 592—594. PMID 7607685 DOI:10.1016/0888-7543(95)80180-T
• Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R. (2000). Characterization of Bax-sigma, a cell death-inducing isoform of Bax. Biochem. Biophys. Res. Commun. 270: 868—879. PMID 10772918 DOI:10.1006/bbrc.2000.2537
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
• Nechushtan A., Smith C.L., Hsu Y.-T., Youle R.J. (1999). Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18: 2330—2341. PMID 10228148 DOI:10.1093/emboj/18.9.2330
• Gustafsson A.B., Tsai J.G., Logue S.E., Crow M.T., Gottlieb R.A. (2004). Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation. J. Biol. Chem. 279: 21233—21238. PMID 15004034 DOI:10.1074/jbc.M400695200

Примітки

1. Human PubMed Reference:.
2. Mouse PubMed Reference:.
3. HUGO Gene Nomenclature Commitee, HGNC:959 (англ.) . Архів оригіналу за 16 липня 2017. Процитовано 12 вересня 2017. [Архівовано 2017-07-16 у Wayback Machine.]
4. UniProt, Q07812 (англ.) . Архів оригіналу за 18 серпня 2017. Процитовано 12 вересня 2017.

Див. також

• Хромосома 19