Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
BAX (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BAX Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. Homodimer. Forms higher oligomers under stress conditions. Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and association with mitochondrial membranes, with subsequent release of cytochrome c. Forms heterodimers with BCL2, E1B 19K protein, BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1. Interacts with SH3GLB1 and HN. Interacts with SFN and YWHAZ; the interaction occurs in the cytoplasm. Under stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ, releases BAX to mitochondria. Isoform Sigma interacts with BCL2A1 and BCL2L1 isoform Bcl-X(L). Interacts with RNF144B, which regulates the ubiquitin-dependent stability of BAX. Interacts with CLU under stress conditions that cause a conformation change leading to BAX oligomerization and association with mitochondria. Does not interact with CLU in unstressed cells. Interacts with FAIM2/LFG2. Interacts with human cytomegalovirus/HHV-5 protein vMIA/UL37. Expressed in a wide variety of tissues. Isoform Psi is found in glial tumors. Isoform Alpha is expressed in spleen, breast, ovary, testis, colon and brain, and at low levels in skin and lung. Isoform Sigma is expressed in spleen, breast, ovary, testis, lung, colon, brain and at low levels in skin. Isoform Alpha and isoform Sigma are expressed in pro- myelocytic leukemia, histiocytic lymphoma, Burkitt's lymphoma, T- cell lymphoma, lymphoblastic leukemia, breast adenocarcinoma, ovary adenocarcinoma, prostate carcinoma, prostate adenocarcinoma, lung carcinoma, epidermoid carcinoma, small cell lung carcinoma and colon adenocarcinoma cell lines. Belongs to the Bcl-2 family. 8 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Tumor suppressor; Membrane protein, integral; Mitochondrial
Chromosomal Location of Human Ortholog: 19q13.3-q13.4
Cellular Component: cytosol; endoplasmic reticulum; endoplasmic reticulum membrane; membrane; mitochondrial outer membrane; mitochondrial permeability transition pore complex; mitochondrion; nuclear envelope; nucleus; perinuclear region of cytoplasm; pore complex
Molecular Function: BH3 domain binding; channel activity; chaperone binding; heat shock protein binding; identical protein binding; lipid binding; protein binding; protein complex binding; protein heterodimerization activity; protein homodimerization activity
Biological Process: aging; apoptosis; apoptotic mitochondrial changes; B cell apoptosis; B cell homeostasis; B cell homeostatic proliferation; B cell negative selection; blood vessel remodeling; caspase activation; caspase activation via cytochrome c; cellular respiration; cerebral cortex development; development of secondary sexual characteristics; DNA damage response, signal transduction resulting in induction of apoptosis; endoplasmic reticulum calcium ion homeostasis; establishment and/or maintenance of transmembrane electrochemical gradient; fertilization; germ cell development; germ cell programmed cell death; glycosphingolipid metabolic process; homeostasis of number of cells within a tissue; hypothalamus development; induction of apoptosis via death domain receptors; inner mitochondrial membrane organization and biogenesis; kidney development; mitochondrial fragmentation during apoptosis; mitochondrial fusion; myeloid cell homeostasis; negative regulation of fibroblast proliferation; negative regulation of neuron apoptosis; negative regulation of peptidyl-serine phosphorylation; negative regulation of protein binding; neuron apoptosis; neuron migration; odontogenesis of dentine-containing teeth; outer mitochondrial membrane organization and biogenesis; ovarian follicle development; positive regulation of apoptosis; positive regulation of apoptosis involved in mammary gland involution; positive regulation of B cell apoptosis; positive regulation of neuron apoptosis; positive regulation of pigmentation; positive regulation of protein oligomerization; positive regulation of release of sequestered calcium ion into cytosol; post-embryonic camera-type eye morphogenesis; programmed cell death; protein homooligomerization; protein insertion into mitochondrial membrane during induction of apoptosis; protein oligomerization; reduction of endoplasmic reticulum calcium ion concentration; regulation of cell cycle; regulation of mammary gland epithelial cell proliferation; regulation of mitochondrial membrane potential; regulation of nitrogen utilization; regulation of protein heterodimerization activity; regulation of protein homodimerization activity; release of cytochrome c from mitochondria; release of matrix enzymes from mitochondria; response to axon injury; response to cocaine; response to copper ion; response to corticosterone stimulus; response to drug; response to gamma radiation; response to salt stress; response to toxin; retina development in camera-type eye; retinal cell programmed cell death; Sertoli cell proliferation; spermatid differentiation; T cell homeostatic proliferation; transformed cell apoptosis; unfolded protein response, activation of signaling protein activity; vagina development; viral reproduction
Reference #:  Q07812 (UniProtKB)
Alt. Names/Synonyms: Apoptosis regulator BAX; BAX; Bcl-2-like protein 4; BCL2-associated X protein; Bcl2-L-4; BCL2L4
Gene Symbols: BAX
Molecular weight: 21,184 Da
Basal Isoelectric point: 5.08  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling  |  SAPK/JNK Signaling Cascades  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BAX

