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Protein Page:
BAK1 (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 Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BAK1 In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti- apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis. Interacts with BCL2A1. Homodimer. Formation of the homodimer is zinc-dependent. Forms heterodimers with BCL2, E1B 19k protein, and BCL2L1 isoform Bcl-X(L). Interacts with myxoma virus protein M11L. Expressed in a wide variety of tissues, with highest levels in the heart and skeletal muscle. Belongs to the Bcl-2 family. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Mitochondrial; Apoptosis; Endoplasmic reticulum
Chromosomal Location of Human Ortholog: 6p21.3
Cellular Component: pore complex; mitochondrial outer membrane; mitochondrion; endoplasmic reticulum; cytosol; integral to mitochondrial outer membrane
Molecular Function: identical protein binding; BH domain binding; protein binding; protein homodimerization activity; protein heterodimerization activity; heat shock protein binding; chaperone binding; metal ion binding
Biological Process: response to fungus; regulation of protein heterodimerization activity; apoptosis; regulation of cell cycle; positive regulation of proteolysis; positive regulation of apoptosis; myeloid cell homeostasis; negative regulation of peptidyl-serine phosphorylation; B cell apoptosis; response to organic cyclic substance; negative regulation of cell proliferation; B cell homeostasis; regulation of mitochondrial membrane potential; response to gamma radiation; establishment and/or maintenance of transmembrane electrochemical gradient; B cell negative selection; aging; response to drug; organ regeneration; release of cytochrome c from mitochondria; response to mycotoxin; mitochondrial fusion; regulation of protein homodimerization activity; vagina development; limb morphogenesis; endocrine pancreas development; response to UV-C; cell proliferation; endoplasmic reticulum calcium ion homeostasis; unfolded protein response, activation of signaling protein activity; response to ethanol; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; reduction of endoplasmic reticulum calcium ion concentration; blood vessel remodeling; regulation of mitochondrial membrane permeability; caspase activation via cytochrome c; brain development; post-embryonic camera-type eye morphogenesis
Reference #:  Q16611 (UniProtKB)
Alt. Names/Synonyms: Apoptosis regulator BAK; BAK; BAK-LIKE; BAK1; Bcl-2 homologous antagonist/killer; Bcl-2-like protein 7; BCL2-antagonist/killer 1; Bcl2-L-7; BCL2-like 7 protein; BCL2L7; CDN1; MGC117255; MGC3887; pro-apoptotic protein BAK
Gene Symbols: BAK1
Molecular weight: 23,409 Da
Basal Isoelectric point: 5.66  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BAK1

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: Y108‑p
apoptosis, inhibited: Y108‑p
activity, inhibited: Y108‑p
protein conformation: Y108‑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

 
0 1 P17 PRQECGEPALPSASE
0 1 S21 CGEPALPSASEEQVA
0 1 S23 EPALPSASEEQVAQD
2 1 Y108-p QPTAENAyEyFTKIA
2 1 Y110-p TAENAyEyFTKIATS
0 1 E120 KIATSLFESGINWGR
0 1 T148-p HVYQHGLtGFLGQVT
  mouse

 
S17-p PKVGCDEsPsPsEQQ
S19-p VGCDEsPsPsEQQVA
S21-p CDEsPsPsEQQVAQD
Y106 QPTAGNAYELFTKIA
L108 TAGNAYELFTKIASS
K118-ub KIASSLFkSGISWGR
T146 YVYQRGLTGFLGQVT
  rat

 
A17 PKGDCDEALSASEQQ
S19 GDCDEALSASEQQVA
S21 CDEALSASEQQVAQD
Y106 QPTAGNAYELFTKIA
L108 TAGNAYELFTKIASS
K118 KIASSLFKSGISWGR
T146 YVYQRGLTGFLGQVT
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