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Protein Page:
BID (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BID a pro-apoptotic member of the Bcl-2 superfamily. Targets intracellular membranes and contains a BH3 death domain. Heterodimerizes with either the pro-apoptotic protein BAX or the anti-apoptotic protein BCL2, antagonizing its protective effect. The activity of BID is regulated by Caspase 8-mediated cleavage, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, causing translocation to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced variants have been found. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Apoptosis
Cellular Component: membrane; mitochondrion; cell; cytoplasm; intracellular; cytosol
Molecular Function: protein binding; ubiquitin protein ligase binding
Biological Process: regulation of apoptosis; caspase activation; positive regulation of protein oligomerization; apoptotic mitochondrial changes; release of cytochrome c from mitochondria; apoptosis; positive regulation of protein homooligomerization; positive regulation of apoptosis; DNA damage response, signal transduction; regulation of protein oligomerization; protein targeting to mitochondrion; protein homooligomerization; regulation of cell proliferation
Reference #:  P70444 (UniProtKB)
Alt. Names/Synonyms: 2700049M22Rik; AI875481; AU022477; BH3 interacting domain death agonist; BH3-interacting domain death agonist; BH3-interacting domain death agonist p11; BH3-interacting domain death agonist p13; BH3-interacting domain death agonist p15; BID; OTTMUSP00000028756; p11 BID; p13 BID; p15 BID; p22 BID
Gene Symbols: Bid
Molecular weight: 21,952 Da
Basal Isoelectric point: 4.71  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BID

Protein Structure Not Found.


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Sites Implicated In
apoptosis, inhibited: S61‑p, S64‑p, S78‑p
cell cycle regulation: S61‑p, S78‑p
protein stabilization: S61‑p, S64‑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


 SS 

SS: 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.


 MS 

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


       mouse

 
0 1 - gap
0 241 E53 AYWEADLEDELQtDG
1 1 T58-p DLEDELQtDGsQAsR
3 0 S61-p DELQtDGsQAsRsFN
3 0 S64-p QtDGsQAsRsFNQGR
1 1 S66-p DGsQAsRsFNQGRIE
5 1 S78-p RIEPDSEsQEEIIHN
0 1 K123-ub GSLSEEDkRNCLAkA
0 1 K129-ub DkRNCLAkALDEVkT
0 1 K135-ub AkALDEVkTAFPRDM
0 29 K158 MTMLLAKKVASHAPS
  human

► Hide Isoforms
 
- gap
Y54-p LAPQWEGyDELQtDG
T59-p EGyDELQtDGNRSSH
N62 DELQtDGNRSSHsRL
S65 QtDGNRSSHsRLGRI
S67-p DGNRSSHsRLGRIEA
S78-p RIEADSEsQEDIIRN
R123 TSRSEEDRNRDLATA
T129 DRNRDLATALEQLLQ
L135 ATALEQLLQAYPRDM
K158-ub LALLLAKkVASHTPS
  BID iso2  
S3-p _____MCsGAGVMMA
Y100 LAPQWEGYDELQTDG
T105 EGYDELQTDGNRSSH
N108 DELQTDGNRSSHSRL
S111 QTDGNRSSHSRLGRI
S113 DGNRSSHSRLGRIEA
S124 RIEADSESQEDIIRN
R169 TSRSEEDRNRDLATA
T175 DRNRDLATALEQLLQ
L181 ATALEQLLQAYPRDM
K204 LALLLAKKVASHTPS
  rat

 
- gap
E54 VYLEGDREDELQTDG
T59 DREDELQTDGSRASR
S62 DELQTDGSRASRSFY
S65 QTDGSRASRSFYHGR
S67 DGSRASRSFYHGRIE
S79 RIEPDSESQDEVIHN
K124 GSLSEEDKRNCLAKA
K130 DKRNCLAKALDEVKT
K136 AKALDEVKTSFPRDM
K159 MTMLLAKKVASHAPS
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