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
apoptosis, induced: S163‑p, T167‑p
apoptosis, inhibited: S184‑p
activity, induced: S163‑p, T167‑p, S184‑p
activity, inhibited: S184‑p
intracellular localization: S60‑p, S163‑p, T167‑p, S184‑p
phosphorylation: T167‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 10 K21‑ub TSSEQIMktGALLLQ
0 1 T22‑p SSEQIMktGALLLQG
0 4 K57‑ub VPQDASTkkLsECLK
0 1 K58‑ub PQDASTkkLsECLKR
1 0 S60‑p DASTkkLsECLKRIG
0 2 S87‑p IAAVDTDsPREVFFR
0 1 T135‑p KVPELIRtIMGWtLD
0 1 T140‑p IRtIMGWtLDFLRER
2 0 S163‑p GGWDGLLsYFGtPTW
0 1 - gap
2 0 T167‑p GLLsYFGtPTWQtVt
1 0 T172‑p FGtPTWQtVtIFVAG
1 0 T174‑p tPTWQtVtIFVAGVL
6 0 S184‑p VAGVLTAsLtIWKKM
1 0 T186‑p GVLTAsLtIWKKMG_
  BAX iso2  
K21 TSSEQIMKTGALLLQ
T22 SSEQIMKTGALLLQG
K57 VPQDASTKKLSECLK
K58 PQDASTKKLSECLKR
S60 DASTKKLSECLKRIG
S87 IAAVDTDSPREVFFR
T135 KVPELIRTIMGWTLD
T140 IRTIMGWTLDFLRER
- gap
K163‑ub GGWVRLLkPPHPHHR
- gap
- gap
- gap
- gap
- gap
  BAX iso5  
K21 TSSEQIMKTGALLLQ
T22 SSEQIMKTGALLLQG
K57 VPQDASTKKLSECLK
K58 PQDASTKKLSECLKR
S60 DASTKKLSECLKRIG
S87 IAAVDTDSPREVFFR
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  BAX iso8  
K21 TSSEQIMKTGALLLQ
T22 SSEQIMKTGALLLQG
K57 VPQDASTKKLSECLK
K58 PQDASTKKLSECLKR
S60 DASTKKLSECLKRIG
S87 IAAVDTDSPREVFFR
T135 KVPELIRTIMGWTLD
T140 IRTIMGWTLDFLRER
- gap
- gap
- gap
- gap
T161 DQGGWTVTIFVAGVL
S171 VAGVLTASLTIWKKM
T173 GVLTASLTIWKKMG_
  mouse

 
K21 TSSEQIMKTGAFLLQ
T22 SSEQIMKTGAFLLQG
K57‑ub PPQDASTkKLSECLR
K58 PQDASTkKLSECLRR
S60 DASTkKLSECLRRIG
S87‑p IADVDTDsPREVFFR
T135 KVPELIRTIMGWTLD
T140 IRTIMGWTLDFLRER
S163 GGWEGLLSYFGTPTW
- gap
T167 GLLSYFGTPTWQTVT
T172 FGTPTWQTVTIFVAG
T174 TPTWQTVTIFVAGVL
S184‑p VAGVLTAsLTIWKKM
T186 GVLTAsLTIWKKMG_
  rat

 
K21 TSSEQIMKTGAFLLQ
T22 SSEQIMKTGAFLLQG
K57 PPQDASTKKLSECLR
K58 PQDASTKKLSECLRR
S60 DASTKKLSECLRRIG
S87 IADVDTDSPREVFFR
T135 KVPELIRTIMGWTLD
T140 IRTIMGWTLDFLRER
S163 GGWDGLLSYFGTPTW
- gap
T167 GLLSYFGTPTWQTVT
T172 FGTPTWQTVTIFVAG
T174 TPTWQTVTIFVAGVL
S184‑p VAGVLTAsLTIWKKM
T186 GVLTAsLTIWKKMG_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.