BAX

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 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	• 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; • 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; • 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; • 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; • 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; • cellular response to unfolded protein; • negative regulation of mitochondrial membrane potential;
	Джерела:Amigo / QuickGO
Шаблон експресії
	; ;
	Більше даних
Ортологи
	581
	12028
	ENSG00000087088
	ENSMUSG00000003873
	Q07812; Q5ZPJ0
	Q07813
NM_001291428; NM_001291429; NM_001291430; NM_001291431; NM_004324;
	NM_138761; NM_138762; NM_138763; NM_138764
	NM_007527
NP_001278357; NP_001278358; NP_001278359; NP_001278360; NP_004315;
	NP_620116; NP_620118; NP_620119; NP_001278358.1
	NP_031553
	Вікідані
Див./Ред. для людей	Див./Ред. для мишей

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

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. PubMed 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. PubMed 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. PubMed 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. PubMed 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. PubMed 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. PubMed DOI:10.1074/jbc.M400695200

Примітки

Human PubMed Reference:.
Mouse PubMed Reference:.
HUGO Gene Nomenclature Commitee, HGNC:959 (англ.). Процитовано 12 вересня 2017.
UniProt, Q07812 (англ.). Процитовано 12 вересня 2017.

Див. також

Хромосома 19

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[1] Human PubMed Reference:.

[2] Mouse PubMed Reference:.

[HGNC-3] HUGO Gene Nomenclature Commitee, HGNC:959 (англ.). Процитовано 12 вересня 2017.

[UniProt-4] UniProt, Q07812 (англ.). Процитовано 12 вересня 2017.