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Bid (human)

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: Apoptosis; Mitochondrial Cellular Component: mitochondrial outer membrane; mitochondrion; membrane; cytosol Molecular Function: protein binding; ubiquitin protein ligase binding; death receptor binding Biological Process: release of cytochrome c from mitochondria; positive regulation of protein homooligomerization; positive regulation of apoptosis; apoptosis; response to estradiol stimulus; regulation of cell proliferation; positive regulation of protein oligomerization; neuron apoptosis; apoptotic mitochondrial changes; induction of apoptosis via death domain receptors; brain development; regulation of mitochondrial membrane permeability; protein targeting to mitochondrion; protein homooligomerization Reference #:  P55957 (UniProtKB) Alt. Names/Synonyms: apoptic death agonist; 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; BID isoform ES(1b); BID isoform L(2); BID isoform Si6; desmocollin type 4; FP497; Human BID coding sequence; MGC15319; MGC42355; p11 BID; p13 BID; p15 BID; p22 BID Gene Symbols: BID Molecular weight: 21,995 Da Basal Isoelectric point: 5.27  Predict pI for various phosphorylation states CST Pathways:  Apoptosis  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below Bid 1ZY3 - B=82-101 (human) 2BID - A=1-195 (human) 2KBW - B=76-106 (human) 4BD2 - A=1-171 (human) 1DDB - A=1-195 (mouse) 2VOI - B=76-109 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1ZY3 2BID 2KBW 4BD2  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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.			human ► Hide Isoforms
0	1		-	gap
0	274		Y54-p	LAPQWEGyDELQtDG
1	1		T59-p	EGyDELQtDGNRSSH
3	0		N62	DELQtDGNRSSHSRL
2	0		S65	QtDGNRSSHSRLGRI
0	1		S67	DGNRSSHSRLGRIEA
3	1		S78-p	RIEADSEsQEDIIRN
0	1		R123	TSRSEEDRNRDLATA
0	1		T129	DRNRDLATALEQLLQ
0	1		L135	ATALEQLLQAYPRDM
0	29		K158-u	LALLLAKkVASHTPS

	Bid iso2
S3-p	_____MCsGAGVMMA
Y100	LAPQWEGYDELQTDG
T105	EGYDELQTDGNRSSH
N108	DELQTDGNRSSHSRL
S111	QTDGNRSSHSRLGRI
S113	DGNRSSHSRLGRIEA
S124	RIEADSESQEDIIRN
-	under review
-	under review
-	under review
K204	LALLLAKKVASHTPS

	mouse
-	gap
E53	AYWEADLEDELQtDG
T58-p	DLEDELQtDGsQAsR
S61-p	DELQtDGsQAsRsFN
S64-p	QtDGsQAsRsFNQGR
S66-p	DGsQAsRsFNQGRIE
S78-p	RIEPDSEsQEEIIHN
K123-u	GSLSEEDkRNCLAkA
K129-u	DkRNCLAkALDEVkT
K135-u	AkALDEVkTAFPRDM
K158	MTMLLAKKVASHAPS

	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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